Relation Results

Identifier	Residue	Sequence	Organism
SIGNOR-123594	Ser113	WKDWEDDsDEDMSNF	Homo sapiens
pmid	sentence
15040786	Several lines of evidence suggest that a cpges-activating protein kinase is ck-ii (casein kinase ii). Recombinant cpges was phosphorylated directly by and associated with ck-ii in vitro, resulting in marked reduction of the k m for the substrate pgh2.

Identifier	Residue	Sequence	Organism
SIGNOR-123598	Ser118	DDSDEDMsNFDRFSE	Homo sapiens
pmid	sentence
15040786	Cpges-activating protein kinase is ck-ii (casein kinase ii). Mutations of either of two predicted ck-ii phosphorylation sites on cpges (ser113 and ser118) abrogated its phosphorylation and activation both in vitro and in vivo. Hypoxia induced the mitogen-activated protein kinase-mediated phosphorylation of a single serine residue, ser(122), in the protein, and site-directed mutagenesis demonstrated that ser(122) phosphorylation was necessary for hypoxic acceleration of tal1 turnover.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-200083	Ser118	EVVGGDDsDGLRAED	Homo sapiens
pmid	sentence
23226345	More recently, we identified and mapped multiple phosphorylation sites in yy1, including, threonine 39, serine 118, serine 247, threonine 348 and threonine 378. The first kinase proven to phosphorylate yy1 in vivo was plk1, which phosphorylates threonine 39 during g2/m stage of the cell cycle [25]. Ck2_ is another kinase identified as constitutively phosphorylating yy1 at serine 118. This modification protects yy1 cleavage by caspase 7 during apoptosis

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250913	Ser1181	GEYRSLEsDNEEKAF	Rattus norvegicus	Brain
pmid	sentence
8592152	Serine to alanine substitutions in these peptides indicate that the CKII phosphorylation site is at Ser1,181. \| Finally, in vivo radiolabeling indicates that Ser1,181 is phosphorylated in newborn rat brain. These data show that CKII is associated with and able to phosphorylate L1.

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism
SIGNOR-187106	Ser119	NRRKVMDsDEDDDY	Homo sapiens
pmid	sentence
19616514	Programmed cell death 5 (pdcd5), a protein involved in cell death and down-regulated in different forms of human tumors. Pdcd5 is phosphorylated in vitro by both ck2alpha subunit and by the ck2 holoenzyme at a residue, s118, which is found phosphorylated in vivo. Transfection of the non-phosphorylatable mutant (s118a) impairs the pdcd5 acceleration of either doxorubimicin- or uv-induced apoptosis in u2os cells

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-53857	Ser121	YRIQEQEsSGEEDSD	Homo sapiens
pmid	sentence
9405437	Recombinant inh2 was phosphorylated by kinases in cytosols prepared from g1 and s phase cells. The amount of inh2 kinase attributed to casein kinase 2, based on inhibition by heparin, increased 2.6-fold from g1 to s phase

Identifier	Residue	Sequence	Organism
SIGNOR-53861	Ser122	RIQEQESsGEEDSDL	Homo sapiens
pmid	sentence
9405437	Recombinant inh2 was phosphorylated by kinases in cytosols prepared from g1 and s phase cells. The amount of inh2 kinase attributed to casein kinase 2, based on inhibition by heparin, increased 2.6-fold from g1 to s phase

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-142343	Ser121	PTEEEEEsESEDSED	Homo sapiens
pmid	sentence
16308564	Casein kinase 2 (ck2)-mediated phosphorylation of three critical serine residues within a cluster of acidic amino acids in nephrocystin mediates pacs-1 binding, and is essential for colocalization of nephrocystin with pacs-1 at the base of cilia. Inhibition of ck2 activity abrogates this interaction and results in the loss of correct nephrocystin targeting.

Identifier	Residue	Sequence	Organism
SIGNOR-142347	Ser123	EEEEESEsEDSEDSG	Homo sapiens
pmid	sentence
16308564	Casein kinase 2 (ck2)-mediated phosphorylation of three critical serine residues within a cluster of acidic amino acids in nephrocystin mediates pacs-1 binding, and is essential for colocalization of nephrocystin with pacs-1 at the base of cilia. Inhibition of ck2 activity abrogates this interaction and results in the loss of correct nephrocystin targeting.

Identifier	Residue	Sequence	Organism
SIGNOR-142351	Ser126	EESESEDsEDSGGEE	Homo sapiens
pmid	sentence
16308564	Casein kinase 2 (ck2)-mediated phosphorylation of three critical serine residues within a cluster of acidic amino acids in nephrocystin mediates pacs-1 binding, and is essential for colocalization of nephrocystin with pacs-1 at the base of cilia. Inhibition of ck2 activity abrogates this interaction and results in the loss of correct nephrocystin targeting.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276038	Ser121	WEEEGFGsSSPVKSP	Homo sapiens	HeLa Cell
pmid	sentence
16085715	In the present study, we show that phosphorylation of S123 (pS123) by CDK promoted the binding of Wee1A to beta-TrCP through three independent mechanisms. S123 phosphorylation creates a PBD-binding motif and accelerates S53 phosphorylation by Plk1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250825	Ser123	HQYWSAPsDKEGYSG	Chlorocebus aethiops	COS Cell
pmid	sentence
10023679	Here we demonstrate that APE/Ref-1 is phosphorylated by casein kinase II (CKII). This was shown for both the recombinant APE/Ref-1 protein (Km=0.55 mM) and for APE/Ref-1 expressed in COS cells. Phosphorylation of APE/Ref-1 did not alter the repair activity of the enzyme, whereas it stimulated its redox capability towards AP-1, thus promoting DNA binding activity of AP-1.

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-266402	Ser127	LKKLQEEsDLELAKE	Homo sapiens	HEK-293 Cell
pmid	sentence
25887626	CK2 phosphorylates the eIF3j subunit at Ser127. CK2-phosphorylation of eIF3j triggers its association with the eIF3 complex.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-174691	Ser129	SGSPSDNsGAEEMEV	Homo sapiens	HEK-293 Cell
pmid	sentence
21735093	CK2 hyperactivates AKT by phosphorylation at Ser129

Identifier	Residue	Organism	Cell Line
SIGNOR-244400		Homo sapiens	JURKAT Cell
pmid	sentence
15818404	Akt/pkb ser129 is phosphorylated by ck2 in vitro and in vivo;(4) such a phosphorylation of activated akt/pkb correlates with a further increase in catalytic activity.

Publications:

2

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252595	Ser129	SGSPSDNsGAEEMEV	Homo sapiens	HEK-293 Cell
pmid	sentence
21735093	CK2 hyperactivates AKT by phosphorylation at Ser129

Identifier	Residue	Sequence	Organism
SIGNOR-135203	Ser129	SGSPSDNsGAEEMEV	Homo sapiens
pmid	sentence
15818404	Akt/pkb ser129 is phosphorylated by ck2 in vitro and in vivo;(4) such a phosphorylation of activated akt/pkb correlates with a further increase in catalytic activity.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-73879	Ser129	PYPSPVLsEEEDLPL	Homo sapiens
pmid	sentence
10618498	Serine residues 37 in the transactivation domain and 129, 144 and 146 in the pest domain of spi-b are phosphorylated by ckii in vitro. The ckii phosphorylation sites mapped in vitro are phosphorylated in vivo. Mutations of the ckii phosphorylation sites increase the ability of spi-b to transactivate. Spi-b phosphorylation by ckii reduces its stability

Identifier	Residue	Sequence	Organism
SIGNOR-73883	Ser144	DSPALEVsDSESDEA	Homo sapiens
pmid	sentence
10618498	Serine residues 37 in the transactivation domain and 129, 144 and 146 in the pest domain of spi-b are phosphorylated by ckii in vitro. The ckii phosphorylation sites mapped in vitro are phosphorylated in vivo. Mutations of the ckii phosphorylation sites increase the ability of spi-b to transactivate. Spi-b phosphorylation by ckii reduces its stability

Identifier	Residue	Sequence	Organism
SIGNOR-73887	Ser146	PALEVSDsESDEALV	Homo sapiens
pmid	sentence
10618498	Serine residues 37 in the transactivation domain and 129, 144 and 146 in the pest domain of spi-b are phosphorylated by ckii in vitro. The ckii phosphorylation sites mapped in vitro are phosphorylated in vivo. Mutations of the ckii phosphorylation sites increase the ability of spi-b to transactivate. Spi-b phosphorylation by ckii reduces its stability

Identifier	Residue	Sequence	Organism
SIGNOR-73891	Ser37	KHSSYPDsEGAPDSL	Homo sapiens
pmid	sentence
10618498	Serine residues 37 in the transactivation domain and 129, 144 and 146 in the pest domain of spi-b are phosphorylated by ckii in vitro. The ckii phosphorylation sites mapped in vitro are phosphorylated in vivo. Mutations of the ckii phosphorylation sites increase the ability of spi-b to transactivate. Spi-b phosphorylation by ckii reduces its stability

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-73803	Ser129	NEAYEMPsEEGYQDY	Homo sapiens
pmid	sentence
10617630	In vitro experiments and two-dimensional phosphopeptide mapping provided further evidence that serine 129 was phosphorylated by ck-1 and ck-2. Moreover, phosphorylation of serine 129 was reduced in vivo upon inhibition of ck-1 or ck-2.\| together, these data may indicate that ck-1 and ck-2 are involved in the regulation of neuronal function and one may speculate that phosphorylation of alpha-synuclein could affect its binding to membranes.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-264425	Ser1299	SHGPQFGsEVELRHS	Sus scrofa	Endothelial Cell
pmid	sentence
12386153	CK2 coprecipitated with ACE from endothelial cells, and CK2 phosphorylated both ACE and a peptide corresponding to the cytoplasmic tail. Mutation of serine(1270) within the CK2 consensus sequence almost abolished ACE phosphorylation.\|These results indicate that the CK2-mediated phosphorylation of ACE regulates its retention in the plasma membrane and may determine plasma ACE levels.

Publications:

1

Organism:

Sus Scrofa

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-250838	Ser13	VWDHIEVsDDEDETH	in vitro
pmid	sentence
12930845	Phosphorylation of serine 13 is required for the proper function of the Hsp90 co-chaperone, Cdc37. \| In this report, we demonstrate that mammalian Cdc37 is phosphorylated on Ser13 in situ in rabbit reticulocyte lysate and in cultured K562 cells and that casein kinase II is capable of quantitatively phosphorylating recombinant Cdc37 at this site.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273622	Ser13	PPPQDYEsDDDSYEV	Homo sapiens	HeLa Cell
pmid	sentence
24746696	Here, we identify that the mitochondrially localized PGAM5 phosphatase interacts with and dephosphorylates FUNDC1 at serine 13 (Ser-13) upon hypoxia or carbonylcyanide p-trifluoromethoxyphenylhydrazone (FCCP) treatment. Dephosphorylation of FUNDC1 catalyzed by PGAM5 enhances its interaction with LC3, which is abrogated following knockdown of PGAM5 or the introduction of a cell-permeable unphosphorylated peptide encompassing the Ser-13 and LIR of FUNDC1. We further observed that CK2 phosphorylates FUNDC1 to reverse the effect of PGAM5 in mitophagy activation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-144004	Ser13	ESFTMASsPAQRRRG	Homo sapiens
pmid	sentence
16446360	In this work, by in vitro kinase reactions and mass spectrometry analysis of the products, we have mapped phosphorylation sites in the n terminus of mcm2 by cdc7, cdk2, cdk1, and ck2

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276902	Ser131	DESLANLsEDEYYSE	Homo sapiens	HEK-293T Cell
pmid	sentence
25999347	We demonstrated here that phosphorylation and dephosphorylation of LSD1 at S131 and S137 was mediated by casein kinase 2 (CK2) and wild-type p53-induced phosphatase 1 (WIP1), respectively. LSD1, RNF168 and 53BP1 interacted with each other directly. CK2-mediated phosphorylation of LSD1 exhibited no impact on its interaction with 53BP1, but promoted its interaction with RNF168 and RNF168-dependent 53BP1 ubiquitination and subsequent recruitment to the DNA damage sites.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276903	Ser137	LSEDEYYsEEERNAK	Homo sapiens	HEK-293T Cell
pmid	sentence
25999347	We demonstrated here that phosphorylation and dephosphorylation of LSD1 at S131 and S137 was mediated by casein kinase 2 (CK2) and wild-type p53-induced phosphatase 1 (WIP1), respectively. LSD1, RNF168 and 53BP1 interacted with each other directly. CK2-mediated phosphorylation of LSD1 exhibited no impact on its interaction with 53BP1, but promoted its interaction with RNF168 and RNF168-dependent 53BP1 ubiquitination and subsequent recruitment to the DNA damage sites.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250902	Ser132	GAQKRKKsTKEKAGP	Homo sapiens	HeLa Cell
pmid	sentence
11115400	Here we examine the functionality of the interferon-induced factor 16 (IFI 16) CcN motif, demonstrating its ability to target a heterologous protein to the nucleus, and to be phosphorylated specifically by the CcN-motif-phosphorylating protein kinase CK2 (CK2). \| Specific phosphorylation of IFI 16 Ser132 in HeLa cell extracts and by purified CK2 in vitro

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250896	Ser133	IYPWMRSsGTDRKRG	Mus musculus	32D Cell
pmid	sentence
11290787	Thus, we concluded that CKII can phosphorylate HOXB7 in vitro and that this phosphorylation occurs at both of the CKII target sites, S133 and T204. \| Wild-type HOXB7 inhibited the differentiation of 32D cells, whereas mutations in the Pbx-binding pentapeptide motif or the DNA-binding homeodomain, as well as internal deletions of the N-terminal unique region, blocked this effect. Interestingly, mutations eliminating two target sites for casein kinase II, the glutamate-rich C terminus, or the first 14 amino acids of HOXB7, led to enhanced 32D differentiation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250897	Thr204	KTAGPGTtGQDRAEA	Mus musculus	32D Cell
pmid	sentence
11290787	Thus, we concluded that CKII can phosphorylate HOXB7 in vitro and that this phosphorylation occurs at both of the CKII target sites, S133 and T204. \| Wild-type HOXB7 inhibited the differentiation of 32D cells, whereas mutations in the Pbx-binding pentapeptide motif or the DNA-binding homeodomain, as well as internal deletions of the N-terminal unique region, blocked this effect. Interestingly, mutations eliminating two target sites for casein kinase II, the glutamate-rich C terminus, or the first 14 amino acids of HOXB7, led to enhanced 32D differentiation.

Publications:

2

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-250922	Ser133	NAIRYIEsLQELLRE	in vitro
pmid	sentence
9461343	Here, we report that Myf-5 protein constitutes a substrate for phosphorylation in vitro by protein kinase CK2. We identified two potential phosphorylation sites at serine49 and serine133, both of which seem to be necessary for Myf-5 activity.

Identifier	Residue	Sequence	Organism
SIGNOR-250923	Ser49	HKAELQGsDEDEHVR	in vitro
pmid	sentence
9461343	Here, we report that Myf-5 protein constitutes a substrate for phosphorylation in vitro by protein kinase CK2. We identified two potential phosphorylation sites at serine49 and serine133, both of which seem to be necessary for Myf-5 activity.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-167168	Ser1364	DDLNNYDsDDQEKQS	Homo sapiens
pmid	sentence
20664522	Herein, we have identified polo-like kinase 1 (plk1) and casein kinase 2 (ck2) as two kinases of clip-170 and mapped s195 and s1318 as their respective phosphorylation sites.Plk1- and ck2-associated phosphorylations of clip-170 are involved in the timely formation of kinetochore-microtubule attachments in mitosis

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276300	Ser1365	TKTSPKLsNKELKPQ	Homo sapiens	PLC-PRF-5 Cell
pmid	sentence
21254166	This study also reports the novel finding that topoIIα may be a target of GSK3β phosphorylation. Evidence suggests that CK2 serves as a priming kinase, through phosphorylation at Ser1365, for GSK3β-mediated phosphorylation at Ser1361.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250965	Ser1377	KPQKSVVsDLEADDV	Homo sapiens	HeLa Cell
pmid	sentence
7961967	Tryptic phosphopeptide mapping revealed that casein kinase II phosphorylated the C-terminal domain primarily on 2 serine residues in vitro, which were shown to be sites of modification in vivo. Site-directed mutagenesis studies identified these casein kinase II-specific phosphorylation sites as serine 1524 and serine 1376.

Identifier	Residue	Sequence	Organism
SIGNOR-250966	Thr1343	FSDFDEKtDDEDFVP	Homo sapiens
pmid	sentence
9804834	Casein kinase II catalyzes a mitotic phosphorylation on threonine 1342 of human DNA topoisomerase IIalpha

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250903	Ser138	PPAPGNAsESEEDRS	Homo sapiens	MCF-7 Cell
pmid	sentence
10650937	The importance of Ser111 and Ser113 as targets for CK2 has also been shown in our laboratory, as mutation of either residue to alanine caused a major decrease in IGFBP-3 phosphorylation by this enzyme in vitro \| These results indicate that IGFBP-3 interaction with acid-labile subunit and with the cell surface, both of which involve basic carboxyl-terminal residues, may be modulated by phosphorylation. Relative resistance to proteolysis and poor binding to cells suggest that CK2-phospho-IGFBP-3 may be a significant inhibitor of IGF activity in the extracellular environment.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250904	Ser140	APGNASEsEEDRSAG	Homo sapiens	MCF-7 Cell
pmid	sentence
10650937	The importance of Ser111 and Ser113 as targets for CK2 has also been shown in our laboratory, as mutation of either residue to alanine caused a major decrease in IGFBP-3 phosphorylation by this enzyme in vitro \| These results indicate that IGFBP-3 interaction with acid-labile subunit and with the cell surface, both of which involve basic carboxyl-terminal residues, may be modulated by phosphorylation. Relative resistance to proteolysis and poor binding to cells suggest that CK2-phospho-IGFBP-3 may be a significant inhibitor of IGF activity in the extracellular environment.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250850	Ser14	PFSFGTLsSWELEAW	Homo sapiens	HeLa Cell
pmid	sentence
12876286	CHOP transcription factor phosphorylation by casein kinase 2 inhibits transcriptional activation. \| The serine to alanine substituted site CHOP mutant was not phosphorylated by CK2, indicating that serines 14–15 and 30–31 of CHOP are the CK2 phosphoacceptor sites

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250851	Ser15	FSFGTLSsWELEAWY	Homo sapiens	HeLa Cell
pmid	sentence
12876286	CHOP transcription factor phosphorylation by casein kinase 2 inhibits transcriptional activation. \| The serine to alanine substituted site CHOP mutant was not phosphorylated by CK2, indicating that serines 14–15 and 30–31 of CHOP are the CK2 phosphoacceptor sites

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250852	Ser30	EDLQEVLsSDENGGT	Homo sapiens	HeLa Cell
pmid	sentence
12876286	CHOP transcription factor phosphorylation by casein kinase 2 inhibits transcriptional activation. \| The serine to alanine substituted site CHOP mutant was not phosphorylated by CK2, indicating that serines 14–15 and 30–31 of CHOP are the CK2 phosphoacceptor sites

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250853	Ser31	DLQEVLSsDENGGTY	Homo sapiens	HeLa Cell
pmid	sentence
12876286	CHOP transcription factor phosphorylation by casein kinase 2 inhibits transcriptional activation. \| The serine to alanine substituted site CHOP mutant was not phosphorylated by CK2, indicating that serines 14–15 and 30–31 of CHOP are the CK2 phosphoacceptor sites

Publications:

4

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-114840	Ser14	ELRTAKDsDDDDDVA	Homo sapiens
pmid	sentence
11846792	In this report, we show that syntaxin-1a is phosphorylated in vitro by cki on thr21. Casein kinase ii (ckii) has been shown previously to phosphorylate syntaxin-1a in vitro and we have identified ser14 as the ckii phosphorylation site. the phosphorylation of syntaxin-1a by ckii enhances its capacity to associate with synaptotagmin [21]. Therefore, phosphorylation of ser14 by ckii suggests an important role for this residue in regulating the interaction between syntaxin-1a and synaptotagmin

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-250949	Ser146	FYKRRGAsDLSSEEG	in vitro
pmid	sentence
8954982	Casein kinase 2 phosphorylates recombinant human spermidine/spermine N1-acetyltransferase on both serine and threonine residues. \| suggesting that the Ser-phosphorylated residues are located in the C-terminus of the protein, probably Ser 146 and 149.

Identifier	Residue	Sequence	Organism
SIGNOR-250950	Ser149	RRGASDLsSEEGWRL	in vitro
pmid	sentence
8954982	Casein kinase 2 phosphorylates recombinant human spermidine/spermine N1-acetyltransferase on both serine and threonine residues. \| suggesting that the Ser-phosphorylated residues are located in the C-terminus of the protein, probably Ser 146 and 149.

Identifier	Residue	Organism
SIGNOR-250951		in vitro
pmid	sentence
8954982	Casein kinase 2 phosphorylates recombinant human spermidine/spermine N1-acetyltransferase on both serine and threonine residues. \| suggesting that the Ser-phosphorylated residues are located in the C-terminus of the protein, probably Ser 146 and 149.

Publications:

3

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-130336	Ser1479	HVYEKLSsIESDV	Homo sapiens	Neuron
pmid	sentence
15537897	Here we show that casein kinase ii (ck2) phosphorylates the serine residue (ser1480) within the c-terminal pdz ligand (iesdv) of the nr2b subunit of nmdar in vitro and in vivo. Phosphorylation of ser1480 disrupts the interaction of nr2b with the pdz domains of psd-95 and sap102 and decreases surface nr2b expression in neurons.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-260748	Ser149	VTEPQEEsEEEVEEP	Homo sapiens	U2-OS Cell
pmid	sentence
27920254	We also show that casein kinase 2 phosphorylates G3BP1 at serine 149 in vitro and in cells. These data support a role for casein kinase 2 in regulation of protein synthesis by downregulating stress granule formation through G3BP1.CK2 regulates SG disassembly during stress recovery.G3BP1 is among the strongest SG nucleating proteins, and previous work indicated that G3BP1 phosphorylation at S149 restricts stress granule assembly by partly inhibiting G3BP1 oligomerization

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-182840	Ser1525	PIKYLEEsDEDDLF	Homo sapiens
pmid	sentence
19098900	Here we report that when phosphorylated, ser 1524 of topo iialpha acts as a binding site for the brct domain of mdc1 (mediator of dna damage checkpoint protein-1), thereby recruiting mdc1 to chromatin

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-273629	Ser153	RAEEARDsDTEGDLV	in vitro
pmid	sentence
30482149	We demonstrated for the first time that LPAP is a substrate for protein kinase CK2 that phosphorylates it at Ser153, presumably ensuring LPAP resistance to degradation.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-170872	Ser154	FLWSPFEsLCEIGEK	Homo sapiens
pmid	sentence
21209074	We report here that phosphorylation of cdc27, a core subunit of apc, in response to tgf- signaling can facilitate the activation of apc.we have demonstrated that casein kinase ii (ckii) is involved in the phosphorylation of cdc27 in response to tgf- signaling.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-140836	Ser157	LYKKLRLsTDTVEHS	Homo sapiens
pmid	sentence
16193064	Here we show that protein kinase (pk) ck2 phosphorylates procaspase-2 directly at serine-157. When intracellular pkck2 activity is low or downregulated by specific inhibitors, procaspase-2 is dephosphorylated, dimerized, and activated in a piddosome-independent manner.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250832	Ser1572	ESGISLFsDDPESDP	in vitro
pmid	sentence
10403822	Subsequent studies showed that BRCA1 was phosphorylated in vitro by CK2. An analysis by site directed mutagenesis of BRCA1 showed that in vitro phosphorylation by CK2 required a serine at aa1572. These data implicate CK2 as a potential mediator of BRCA1 activity.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-263114	Ser1575	PEICRTVsGDLAAEE	in vitro
pmid	sentence
20937870	To identify the regulatory sites of phosphorylation under physiologically relevant conditions, Ca(V)1.1 channels were purified from skeletal muscle and sites of phosphorylation on the α1 subunit were identified by mass spectrometry. Two phosphorylation sites were identified in the proximal C-terminal domain, serine 1575 (S1575) and threonine 1579 (T1579), which are conserved in cardiac Ca(V)1.2 channels (S1700 and T1704, respectively). In vitro phosphorylation revealed that Ca(V)1.1-S1575 is a substrate for both cAMP-dependent protein kinase and calcium/calmodulin-dependent protein kinase II, whereas Ca(V)1.1-T1579 is a substrate for casein kinase 2.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence
SIGNOR-276527	Ser16	QKQEPLGsDSEGVNC
pmid	sentence
34785775	Casein kinase 2 (CK2)-dependent phosphorylation of OTUB1 at Ser16 played a critical role in ODN- and cathepsin K siRNA-mediated p53 stabilization. \|Furthermore, although OTUB1 dramatically induced p53 deubiquitination, its mutant (S16A) and deletion mutant did not have this effec

Publications:

1

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-176632	Ser162	DDIDLFGsDNEEEDK	Homo sapiens	HeLa Cell
pmid	sentence
21936567	Direct phosphorylation of eef1d by ck2 was shown by performing ck2 assays with eef1d -flag from hela cells. Dramatic increases in eef1d phosphorylation following _-phosphatase treatment and phospho- eef1d antibody recognizing eef1d ps162 indicated phosphorylation at the ck2 site in cells.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250924	Ser164	FKQQRYLsAPERDQL	Chlorocebus aethiops	COS Cell
pmid	sentence
9858576	Mutational analysis and in vitro kinase assays suggested that this 40-kDa Csx/Nkx2.5 kinase is a catalytic subunit of casein kinase II (CKII) that phosphorylates the serine residue between the first and second helix of the homeodomain. This CKII site is phosphorylated in vivo. CKII-dependent phosphorylation of the homeodomain increased Csx/Nkx2. 5 DNA binding. Serine-to-alanine mutation at the CKII phosphorylation site reduced transcriptional activity when the carboxyl-terminal repressor domain was deleted.

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism
SIGNOR-178939	Ser170	KEGDVDVsDSDDEDD	Homo sapiens
pmid	sentence
18559419	Here we show that ck2 phosphorylates the transcription initiation factor tif-ia at serines 170 and 172 (ser170/172), and this phosphorylation triggers the release of tif-ia from pol i after transcription initiation.

Identifier	Residue	Sequence	Organism
SIGNOR-178943	Ser172	GDVDVSDsDDEDDNL	Homo sapiens
pmid	sentence
18559419	Here we show that ck2 phosphorylates the transcription initiation factor tif-ia at serines 170 and 172 (ser170/172), and this phosphorylation triggers the release of tif-ia from pol i after transcription initiation.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250861	Ser174	DKENGSVsSSETPPP	Homo sapiens
pmid	sentence
11861906	Mass spectrometric analysis of maximally in vitro phosphorylated eIF5 localized the major phosphorylation sites at Ser-387 and Ser-388 near the C-terminus of eIF5. These serine residues are embedded within a cluster of acidic amino acid residues and account for nearly 90% of the total in vitro eIF5 phosphorylation. A minor phosphorylation site at Ser-174 was also observed. \| The results suggest that phosphorylation of eIF5 may have a role in stimulating the rate of eIF5-promoted GTP hydrolysis.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-265872	Ser177	EVGAGYNsEDEYEAA	in vitro
pmid	sentence
22245969	Here we show that phosphorylation of the human deubiquitinase DUBA (OTUD5) at a single residue, Ser177, is both necessary and sufficient to activate the enzyme. Treatment with CK2 could activate DUBA purified from E. coli, and this activity was associated with a species monophosphorylated at Ser177 (Fig. 1d).

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-273979	Ser179	KTRAKGPsESSKERN	in vitro
pmid	sentence
25258324	Here we show that DUE-B is de-phosphorylated in M phase and phosphorylated in G1/S phase. Phosphorylated DUE-B forms homodimers, whereas de-phosphorylated DUE-B interacts with the Mcm2–7 complex and aminoacyl-tRNA synthetases. We find that CKII can prime DUE-B for Cdc7 phosphorylation. Confirming the importance of DUE-B phosphorylation in replication initiation, a C-terminal Ser/Thr to Ala mutant blocks Cdc45 and RPA loading on sperm chromatin and inhibits DNA replication. DUE-B C-terminal phosphorylation sites (serine 179, 181, 182, 194, 196, 197, 204, 205, and threonine 187) were mutated to unphosphorylatable alanine (DUE-B(S/T)-A) or phosphomimic aspartic acid (DUE-B(S/T)-D).

Identifier	Residue	Sequence	Organism
SIGNOR-273977	Ser181	RAKGPSEsSKERNTP	in vitro
pmid	sentence
25258324	Here we show that DUE-B is de-phosphorylated in M phase and phosphorylated in G1/S phase. Phosphorylated DUE-B forms homodimers, whereas de-phosphorylated DUE-B interacts with the Mcm2–7 complex and aminoacyl-tRNA synthetases. We find that CKII can prime DUE-B for Cdc7 phosphorylation. Confirming the importance of DUE-B phosphorylation in replication initiation, a C-terminal Ser/Thr to Ala mutant blocks Cdc45 and RPA loading on sperm chromatin and inhibits DNA replication. DUE-B C-terminal phosphorylation sites (serine 179, 181, 182, 194, 196, 197, 204, 205, and threonine 187) were mutated to unphosphorylatable alanine (DUE-B(S/T)-A) or phosphomimic aspartic acid (DUE-B(S/T)-D).

Identifier	Residue	Sequence	Organism
SIGNOR-273978	Ser182	AKGPSESsKERNTPR	in vitro
pmid	sentence
25258324	Here we show that DUE-B is de-phosphorylated in M phase and phosphorylated in G1/S phase. Phosphorylated DUE-B forms homodimers, whereas de-phosphorylated DUE-B interacts with the Mcm2–7 complex and aminoacyl-tRNA synthetases. We find that CKII can prime DUE-B for Cdc7 phosphorylation. Confirming the importance of DUE-B phosphorylation in replication initiation, a C-terminal Ser/Thr to Ala mutant blocks Cdc45 and RPA loading on sperm chromatin and inhibits DNA replication. DUE-B C-terminal phosphorylation sites (serine 179, 181, 182, 194, 196, 197, 204, 205, and threonine 187) were mutated to unphosphorylatable alanine (DUE-B(S/T)-A) or phosphomimic aspartic acid (DUE-B(S/T)-D).

Identifier	Residue	Sequence	Organism
SIGNOR-273970	Ser194	TPRKEDRsASSGAEG	in vitro
pmid	sentence
25258324	Here we show that DUE-B is de-phosphorylated in M phase and phosphorylated in G1/S phase. Phosphorylated DUE-B forms homodimers, whereas de-phosphorylated DUE-B interacts with the Mcm2–7 complex and aminoacyl-tRNA synthetases. We find that CKII can prime DUE-B for Cdc7 phosphorylation. Confirming the importance of DUE-B phosphorylation in replication initiation, a C-terminal Ser/Thr to Ala mutant blocks Cdc45 and RPA loading on sperm chromatin and inhibits DNA replication. DUE-B C-terminal phosphorylation sites (serine 179, 181, 182, 194, 196, 197, 204, 205, and threonine 187) were mutated to unphosphorylatable alanine (DUE-B(S/T)-A) or phosphomimic aspartic acid (DUE-B(S/T)-D).

Identifier	Residue	Sequence	Organism
SIGNOR-273971	Ser196	RKEDRSAsSGAEGDV	in vitro
pmid	sentence
25258324	Here we show that DUE-B is de-phosphorylated in M phase and phosphorylated in G1/S phase. Phosphorylated DUE-B forms homodimers, whereas de-phosphorylated DUE-B interacts with the Mcm2–7 complex and aminoacyl-tRNA synthetases. We find that CKII can prime DUE-B for Cdc7 phosphorylation. Confirming the importance of DUE-B phosphorylation in replication initiation, a C-terminal Ser/Thr to Ala mutant blocks Cdc45 and RPA loading on sperm chromatin and inhibits DNA replication. DUE-B C-terminal phosphorylation sites (serine 179, 181, 182, 194, 196, 197, 204, 205, and threonine 187) were mutated to unphosphorylatable alanine (DUE-B(S/T)-A) or phosphomimic aspartic acid (DUE-B(S/T)-D).

Identifier	Residue	Sequence	Organism
SIGNOR-273972	Ser197	KEDRSASsGAEGDVS	in vitro
pmid	sentence
25258324	Here we show that DUE-B is de-phosphorylated in M phase and phosphorylated in G1/S phase. Phosphorylated DUE-B forms homodimers, whereas de-phosphorylated DUE-B interacts with the Mcm2–7 complex and aminoacyl-tRNA synthetases. We find that CKII can prime DUE-B for Cdc7 phosphorylation. Confirming the importance of DUE-B phosphorylation in replication initiation, a C-terminal Ser/Thr to Ala mutant blocks Cdc45 and RPA loading on sperm chromatin and inhibits DNA replication. DUE-B C-terminal phosphorylation sites (serine 179, 181, 182, 194, 196, 197, 204, 205, and threonine 187) were mutated to unphosphorylatable alanine (DUE-B(S/T)-A) or phosphomimic aspartic acid (DUE-B(S/T)-D).

Identifier	Residue	Sequence	Organism
SIGNOR-273976	Ser204	SGAEGDVsSEREP	in vitro
pmid	sentence
25258324	Here we show that DUE-B is de-phosphorylated in M phase and phosphorylated in G1/S phase. Phosphorylated DUE-B forms homodimers, whereas de-phosphorylated DUE-B interacts with the Mcm2–7 complex and aminoacyl-tRNA synthetases. We find that CKII can prime DUE-B for Cdc7 phosphorylation. Confirming the importance of DUE-B phosphorylation in replication initiation, a C-terminal Ser/Thr to Ala mutant blocks Cdc45 and RPA loading on sperm chromatin and inhibits DNA replication. DUE-B C-terminal phosphorylation sites (serine 179, 181, 182, 194, 196, 197, 204, 205, and threonine 187) were mutated to unphosphorylatable alanine (DUE-B(S/T)-A) or phosphomimic aspartic acid (DUE-B(S/T)-D).

Identifier	Residue	Sequence	Organism
SIGNOR-273980	Ser205	GAEGDVSsEREP	in vitro
pmid	sentence
25258324	Here we show that DUE-B is de-phosphorylated in M phase and phosphorylated in G1/S phase. Phosphorylated DUE-B forms homodimers, whereas de-phosphorylated DUE-B interacts with the Mcm2–7 complex and aminoacyl-tRNA synthetases. We find that CKII can prime DUE-B for Cdc7 phosphorylation. Confirming the importance of DUE-B phosphorylation in replication initiation, a C-terminal Ser/Thr to Ala mutant blocks Cdc45 and RPA loading on sperm chromatin and inhibits DNA replication. DUE-B C-terminal phosphorylation sites (serine 179, 181, 182, 194, 196, 197, 204, 205, and threonine 187) were mutated to unphosphorylatable alanine (DUE-B(S/T)-A) or phosphomimic aspartic acid (DUE-B(S/T)-D).

Identifier	Residue	Sequence	Organism
SIGNOR-273975	Thr187	ESSKERNtPRKEDRS	in vitro
pmid	sentence
25258324	Here we show that DUE-B is de-phosphorylated in M phase and phosphorylated in G1/S phase. Phosphorylated DUE-B forms homodimers, whereas de-phosphorylated DUE-B interacts with the Mcm2–7 complex and aminoacyl-tRNA synthetases. We find that CKII can prime DUE-B for Cdc7 phosphorylation. Confirming the importance of DUE-B phosphorylation in replication initiation, a C-terminal Ser/Thr to Ala mutant blocks Cdc45 and RPA loading on sperm chromatin and inhibits DNA replication. DUE-B C-terminal phosphorylation sites (serine 179, 181, 182, 194, 196, 197, 204, 205, and threonine 187) were mutated to unphosphorylatable alanine (DUE-B(S/T)-A) or phosphomimic aspartic acid (DUE-B(S/T)-D).

Publications:

9

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-173668	Ser18	SPADDSLsNSEEEPD	Homo sapiens
pmid	sentence
21559372	Further investigation revealed that il-6 stabilizes twist in scchn cell lines through casein kinase 2 (ck2) phosphorylation of twist residues s18 and s20, and that this phosphorylation inhibits degradation of twist.

Identifier	Residue	Sequence	Organism
SIGNOR-173672	Ser20	ADDSLSNsEEEPDRQ	Homo sapiens
pmid	sentence
21559372	Further investigation revealed that il-6 stabilizes twist in scchn cell lines through casein kinase 2 (ck2) phosphorylation of twist residues s18 and s20, and that this phosphorylation inhibits degradation of twist.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-146825	Ser18	EKLQYYYsSSEDEDS	Homo sapiens
pmid	sentence
16717095	Phosducin-like protein (phlp) is a widely expressed binding partner of the g protein betagamma subunit complex (gbetagamma) that has been recently shown to catalyze the formation of the gbetagamma dimer from its nascent polypeptides. Phosphorylation of phlp at one or more of three consecutive serines (ser-18, ser-19, and ser-20) is necessary for gbetagamma dimer formation and is believed to be mediated by the protein kinase ck2.

Identifier	Residue	Sequence	Organism
SIGNOR-146829	Ser19	KLQYYYSsSEDEDSD	Homo sapiens
pmid	sentence
16717095	Phosducin-like protein (phlp) is a widely expressed binding partner of the g protein betagamma subunit complex (gbetagamma) that has been recently shown to catalyze the formation of the gbetagamma dimer from its nascent polypeptides. Phosphorylation of phlp at one or more of three consecutive serines (ser-18, ser-19, and ser-20) is necessary for gbetagamma dimer formation and is believed to be mediated by the protein kinase ck2.

Identifier	Residue	Sequence	Organism
SIGNOR-146833	Ser20	LQYYYSSsEDEDSDH	Homo sapiens
pmid	sentence
16717095	Phosducin-like protein (phlp) is a widely expressed binding partner of the g protein betagamma subunit complex (gbetagamma) that has been recently shown to catalyze the formation of the gbetagamma dimer from its nascent polypeptides. Phosphorylation of phlp at one or more of three consecutive serines (ser-18, ser-19, and ser-20) is necessary for gbetagamma dimer formation and is believed to be mediated by the protein kinase ck2.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-276530	Ser18	KAGEQQLsEPEDMEM
pmid	sentence
22361354	We find that stabilization of Mdm2, and correspondingly p53 downregulation in unstressed cells, is accomplished by a specific isoform of USP7 (USP7S), which is phosphorylated at serine 18 by the protein kinase CK2. Phosphorylation stabilizes USP7S and thus contributes to Mdm2 stabilization and downregulation of p53.

Publications:

1

Identifier	Residue	Sequence	Organism
SIGNOR-250890	Ser183	GPGDDLCsDLEEAPE	in vitro
pmid	sentence
12972610	Hes6 inhibits the interaction of Hes1 with its transcriptional corepressor Gro/TLE. Moreover, it promotes proteolytic degradation of Hes1. This effect is maximal when both Hes1 and Hes6 contain the WRPW motif and is reduced when Hes6 is mutated to eliminate a conserved site (Ser183) that can be phosphorylated by protein kinase CK2.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250869	Ser185	GPRVWYVsNIDGTHI	Homo sapiens	Fibrosarcoma Cell
pmid	sentence
15637053	It is known that human PGI/AMF is phosphorylated at Ser(185) by protein kinase CK2 (CK2) \| These results demonstrate that phosphorylation affects the allosteric kinetic properties of the enzyme, resulting in a less active form of PGI, whereas non-phosphorylated protein species retain cytokine activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250836	Ser186	EAGSGAAsSSGEDKE	in vitro
pmid	sentence
12527891	Mass spectrometry analysis demonstrates that at least two serine residues, Ser-186 and Ser-187, are phosphorylated in vivo. \| Finally, we demonstrate that phosphorylation of CDC25B by protein kinase CK2 increases the catalytic activity of the phosphatase in vitro as well as in vivo.

Identifier	Residue	Sequence	Organism
SIGNOR-250837	Ser187	AGSGAASsSGEDKEN	in vitro
pmid	sentence
12527891	Mass spectrometry analysis demonstrates that at least two serine residues, Ser-186 and Ser-187, are phosphorylated in vivo. \| Finally, we demonstrate that phosphorylation of CDC25B by protein kinase CK2 increases the catalytic activity of the phosphatase in vitro as well as in vivo.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-250932	Ser19	EVCDERTsLMSAESP	in vitro
pmid	sentence
8972483	In vivo phosphorylation of PS-2 was mapped to serine residues 7, 9, and 19 within an acidic stretch at the N terminus, which is absent in PS-1. casein kinase (CK)-1 and CK-2 were shown to phosphorylate the N terminus of PS-2 in vitro.

Identifier	Residue	Sequence	Organism
SIGNOR-250936	Ser7	sDSEEEVC	in vitro
pmid	sentence
8972483	In vivo phosphorylation of PS-2 was mapped to serine residues 7, 9, and 19 within an acidic stretch at the N terminus, which is absent in PS-1. casein kinase (CK)-1 and CK-2 were shown to phosphorylate the N terminus of PS-2 in vitro.

Identifier	Residue	Sequence	Organism
SIGNOR-250937	Ser9	LTFMASDsEEEVCDE	in vitro
pmid	sentence
8972483	In vivo phosphorylation of PS-2 was mapped to serine residues 7, 9, and 19 within an acidic stretch at the N terminus, which is absent in PS-1. casein kinase (CK)-1 and CK-2 were shown to phosphorylate the N terminus of PS-2 in vitro.

Publications:

3

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-265753	Ser19	AGKGGAAsGSDSADK	Homo sapiens	HeLa Cell
pmid	sentence
12860119	As proved by MALDI-TOF mass spectrometry and MS/MS fragmentation, hPar14 is phosphorylated at Ser19 in vitro and in vivo. In human HeLa cells the protein is most likely modified by casein kinase 2 (CK2). \|In contrast to wild-type hPar14, the in vitro DNA-binding affinity of the Glu19 mutant is strongly reduced, suggesting that only the dephosphorylated protein is the active DNA-binding form of hPar14 in the nucleus.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-171907	Ser1943	RKGAGDGsDEEVDGK	Homo sapiens	Breast Cancer Cell
pmid	sentence
21316371	In egf-stimulated cells, the myosin-iia heavy chain is phosphorylated on the casein kinase 2 site (s1943)

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-155987	Ser1943	RKGAGDGsDEEVDGK	Homo sapiens	Breast Cancer Cell
pmid	sentence
17567956	In egf-stimulated cells, the myosin-iia heavy chain is phosphorylated on the casein kinase 2 site (s1943)

Identifier	Residue	Sequence	Organism
SIGNOR-177818	Ser1943	RKGAGDGsDEEVDGK	Homo sapiens
pmid	sentence
22123909	In egf-stimulated cells, the myosin-iia heavy chain is phosphorylated on the casein kinase 2 site (s1943)

Identifier	Residue	Sequence	Organism
SIGNOR-181811	Ser1943	RKGAGDGsDEEVDGK	Homo sapiens
pmid	sentence
18971378	In egf-stimulated cells, the myosin-iia heavy chain is phosphorylated on the casein kinase 2 site (s1943)

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-160640	Ser198	SLPPRASsPPQILPQ	Homo sapiens	Macrophage
pmid	sentence
18250151	Ck2? Also phosphorylated lxr? At s198 in vitro, suggesting that ck2 may be a bona fide s198 kinase. our results show that macrophage lxr? Phosphorylation at s198 affects the transcriptional activity of the receptor in a gene-specific manner (fig. ?(Fig.3a)3a) and restricts the repertoire of genes regulated by lxr?

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-140994	Ser2	sGDEMIFD	Homo sapiens	HeLa Cell
pmid	sentence
16225457	The n-terminal domain of the human eif2beta subunit and the ck2 phosphorylation sites are required for its function. These results suggest that ser2 and ser67 contribute to the important role of the n-terminal region of eif2beta for its function in mammals.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-141051	Ser67	DTRKKDAsDDLDDLN	Homo sapiens	HeLa Cell
pmid	sentence
16225457	The n-terminal domain of the human eif2beta subunit and the ck2 phosphorylation sites are required for its function. These results suggest that ser2 and ser67 contribute to the important role of the n-terminal region of eif2beta for its function in mammals.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250866	Ser202	PPTETGEsSQAEENI	in vitro
pmid	sentence
1828073	Two serines located in the C-terminal end of neuromodulin, Ser-192 and Ser-193, were identified as the major casein kinase II phosphorylation sites.

Identifier	Residue	Sequence	Organism
SIGNOR-250867	Ser203	PTETGESsQAEENIE	in vitro
pmid	sentence
1828073	Phosphorylation of neuromodulin (GAP-43) by casein kinase II. Identification of phosphorylation sites and regulation by calmodulin.\|

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-110383	Ser203	APAPDEGsDLFYDDY	Homo sapiens	HeLa Cell
pmid	sentence
11546811	The ubiquitin-conjugating enzyme, cdc34, has been implicated in the ubiquitination of a number of vertebrate substrates, including p27(kip1), ikappabalpha, wee1, and myod. We show that mammalian cdc34 is a phosphoprotein that is phosphorylated in proliferating cells. Phosphorylation of cdc34 by the associated kinase maps predominantly to residues 203 and 222. Mutation of cdc34 at ck2-targeted residues, ser-203, ser-222, ser-231, thr-233, and ser-236, abolishes the phosphorylation of cdc34 observed in vivo and markedly shifts nuclearly localized cdc34 to the cytoplasm.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-110395	Ser222	EVEEEADsCFGDDED	Homo sapiens	HeLa Cell
pmid	sentence
11546811	The ubiquitin-conjugating enzyme, cdc34, has been implicated in the ubiquitination of a number of vertebrate substrates, including p27(kip1), ikappabalpha, wee1, and myod. We show that mammalian cdc34 is a phosphoprotein that is phosphorylated in proliferating cells. Phosphorylation of cdc34 by the associated kinase maps predominantly to residues 203 and 222. Mutation of cdc34 at ck2-targeted residues, ser-203, ser-222, ser-231, thr-233, and ser-236, abolishes the phosphorylation of cdc34 observed in vivo and markedly shifts nuclearly localized cdc34 to the cytoplasm.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-110399	Ser231	FGDDEDDsGTEES	Homo sapiens	HeLa Cell
pmid	sentence
11546811	The ubiquitin-conjugating enzyme, cdc34, has been implicated in the ubiquitination of a number of vertebrate substrates, including p27(kip1), ikappabalpha, wee1, and myod. We show that mammalian cdc34 is a phosphoprotein that is phosphorylated in proliferating cells. Phosphorylation of cdc34 by the associated kinase maps predominantly to residues 203 and 222. Mutation of cdc34 at ck2-targeted residues, ser-203, ser-222, ser-231, thr-233, and ser-236, abolishes the phosphorylation of cdc34 observed in vivo and markedly shifts nuclearly localized cdc34 to the cytoplasm.

Identifier	Residue	Sequence	Organism
SIGNOR-110403	Ser236	DDSGTEEs	Homo sapiens
pmid	sentence
11546811	The ubiquitin-conjugating enzyme, cdc34, has been implicated in the ubiquitination of a number of vertebrate substrates, including p27(kip1), ikappabalpha, wee1, and myod. We show that mammalian cdc34 is a phosphoprotein that is phosphorylated in proliferating cells. Phosphorylation of cdc34 by the associated kinase maps predominantly to residues 203 and 222. Mutation of cdc34 at ck2-targeted residues, ser-203, ser-222, ser-231, thr-233, and ser-236, abolishes the phosphorylation of cdc34 observed in vivo and markedly shifts nuclearly localized cdc34 to the cytoplasm.

Identifier	Residue	Sequence	Organism
SIGNOR-110407	Thr233	DDEDDSGtEES	Homo sapiens
pmid	sentence
11546811	The ubiquitin-conjugating enzyme, cdc34, has been implicated in the ubiquitination of a number of vertebrate substrates, including p27(kip1), ikappabalpha, wee1, and myod. We show that mammalian cdc34 is a phosphoprotein that is phosphorylated in proliferating cells. Phosphorylation of cdc34 by the associated kinase maps predominantly to residues 203 and 222. Mutation of cdc34 at ck2-targeted residues, ser-203, ser-222, ser-231, thr-233, and ser-236, abolishes the phosphorylation of cdc34 observed in vivo and markedly shifts nuclearly localized cdc34 to the cytoplasm.

Publications:

5

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250930	Ser204	KNSRVTFsEDDEIIN	in vitro
pmid	sentence
9407077	Phosphorylation of NIPP-1 in a heterodimeric complex with the catalytic subunit of protein phosphatase-1 resulted in an activation of the holoenzyme without a release of NIPP-1. Sequencing and phosphoamino acid analysis of tryptic phosphopeptides enabled us to identify Ser178 and Ser199 as the phosphorylation sites of protein kinase A, whereas Thr161 and Ser204 were phosphorylated by protein kinase CK2.

Identifier	Residue	Sequence	Organism
SIGNOR-250931	Thr161	LGLPEEEtELDNLTE	in vitro
pmid	sentence
9407077	Phosphorylation of NIPP-1 in a heterodimeric complex with the catalytic subunit of protein phosphatase-1 resulted in an activation of the holoenzyme without a release of NIPP-1. Sequencing and phosphoamino acid analysis of tryptic phosphopeptides enabled us to identify Ser178 and Ser199 as the phosphorylation sites of protein kinase A, whereas Thr161 and Ser204 were phosphorylated by protein kinase CK2.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-250833	Ser206	TEASGYIsSLEYPRS	in vitro
pmid	sentence
8635594	We provide evidence that this kinase phosphorylates Clr at the level of Ser189. \| Accessibility of Ser189 was low in intact C1r, due in part to the presence of one of the oligosaccharides borne by the alpha region, further reduced in the presence of calcium, and abolished when C1r was incorporated into the C1s-C1r-C1r-C1s tetramer or the C1 complex.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-153711	Ser208	SFSNLDLsEEDSDDP	Homo sapiens
pmid	sentence
17368182	Casein kinase ii (ckii) phosphorylates vdr both in vitro and in vivo at serine 208 within the hinge domain. This phosphorylation does not affect the ability of vdr to bind dna, but increases its ability to transactivate target promoters

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-150467	Ser2110	PEPSTKVsEEAESQQ	Homo sapiens
pmid	sentence
17088250	We show here that the short c-terminal splice variant of betaii-spectrin (betaiisigma2) is a substrate for phosphorylation. In vitro, protein kinase ck2 phosphorylates ser-2110 and thr-2159 / phosphorylation of ?II?2 C-terminal fragment inhibits its interaction with ?II N-terminal fragment.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-150471	Thr2159	NGATEQRtSSKESSP	Homo sapiens	Neuron
pmid	sentence
17088250	We show here that the short c-terminal splice variant of betaii-spectrin (betaiisigma2) is a substrate for phosphorylation. In vitro, protein kinase ck2 phosphorylates ser-2110 and thr-2159 / phosphorylation of ?II?2 C-terminal fragment inhibits its interaction with ?II N-terminal fragment.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250944	Ser214	LVRSREVsVDEGRAC	in vitro
pmid	sentence
9677319	CKII phosphorylate multiple C-terminal serine residues, including Ser214, Ser257, Ser273, Ser290 and Ser299. \| However, phosphorylation of Rad by PKC and CKII abolishes the interaction of Rad with calmodulin.

Identifier	Residue	Sequence	Organism
SIGNOR-250945	Ser257	QIRLRRDsKEANARR	in vitro
pmid	sentence
9677319	CKII phosphorylate multiple C-terminal serine residues, including Ser214, Ser257, Ser273, Ser290 and Ser299. \| However, phosphorylation of Rad by PKC and CKII abolishes the interaction of Rad with calmodulin.

Identifier	Residue	Sequence	Organism
SIGNOR-250947	Ser273	AGTRRREsLGKKAKR	in vitro
pmid	sentence
9677319	CKII phosphorylate multiple C-terminal serine residues, including Ser214, Ser257, Ser273, Ser290 and Ser299. \| However, phosphorylation of Rad by PKC and CKII abolishes the interaction of Rad with calmodulin.

Identifier	Residue	Sequence	Organism
SIGNOR-250948	Ser290	GRIVARNsRKMAFRA	in vitro
pmid	sentence
9677319	CKII phosphorylate multiple C-terminal serine residues, including Ser214, Ser257, Ser273, Ser290 and Ser299. \| However, phosphorylation of Rad by PKC and CKII abolishes the interaction of Rad with calmodulin.

Identifier	Residue	Sequence	Organism
SIGNOR-250946	Ser299	KMAFRAKsKSCHDLS	in vitro
pmid	sentence
9677319	CKII phosphorylate multiple C-terminal serine residues, including Ser214, Ser257, Ser273, Ser290 and Ser299. \| However, phosphorylation of Rad by PKC and CKII abolishes the interaction of Rad with calmodulin.

Publications:

5

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276425	Ser215	IKEEDTPsDNDSGIC	Homo sapiens	HeLa Cell
pmid	sentence
23123191	By using mutants of ATF4 we identified serine 215 as the main CK2 phosphorylation site. The ATF4 S215A mutant turned out to be more stable than the wild-type form.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-148010	Ser218	YHLPDAEsDEDEDFK	Homo sapiens
pmid	sentence
16857012	Here we show that human septin 2 is phosphorylated in vivo at ser218 by casein kinase ii. Septin 2 binds and hydrolyses gtp. The purified protein has the capacity to polymerize into long filaments when loaded with gtp or gdp. Moreover, we show that the endogenous protein in hela cells, like that produced in insect cells, is phosphorylated by casein kinase ii and that this phosphorylation alters nucleotide binding.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-179260	Ser226	KEREKEIsDDEAEEE	Homo sapiens
pmid	sentence
18591256	Although the kinase responsible for hsp90? Phosphorylation in vivo is not known, it has been reported that ck2 can phosphorylate these sites in vitro (24). Thus, we prephosphorylated recombinant hsp90? With ck2 before addition to the reaction. Remarkably, hsp90? Phosphorylation greatly reduced its ability to inhibit apaf-1 oligomerization and caspase-9 recruitment (fig. 5b). These results indicate that the phosphorylation status of hsp90? Significantly impacts its ability to inhibit apoptosome formation.

Identifier	Residue	Sequence	Organism
SIGNOR-179264	Ser255	PKIEDVGsDEEDDSG	Homo sapiens
pmid	sentence
18591256	Although the kinase responsible for hsp90? Phosphorylation in vivo is not known, it has been reported that ck2 can phosphorylate these sites in vitro (24). Thus, we prephosphorylated recombinant hsp90? With ck2 before addition to the reaction. Remarkably, hsp90? Phosphorylation greatly reduced its ability to inhibit apaf-1 oligomerization and caspase-9 recruitment (fig. 5b). These results indicate that the phosphorylation status of hsp90? Significantly impacts its ability to inhibit apoptosome formation.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-275738	Ser228	PGVTPSKsTSASAIM	Homo sapiens	Neuron
pmid	sentence
26917740	Bioluminescence-based screening of small molecule modulators of the FGF14:Nav1.6 complex identified 4,5,6,7 -: tetrabromobenzotriazole (TBB), a potent casein kinase 2 (CK2) inhibitor, as a strong suppressor of FGF14:Nav1.6 interaction. Inhibition of CK2 through TBB reduces the interaction of FGF14 with Nav1.6 and Nav1.2 channels. Mass spectrometry confirmed direct phosphorylation of FGF14 by CK2 at S228 and S230, and mutation to alanine at these sites modified FGF14 modulation of Nav1.6-mediated currents.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-275739	Ser230	VTPSKSTsASAIMNG	Homo sapiens	Neuron
pmid	sentence
26917740	Bioluminescence-based screening of small molecule modulators of the FGF14:Nav1.6 complex identified 4,5,6,7 -: tetrabromobenzotriazole (TBB), a potent casein kinase 2 (CK2) inhibitor, as a strong suppressor of FGF14:Nav1.6 interaction. Inhibition of CK2 through TBB reduces the interaction of FGF14 with Nav1.6 and Nav1.2 channels. Mass spectrometry confirmed direct phosphorylation of FGF14 by CK2 at S228 and S230, and mutation to alanine at these sites modified FGF14 modulation of Nav1.6-mediated currents.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-101106	Ser23	DDSYSHHsGLEYADP	Homo sapiens	Prostate Gland Cancer Cell
pmid	sentence
12743374	We show that caveolin-2 is phosphorylated in vivo at two serine residues and that the phosphorylation of caveolin-2 is necessary for its actions as a positive regulator of caveolin-1 during organelle biogenesis in prostate cancer cells. Mutation of the primary phosphorylation sites on caveolin-2, serine 23 and 36, reduces the number of plasmalemma-attached caveolae

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-101110	Ser36	DPEKFADsDQDRDPH	Homo sapiens	Prostate Gland Cancer Cell
pmid	sentence
12743374	We show that caveolin-2 is phosphorylated in vivo at two serine residues and that the phosphorylation of caveolin-2 is necessary for its actions as a positive regulator of caveolin-1 during organelle biogenesis in prostate cancer cells. Mutation of the primary phosphorylation sites on caveolin-2, serine 23 and 36, reduces the number of plasmalemma-attached caveolae

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250915	Ser231	KSNIVLLsAEEKKEQ	Homo sapiens
pmid	sentence
7678037	These data suggest taht CKII can phosphorylate more than one site on CD20 molecule. \| Taken together, this data shown that insulin can increase serine/ threonine phosphorylation and may stimulate CKII activity in B cells.

Identifier	Residue	Sequence	Organism
SIGNOR-250916	Ser289	PPQDQESsPIENDSS	Homo sapiens
pmid	sentence
7678037	These data suggest taht CKII can phosphorylate more than one site on CD20 molecule. \| Taken together, this data shown that insulin can increase erine threonine phosphorylation and may stimulate CKII activity in B cells.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250917	Thr250	KEEVVGLtETSSQPK	Homo sapiens	B-lymphocyte
pmid	sentence
7678037	These data suggest taht CKII can phosphorylate more than one site on CD20 molecule. \| Taken together, this data shown that insulin can increase erine threonine phosphorylation and may stimulate CKII activity in B cells.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250899	Ser231	KERDKEVsDDEAEEK	Homo sapiens	HeLa Cell
pmid	sentence
2492519	Both hsp 90 proteins are phosphorylated at two homologous sites. For the alpha protein, these sites correspond to serine 231 and serine 263. \| Dephosphorylated hsp 90 is phosphorylated at both sites by casein kinase II from HeLa cells, calf thymus, or rabbit reticulocytes; no other hsp 90 residues were phosphorylated by casein kinase II in vitro.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250900	Ser263	PEIEDVGsDEEEEKK	Homo sapiens	HeLa Cell
pmid	sentence
2492519	Both hsp 90 proteins are phosphorylated at two homologous sites. For the alpha protein, these sites correspond to serine 231 and serine 263. \| Dephosphorylated hsp 90 is phosphorylated at both sites by casein kinase II from HeLa cells, calf thymus, or rabbit reticulocytes; no other hsp 90 residues were phosphorylated by casein kinase II in vitro.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-264405	Ser232	LTLWTSDsAGEECDA	Homo sapiens
pmid	sentence
25862939	The neuroprotective effect of 14-3-3theta against rotenone toxicity is dependent on the inhibition of the pro-apoptotic factor Bax\|Phosphorylation at S232 induced by rotenone is reduced by casein kinase inhibitors, and is not dependent on alphasyn.\| The S232D mutant partially reduced the ability of 14-3-3theta to inhibit Bax activation in response to rotenone. Based on these findings, we propose that phosphorylation of 14-3-3s at serine 232 contributes to the neurodegenerative process in PD.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-88050	Ser233	DCYDDDDsGNEES	Homo sapiens
pmid	sentence
12037680	Ck2-dependent phosphorylation of the e2 ubiquitin conjugating enzyme ubc3b induces its interaction with beta-trcp and enhances beta-catenin degradation

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276225	Ser236	LQRALALsRQEIDME	Homo sapiens	HEK-293 Cell
pmid	sentence
19542537	Here we show that protein casein kinase 2 (CK2)-dependent phosphorylation controls the nuclear localization, aggregation and stability of ataxin-3 (ATXN3), the disease protein in spinocerebellar ataxia type 3 (SCA3). The main phosphorylation of ATXN3 in vivo thus occurred at serine residues within the three conserved UIMs.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276226	Ser335	SDLGDAMsEEDMLQA	Homo sapiens	HEK-293 Cell
pmid	sentence
19542537	Here we show that protein casein kinase 2 (CK2)-dependent phosphorylation controls the nuclear localization, aggregation and stability of ataxin-3 (ATXN3), the disease protein in spinocerebellar ataxia type 3 (SCA3). The main phosphorylation of ATXN3 in vivo thus occurred at serine residues within the three conserved UIMs.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276224	Ser347	LQAAVTMsLETVRND	Homo sapiens	HEK-293 Cell
pmid	sentence
19542537	Here we show that protein casein kinase 2 (CK2)-dependent phosphorylation controls the nuclear localization, aggregation and stability of ataxin-3 (ATXN3), the disease protein in spinocerebellar ataxia type 3 (SCA3). The main phosphorylation of ATXN3 in vivo thus occurred at serine residues within the three conserved UIMs.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-129026	Ser239	KDSSHYDsDGDKSDD	Homo sapiens
pmid	sentence
15367661	These results suggest that ck2 phosphorylation of serine 239 of gro/tle1 is important for its function during neuronal differentiation.

Identifier	Residue	Sequence	Organism
SIGNOR-196146	Ser253	DNLVVDVsNEDPSSP	Homo sapiens
pmid	sentence
22354967	These results show that tle1 is necessary for the maintenance of neuronal survival. Experiments using pharmacological inhibitors as well as expression of point mutants indicate that phosphorylation of tle1 by casein kinase-2 (ck2) at ser-239 and ser-253 is necessary for its survival-promoting activity.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250907	Ser24	GYLRKPKsMHKRFFV	in vitro
pmid	sentence
8349691	These data suggest that casein kinase II mediates a portion of the insulin-stimulated serine/threonine phosphorylation of overexpressed IRS-1 in vivo. \| Thr-502 was identified as the major casein kinase II-catalyzed phosphorylation site in rat IRS-1.

Identifier	Residue	Sequence	Organism
SIGNOR-250908	Ser330	SFRVRASsDGEGTMS	in vitro
pmid	sentence
8349691	These data suggest that casein kinase II mediates a portion of the insulin-stimulated serine/threonine phosphorylation of overexpressed IRS-1 in vivo. \| Thr-502 was identified as the major casein kinase II-catalyzed phosphorylation site in rat IRS-1.

Identifier	Residue	Sequence	Organism
SIGNOR-250909	Ser99	HFAIAADsEAEQDSW	in vitro
pmid	sentence
8349691	These data suggest that casein kinase II mediates a portion of the insulin-stimulated serine/threonine phosphorylation of overexpressed IRS-1 in vivo. \| Thr-502 was identified as the major casein kinase II-catalyzed phosphorylation site in rat IRS-1.

Identifier	Residue	Sequence	Organism
SIGNOR-250906	Thr502	TPGTGLGtSPALAGD	in vitro
pmid	sentence
8349691	These data suggest that casein kinase II mediates a portion of the insulin-stimulated serine/threonine phosphorylation of overexpressed IRS-1 in vivo. \| Thr-502 was identified as the major casein kinase II-catalyzed phosphorylation site in rat IRS-1.

Identifier	Residue	Sequence	Organism
SIGNOR-250910	Thr811	ADDSSSStSSDSLGG	in vitro
pmid	sentence
8349691	These data suggest that casein kinase II mediates a portion of the insulin-stimulated serine/threonine phosphorylation of overexpressed IRS-1 in vivo. \| Thr-502 was identified as the major casein kinase II-catalyzed phosphorylation site in rat IRS-1.

Identifier	Residue	Sequence	Organism
SIGNOR-250911	Thr88	KHLVALYtRDEHFAI	in vitro
pmid	sentence
8349691	These data suggest that casein kinase II mediates a portion of the insulin-stimulated serine/threonine phosphorylation of overexpressed IRS-1 in vivo. \| Thr-502 was identified as the major casein kinase II-catalyzed phosphorylation site in rat IRS-1.

Publications:

6

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-250943	Ser24	ADRPPSMsSHDTASP	in vitro
pmid	sentence
10760275	Phosphorylation was Mn(2+)-dependent, using both purified CK2 and CCVs. Ser-24 was identified as one of the phosphorylation sites. Our results establish that GAIP is phosphorylated and that only the membrane pool is phosphorylated, suggesting that GAIP can be regulated by phosphorylation events taking place at the level of clathrin-coated pits and vesicles.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-37831	Ser2409	LHGDDQDsEDEVLTI	Homo sapiens
pmid	sentence
8318012	The two sites phosphorylated by ck ii in vivo and in vitro are ser82 and ser157.

Identifier	Residue	Sequence	Organism
SIGNOR-37835	Ser2484	LVSFHDDsDEDLLHI	Homo sapiens
pmid	sentence
8318012	The two sites phosphorylated by ck ii in vivo and in vitro are ser82 and ser157.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250938	Ser243	AEKYAKEsLKEEDES	in vitro
pmid	sentence
8619999	Several C8 protein constructs allow the location of the CKII phosphorylation sites to be the COOH terminal portion of the protein, and direct mutational analyses show that Ser-243 and Ser-250 are the residues of the C8 subunit phosphorylated by CKII. The in vitro phosphorylation of the proteasome by CKII does not affect its proteolytic activity (on proteins or fluorogenic synthetic peptides), therefore suggesting its involvement in the interaction of the proteasome with other cellular proteins, i.e. in the formation of the 26S complex and/or in the interaction with the nuclear translocation machinery.

Identifier	Residue	Sequence	Organism
SIGNOR-250939	Ser250	SLKEEDEsDDDNM	in vitro
pmid	sentence
8619999	Several C8 protein constructs allow the location of the CKII phosphorylation sites to be the COOH terminal portion of the protein, and direct mutational analyses show that Ser-243 and Ser-250 are the residues of the C8 subunit phosphorylated by CKII. The in vitro phosphorylation of the proteasome by CKII does not affect its proteolytic activity (on proteins or fluorogenic synthetic peptides), therefore suggesting its involvement in the interaction of the proteasome with other cellular proteins, i.e. in the formation of the 26S complex and/or in the interaction with the nuclear translocation machinery.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-19603	Ser249	LSPIDMEsQERIKAE	Homo sapiens
pmid	sentence
1516134	Casein kinase ii is a negative regulator of c-jun dna binding and ap-1 activitywe show that two of these sites, thr-231 and ser-249, are phosphorylated by casein kinase ii (ckii).

Identifier	Residue	Sequence	Organism
SIGNOR-19607	Thr231	ALKEEPQtVPEMPGE	Homo sapiens
pmid	sentence
1516134	Casein kinase ii is a negative regulator of c-jun dna binding and ap-1 activitywe show that two of these sites, thr-231 and ser-249, are phosphorylated by casein kinase ii (ckii).

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-146837	Ser25	SSSEDEDsDHEDKDR	Homo sapiens
pmid	sentence
16717095	Together, these data make a strong case for ck2 phosphorylation events within the serines 18-20 and 25 sites in vivo. hey also show that phosphorylation of ser-25 and ser-296 plays no additional role in g__ expression.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-276063	Ser254	ETKLDLIsKGEEPRA	in vitro
pmid	sentence
17520485	These data suggest that inhibition of CK2-mediated phosphorylation at Ser254 had the same effect on transporter function as the actual loss of Ser254 in mENT1a, implying that this site is constitutively phosphorylated by CK2.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-133540	Ser260	SEGGADDsAEEGDLL	Homo sapiens
pmid	sentence
15687492	In contrast, hnRNP-C1 that was also modified at the CK1alpha phosphorylation sites exhibited a 14-500-fold decrease in binding affinity, demonstrating that CK1alpha-mediated phosphorylation modulates the mRNA binding ability of hnRNP-C.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250920	Ser261	TSGEDTLsDSDDEDD	in vitro
pmid	sentence
1425701	Analysis of phosphorylation sites in synthetic peptides of this acidic region identified the major sites phosphorylated by CKII as Ser261 and Ser263.

Identifier	Residue	Sequence	Organism
SIGNOR-250921	Ser263	GEDTLSDsDDEDDEE	in vitro
pmid	sentence
1425701	Analysis of phosphorylation sites in synthetic peptides of this acidic region identified the major sites phosphorylated by CKII as Ser261 and Ser263.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276388	Ser267	PPTTSSDsEEEQEDE	Homo sapiens	HEK-293 Cell
pmid	sentence
22025562	Together, our findings provide evidence for CK1α-mediated destruction of c-Myc and identify c-Myc S252 as a crucial CK1α phosphorylation site for c-Myc degradation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-152403	Ser27	SAESQYLsSVDSFGS	Homo sapiens
pmid	sentence
17241283	Our findings indicate that ck2 activation increases deltafosb's transactivation potential, while ck2 inhibition decreases it. Further, we show that preventing ser27 phosphorylation by mutating the site to ala results in a significant decrease in deltafosb transactivation

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250826	Ser276	AAQQTKGsYMEVEDN	Canis lupus familiaris	MDCK Cell
pmid	sentence
11742978	We found that the stress-induced kinase casein kinase (CK)II phosphorylates the Ser276 immediately preceding the tyrosine motif, increasing AQP4-mu 3A interaction and enhancing AQP4-lysosomal targeting and degradation. AQP4 phosphorylation by CKII may thus provide a mechanism that regulates AQP4 cell surface expression. \| To determine whether Ser276 is an actual CKII substrate, we used GST–AQP4-Cter proteins in which only one out of the three C-terminal CKII consensus sites was sequentially conserved (Ser276, Ser285 and Ser315, respectively). Figure 7B (right panel) shows that the three serine residues, including Ser276, were indeed efficiently phosphorylated by CKII.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250827	Ser285	MEVEDNRsQVETDDL	Canis lupus familiaris	MDCK Cell
pmid	sentence
11742978	We found that the stress-induced kinase casein kinase (CK)II phosphorylates the Ser276 immediately preceding the tyrosine motif, increasing AQP4-mu 3A interaction and enhancing AQP4-lysosomal targeting and degradation. AQP4 phosphorylation by CKII may thus provide a mechanism that regulates AQP4 cell surface expression. \| To determine whether Ser276 is an actual CKII substrate, we used GST–AQP4-Cter proteins in which only one out of the three C-terminal CKII consensus sites was sequentially conserved (Ser276, Ser285 and Ser315, respectively). Figure 7B (right panel) shows that the three serine residues, including Ser276, were indeed efficiently phosphorylated by CKII.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250828	Ser316	EKKGKDQsGEVLSSV	Canis lupus familiaris	MDCK Cell
pmid	sentence
11742978	We found that the stress-induced kinase casein kinase (CK)II phosphorylates the Ser276 immediately preceding the tyrosine motif, increasing AQP4-mu 3A interaction and enhancing AQP4-lysosomal targeting and degradation. AQP4 phosphorylation by CKII may thus provide a mechanism that regulates AQP4 cell surface expression. \| To determine whether Ser276 is an actual CKII substrate, we used GST–AQP4-Cter proteins in which only one out of the three C-terminal CKII consensus sites was sequentially conserved (Ser276, Ser285 and Ser315, respectively). Figure 7B (right panel) shows that the three serine residues, including Ser276, were indeed efficiently phosphorylated by CKII.

Publications:

3

Organism:

Canis Lupus Familiaris

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250925	Ser278	SPDIDNYsEEEEESF	Mus musculus	A7 Cell
pmid	sentence
14633983	Phosphorylation of Ser278 by CK2 or a Ser278-->Asp mutation increased the interaction between PACS-1 and cargo, whereas a Ser278-->Ala substitution decreased this interaction. Moreover, the Ser278-->Ala mutation yields a dominant-negative PACS-1 molecule that selectively blocks retrieval of PACS-1-regulated cargo molecules to the TGN.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-250874	Ser280	VDGTGDTsSEEDEDE	in vitro
pmid	sentence
11278496	We now show that human TFIIA is phosphorylated in vivo on serine residues that are partially conserved between yeast and human TFIIA large subunits. Alanine substitution mutation of serine residues 316 and 321 in TFIIA alphabeta reduced TFIIA phosphorylation significantly in vivo. Additional alanine substitutions at serines 280 and 281 reduced phosphorylation to undetectable levels. Mutation of all four serine residues reduced the ability of TFIIA to stimulate transcription in transient transfection assays with various activators and promoters, indicating that TFIIA phosphorylation is required globally for optimal function.

Identifier	Residue	Sequence	Organism
SIGNOR-250875	Ser281	DGTGDTSsEEDEDEE	in vitro
pmid	sentence
11278496	We now show that human TFIIA is phosphorylated in vivo on serine residues that are partially conserved between yeast and human TFIIA large subunits. Alanine substitution mutation of serine residues 316 and 321 in TFIIA alphabeta reduced TFIIA phosphorylation significantly in vivo. Additional alanine substitutions at serines 280 and 281 reduced phosphorylation to undetectable levels. Mutation of all four serine residues reduced the ability of TFIIA to stimulate transcription in transient transfection assays with various activators and promoters, indicating that TFIIA phosphorylation is required globally for optimal function.

Identifier	Residue	Sequence	Organism
SIGNOR-250876	Ser316	VEEEPLNsEDDVSDE	in vitro
pmid	sentence
11278496	We now show that human TFIIA is phosphorylated in vivo on serine residues that are partially conserved between yeast and human TFIIA large subunits. Alanine substitution mutation of serine residues 316 and 321 in TFIIA alphabeta reduced TFIIA phosphorylation significantly in vivo. Additional alanine substitutions at serines 280 and 281 reduced phosphorylation to undetectable levels. Mutation of all four serine residues reduced the ability of TFIIA to stimulate transcription in transient transfection assays with various activators and promoters, indicating that TFIIA phosphorylation is required globally for optimal function.

Identifier	Residue	Sequence	Organism
SIGNOR-250877	Ser321	LNSEDDVsDEEGQEL	in vitro
pmid	sentence
11278496	We now show that human TFIIA is phosphorylated in vivo on serine residues that are partially conserved between yeast and human TFIIA large subunits. Alanine substitution mutation of serine residues 316 and 321 in TFIIA alphabeta reduced TFIIA phosphorylation significantly in vivo. Additional alanine substitutions at serines 280 and 281 reduced phosphorylation to undetectable levels. Mutation of all four serine residues reduced the ability of TFIIA to stimulate transcription in transient transfection assays with various activators and promoters, indicating that TFIIA phosphorylation is required globally for optimal function.

Publications:

4

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-188849	Ser280	SRSQASPsEDEETFE	Homo sapiens	HeLa Cell
pmid	sentence
19851886	It was demonstrated that ck2 could phosphorylate tnfaip1 in vitro and in vivo, which facilitated the distribution of tnfaip1 in nucleus and enhanced its interaction with pcna. It is suggested that the phosphorylation of tnfaip1 may be required for its functions.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-162653	Ser282	EGRGEVGsAGDMRAA	Homo sapiens	Breast Cancer Cell, HeLa Cell
pmid	sentence
20043841	Additionally protein kinase ck2 was identified as a kinase that phosphorylated eralpha at s282 and s559 s282 and s559 represent the second and third sites of er_ regulation by ck2. Remarkably, mutation of s282 or s559 to alanine resulted in near opposite functional effects on er_ as compared to mutation of s167 to alanine. Er_ ligand independent transcriptional activity was markedly enhanced upon mutation of s282 and s559 to alanine

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-162657	Ser559	PTSRGGAsVEETDQS	Homo sapiens	Breast Cancer Cell, HeLa Cell
pmid	sentence
20043841	Additionally protein kinase ck2 was identified as a kinase that phosphorylated eralpha at s282 and s559 s282 and s559 represent the second and third sites of er_ regulation by ck2. Remarkably, mutation of s282 or s559 to alanine resulted in near opposite functional effects on er_ as compared to mutation of s167 to alanine. Er_ ligand independent transcriptional activity was markedly enhanced upon mutation of s282 and s559 to alanine

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-40502	Ser283	NLQMLPEsEDEESYD	Homo sapiens	T-lymphocyte
pmid	sentence
8622692	Casein kinase ii phosphorylates i kappa b alpha at s-283, s-289, s-293, and t-291 and is required for its degradation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-40506	Ser288	PESEDEEsYDTESEF	Homo sapiens	T-lymphocyte
pmid	sentence
8622692	Casein kinase ii phosphorylates i kappa b alpha at s-283, s-289, s-293, and t-291 and is required for its degradation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-40510	Ser293	EESYDTEsEFTEFTE	Homo sapiens	T-lymphocyte
pmid	sentence
8622692	Casein kinase ii phosphorylates i kappa b alpha at s-283, s-289, s-293, and t-291 and is required for its degradation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-40514	Thr291	EDEESYDtESEFTEF	Homo sapiens	T-lymphocyte
pmid	sentence
8622692	Casein kinase ii phosphorylates i kappa b alpha at s-283, s-289, s-293, and t-291 and is required for its degradation.

Publications:

4

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-155740	Ser284	GGAGGEGsDDDTSLT	Homo sapiens	HEK-293T Cell
pmid	sentence
17561512	Interestingly, hypotonic extracts prepared from hek293t cells expressing the serine to alanine mutant exhibited increased lipid transfer activity compared with those from wild-type stard10-expressing cells, suggesting that, in a cellular context, phosphorylation on serine 284 negatively regulates stard10 activity

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250863	Ser289	ITDVHMVsDSDGDDF	Chlorocebus aethiops
pmid	sentence
12832043	We previously identified the Fas-associated factor FAF1 as an in vitro substrate of protein kinase CK2 and determined Ser289 and Ser291 as phosphorylation sites.\|Therefore we assume that CK2‐mediated FAF1 phosphorylation influences the nuclear localization of FAF1 \| it implies that the major function of FAF1 might not be in the cytoplasm as an interacting partner of Fas.

Identifier	Residue	Sequence	Organism
SIGNOR-250864	Ser291	DVHMVSDsDGDDFED	Chlorocebus aethiops
pmid	sentence
12832043	We previously identified the Fas-associated factor FAF1 as an in vitro substrate of protein kinase CK2 and determined Ser289 and Ser291 as phosphorylation sites.\|Therefore we assume that CK2‐mediated FAF1 phosphorylation influences the nuclear localization of FAF1 \| it implies that the major function of FAF1 might not be in the cytoplasm as an interacting partner of Fas.

Publications:

2

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250846	Ser29	VSHWQQQsYLDSGIH	Homo sapiens	HEK-293 Cell
pmid	sentence
12432063	We show that CKII phosphorylates the N-terminal region of beta-catenin and we identified Ser29, Thr102, and Thr112 as substrates for the enzyme. We provide evidence that CKII regulates the cytoplasmic stability of beta-catenin and acts synergistically with GSK-3beta in the multi-protein complex that controls the degradation of beta-catenin

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250847	Thr102	RAAMFPEtLDEGMQI	Homo sapiens	HEK-293 Cell
pmid	sentence
12432063	We show that CKII phosphorylates the N-terminal region of beta-catenin and we identified Ser29, Thr102, and Thr112 as substrates for the enzyme. We provide evidence that CKII regulates the cytoplasmic stability of beta-catenin and acts synergistically with GSK-3beta in the multi-protein complex that controls the degradation of beta-catenin

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250848	Thr112	EGMQIPStQFDAAHP	Homo sapiens	HEK-293 Cell
pmid	sentence
12432063	We show that CKII phosphorylates the N-terminal region of beta-catenin and we identified Ser29, Thr102, and Thr112 as substrates for the enzyme. We provide evidence that CKII regulates the cytoplasmic stability of beta-catenin and acts synergistically with GSK-3beta in the multi-protein complex that controls the degradation of beta-catenin

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250849	Thr393	RNLSDAAtKQEGMEG	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
12700239	The major CK2 phosphorylation site in this domain is Thr393, a solvent-accessible residue in a key hinge region of the molecule. Mutation of this single amino acid reduces beta-catenin phosphorylation, cotranscriptional activity, and stability.

Publications:

4

Organism:

Homo Sapiens, Chlorocebus Aethiops

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-250823	Ser29	GSVSEDNsEDEISNL	in vitro
pmid	sentence
2900140	These results show that casein kinase-2 phosphorylates site 6 exclusively

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-275998	Ser29	VSHWQQQsYLDSGIH	in vitro
pmid	sentence
12432063	We show that CKII phosphorylates the N-terminal region of beta-catenin and we identified Ser29, Thr102, and Thr112 as substrates for the enzyme. We provide evidence that CKII regulates the cytoplasmic stability of beta-catenin and acts synergistically with GSK-3beta in the multi-protein complex that controls the degradation of beta-catenin.

Identifier	Residue	Sequence	Organism
SIGNOR-275996	Thr102	RAAMFPEtLDEGMQI	in vitro
pmid	sentence
12432063	We show that CKII phosphorylates the N-terminal region of beta-catenin and we identified Ser29, Thr102, and Thr112 as substrates for the enzyme. We provide evidence that CKII regulates the cytoplasmic stability of beta-catenin and acts synergistically with GSK-3beta in the multi-protein complex that controls the degradation of beta-catenin.

Identifier	Residue	Sequence	Organism
SIGNOR-275997	Thr112	EGMQIPStQFDAAHP	in vitro
pmid	sentence
12432063	We show that CKII phosphorylates the N-terminal region of beta-catenin and we identified Ser29, Thr102, and Thr112 as substrates for the enzyme. We provide evidence that CKII regulates the cytoplasmic stability of beta-catenin and acts synergistically with GSK-3beta in the multi-protein complex that controls the degradation of beta-catenin.

Publications:

3

Organism:

In Vitro

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277397	Ser292	VVSPSTDsGLEFSSQ	Homo sapiens	HEK-293T Cell
pmid	sentence
29898406	We show that, in mitosis, GBF1 is phosphorylated on Ser292 and Ser297 by casein kinase-2 allowing recognition by the F-box protein βTrCP. GBF1 interaction with βTrCP recruits GBF1 to the SCFβTrCP ubiquitin ligase complex, triggering its degradation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277398	Ser297	TDSGLEFsSQTTSKE	Homo sapiens	HEK-293T Cell
pmid	sentence
29898406	We show that, in mitosis, GBF1 is phosphorylated on Ser292 and Ser297 by casein kinase-2 allowing recognition by the F-box protein βTrCP. GBF1 interaction with βTrCP recruits GBF1 to the SCFβTrCP ubiquitin ligase complex, triggering its degradation.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-179875	Ser299	SQPPGEDsDTDVDDD	Homo sapiens
pmid	sentence
18678890	The mdc1-nbs1 interaction occurs through a specific region (residues 200-420) of mdc1, which contains multiple consensus casein kinase 2 (ck2) phosphorylation sites.

Identifier	Residue	Sequence	Organism
SIGNOR-179879	Ser376	LQESQAGsDTDVEEG	Homo sapiens
pmid	sentence
18678890	The mdc1-nbs1 interaction occurs through a specific region (residues 200-420) of mdc1, which contains multiple consensus casein kinase 2 (ck2) phosphorylation sites.

Identifier	Residue	Sequence	Organism
SIGNOR-179883	Thr301	PPGEDSDtDVDDDSR	Homo sapiens
pmid	sentence
18678890	The mdc1-nbs1 interaction occurs through a specific region (residues 200-420) of mdc1, which contains multiple consensus casein kinase 2 (ck2) phosphorylation sites.

Identifier	Residue	Sequence	Organism
SIGNOR-179887	Thr378	ESQAGSDtDVEEGKA	Homo sapiens
pmid	sentence
18678890	The mdc1-nbs1 interaction occurs through a specific region (residues 200-420) of mdc1, which contains multiple consensus casein kinase 2 (ck2) phosphorylation sites.

Identifier	Residue	Sequence	Organism
SIGNOR-179891	Thr455	TTERDSDtDVEEEEL	Homo sapiens
pmid	sentence
18678890	The mdc1-nbs1 interaction occurs through a specific region (residues 200-420) of mdc1, which contains multiple consensus casein kinase 2 (ck2) phosphorylation sites.

Identifier	Residue	Organism
SIGNOR-184130		Homo sapiens
pmid	sentence
19230643	Mdc1 also undergoes phosphorylation by ck2 after dna damage to generate a phospho-motif on mdc1, which binds directly to nbs1.

Publications:

6

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-119090	Ser30	RNLLEDDsDEEEDFF	Homo sapiens
pmid	sentence
14608369	The r-snare vamp4, which contains a dileucine motif, binds to the ap-1 or the ggas. Serine 20 and leucines 25,26 are essential for this binding. Ap-1 association with vamp4 is enhanced when serine 30 is phosphorylated by casein kinase 2. This phosphorylation-dependent modulation of ap-1 binding is mediated by pacs-1 (phosphofurin acidic cluster sorting protein). Ablation of both the dileucine motif and serine 30 results in a dramatic mislocalization of vamp4 in the regulated secretory pathway.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-266407	Ser30	MNGEEEEsEEERSGS	in vitro
pmid	sentence
26980766	We show that BRMS1 is posttranslationally regulated by TNF-induced casein kinase 2 catalytic subunit (CK2α') phosphorylation of nuclear BRMS1 on serine 30 (S30), resulting in 14-3-3ε-mediated nuclear exportation, increased BRMS1 cytosolic expression, and ubiquitin-proteasome-induced BRMS1 degradation.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-71014	Ser304	DGEEEGEsDGTHPVG	Homo sapiens	HeLa Cell
pmid	sentence
10508590	Here, we demonstrate the partial purification of a protein kinase that phosphorylates the type iialpha pip kinase at a single site unique to that isoform - ser304. This kinase was identified as protein kinase ck2 (formerly casein kinase 2). Mutation of ser304 to aspartate to mimic its phosphorylation had no effect on pip kinase activity, but promoted both redistribution of the green fluorescent protein (gfp)-tagged enzyme in hela cells from the cytosol to the plasma membrane, and membrane ruffling.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-249332	Ser32	LLDDRHDsGLDSMKD
pmid	sentence
10398585	Serine 32 and serine 36 of IkappaBalpha are directly phosphorylated by protein kinase CKII in vitro\|Phosphorylation of IkappaBalpha at serine 32 (S32) and serine 36 (S36) is necessary for this stimuli-induced degradation

Identifier	Residue	Sequence
SIGNOR-249333	Ser36	RHDSGLDsMKDEEYE
pmid	sentence
10398585	Serine 32 and serine 36 of IkappaBalpha are directly phosphorylated by protein kinase CKII in vitro\|Phosphorylation of IkappaBalpha at serine 32 (S32) and serine 36 (S36) is necessary for this stimuli-induced degradation

Publications:

2

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-147365	Ser32	MPGPREEsEEEEDED	Homo sapiens
pmid	sentence
16809543	Dek phosphorylated at serines 19 and 32. Dek and its phosphorylation are required for intron removal

Identifier	Residue	Sequence	Organism
SIGNOR-125912	Ser32	MPGPREEsEEEEDED	Homo sapiens
pmid	sentence
15199154	Dek is phosphorylated by the protein kinase ck2 in vitro and in vivo on ser32

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276268	Ser324	PFRPQIRsELDVGNF	Homo sapiens	HEK-293T Cell
pmid	sentence
19933278	Here we report that the CK2 protein kinase, which contributes to NF-kappaB activation following UV radiation in a p38-dependent manner, physically interacts with MSK2 but not MSK1 and that CK2 inhibition specifically impairs UV-induced MSK2 kinase activation. A putative site of CK2 phosphorylation was mapped to MSK2 residue Ser(324) and when substituted to alanine (S324A) also compromised MSK2 activity.Serine 324 is required for UV-induced MSK2 activation and for autophosphorylation at MSK2-Ser196.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250933	Ser327	DPEMEEDsYDSFGEP	in vitro
pmid	sentence
9558331	In vitro the large hydrophilic loop of PS-2 between transmembrane domains 6 and 7 can be phosphorylated by casein kinase-1 (CK-1) and CK-2, but not by PKA or PKC. Quantitative analysis of in vitro phosphorylation demonstrates the presence of two phosphorylation sites for CK-1 and a single site for CK-2. A deletion analysis revealed that the CTF of PS-2 is phosphorylated in vivo within an acidic sequence containing three potential phosphorylation sites for CKs (serines 327, 330, and 335). These data suggest that CK type protein kinases phosphorylate the CTF of PS-2 within its hydrophilic loop domain in vivo. Interestingly, the potential phosphorylation sites are located directly adjacent to the recently identified caspase cleavage sites.

Identifier	Residue	Sequence	Organism
SIGNOR-250934	Ser330	MEEDSYDsFGEPSYP	in vitro
pmid	sentence
9558331	In vitro the large hydrophilic loop of PS-2 between transmembrane domains 6 and 7 can be phosphorylated by casein kinase-1 (CK-1) and CK-2, but not by PKA or PKC. Quantitative analysis of in vitro phosphorylation demonstrates the presence of two phosphorylation sites for CK-1 and a single site for CK-2. A deletion analysis revealed that the CTF of PS-2 is phosphorylated in vivo within an acidic sequence containing three potential phosphorylation sites for CKs (serines 327, 330, and 335). These data suggest that CK type protein kinases phosphorylate the CTF of PS-2 within its hydrophilic loop domain in vivo. Interestingly, the potential phosphorylation sites are located directly adjacent to the recently identified caspase cleavage sites.

Identifier	Residue	Sequence	Organism
SIGNOR-250935	Ser335	YDSFGEPsYPEVFEP	in vitro
pmid	sentence
9558331	In vitro the large hydrophilic loop of PS-2 between transmembrane domains 6 and 7 can be phosphorylated by casein kinase-1 (CK-1) and CK-2, but not by PKA or PKC. Quantitative analysis of in vitro phosphorylation demonstrates the presence of two phosphorylation sites for CK-1 and a single site for CK-2. A deletion analysis revealed that the CTF of PS-2 is phosphorylated in vivo within an acidic sequence containing three potential phosphorylation sites for CKs (serines 327, 330, and 335). These data suggest that CK type protein kinases phosphorylate the CTF of PS-2 within its hydrophilic loop domain in vivo. Interestingly, the potential phosphorylation sites are located directly adjacent to the recently identified caspase cleavage sites.

Publications:

3

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273990	Ser341	KVSKDDRsDIESSSD	Homo sapiens	HEK-293 Cell
pmid	sentence
26887952	Most of the phosphorylated residues conformed to a consensus motif for phosphorylation by casein kinase 2 (CK2), and treatment of cells with the CK2-specific inhibitor CX-4945 lowered the phosphorylation levels of CERS2, -4, -5, and -6. Phosphorylation of CERS2 was especially important for its catalytic activity, acting mainly by increasing itsVmaxvalue.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273991	Ser345	DDRSDIEsSSDEEDS	Homo sapiens	HEK-293 Cell
pmid	sentence
26887952	Most of the phosphorylated residues conformed to a consensus motif for phosphorylation by casein kinase 2 (CK2), and treatment of cells with the CK2-specific inhibitor CX-4945 lowered the phosphorylation levels of CERS2, -4, -5, and -6. Phosphorylation of CERS2 was especially important for its catalytic activity, acting mainly by increasing itsVmaxvalue.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273992	Ser346	DRSDIESsSDEEDSE	Homo sapiens	HEK-293 Cell
pmid	sentence
26887952	Most of the phosphorylated residues conformed to a consensus motif for phosphorylation by casein kinase 2 (CK2), and treatment of cells with the CK2-specific inhibitor CX-4945 lowered the phosphorylation levels of CERS2, -4, -5, and -6. Phosphorylation of CERS2 was especially important for its catalytic activity, acting mainly by increasing itsVmaxvalue.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273989	Ser347	RSDIESSsDEEDSEP	Homo sapiens	HEK-293 Cell
pmid	sentence
26887952	Most of the phosphorylated residues conformed to a consensus motif for phosphorylation by casein kinase 2 (CK2), and treatment of cells with the CK2-specific inhibitor CX-4945 lowered the phosphorylation levels of CERS2, -4, -5, and -6. Phosphorylation of CERS2 was especially important for its catalytic activity, acting mainly by increasing itsVmaxvalue.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273981	Ser342	QMEKDIRsDVEESDS	Homo sapiens	HEK-293 Cell
pmid	sentence
26887952	Most of the phosphorylated residues conformed to a consensus motif for phosphorylation by casein kinase 2 (CK2), and treatment of cells with the CK2-specific inhibitor CX-4945 lowered the phosphorylation levels of CERS2, -4, -5, and -6. Phosphorylation of CERS2 was especially important for its catalytic activity, acting mainly by increasing itsVmaxvalue.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273983	Ser347	IRSDVEEsDSSEEAA	Homo sapiens	HEK-293 Cell
pmid	sentence
26887952	Most of the phosphorylated residues conformed to a consensus motif for phosphorylation by casein kinase 2 (CK2), and treatment of cells with the CK2-specific inhibitor CX-4945 lowered the phosphorylation levels of CERS2, -4, -5, and -6. Phosphorylation of CERS2 was especially important for its catalytic activity, acting mainly by increasing itsVmaxvalue.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273984	Ser349	SDVEESDsSEEAAAA	Homo sapiens	HEK-293 Cell
pmid	sentence
26887952	Most of the phosphorylated residues conformed to a consensus motif for phosphorylation by casein kinase 2 (CK2), and treatment of cells with the CK2-specific inhibitor CX-4945 lowered the phosphorylation levels of CERS2, -4, -5, and -6. Phosphorylation of CERS2 was especially important for its catalytic activity, acting mainly by increasing itsVmaxvalue.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273982	Ser350	DVEESDSsEEAAAAQ	Homo sapiens	HEK-293 Cell
pmid	sentence
26887952	Most of the phosphorylated residues conformed to a consensus motif for phosphorylation by casein kinase 2 (CK2), and treatment of cells with the CK2-specific inhibitor CX-4945 lowered the phosphorylation levels of CERS2, -4, -5, and -6. Phosphorylation of CERS2 was especially important for its catalytic activity, acting mainly by increasing itsVmaxvalue.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-147879	Ser347	SSDLSIAsSEEDKLS	Homo sapiens
pmid	sentence
16837460	Slk down-regulation by v-src is indirect and is accompanied by slk hyperphosphorylation on serine residues. Deletion analysis revealed that casein kinase ii (ck2) sites at position 347/348 are critical for v-src-dependent modulation of slk activity.

Identifier	Residue	Sequence	Organism
SIGNOR-147883	Ser348	SDLSIASsEEDKLSQ	Homo sapiens
pmid	sentence
16837460	Slk down-regulation by v-src is indirect and is accompanied by slk hyperphosphorylation on serine residues. Deletion analysis revealed that casein kinase ii (ck2) sites at position 347/348 are critical for v-src-dependent modulation of slk activity.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273624	Ser347	RPEVVLDsDAEDLED	Homo sapiens	HEK-293 Cell
pmid	sentence
21262846	CK2 physiologically phosphorylates IP6K2 at amino acid residues S347 and S356 contained within a PEST sequence, a consensus site for ubiquitination. HCT116 cells depleted of IP6K2 are resistant to cell death elicited by CK2 inhibitors. CK2 phosphorylation at the degradation motif of IP6K2 enhances its ubiquitination and subsequent degradation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273625	Ser356	AEDLEDLsEESADES	Homo sapiens	HEK-293 Cell
pmid	sentence
21262846	CK2 physiologically phosphorylates IP6K2 at amino acid residues S347 and S356 contained within a PEST sequence, a consensus site for ubiquitination. HCT116 cells depleted of IP6K2 are resistant to cell death elicited by CK2 inhibitors. CK2 phosphorylation at the degradation motif of IP6K2 enhances its ubiquitination and subsequent degradation.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273988	Ser350	KVSKDDRsDVESSSE	Homo sapiens	HEK-293 Cell
pmid	sentence
26887952	Most of the phosphorylated residues conformed to a consensus motif for phosphorylation by casein kinase 2 (CK2), and treatment of cells with the CK2-specific inhibitor CX-4945 lowered the phosphorylation levels of CERS2, -4, -5, and -6. Phosphorylation of CERS2 was especially important for its catalytic activity, acting mainly by increasing itsVmaxvalue.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273985	Ser354	DDRSDVEsSSEEEDV	Homo sapiens	HEK-293 Cell
pmid	sentence
26887952	Most of the phosphorylated residues conformed to a consensus motif for phosphorylation by casein kinase 2 (CK2), and treatment of cells with the CK2-specific inhibitor CX-4945 lowered the phosphorylation levels of CERS2, -4, -5, and -6. Phosphorylation of CERS2 was especially important for its catalytic activity, acting mainly by increasing itsVmaxvalue.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273987	Ser355	DRSDVESsSEEEDVT	Homo sapiens	HEK-293 Cell
pmid	sentence
26887952	Most of the phosphorylated residues conformed to a consensus motif for phosphorylation by casein kinase 2 (CK2), and treatment of cells with the CK2-specific inhibitor CX-4945 lowered the phosphorylation levels of CERS2, -4, -5, and -6. Phosphorylation of CERS2 was especially important for its catalytic activity, acting mainly by increasing itsVmaxvalue.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273986	Ser356	RSDVESSsEEEDVTT	Homo sapiens	HEK-293 Cell
pmid	sentence
26887952	Most of the phosphorylated residues conformed to a consensus motif for phosphorylation by casein kinase 2 (CK2), and treatment of cells with the CK2-specific inhibitor CX-4945 lowered the phosphorylation levels of CERS2, -4, -5, and -6. Phosphorylation of CERS2 was especially important for its catalytic activity, acting mainly by increasing itsVmaxvalue.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273623	Ser355	EQPSASVsLLDDELM	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
12060753	Serine-355 of GGA1 is phosphorylated in vivo and in vitro. This inhibition is caused by the binding of an AC-LL sequence present in the hinge segment to the ligand-binding site in the VHS domain. The inhibition depends on the phosphorylation of a serine located three residues upstream of the AC-LL motif. The serine is phosphorylated by casein kinase 2 in in vitro assays.

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism
SIGNOR-250870	Ser356	VDGSGDTsSNEEIGS	in vitro
pmid	sentence
12107178	ALF was able to stabilize the binding of TBP to DNA, but it could not stabilize TBP mutants A184E, N189E, E191R, and R205E nor could it facilitate binding of the TBP-like factor TRF2/TLF to a consensus TATA element. However, phosphorylation of ALF with casein kinase II resulted in the partial restoration of complex formation using mutant TBPs. \| Because the residues involved (Ser-280, Ser-281, Ser-316, and Ser-321) are conserved in ALF (Ser-356, Ser-357, Ser-418, and Ser-423), we tested whether its activity might also be affected by this modification. We first showed that ALF and TFIIAα/β polypeptides incubated with casein kinase II and [γ-32P]ATP could be labeled.

Identifier	Residue	Sequence	Organism
SIGNOR-250871	Ser357	DGSGDTSsNEEIGST	in vitro
pmid	sentence
12107178	ALF was able to stabilize the binding of TBP to DNA, but it could not stabilize TBP mutants A184E, N189E, E191R, and R205E nor could it facilitate binding of the TBP-like factor TRF2/TLF to a consensus TATA element. However, phosphorylation of ALF with casein kinase II resulted in the partial restoration of complex formation using mutant TBPs. \| Because the residues involved (Ser-280, Ser-281, Ser-316, and Ser-321) are conserved in ALF (Ser-356, Ser-357, Ser-418, and Ser-423), we tested whether its activity might also be affected by this modification. We first showed that ALF and TFIIAα/β polypeptides incubated with casein kinase II and [γ-32P]ATP could be labeled.

Identifier	Residue	Sequence	Organism
SIGNOR-250872	Ser418	VEEDPLNsGDDVSEQ	in vitro
pmid	sentence
12107178	ALF was able to stabilize the binding of TBP to DNA, but it could not stabilize TBP mutants A184E, N189E, E191R, and R205E nor could it facilitate binding of the TBP-like factor TRF2/TLF to a consensus TATA element. However, phosphorylation of ALF with casein kinase II resulted in the partial restoration of complex formation using mutant TBPs. \| Because the residues involved (Ser-280, Ser-281, Ser-316, and Ser-321) are conserved in ALF (Ser-356, Ser-357, Ser-418, and Ser-423), we tested whether its activity might also be affected by this modification. We first showed that ALF and TFIIAα/β polypeptides incubated with casein kinase II and [γ-32P]ATP could be labeled.

Identifier	Residue	Sequence	Organism
SIGNOR-250873	Ser423	LNSGDDVsEQDVPDL	in vitro
pmid	sentence
12107178	ALF was able to stabilize the binding of TBP to DNA, but it could not stabilize TBP mutants A184E, N189E, E191R, and R205E nor could it facilitate binding of the TBP-like factor TRF2/TLF to a consensus TATA element. However, phosphorylation of ALF with casein kinase II resulted in the partial restoration of complex formation using mutant TBPs. \| Because the residues involved (Ser-280, Ser-281, Ser-316, and Ser-321) are conserved in ALF (Ser-356, Ser-357, Ser-418, and Ser-423), we tested whether its activity might also be affected by this modification. We first showed that ALF and TFIIAα/β polypeptides incubated with casein kinase II and [γ-32P]ATP could be labeled.

Publications:

4

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-143948	Ser358	AKVLASLsDDEDEEE	Homo sapiens
pmid	sentence
16428860	Phosphorylation of rangap1 stabilizes its interaction with ran and ranbp1. Serine-358 (358s) was identified as the major phosphorylation site. Experiments using purified recombinant kinase and specific inhibitors such as drb and apigenin strongly suggest that casein kinase ii (ck2) is the responsible kinase

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-167544	Ser36	AQQVSSLsESEESQD	Homo sapiens
pmid	sentence
20730097	Although the functional impact of ck-mediated atf1 phosphorylation is still unclear, we found that mutation of ser-36 and ser-41 increased cbp kix domain binding by up to four fold (fig. 2g). This result is consistent with the negative impact of ck-mediated phosphorylation on cbp binding affinity of creb that we previously reported

Identifier	Residue	Sequence	Organism
SIGNOR-167548	Ser38	QVSSLSEsEESQDSS	Homo sapiens
pmid	sentence
20730097	These data suggested that atf1 is always hyperphosphorylated on the ck sites in vivo. Also, the antibody reactivity suggested that in addition to ser-36 and ser-41, ser-38 and ser-44 were phosphorylated in vivo. To accommodate these findings, we propose that constitutive hyperphosphorylation by ck1/ck2 maintains atf1 in an inactive state that promotes transcriptional repression.

Identifier	Residue	Sequence	Organism
SIGNOR-167552	Ser41	SLSESEEsQDSSDSI	Homo sapiens
pmid	sentence
20730097	Although the functional impact of ck-mediated atf1 phosphorylation is still unclear, we found that mutation of ser-36 and ser-41 increased cbp kix domain binding by up to four fold (fig. 2g). This result is consistent with the negative impact of ck-mediated phosphorylation on cbp binding affinity of creb that we previously reported

Identifier	Residue	Sequence	Organism
SIGNOR-167556	Ser44	ESEESQDsSDSIGSS	Homo sapiens
pmid	sentence
20730097	These data suggested that atf1 is always hyperphosphorylated on the ck sites in vivo. Also, the antibody reactivity suggested that in addition to ser-36 and ser-41, ser-38 and ser-44 were phosphorylated in vivo. To accommodate these findings, we propose that constitutive hyperphosphorylation by ck1/ck2 maintains atf1 in an inactive state that promotes transcriptional repression.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-244521	Ser362	ISSVPTPsPLGPLAG	Homo sapiens	Glioblastoma Cell
pmid	sentence
19941816	Erk2, which is activated by egfr signaling, directly binds to ck2alpha via the erk2 docking groove and phosphorylates ck2alpha primarily at t360/s362, subsequently enhancing ck2alpha activity

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-244525	Thr360	SGISSVPtPSPLGPL	Homo sapiens	Glioblastoma Cell
pmid	sentence
19941816	Erk2, which is activated by egfr signaling, directly binds to ck2alpha via the erk2 docking groove and phosphorylates ck2alpha primarily at t360/s362, subsequently enhancing ck2alpha activity

Publications:

2

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-161839	Ser362	ISSVPTPsPLGPLAG	Homo sapiens	Glioblastoma Cell
pmid	sentence
19941816	The mitotic phosphorylation sites on the alpha subunit of casein kinase ii can be phosphorylated in vitro by p34cdc2.

Identifier	Residue	Sequence	Organism
SIGNOR-29521	Ser370	PLGPLAGsPVIAAAN	Homo sapiens
pmid	sentence
7592773	Four residues within this domain, thr-344, thr-360, ser-362, and ser-370, conform to the minimal consensus sequence for p34cdc2 phosphorylationthe high stoichiometry of phosphorylation suggests that phosphorylation could regulate functional properties of ckii and that it could in some way participate in the burst of phosphorylation that accompanies the activation of p34graphic at the ggraphic-m transition

Identifier	Residue	Sequence	Organism
SIGNOR-29525	Thr344	SSMPGGStPVSSANM	Homo sapiens
pmid	sentence
7592773	Four residues within this domain, thr-344, thr-360, ser-362, and ser-370, conform to the minimal consensus sequence for p34cdc2 phosphorylationthe high stoichiometry of phosphorylation suggests that phosphorylation could regulate functional properties of ckii and that it could in some way participate in the burst of phosphorylation that accompanies the activation of p34graphic at the ggraphic-m transition

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-161843	Thr360	SGISSVPtPSPLGPL	Homo sapiens	Glioblastoma Cell
pmid	sentence
19941816	It has been shown that the c-terminal domains of ck2? Are phosphorylated by cdc2 and interact with the peptidyl-prolyl isomerase pin1 in a cell cycle-dependent manner

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-161851	Ser362	ISSVPTPsPLGPLAG	Homo sapiens	Glioblastoma Cell
pmid	sentence
19941816	Erk2, which is activated by egfr signaling, directly binds to ck2alpha via the erk2 docking groove and phosphorylates ck2alpha primarily at t360/s362, subsequently enhancing ck2alpha activity

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-161855	Thr360	SGISSVPtPSPLGPL	Homo sapiens	Glioblastoma Cell
pmid	sentence
19941816	Erk2, which is activated by egfr signaling, directly binds to ck2alpha via the erk2 docking groove and phosphorylates ck2alpha primarily at t360/s362, subsequently enhancing ck2alpha activity

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-160761	Ser366	GKKTKFAsDDEHDEH	Homo sapiens
pmid	sentence
18257391	Prior studies indicate that hla is activated by phosphorylation of serine-366 by protein kinase ck2, neutralizing a negative effect of a short basic motif (sbm)

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-89818	Ser370	TSVTPDVsDNEPDHY	Homo sapiens
pmid	sentence
21779440	The C-terminal tail of PTEN is also the target of mutations in tumors. As mentioned, this region contains the main phosphorylation sites mapped to residues Ser362, Thr366, Ser370, Ser380, Thr382, Thr383, and Ser385, and the kinases involved are casein kinase 2 (CK2), GSK3_, LKB1, and MAST.84,97-101 The phosphorylation of the tail has been shown to enhance PTEN stability but at the same time decrease its phosphatase activity

Identifier	Residue	Sequence	Organism
SIGNOR-152348	Ser380	EPDHYRYsDTTDSDP	Homo sapiens
pmid	sentence
21779440	The C-terminal tail of PTEN is also the target of mutations in tumors. As mentioned, this region contains the main phosphorylation sites mapped to residues Ser362, Thr366, Ser370, Ser380, Thr382, Thr383, and Ser385, and the kinases involved are casein kinase 2 (CK2), GSK3_, LKB1, and MAST.84,97-101 The phosphorylation of the tail has been shown to enhance PTEN stability but at the same time decrease its phosphatase activity

Identifier	Residue	Sequence	Organism
SIGNOR-89822	Ser385	RYSDTTDsDPENEPF	Homo sapiens
pmid	sentence
21779440	The C-terminal tail of PTEN is also the target of mutations in tumors. As mentioned, this region contains the main phosphorylation sites mapped to residues Ser362, Thr366, Ser370, Ser380, Thr382, Thr383, and Ser385, and the kinases involved are casein kinase 2 (CK2), GSK3_, LKB1, and MAST.84,97-101 The phosphorylation of the tail has been shown to enhance PTEN stability but at the same time decrease its phosphatase activity

Identifier	Residue	Sequence	Organism
SIGNOR-250940	Thr366	ASSSTSVtPDVSDNE	in vitro
pmid	sentence
12297295	We used mass spectrometric methods to identify Ser(370) and Ser(385) as in vivo phosphorylation sites of PTEN. These sites also are phosphorylated by CK2 in vitro, and phosphorylation inhibits PTEN activity towards its substrate, PIP3. We also identify a novel in vivo phosphorylation site, Thr(366).

Identifier	Residue	Sequence	Organism
SIGNOR-89826	Thr382	DHYRYSDtTDSDPEN	Homo sapiens
pmid	sentence
21779440	The C-terminal tail of PTEN is also the target of mutations in tumors. As mentioned, this region contains the main phosphorylation sites mapped to residues Ser362, Thr366, Ser370, Ser380, Thr382, Thr383, and Ser385, and the kinases involved are casein kinase 2 (CK2), GSK3_, LKB1, and MAST.84,97-101 The phosphorylation of the tail has been shown to enhance PTEN stability but at the same time decrease its phosphatase activity

Identifier	Residue	Sequence	Organism
SIGNOR-89830	Thr383	HYRYSDTtDSDPENE	Homo sapiens
pmid	sentence
21779440	The C-terminal tail of PTEN is also the target of mutations in tumors. As mentioned, this region contains the main phosphorylation sites mapped to residues Ser362, Thr366, Ser370, Ser380, Thr382, Thr383, and Ser385, and the kinases involved are casein kinase 2 (CK2), GSK3_, LKB1, and MAST.84,97-101 The phosphorylation of the tail has been shown to enhance PTEN stability but at the same time decrease its phosphatase activity

Publications:

6

Organism:

Homo Sapiens, In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250856	Ser378	RICMRNFsRSDHLTT	Mus musculus	NIH-3T3 Cell
pmid	sentence
8662759	Casein kinase II associates with Egr-1 and acts as a negative modulator of its DNA binding and transcription activities in NIH 3T3 cells. \| There are three CKII recognition sites (S376XXD, T389XE, and T516XXXD) in fragment 10.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250857	Thr391	TTHIRTHtGEKPFAC	Mus musculus	NIH-3T3 Cell
pmid	sentence
8662759	Casein kinase II associates with Egr-1 and acts as a negative modulator of its DNA binding and transcription activities in NIH 3T3 cells. \| There are three CKII recognition sites (S376XXD, T389XE, and T516XXXD) in fragment 10.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250858	Thr526	TNSFSAStGLSDMTA	Mus musculus	NIH-3T3 Cell
pmid	sentence
8662759	Casein kinase II associates with Egr-1 and acts as a negative modulator of its DNA binding and transcription activities in NIH 3T3 cells. \| There are three CKII recognition sites (S376XXD, T389XE, and T516XXXD) in fragment 10.

Publications:

3

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-273631	Ser380	ILGDTTTsGASDEED	in vitro
pmid	sentence
30135209	The two serines within the PSAC of Serinc3 are phosphorylated by casein kinase II and mediate interaction with the μ subunits in vitro.

Identifier	Residue	Sequence	Organism
SIGNOR-273632	Ser383	DTTTSGAsDEEDGQP	in vitro
pmid	sentence
30135209	The two serines within the PSAC of Serinc3 are phosphorylated by casein kinase II and mediate interaction with the μ subunits in vitro.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-276077	Ser385	AGNRTANsEDSDEQD	in vitro
pmid	sentence
17911614	Functional studies of the wild-type receptor and serine/threonine mutants indicated that phosphorylation of Ser(394) by protein kinase C slightly suppresses KIR3DL1 inhibitory function, and reduces receptor internalization and turnover.Both CKII and PKC phosphorylate KIR3DL1 in vitro. Ser364 can be phosphorylated after phosphorylation of Ser367 by CKII. It seems that phosphorylation of 3DL1 by CK does not significantly affect receptor inhibitory function or turnover, at least in the assays that we have used so far.

Identifier	Residue	Sequence	Organism
SIGNOR-276078	Ser388	RTANSEDsDEQDPEE	in vitro
pmid	sentence
17911614	Functional studies of the wild-type receptor and serine/threonine mutants indicated that phosphorylation of Ser(394) by protein kinase C slightly suppresses KIR3DL1 inhibitory function, and reduces receptor internalization and turnover.Both CKII and PKC phosphorylate KIR3DL1 in vitro. Ser364 can be phosphorylated after phosphorylation of Ser367 by CKII. It seems that phosphorylation of 3DL1 by CK does not significantly affect receptor inhibitory function or turnover, at least in the assays that we have used so far.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-250834	Ser385	DDDDDDNsDEEDNDD	in vitro
pmid	sentence
1985907	Both cardiac and skeletal muscle calsequestrins were phosphorylated by casein kinase II, but cardiac calsequestrin was phosphorylated to a higher stoichiometry and at least 50 times more rapidly. The site of rapid phosphorylation of cardiac calsequestrin was localized to the distinct COOH terminus, where a cluster of three closely spaced serine residues are found (S378DEESN-DDSDDDDE-COOH).

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-179542	Ser389	LKEAEEEsSGGEEED	Homo sapiens
pmid	sentence
18649047	We find that eif5 is associated with ck2 when the kinase activity is at the highest level in vivo, and is phosphorylated at ser389 and ser390 by ck2.

Identifier	Residue	Sequence	Organism
SIGNOR-141159	Ser390	KEAEEESsGGEEEDE	Homo sapiens
pmid	sentence
16227438	We find that eif5 is associated with ck2 when the kinase activity is at the highest level in vivo, and is phosphorylated at ser389 and ser390 by ck2.

Identifier	Residue	Sequence	Organism
SIGNOR-179546	Ser390	KEAEEESsGGEEEDE	Homo sapiens
pmid	sentence
18649047	We find that eif5 is associated with ck2 when the kinase activity is at the highest level in vivo, and is phosphorylated at ser389 and ser390 by ck2.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-134846	Ser39	MKKIRLEsEEEGVPS	Homo sapiens
pmid	sentence
15788687	Additionally, transfection of cdc2 with a mutation at ser(39) to ala, which is the ck2 phosphorylation site, partially inhibits cell cycle progression in g(1) to g(2) phase following 6-tg treatment.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-276650	Ser390	LFPVCHDsDESDTAK	in vitro
pmid	sentence
25066127	This modulation can be directly attributed to CK2-mediated phosphorylation of Dnmt3a. We also find that CK2-mediated phosphorylation is required for localization of Dnmt3a to heterochromatin.

Identifier	Residue	Sequence	Organism
SIGNOR-276649	Ser393	VCHDSDEsDTAKAVE	in vitro
pmid	sentence
25066127	This modulation can be directly attributed to CK2-mediated phosphorylation of Dnmt3a. We also find that CK2-mediated phosphorylation is required for localization of Dnmt3a to heterochromatin.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-184031	Ser392	QDAPIILsDSEEEEM	Homo sapiens
pmid	sentence
19217413	Indeed recombinant pmscl1 undergoes ck2-mediated phosphorylation in vitro at various serine residues, including serines 409 and 411, which reside within the phosphosim region. the exchange of hydrophobic core residues or serines 409 and 411 to alanine attenuates binding of sumo to the phosphosim-containing fragment of pmscl1 in a yeast two-hybrid assay

Identifier	Residue	Sequence	Organism
SIGNOR-184035	Ser394	APIILSDsEEEEMII	Homo sapiens
pmid	sentence
19217413	Indeed recombinant pmscl1 undergoes ck2-mediated phosphorylation in vitro at various serine residues, including serines 409 and 411, which reside within the phosphosim region. the exchange of hydrophobic core residues or serines 409 and 411 to alanine attenuates binding of sumo to the phosphosim-containing fragment of pmscl1 in a yeast two-hybrid assay

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250967	Ser392	FKTEGPDsD	Homo sapiens	HeLa-S3 Cell
pmid	sentence
10747897	Furthermore, we demonstrate that anisomycin- and tumor necrosis factor-alpha-induced phosphorylation of p53 at Ser-392, which is important for the transcriptional activity of this growth suppressor protein, requires p38 MAP kinase and CK2 activities.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-89937	Ser394	EDAVHEDsGDEDGED	Homo sapiens
pmid	sentence
12082111	Protein kinase ck2-mediated phosphorylation of hdac2 regulates co-repressor formation, deacetylase activity and acetylation of hdac2 by cigarette smoke and aldehydesstudies using unfractionated cell extracts with ck2 inhibitors suggest that protein kinase ck2 is the major source of hdac2 kinase. Finally, and perhaps most interesting, hdac2 phosphorylation promotes enzymatic activity, selectively regulates complex formation, but has no effect on transcriptional repression. Together, our data indicate that like many hdacs, hdac2 is regulated by post-translational modification, particularly phosphorylation.

Identifier	Residue	Sequence	Organism
SIGNOR-164795	Ser394	EDAVHEDsGDEDGED	Homo sapiens
pmid	sentence
20388487	Protein kinase ck2-mediated phosphorylation of hdac2 regulates co-repressor formation, deacetylase activity and acetylation of hdac2 by cigarette smoke and aldehydesstudies using unfractionated cell extracts with ck2 inhibitors suggest that protein kinase ck2 is the major source of hdac2 kinase. Finally, and perhaps most interesting, hdac2 phosphorylation promotes enzymatic activity, selectively regulates complex formation, but has no effect on transcriptional repression. Together, our data indicate that like many hdacs, hdac2 is regulated by post-translational modification, particularly phosphorylation.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-83711	Ser407	STEQTLAsDTDSSLD	Homo sapiens
pmid	sentence
11062067	The phosphorylation of thr-404 and ser-407 is not increased in response to other agonists that activate mkk7 and sapk1/jnk, suggesting that phosphorylation of these residues is catalysed by another protein kinase, such as ck2, which also phosphorylates thr-404 and ser-407 in vitro.

Identifier	Residue	Sequence	Organism
SIGNOR-83715	Thr404	SSMSTEQtLASDTDS	Homo sapiens
pmid	sentence
11062067	The phosphorylation of thr-404 and ser-407 is not increased in response to other agonists that activate mkk7 and sapk1/jnk, suggesting that phosphorylation of these residues is catalysed by another protein kinase, such as ck2, which also phosphorylates thr-404 and ser-407 in vitro.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-111011	Ser421	IACEEEFsDSEEEGE	Homo sapiens
pmid	sentence
11602581	Human hdac1 protein was analyzed by ion trap mass spectrometry, and two phosphorylated serine residues, ser(421) and ser(423), were unambiguously identified. Loss of phosphorylation at ser(421) and ser(423) due to mutation to alanine or disruption of the casein kinase 2 consensus sequence directing phosphorylation reduced the enzymatic activity and complex formation of hdac1.

Identifier	Residue	Sequence	Organism
SIGNOR-111015	Ser423	CEEEFSDsEEEGEGG	Homo sapiens
pmid	sentence
11602581	Human hdac1 protein was analyzed by ion trap mass spectrometry, and two phosphorylated serine residues, ser(421) and ser(423), were unambiguously identified. Loss of phosphorylation at ser(421) and ser(423) due to mutation to alanine or disruption of the casein kinase 2 consensus sequence directing phosphorylation reduced the enzymatic activity and complex formation of hdac1.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250887	Ser422	IACDEEFsDSEDEGE	Homo sapiens	HeLa Cell
pmid	sentence
12082111	HDAC2 is phosphorylated uniquely by protein kinase CK2 in vitro. Studies using unfractionated cell extracts with CK2 inhibitors suggest that protein kinase CK2 is the major source of HDAC2 kinase. Finally, and perhaps most interesting, HDAC2 phosphorylation promotes enzymatic activity, selectively regulates complex formation, but has no effect on transcriptional repression. \| Since our data suggest that protein kinase CK2 is the major kinase responsible for HDAC2 phosphorylation, and because Ser422 and Ser424, but not Ser411, lie within CK2 recognition sequences, we believe that Ser394, Ser422, and Ser424 constitute the three phosphorylated residues in HDAC2.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250888	Ser424	CDEEFSDsEDEGEGG	Homo sapiens	HeLa Cell
pmid	sentence
12082111	HDAC2 is phosphorylated uniquely by protein kinase CK2 in vitro. Studies using unfractionated cell extracts with CK2 inhibitors suggest that protein kinase CK2 is the major source of HDAC2 kinase. Finally, and perhaps most interesting, HDAC2 phosphorylation promotes enzymatic activity, selectively regulates complex formation, but has no effect on transcriptional repression. \| Since our data suggest that protein kinase CK2 is the major kinase responsible for HDAC2 phosphorylation, and because Ser422 and Ser424, but not Ser411, lie within CK2 recognition sequences, we believe that Ser394, Ser422, and Ser424 constitute the three phosphorylated residues in HDAC2.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-176619	Ser422	NNNNRKTsNGDDSLF	Homo sapiens
pmid	sentence
21930781	Cftr possesses two ck2 phosphorylation sites (s422 and t1471)this is consistent with an important role for s422 phosphorylation in increasing cftr activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250889	Ser424	DHDNDKEsDVEI	Homo sapiens
pmid	sentence
15805470	A protein kinase CK2 phosphoacceptor site in the HDAC3 protein was identified at position Ser424, which is a nonconserved residue among the class I HDACs. Mutation of this residue was found to reduce deacetylase activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-175130	Ser429	TDNNAKSsDKEEKHR	Homo sapiens
pmid	sentence
21777522	Ck2 phosphorylates ap-2_ and increases its transcriptional activity

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250824	Ser43	FHYRTLHsDDEGTVL	Chlorocebus aethiops
pmid	sentence
12361709	Protein kinase CK2 (CK2) was identified as the 45-kDa kinase from COS 1 cell or liver extracts that was responsible for phosphorylation of serine 43 in the XAP2 peptide 39-57. Loss of phosphorylation at any or all of the serine residues did not significantly affect the ability of XAP2-FLAG to bind to the murine AhR in rabbit reticulocyte lysate or Hsp90 in COS-1 cells.

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism
SIGNOR-277501	Ser46	LPLSEVPsDWEVDDL	in vitro
pmid	sentence
31941600	Here, we found that human CREB3 is phosphorylated within its transcription activation domain on serine 46 by protein kinase CK2. However, phosphorylation at serine 46 reduced the stability of CREB3.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-70082	Ser460	PTAVGSLsGAEGVPV	Homo sapiens	HeLa Cell
pmid	sentence
10448092	Site-specific mutagenesis of maz revealed that the serine residue at position 480 was the major site of phosphorylation by ckii both in vitro and in vivo. Phosphorylation of maz by ckii at this serine residue was required for maximum binding of maz to the pyrimidine-rich dna of the nuclease-hypersensitive element (nhe) in the 5'-end promoter region of the c-myc gene. Mutation of serine at position 480 to alanine eliminated the dna-binding activity of maz to this element.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-196193	Ser463	CNQDERIsKLEQQMA	Homo sapiens
pmid	sentence
22355754	We demonstrate that crn2 is a binding partner and substrate of protein kinase ck2, which phosphorylates crn2 at s463 in its c-terminal coiled coil domain

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-184039	Ser466	VIDLTIDsSSDEEEE	Homo sapiens
pmid	sentence
19217413	Ck2 phosphorylates serine residues adjacent to the sim of pias1 these findings show that the phosphosim module mediates binding to free sumo and sumo conjugates in a phosphorylation-dependent mode, with ck2 being the critical kinase involvedin this process.

Identifier	Residue	Sequence	Organism
SIGNOR-184043	Ser467	IDLTIDSsSDEEEEE	Homo sapiens
pmid	sentence
19217413	Ck2 phosphorylates serine residues adjacent to the sim of pias1 these findings show that the phosphosim module mediates binding to free sumo and sumo conjugates in a phosphorylation-dependent mode, with ck2 being the critical kinase involvedin this process.

Identifier	Residue	Sequence	Organism
SIGNOR-184047	Ser468	DLTIDSSsDEEEEEP	Homo sapiens
pmid	sentence
19217413	Ck2 phosphorylates serine residues adjacent to the sim of pias1 these findings show that the phosphosim module mediates binding to free sumo and sumo conjugates in a phosphorylation-dependent mode, with ck2 being the critical kinase involvedin this process.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250972	Ser475	IDIEGVQsEGQDNGA	Cricetulus griseus	CHO-EM9 Cell
pmid	sentence
15066279	We show that inhibiting XRCC1 phosphorylation by mutation of the CK2 phosphorylation sites or preventing CK2 activity using a highly specific inhibitor ablates the rapid repair of cellular DNA single-strand breaks by XRCC1. \|

Publications:

1

Organism:

Cricetulus Griseus

Identifier	Residue	Sequence	Organism
SIGNOR-62303	Ser482	SSMQPDNsSDSDYDL	Homo sapiens
pmid	sentence
9834084	In this study, we use jurkat t cell transfectants of cd5 cytoplasmic tail mutants to reveal phosphorylation sites relevant to signal transduction. Our results show that casein kinase ii (ckii) is responsible for the constitutive phosphorylation of cd5 molecules at a cluster of three serine residues located at the extreme c terminus (s458, s459, and s461)

Identifier	Residue	Sequence	Organism
SIGNOR-62307	Ser483	SMQPDNSsDSDYDLH	Homo sapiens
pmid	sentence
9834084	In this study, we use jurkat t cell transfectants of cd5 cytoplasmic tail mutants to reveal phosphorylation sites relevant to signal transduction. Our results show that casein kinase ii (ckii) is responsible for the constitutive phosphorylation of cd5 molecules at a cluster of three serine residues located at the extreme c terminus (s458, s459, and s461)

Identifier	Residue	Sequence	Organism
SIGNOR-62311	Ser485	QPDNSSDsDYDLHGA	Homo sapiens
pmid	sentence
9834084	In this study, we use jurkat t cell transfectants of cd5 cytoplasmic tail mutants to reveal phosphorylation sites relevant to signal transduction. Our results show that casein kinase ii (ckii) is responsible for the constitutive phosphorylation of cd5 molecules at a cluster of three serine residues located at the extreme c terminus (s458, s459, and s461)

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-182350	Ser482	RRIAVEYsDSEDDSS	Homo sapiens
pmid	sentence
19012317	Here we identify five casein kinase 2 (ck2) phosphorylation sites within the vca domain of wave2, serines 482, 484, 488, 489, and 497. Phosphorylation of these sites is required for a high affinity interaction with the arp2/3 complex;we and show that their mutation to non-phosphorylatable alanine residues inhibits wave2 function in vivo.

Identifier	Residue	Sequence	Organism
SIGNOR-182354	Ser484	IAVEYSDsEDDSSEF	Homo sapiens
pmid	sentence
19012317	Here we identify five casein kinase 2 (ck2) phosphorylation sites within the vca domain of wave2, serines 482, 484, 488, 489, and 497. Phosphorylation of these sites is required for a high affinity interaction with the arp2/3 complex;we and show that their mutation to non-phosphorylatable alanine residues inhibits wave2 function in vivo.

Identifier	Residue	Sequence	Organism
SIGNOR-182358	Ser488	YSDSEDDsSEFDEDD	Homo sapiens
pmid	sentence
19012317	Here we identify five casein kinase 2 (ck2) phosphorylation sites within the vca domain of wave2, serines 482, 484, 488, 489, and 497. Phosphorylation of these sites is required for a high affinity interaction with the arp2/3 complex;we and show that their mutation to non-phosphorylatable alanine residues inhibits wave2 function in vivo.

Identifier	Residue	Sequence	Organism
SIGNOR-182362	Ser497	EFDEDDWsD	Homo sapiens
pmid	sentence
19012317	Here we identify five casein kinase 2 (ck2) phosphorylation sites within the vca domain of wave2, serines 482, 484, 488, 489, and 497. Phosphorylation of these sites is required for a high affinity interaction with the arp2/3 complex;we and show that their mutation to non-phosphorylatable alanine residues inhibits wave2 function in vivo.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-101264	Ser483	KRSRAIHsSDEGEDQ	Homo sapiens
pmid	sentence
12769847	Here we identify two phosphorylation sites in the vca domain of wasp at serines 483 and 484. S483 and s484 are substrates for casein kinase 2 in vitro and in vivo. Phosphorylation of these residues increases the affinity of the vca domain for the arp2/3 complex 7-fold and is required for efficient in vitro actin polymerization by the full-length wasp molecule.

Identifier	Residue	Sequence	Organism
SIGNOR-101268	Ser484	RSRAIHSsDEGEDQA	Homo sapiens
pmid	sentence
12769847	Here we identify two phosphorylation sites in the vca domain of wasp at serines 483 and 484. S483 and s484 are substrates for casein kinase 2 in vitro and in vivo. Phosphorylation of these residues increases the affinity of the vca domain for the arp2/3 complex 7-fold and is required for efficient in vitro actin polymerization by the full-length wasp molecule.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-165419	Ser485	QDNGAEDsGDTEDEL	Homo sapiens
pmid	sentence
20471329	Xrcc1 phosphorylation by ck2 is required for its stability and efficient dna repair

Identifier	Residue	Sequence	Organism
SIGNOR-165423	Ser518	GEDPYAGsTDENTDS	Homo sapiens
pmid	sentence
20471329	Xrcc1 phosphorylation by ck2 is required for its stability and efficient dna repair. Rcc1 is phosphorylated in vivo and in vitro by ck2, and ck2 phosphorylation of xrcc1 on s518, t519, and t523

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-128893	Ser518	GEDPYAGsTDENTDS	Homo sapiens	HeLa Cell
pmid	sentence
15367657	Xrcc1 phosphorylation by ck2 is required for its stability and efficient dna repair. Rcc1 is phosphorylated in vivo and in vitro by ck2, and ck2 phosphorylation of xrcc1 on s518, t519, and t523

Identifier	Residue	Sequence	Organism
SIGNOR-165427	Thr488	GAEDSGDtEDELRRV	Homo sapiens
pmid	sentence
20471329	Xrcc1 phosphorylation by ck2 is required for its stability and efficient dna repair

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-128897	Thr519	EDPYAGStDENTDSE	Homo sapiens	HeLa Cell
pmid	sentence
15367657	Xrcc1 phosphorylation by ck2 is required for its stability and efficient dna repair. Rcc1 is phosphorylated in vivo and in vitro by ck2, and ck2 phosphorylation of xrcc1 on s518, t519, and t523

Identifier	Residue	Sequence	Organism
SIGNOR-165431	Thr519	EDPYAGStDENTDSE	Homo sapiens
pmid	sentence
20471329	Xrcc1 phosphorylation by ck2 is required for its stability and efficient dna repair. Rcc1 is phosphorylated in vivo and in vitro by ck2, and ck2 phosphorylation of xrcc1 on s518, t519, and t523

Identifier	Residue	Sequence	Organism
SIGNOR-165435	Thr523	AGSTDENtDSEEHQE	Homo sapiens
pmid	sentence
20471329	Xrcc1 phosphorylation by ck2 is required for its stability and efficient dna repair. Rcc1 is phosphorylated in vivo and in vitro by ck2, and ck2 phosphorylation of xrcc1 on s518, t519, and t523

Publications:

7

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-200202	Ser487	AQLAGSDsDLDSDDE	Homo sapiens
pmid	sentence
23263282	Here we report that tel2 and tti1 are targeted for degradation within mtorc1 by the scffbxo9 ubiquitin ligase to adjust mtor signalling to growth factor availability. This process is primed by ck2, which translocates to the cytoplasm to mediate mtorc1-specific phosphorylation of tel2/tti1. ere, we show that tel2 is constitutively phosphorylated on conserved serines 487 and 491 by casein kinase 2 (ck2)

Identifier	Residue	Sequence	Organism
SIGNOR-168036	Ser487	AQLAGSDsDLDSDDE	Homo sapiens
pmid	sentence
20864032	Here we report that tel2 and tti1 are targeted for degradation within mtorc1 by the scffbxo9 ubiquitin ligase to adjust mtor signalling to growth factor availability. This process is primed by ck2, which translocates to the cytoplasm to mediate mtorc1-specific phosphorylation of tel2/tti1. ere, we show that tel2 is constitutively phosphorylated on conserved serines 487 and 491 by casein kinase 2 (ck2)

Identifier	Residue	Sequence	Organism
SIGNOR-200206	Ser491	GSDSDLDsDDEFVPY	Homo sapiens
pmid	sentence
23263282	Here we report that tel2 and tti1 are targeted for degradation within mtorc1 by the scffbxo9 ubiquitin ligase to adjust mtor signalling to growth factor availability. This process is primed by ck2, which translocates to the cytoplasm to mediate mtorc1-specific phosphorylation of tel2/tti1. Here, we show that tel2 is constitutively phosphorylated on conserved serines 487 and 491 by casein kinase 2 (ck2)

Identifier	Residue	Sequence	Organism
SIGNOR-168040	Ser491	GSDSDLDsDDEFVPY	Homo sapiens
pmid	sentence
20864032	Here we report that tel2 and tti1 are targeted for degradation within mtorc1 by the scffbxo9 ubiquitin ligase to adjust mtor signalling to growth factor availability. This process is primed by ck2, which translocates to the cytoplasm to mediate mtorc1-specific phosphorylation of tel2/tti1. Here, we show that tel2 is constitutively phosphorylated on conserved serines 487 and 491 by casein kinase 2 (ck2)

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-273627	Ser497	TEEMPNDsVLENKSL	Homo sapiens
pmid	sentence
29733298	Here, we show that somatic nuclear autoantigenic sperm protein (sNASP) binds to TRAF6 to prevent TRAF6 autoubiquitination in unstimulated macrophages. Following LPS stimulation, a complex consisting of sNASP, TRAF6, IRAK4, and casein kinase 2 (CK2) is formed. CK2 phosphorylates sNASP at serine 158, allowing sNASP to dissociate from TRAF6. Free TRAF6 is then autoubiquitinated, followed by activation of downstream signaling pathways.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250901	Ser509	PTEENEMsSEADMEC	in vitro
pmid	sentence
12558502	Protein kinase CK2 phosphorylates Hsp105 alpha at Ser509 and modulates its function. \| the phosphorylation of Hsp105 alpha at Ser(509) abolished the inhibitory activity of Hsp105 alpha in vitro.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250959	Ser510	SSSNEGDsDRDEKKR	Homo sapiens	HEK-293 Cell
pmid	sentence
15659405	CK2 phosphorylates SSRP1 and inhibits its DNA-binding activity. \| we identified serines 510, 657, and 688 as phosphorylation targets of CK2 in vitro. Mutagenesis of the three serines revealed that serine 510 was more important for the regulation of SSRP1 DNA-binding activity.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250960	Ser657	KSSSRQLsESFKSKE	Homo sapiens	HEK-293 Cell
pmid	sentence
15659405	CK2 phosphorylates SSRP1 and inhibits its DNA-binding activity. \| we identified serines 510, 657, and 688 as phosphorylation targets of CK2 in vitro. Mutagenesis of the three serines revealed that serine 510 was more important for the regulation of SSRP1 DNA-binding activity.

Identifier	Residue	Sequence	Organism
SIGNOR-250961	Ser688	KRRRSEDsEEEELAS	Homo sapiens
pmid	sentence
15659405	CK2 phosphorylates SSRP1 and inhibits its DNA-binding activity. \| we identified serines 510, 657, and 688 as phosphorylation targets of CK2 in vitro. Mutagenesis of the three serines revealed that serine 510 was more important for the regulation of SSRP1 DNA-binding activity.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250953	Ser511	PIGEDEEsESD	in vitro
pmid	sentence
9045708	Purified CKI and CKII phosphorylate the wild-type carboxyl terminus of VMAT2, but not a double mutant with both serines 512 and 514 replaced by alanine. The protein kinase inhibitor CKI-7 and unlabeled GTP both block in vitro phosphorylation by cell homogenates, indicating a role for CKII and possibly CKI in vivo. Both kinases phosphorylate the VMAT2 fusion protein to a much greater extent than a similar fusion protein containing the carboxyl terminus of VMAT1, consistent with differential phosphorylation of the two transporters observed in intact cells.

Identifier	Residue	Sequence	Organism
SIGNOR-250952	Ser513	GEDEESEsD	in vitro
pmid	sentence
9045708	Purified CKI and CKII phosphorylate the wild-type carboxyl terminus of VMAT2, but not a double mutant with both serines 512 and 514 replaced by alanine. The protein kinase inhibitor CKI-7 and unlabeled GTP both block in vitro phosphorylation by cell homogenates, indicating a role for CKII and possibly CKI in vivo. Both kinases phosphorylate the VMAT2 fusion protein to a much greater extent than a similar fusion protein containing the carboxyl terminus of VMAT1, consistent with differential phosphorylation of the two transporters observed in intact cells.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-176623	Ser511	ENIIFGVsYDEYRYR	Homo sapiens
pmid	sentence
21930781	Serine 511 has been previously implicated in the regulation of cftr by ck2, as the mutant s511d was found to be insensitive to tbb in xenopus oocytes but to have no major impact on the single-channel behavior of cftr

Identifier	Residue	Sequence	Organism
SIGNOR-176627	Thr1471	IAALKEEtEEEVQDT	Homo sapiens
pmid	sentence
21930781	Cftr possesses two ck2 phosphorylation sites (s422 and t1471) the t1471 residue, previously described as a site for cftr phosphorylation by ck2 (25), seems to be critical for cftr turnover and processing.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-148306	Ser518	PSTSKAVsPPHLDGP	Homo sapiens	Lung Cancer Cell
pmid	sentence
16873060	Here we show that ck2 regulates pml protein levels by promoting its ubiquitin-mediated degradation dependent on direct phosphorylation at ser517.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-148310	Ser565	VISSSEDsDAENSSS	Homo sapiens	Lung Cancer Cell
pmid	sentence
16873060	Here we show that ck2 regulates pml protein levels by promoting its ubiquitin-mediated degradation dependent on direct phosphorylation at ser517.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-149635	Ser529	GLPNGLLsGDEDFSS	Homo sapiens
pmid	sentence
10938077	Tumor necrosis factor alpha-induced phosphorylation of RelA/p65 on Ser529 is controlled by casein kinase II.\|Furthermore, our results indicate that the association between IkappaBalpha and p65 inhibits p65 phosphorylation by CKII and that degradation of IkappaBalpha allows CKII to phosphorylate p65 to increase NF-kappaB transactivation potential.

Identifier	Residue	Sequence	Organism
SIGNOR-250942	Ser543	SIADMDFsALLSQIS	Homo sapiens
pmid	sentence
10938077	We demonstrate that casein kinase II (CKII) interacts with p65 in vivo and can phosphorylate p65 at serine 529 in vitro. A CKII inhibitor (PD144795) inhibited TNFalpha-induced p65 phosphorylation in vivo. Furthermore, our results indicate that the association between IkappaBalpha and p65 inhibits p65 phosphorylation by CKII and that degradation of IkappaBalpha allows CKII to phosphorylate p65 to increase NF-kappaB transactivation potential.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250868	Ser53	DEELEGIsPDELKDE	in vitro
pmid	sentence
7598724	We report that recombinant glia maturation factor (GMF), a 17-kD brain protein, can be phosphorylated in vitro at the serine residue by protein kinase C (PKC), protein kinase A (PKA), and casein kinase II (CKII), and at the threonine residue by p90 ribosomal S6 kinase (RSK).

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-265896	Ser558	AEQMANDsDDSISAA	in vitro
pmid	sentence
28436950	Here we show that MRE11 directly interacts with PIH1D1, a subunit of heat-shock protein 90 cochaperone R2TP complex, which is required for the assembly of large protein complexes, such as RNA polymerase II, small nucleolar ribonucleoproteins and mammalian target of rapamycin complex 1. The MRE11-PIH1D1 interaction is dependent on casein kinase 2 (CK2) phosphorylation of two acidic sequences within the MRE11 C terminus containing serines 558/561 and 688/689.

Identifier	Residue	Sequence	Organism
SIGNOR-265894	Ser561	MANDSDDsISAATNK	in vitro
pmid	sentence
28436950	Here we show that MRE11 directly interacts with PIH1D1, a subunit of heat-shock protein 90 cochaperone R2TP complex, which is required for the assembly of large protein complexes, such as RNA polymerase II, small nucleolar ribonucleoproteins and mammalian target of rapamycin complex 1. The MRE11-PIH1D1 interaction is dependent on casein kinase 2 (CK2) phosphorylation of two acidic sequences within the MRE11 C terminus containing serines 558/561 and 688/689.

Identifier	Residue	Sequence	Organism
SIGNOR-265893	Ser688	SKGVDFEsSEDDDDD	in vitro
pmid	sentence
28436950	Here we show that MRE11 directly interacts with PIH1D1, a subunit of heat-shock protein 90 cochaperone R2TP complex, which is required for the assembly of large protein complexes, such as RNA polymerase II, small nucleolar ribonucleoproteins and mammalian target of rapamycin complex 1. The MRE11-PIH1D1 interaction is dependent on casein kinase 2 (CK2) phosphorylation of two acidic sequences within the MRE11 C terminus containing serines 558/561 and 688/689.

Identifier	Residue	Sequence	Organism
SIGNOR-265895	Ser689	KGVDFESsEDDDDDP	in vitro
pmid	sentence
28436950	Here we show that MRE11 directly interacts with PIH1D1, a subunit of heat-shock protein 90 cochaperone R2TP complex, which is required for the assembly of large protein complexes, such as RNA polymerase II, small nucleolar ribonucleoproteins and mammalian target of rapamycin complex 1. The MRE11-PIH1D1 interaction is dependent on casein kinase 2 (CK2) phosphorylation of two acidic sequences within the MRE11 C terminus containing serines 558/561 and 688/689.

Publications:

4

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-276886	Ser57	PAMYDDEsAIDFSAY	in vitro
pmid	sentence
25680545	Here, we have identified the CCAAT/enhancer binding protein δ (C/EBPδ) as a new substrate for CK2. Using point mutants of C/EBPδ the major phosphorylation site for CK2 was mapped to serine 57, which is located within the transactivation domain of C/EBPδ. For proper functioning as a transcription factor C/EBPδ has to be translocated into the nucleus where it forms heterodimers with other members of the C/EBP family of proteins and ATF4. Here, we found that CK2 phosphorylation does neither influence the subcellular localization of C/EBPδ nor its interaction with C/EBPβ, but rather does CK2 phosphorylation modulate the transcriptional activity of C/EBPδ.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-265269	Ser574	EEVSDKGsDSEEEET	Homo sapiens
pmid	sentence
23287549	Sec63 was identified as a novel substrate and binding partner of protein kinase CK2. We identified serine 574, serine 576 and serine 748 as CK2 phosphorylation sites. Phosphorylation of Sec63 by CK2 enhanced its binding to Sec62.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-265267	Ser576	VSDKGSDsEEEETNR	Homo sapiens	Hep-G2 Cell
pmid	sentence
23287549	Sec63 was identified as a novel substrate and binding partner of protein kinase CK2. We identified serine 574, serine 576 and serine 748 as CK2 phosphorylation sites. Phosphorylation of Sec63 by CK2 enhanced its binding to Sec62.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-265271	Ser748	DSEGFEDsFEEEEEE	Homo sapiens	Hep-G2 Cell
pmid	sentence
23287549	Sec63 was identified as a novel substrate and binding partner of protein kinase CK2. We identified serine 574, serine 576 and serine 748 as CK2 phosphorylation sites. Phosphorylation of Sec63 by CK2 enhanced its binding to Sec62.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250844	Ser575	AGESLDQsMEEEEEE	Homo sapiens	HeLa Cell
pmid	sentence
12591939	We found that only phosphorylated FCP1 can physically interact with TFIIF. We set out to purify an FCP1 kinase from HeLa cells and identified casein kinase 2, which, surprisingly, displayed a negative effect on FCP1-associated activities.\| Phosphorylation of FCP1 by CK2 Inhibits the Transcription Elongation Activity of FCP1. \| Two in vivo phosphorylation sites within the C terminus of FCP1 at Ser-575 and Ser-740 were identified

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250845	Ser740	TKAQRENsPAAFPDR	Homo sapiens	HeLa Cell
pmid	sentence
12591939	We found that only phosphorylated FCP1 can physically interact with TFIIF. We set out to purify an FCP1 kinase from HeLa cells and identified casein kinase 2, which, surprisingly, displayed a negative effect on FCP1-associated activities.\| Phosphorylation of FCP1 by CK2 Inhibits the Transcription Elongation Activity of FCP1. \| Two in vivo phosphorylation sites within the C terminus of FCP1 at Ser-575 and Ser-740 were identified

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250962	Ser58	ESETNQNsSSDSEAE	in vitro
pmid	sentence
11711551	We show here that Tcf-4 can be phosphorylated in vitro by protein kinase CK2 stoichiometrically in amino acids Ser-58-Ser-59-Ser-60. Phosphorylation of these residues does not modify the interaction of Tcf-4 with beta-catenin but reduces its association to plakoglobin. \| Experiments performed using a Tcf-4 mutant with decreased interaction to plakoglobin demonstrated that binding to this protein negatively affected the transcriptional activity of Tcf-4.

Identifier	Residue	Sequence	Organism
SIGNOR-250963	Ser59	SETNQNSsSDSEAER	in vitro
pmid	sentence
11711551	We show here that Tcf-4 can be phosphorylated in vitro by protein kinase CK2 stoichiometrically in amino acids Ser-58-Ser-59-Ser-60. Phosphorylation of these residues does not modify the interaction of Tcf-4 with beta-catenin but reduces its association to plakoglobin. \| Experiments performed using a Tcf-4 mutant with decreased interaction to plakoglobin demonstrated that binding to this protein negatively affected the transcriptional activity of Tcf-4.

Identifier	Residue	Sequence	Organism
SIGNOR-250964	Ser60	ETNQNSSsDSEAERR	in vitro
pmid	sentence
11711551	We show here that Tcf-4 can be phosphorylated in vitro by protein kinase CK2 stoichiometrically in amino acids Ser-58-Ser-59-Ser-60. Phosphorylation of these residues does not modify the interaction of Tcf-4 with beta-catenin but reduces its association to plakoglobin. \| Experiments performed using a Tcf-4 mutant with decreased interaction to plakoglobin demonstrated that binding to this protein negatively affected the transcriptional activity of Tcf-4.

Publications:

3

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-250914	Ser59	NKLFQYAsTDMDKVL	in vitro
pmid	sentence
8663403	We show that serine 59 located between the MADS and MEF2 domains of MEF2C is phosphorylated in vivo and can be phosphorylated in vitro by casein kinase-II (CKII). Phosphorylation of this site enhanced the DNA binding and transcriptional activity of MEF2C by increasing its DNA binding activity 5-fold.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-168673	Ser6	sQMDITDI	Homo sapiens
pmid	sentence
20957047	The cytoplasmic n-terminal domain of nep interacts with the phosphatase and tensin homologue deleted on chromosome 10 (pten) thereby regulating intracellular signaling via akt. Ser 6 is efficiently phosphorylated by protein kinase ck2. The phosphorylation of the cytoplasmic domain of nep inhibits its interaction with pten.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-276005	Ser608	ENTEDQYsLVEDDED	in vitro
pmid	sentence
14729945	Protein kinase CK2 phosphorylates p85α on Ser608 when p85α is free but not when it is complexed with p110α.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-266373	Ser621	GYEGDQEsEGEKEGD	Homo sapiens
pmid	sentence
29021214	We determined that casein kinase II (CK2) can phosphorylate Ser621 and thereby regulate the E3 ligase activity of the SCF(cyclin F) complex.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-42565	Ser63	GILARRPsYRKILKD	Homo sapiens
pmid	sentence
8663317	Camk ii phosphorylates only ser63 (corresponding to ser133 of creb), which is essential for the activation, and not ser72 (corresponding to ser142 of creb), which is a negative regulation site

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250830	Ser64	LQTDGNRsSHSRLGR	Homo sapiens	HeLa Cell
pmid	sentence
11583622	Here we report that Bid is phosphorylated by casein kinase I (CKI) and casein kinase II (CKII). Inhibition of CKI and CKII accelerated Fas-mediated apoptosis and Bid cleavage, whereas hyperactivity of the kinases delayed apoptosis. \| These results suggest that residues S61, S64, and to a much lesser extent T58 are sites of phosphorylation of Bid.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250831	Thr59	EGYDELQtDGNRSSH	Homo sapiens	HeLa Cell
pmid	sentence
11583622	Here we report that Bid is phosphorylated by casein kinase I (CKI) and casein kinase II (CKII). Inhibition of CKI and CKII accelerated Fas-mediated apoptosis and Bid cleavage, whereas hyperactivity of the kinases delayed apoptosis. \| These results suggest that residues S61, S64, and to a much lesser extent T58 are sites of phosphorylation of Bid.

Publications:

2

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-161847	Ser641	TPEELDDsDFETEDF	Homo sapiens	Glioblastoma Cell
pmid	sentence
19941816	We demonstrate here that egfr activation results in disruption of the complex of beta-catenin and alpha-catenin, thereby abrogating the inhibitory effect of alpha-catenin on beta-catenin transactivation via ck2alpha-dependent phosphorylation of alpha-catenin at s641.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277388	Ser655	QDPIDALsGDLDSCP	Homo sapiens	U-87MG Cell
pmid	sentence
29581866	We also showed that casein kinase 2, a pro-survival kinase overexpressed in many cancer types, phosphorylated calpastatin at Ser-633. Our results indicate that calpastatin phosphorylation promotes radiation resistance in GBM cells by increasing the activity of calpain proteases, which are known to promote survival and invasion in cancer.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-184151	Ser659	FHGAEVYsDSEDDVL	Homo sapiens
pmid	sentence
19236849	We demonstrate that sirt1 is a substrate for protein kinase ck2 both in vitro and in vivo. Both, deletion construct analyses and serine-to-alanine mutations identified sirt1 ser-659 and ser-661 as major ck2 phosphorylation sites that are phosphorylated in vivo as well.

Identifier	Residue	Sequence	Organism
SIGNOR-184155	Ser661	GAEVYSDsEDDVLSS	Homo sapiens
pmid	sentence
19236849	We demonstrate that sirt1 is a substrate for protein kinase ck2 both in vitro and in vivo. Both, deletion construct analyses and serine-to-alanine mutations identified sirt1 ser-659 and ser-661 as major ck2 phosphorylation sites that are phosphorylated in vivo as well.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-103258	Ser66	KAARVLGsEGEEEDE	Homo sapiens	HeLa Cell
pmid	sentence
12851383	Moreover, these data confirmed the occurrence of Ser66 phosphorylation, which was previously studied with a specific monoclonal antibody (23).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250862	Ser692	IPDDDEDsYEIFEPP	in vitro
pmid	sentence
9525959	Factor Va, the essential cofactor for prothrombinase, is phosphorylated on the acidic COOH terminus of the heavy chain of the cofactor, at Ser692, by a platelet membrane-associated casein kinase II (CKII). \| The phosphorylated cofactor has increased susceptibility to inactivation by activated protein C, since phosphorylated factor Va was found to be inactivated approximately 3-fold faster than its native counterpart.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-273633	Ser695	DCGSHSLsD	in vitro
pmid	sentence
19640509	In our studies, SICD was phosphorylated by PKA, PKC, and CK2, and association of SLITRK1 with 14-3-3 was regulated by phosphorylation at Ser695. Co-precipitation experiments demonstrated much greater recovery of 14-3-3 in SLITRK1 precipitates when wild-type or S695E was used, as compared with S695A, consistent with the results with purified peptides.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-76266	Ser7	sSAEGAAK	Homo sapiens
pmid	sentence
10739259	Peptide mass and sequence analysis showed major and minor phosphorylation sites, respectively, at ser24 and ser28 in hmg-17, and ser20 and ser24 in hmg-14 a third phosphorylation site in hmg-14 was located at either ser6 or ser7phosphorylation of ser6 and ser7 may compromise the binding of hmgn1 protein to the binding domain of importin proteins, which in turn affects the nuclear transport and sub-cellular localization of hmgn1 protein. Protein kinase ck2 could potentially be an enzyme that regulates this process.

Identifier	Residue	Sequence	Organism
SIGNOR-76270	Ser8	MPKRKVSsAEGAAKE	Homo sapiens
pmid	sentence
10739259	Peptide mass and sequence analysis showed major and minor phosphorylation sites, respectively, at ser24 and ser28 in hmg-17, and ser20 and ser24 in hmg-14 a third phosphorylation site in hmg-14 was located at either ser6 or ser7phosphorylation of ser6 and ser7 may compromise the binding of hmgn1 protein to the binding domain of importin proteins, which in turn affects the nuclear transport and sub-cellular localization of hmgn1 protein. Protein kinase ck2 could potentially be an enzyme that regulates this process.

Identifier	Residue	Sequence	Organism
SIGNOR-76274	Ser89	KTEESPAsDEAGEKE	Homo sapiens
pmid	sentence
10739259	Protein kinases that phosphorylate hmg-14 17 at the major sites have been implicated from previous in vitro studies. Protein kinase c and a similar calcium phospholipid-dependent kinase have been reported to phosphorylate both proteins in vitro, where the phosphorylation of hmg-17 occurs predominantly at ser24 and to a lesser degree at ser28. Phosphorylation of hmg-14 at ser6 by camp- or cgmp-dependent kinases has also been reported. Thus, other kinases may contribute to phosphorylation at ser6 in response to oa. Ser88 and ser98 on hmg-14 are also phosphorylated by casein kinase ii in vitro. we conclude that the correlation we observe reflects a causal relationship, in which phosphorylation somehow facilitates the redistribution of hmg-14 and -17 toward non-nuclear pools.

Identifier	Residue	Sequence	Organism
SIGNOR-76278	Ser99	AGEKEAKsD	Homo sapiens
pmid	sentence
10739259	Protein kinases that phosphorylate hmg-14 17 at the major sites have been implicated from previous in vitro studies. Protein kinase c and a similar calcium phospholipid-dependent kinase have been reported to phosphorylate both proteins in vitro, where the phosphorylation of hmg-17 occurs predominantly at ser24 and to a lesser degree at ser28. Phosphorylation of hmg-14 at ser6 by camp- or cgmp-dependent kinases has also been reported. Thus, other kinases may contribute to phosphorylation at ser6 in response to oa. Ser88 and ser98 on hmg-14 are also phosphorylated by casein kinase ii in vitro. we conclude that the correlation we observe reflects a causal relationship, in which phosphorylation somehow facilitates the redistribution of hmg-14 and -17 toward non-nuclear pools.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-276253	Ser702	AVILTVEsEEEEEES	in vitro
pmid	sentence
21296876	CK2 phosphorylation of an acidic Ser/Thr di-isoleucine motif in the Na+/H+ exchanger NHE5 isoform promotes association with beta-arrestin2 and endocytosis

Identifier	Residue	Sequence	Organism
SIGNOR-276252	Ser709	SEEEEEEsDSSETEK	in vitro
pmid	sentence
21296876	CK2 phosphorylation of an acidic Ser/Thr di-isoleucine motif in the Na+/H+ exchanger NHE5 isoform promotes association with beta-arrestin2 and endocytosis

Identifier	Residue	Sequence	Organism
SIGNOR-276251	Ser711	EEEEESDsSETEKED	in vitro
pmid	sentence
21296876	CK2 phosphorylation of an acidic Ser/Thr di-isoleucine motif in the Na+/H+ exchanger NHE5 isoform promotes association with beta-arrestin2 and endocytosis

Identifier	Residue	Sequence	Organism
SIGNOR-276249	Ser712	EEEESDSsETEKEDD	in vitro
pmid	sentence
21296876	CK2 phosphorylation of an acidic Ser/Thr di-isoleucine motif in the Na+/H+ exchanger NHE5 isoform promotes association with beta-arrestin2 and endocytosis

Identifier	Residue	Sequence	Organism
SIGNOR-276250	Thr714	EESDSSEtEKEDDEG	in vitro
pmid	sentence
21296876	CK2 phosphorylation of an acidic Ser/Thr di-isoleucine motif in the Na+/H+ exchanger NHE5 isoform promotes association with beta-arrestin2 and endocytosis

Publications:

5

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250859	Ser717	LKEAEEEsSEDD	Homo sapiens	HEK-293 Cell
pmid	sentence
11500362	Two conserved sites (Ser712/713) are phosphorylated by casein kinase 2. They lie at the extreme C-terminus and are required for the interaction of eIF2Bepsilon with its substrate, eIF2, in vivo and for eIF2B activity in vitro.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250860	Ser718	KEAEEESsEDD	Homo sapiens	HEK-293 Cell
pmid	sentence
11500362	Two conserved sites (Ser712/713) are phosphorylated by casein kinase 2. They lie at the extreme C-terminus and are required for the interaction of eIF2Bepsilon with its substrate, eIF2, in vivo and for eIF2B activity in vitro.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-173105	Ser737	PEEIIVLsDSD	Homo sapiens
pmid	sentence
21474068	Daxx-sim is phosphorylated by ck2 kinase at residues s737 and s739. Phosphorylation promotes daxx-sim binding affinity toward sumo-1 over sumo-2/3, causing daxx preference for sumo-1 conjugation and interaction with sumo-1-modified factors.

Identifier	Residue	Sequence	Organism
SIGNOR-173109	Ser739	EIIVLSDsD	Homo sapiens
pmid	sentence
21474068	Daxx-sim is phosphorylated by ck2 kinase at residues s737 and s739. Phosphorylation promotes daxx-sim binding affinity toward sumo-1 over sumo-2/3, causing daxx preference for sumo-1 conjugation and interaction with sumo-1-modified factors.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250905	Ser743	MPLQPNAsLNEEEGT	in vitro
pmid	sentence
12450396	We now show that N-terminal to the NLS domain of pro-IL-16 are protein kinase CK2 substrate and cdc2 kinase substrate sites which, along with the NLS, constitute a dual phosphorylation-regulated CcN motif which regulates nuclear localization of pro-IL-16. In addition, we demonstrate that mutation of either site is associated with impairment of the N-terminal domain's ability to induce G(0)/G(1) cell cycle arrest. \| Thus, we confirm that the N-terminal (42SLNEE46) sequence of pro-IL-16 is in fact a site for protein kinase CK2 phosphorylation.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-276013	Ser751	FGTMSSMsGADDTVY	in vitro
pmid	sentence
15549133	Phosphorylation of S751 by CKII inhibits 5′ incision.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-250955	Ser77	PTAGALYsGSEGDSE	in vitro
pmid	sentence
2046671	Casein kinase II (CKII) phosphorylates the mammalian transcription factor serum response factor (SRF) on a serine residue(s) located within a region of the protein spanning amino acids 70 to 92, thereby enhancing its DNA-binding activity in vitro.\| Nevertheless, additional mutation of serines 77 and 79 was required before phosphorylation and enhanced binding were completely abolished. Thus, serines 77 and 79 could also be recognized by CKII if serines 83 and 85 were mutated.

Identifier	Residue	Sequence	Organism
SIGNOR-250956	Ser79	AGALYSGsEGDSESG	in vitro
pmid	sentence
2046671	Casein kinase II (CKII) phosphorylates the mammalian transcription factor serum response factor (SRF) on a serine residue(s) located within a region of the protein spanning amino acids 70 to 92, thereby enhancing its DNA-binding activity in vitro.\| Nevertheless, additional mutation of serines 77 and 79 was required before phosphorylation and enhanced binding were completely abolished. Thus, serines 77 and 79 could also be recognized by CKII if serines 83 and 85 were mutated.

Identifier	Residue	Sequence	Organism
SIGNOR-250958	Ser83	YSGSEGDsESGEEEE	in vitro
pmid	sentence
2046671	Casein kinase II (CKII) phosphorylates the mammalian transcription factor serum response factor (SRF) on a serine residue(s) located within a region of the protein spanning amino acids 70 to 92, thereby enhancing its DNA-binding activity in vitro. We report here that serine 83 appears to be the residue phosphorylated by CKII but that three other serines in this region can also be involved in phosphorylation and the enhancement of DNA-binding activity.

Identifier	Residue	Sequence	Organism
SIGNOR-250957	Ser85	GSEGDSEsGEEEELG	in vitro
pmid	sentence
2046671	Casein kinase II (CKII) phosphorylates the mammalian transcription factor serum response factor (SRF) on a serine residue(s) located within a region of the protein spanning amino acids 70 to 92, thereby enhancing its DNA-binding activity in vitro.\| Mutation of serine 85 alone had a smaller but significant effect on phosphorylation that may be due to alteration in the protein kinase recognition site.

Publications:

4

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-140034	Ser77	DKERFARsDDEQSSA	Homo sapiens
pmid	sentence
16129408	Here, we show that arnt and alt arnt proteins are differentially phosphorylated by protein kinase ckii in vitro. Phosphorylation had an inhibitory effect on dna-binding to an e-box probe by alt arnt, but not arnt, homodimers. This inhibitory phosphorylation occurs through ser77.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250895	Ser79	TALYFTYsALEEEME	Rattus norvegicus	Hippocampal Cell Line
pmid	sentence
14527438	Carbon monoxide neurotransmission activated by CK2 phosphorylation of heme oxygenase-2. \| CK2 activation is abolished by the S79A mutation but preserved in S179A and T248A mutations, indicating that S79 is the target of CK2-dependent activation of HO2

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism
SIGNOR-250926	Ser81	TQDQQSLsDVEGAYS	in vitro
pmid	sentence
7983041	Although human PR contains 11 potential CKII consensus sequences, CKII in vitro phosphorylated purified PR-B only at Ser81 suggesting that this may be an authentic site for CKII in vivo.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-121572	Ser812	FPRSLDDsEEDDDED	Homo sapiens
pmid	sentence
14742446	Ser(812) can be phosphorylated by ck2 in vitro and substitution s812a results in failure to incorporate phosphate in cultured epithelial cells.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-200240	Ser828	DVADGNVsDFDNEEE	Homo sapiens
pmid	sentence
23263282	Here we report that tel2 and tti1 are targeted for degradation within mtorc1 by the scffbxo9 ubiquitin ligase to adjust mtor signalling to growth factor availability. This process is primed by ck2, which translocates to the cytoplasm to mediate mtorc1-specific phosphorylation of tel2/tti1

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250839	Ser838	LVFDYEGsGSEAASL	Mus musculus	NIH-3T3 Cell
pmid	sentence
10671552	Casein kinase II phosphorylation of E-cadherin increases E-cadherin/beta-catenin interaction and strengthens cell-cell adhesion. \| All mutants showed a clear reduction in phosphorylation. Phosphorylation was completely abolished in the single mutant S855A and the double mutant S853/855A, and phosphorylation in S840A and S853A mutants was reduced to 43 and 28% that of wt GST-ECT. \| Expression of the E-cadherin double mutant S853A/S855A in NIH3T3 cells expressing Wnt-1 reduces cell-cell adhesion.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250840	Ser851	SLSSLNSsESDKDQD	Mus musculus	NIH-3T3 Cell
pmid	sentence
10671552	Casein kinase II phosphorylation of E-cadherin increases E-cadherin/beta-catenin interaction and strengthens cell-cell adhesion. \| Under these conditions, phosphorylation of the E-cadherin double mutant S853A/S855A was reduced by 25% as compared with wt E-cadherin. \| Expression of the E-cadherin double mutant S853A/S855A in NIH3T3 cells expressing Wnt-1 reduces cell-cell adhesion.

Identifier	Residue	Sequence	Organism
SIGNOR-250841	Ser853	SSLNSSEsDKDQDYD	Mus musculus
pmid	sentence
10671552	Casein kinase II phosphorylation of E-cadherin increases E-cadherin/beta-catenin interaction and strengthens cell-cell adhesion. \| Under these conditions, phosphorylation of the E-cadherin double mutant S853A/S855A was reduced by 25% as compared with wt E-cadherin. \| Expression of the E-cadherin double mutant S853A/S855A in NIH3T3 cells expressing Wnt-1 reduces cell-cell adhesion.

Publications:

3

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-169400	Ser854	HPKPKQFsSFEKRAK	Homo sapiens
pmid	sentence
21068236	Phosphorylation of rig-i by casein kinase ii inhibits its antiviral response. Threonine at amino acid (aa) 770 and serine at aa 854 to 855 of rig-i are phosphorylated by casein kinase ii (ck2)

Identifier	Residue	Sequence	Organism
SIGNOR-169404	Ser855	PKPKQFSsFEKRAKI	Homo sapiens
pmid	sentence
21068236	Threonine at amino acid (aa) 770 and serine at aa 854 to 855 of rig-i are phosphorylated by casein kinase ii (ck2) in the resting state of the cell and dephosphorylated when cells are infected by rna virus. Mutation at aa position 770 or 854 to 855 of rig-i renders it constitutively active

Identifier	Residue	Sequence	Organism
SIGNOR-169408	Thr770	DSILRLQtWDEAVFR	Homo sapiens
pmid	sentence
21068236	Threonine at amino acid (aa) 770 and serine at aa 854 to 855 of rig-i are phosphorylated by casein kinase ii (ck2) in the resting state of the cell and dephosphorylated when cells are infected by rna virus. Mutation at aa position 770 or 854 to 855 of rig-i renders it constitutively active

Publications:

3

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273628	Ser854	DAEYIYPsLESDDDD	Homo sapiens	HeLa Cell
pmid	sentence
33010150	The CK2 kinase is responsible for PHF8 phosphorylation at Ser854. PHF8 is phosphorylated by CK2, which regulates binding of PHF8 to TopBP1. The Ser854 residue of PHF8 is required for its interaction with TopBP1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273626	Ser87	RLQRHRTsGGDHAPD	Homo sapiens	HEK-293 Cell
pmid	sentence
29850896	Here, we show that the CK2 kinase phosphorylates MUS81 at Serine 87 in late-G2/mitosis, and upon mild replication stress. Phosphorylated MUS81 interacts with SLX4, and this association promotes the function of the MUS81 complex.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-73807	Ser87	KTVEGAGsIAAATGF	Homo sapiens	Neuron
pmid	sentence
10617630	In vitro experiments and two-dimensional phosphopeptide mapping provided further evidence that serine 129 was phosphorylated by ck-1 and ck-2. Moreover, phosphorylation of serine 129 was reduced in vivo upon inhibition of ck-1 or ck-2. These data demonstrate that alpha-synuclein is constitutively phosphorylated within its c terminus and may indicate that the function of alpha-synuclein is regulated by phosphorylation/dephosphorylation.From these data we conclude that _-synuclein is predominantly phosphorylated at serine residue 129. However, a second serine at position 87 is also used for phosphorylation to some extent. together, these data may indicate that ck-1 and ck-2 are involved in the regulation of neuronal function and one may speculate that phosphorylation of _-synuclein could affect its binding to membranes.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-250929	Ser87	GDDEDACsDTEATEA	in vitro
pmid	sentence
8288648	Recombinant wild-type I-2 and the Ala-120/121 mutant were phosphorylated synergistically by GSK-3 and casein kinase II. The Thr-72 and Ser-86 mutants, however, did not undergo this synergistic phosphorylation. Our studies indicate that Thr-72 is the only GSK-3 site and that Ser-86 is the casein kinase II site required for the potentiation of GSK-3 action.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-250835	Ser88	FDGIWKAsFTTFTVT	in vitro
pmid	sentence
8058322	Here, we have identified this serine kinase activity as a casein kinase II-like enzyme, since the phosphorylation of caveolin-rich membrane domains is stimulated and inhibited by known effectors of casein kinase II (poly-L-lysine, endogenous polyamines, and a casein kinase II inhibitor peptide), but is unaffected by modulators of other known kinases. In support of these observations, caveolin contains a consensus sequence for casein kinase II phosphorylation in its cytoplasmic N-terminal domain (Ser-88)

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276730	Ser882	DGSKTSSsDTLSEEK	Homo sapiens	HeLa Cell
pmid	sentence
31167143	Here, we report a cluster of phosphosites on FANCD2 whose phosphorylation by CK2 inhibits both FANCD2 recruitment to ICLs and its monoubiquitination in vitro and in vivo. We have found that phosphorylated FANCD2 possesses reduced DNA binding activity, explaining the previous observations.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276731	Ser886	TSSSDTLsEEKNSEC	Homo sapiens	HeLa Cell
pmid	sentence
31167143	Here, we report a cluster of phosphosites on FANCD2 whose phosphorylation by CK2 inhibits both FANCD2 recruitment to ICLs and its monoubiquitination in vitro and in vivo. We have found that phosphorylated FANCD2 possesses reduced DNA binding activity, explaining the previous observations.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276728	Ser891	TLSEEKNsECDPTPS	Homo sapiens	HeLa Cell
pmid	sentence
31167143	Here, we report a cluster of phosphosites on FANCD2 whose phosphorylation by CK2 inhibits both FANCD2 recruitment to ICLs and its monoubiquitination in vitro and in vivo. We have found that phosphorylated FANCD2 possesses reduced DNA binding activity, explaining the previous observations.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276729	Ser898	SECDPTPsHRGQLNK	Homo sapiens	HeLa Cell
pmid	sentence
31167143	Here, we report a cluster of phosphosites on FANCD2 whose phosphorylation by CK2 inhibits both FANCD2 recruitment to ICLs and its monoubiquitination in vitro and in vivo. We have found that phosphorylated FANCD2 possesses reduced DNA binding activity, explaining the previous observations.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276732	Thr884	SKTSSSDtLSEEKNS	Homo sapiens	HeLa Cell
pmid	sentence
31167143	Here, we report a cluster of phosphosites on FANCD2 whose phosphorylation by CK2 inhibits both FANCD2 recruitment to ICLs and its monoubiquitination in vitro and in vivo. We have found that phosphorylated FANCD2 possesses reduced DNA binding activity, explaining the previous observations.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276733	Thr896	KNSECDPtPSHRGQL	Homo sapiens	HeLa Cell
pmid	sentence
31167143	Here, we report a cluster of phosphosites on FANCD2 whose phosphorylation by CK2 inhibits both FANCD2 recruitment to ICLs and its monoubiquitination in vitro and in vivo. We have found that phosphorylated FANCD2 possesses reduced DNA binding activity, explaining the previous observations.

Publications:

6

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-200798	Ser9	SAPAAKVsKKELNSN	Homo sapiens	Neuron
pmid	sentence
23374587	Ckii-mediated phosphorylation at ser9 hinders nuclear import of set

Publications:

1

Organism:

Homo Sapiens

Tissue:

Brain

Identifier	Residue	Sequence	Organism
SIGNOR-135422	Ser9	ADFDDRVsDEEKVRI	Homo sapiens
pmid	sentence
15831458	We demonstrate that ser9 of cpalpha is phosphorylated by protein kinase ck2 in vitro, that cpalpha is phosphorylated in vivo. Finally, we demonstrate that ckip-1 and ck2 inhibit the activity of actin capping protein at the barbed ends of actin filaments.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-266384	Ser902	ETAEEEEsEEEAD	Homo sapiens	HEK-293 Cell
pmid	sentence
29530922	DAP5(S902) is phosphorylated by CK2α. Phosphorylation of DAP5(S902) by CK2α is required for eIF2β binding.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-161775	Ser92	VAELTSLsDEDSGKG	Homo sapiens
pmid	sentence
19923321	Serines 11 and 92 participate in the control of snail1 stability and positively regulate snail1 repressive function and its interaction with msin3a corepressor. Furthermore, serines 11 and 92 are required for snail1-mediated emt and cell viability, respectively. Pka and ck2 have been characterized as the main kinases responsible for in vitro snail1 phosphorylation at serine 11 and 92, respectively.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277389	Ser94	VIKDEALsDGDDLRD	Homo sapiens	HaCaT Cell
pmid	sentence
29660033	CK2 kinase mediates XPC phosphorylation at serine 94, and also promotes recruitment of ubiquitinated XPC to the chromatin after UVB irradiation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-101187	Thr10	DVEDGEEtCALASHS	Homo sapiens	HeLa Cell
pmid	sentence
12748192	Ckbbp1 is phosphorylated in vivo and threonine to alanine mutation at residue 10 abrogates the phosphorylation of ckbbp1 observed in vivo, indicating that ckii is a major kinase that is responsible for in vivo phosphorylation of ckbbp1. As compared with the wild-type ckbbp1 or ckbbp1t10e (in which threonine 10 is replaced by glutamate), overexpression of nonphosphorylatable ckbbp1 (ckbbp1t10a) results in accumulation of ikappabalpha and p27kip1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-178034	Thr122	LTACQLRtIYICQFL	Homo sapiens
pmid	sentence
18347021	Regulation of telomeric repeat binding factor 1 binding to telomeres by casein kinase 2-mediated phosphorylation. Mapping of the ck2 target site identified threonine 122 as a substrate in trf1. A threonine to alanine change at this position led to a diminished dna binding due to reduced dimerization of trf1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250898	Thr142	DSVTKLLtDVQLMKG	in vitro
pmid	sentence
12659875	Transcriptional activity and DNA binding of heat shock factor-1 involve phosphorylation on threonine 142 by CK2.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-250865	Thr143	EFKGEDLtEEEDGGI	in vitro
pmid	sentence
9405642	Thr-143 in the hinge I region was identified as the major phosphorylation site for CK2. \| Most importantly, CK2-phosphorylated FKBP52 did not bind to HSP90

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262837	Thr149	SEAVQSGtPEEPEPE	Homo sapiens	HEK-293 Cell
pmid	sentence
12191471	Phosphorylation of ARC at T149 Is Required for Its Antiapoptotic Effect. Here we report that the function of ARC is regulated by protein kinase CK2. ARC at threonine 149 is phosphorylated by CK2. This phosphorylation targets ARC to mitochondria. ARC is able to bind to caspase-8 only when it is localized to mitochondria but not to the cytoplasm.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250968	Thr155	DSTPPPGtRVRAMAI	in vitro
pmid	sentence
12628923	CK2 phosphoryl ates Thr155, which targets p53 to degradation by the Ub system.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-250885	Thr16	DVSVSVEtQGDDWDT	Homo sapiens
pmid	sentence
10806407	The in vivo Ser/Thr phosphorylation of HS1 is enhanced by okadaic acid and reduced by specific inhibitors of casein kinase (CK)2. In vitro, HS1 is an excellent substrate for either CK2 alpha subunit alone (Km = 47 nM) or CK2 holoenzyme \| It is likely therefore that Thr16 and/or Thr23 account for the phosphate incorporated into HS1 threonyl residue(s) upon incubation with CK2.

Identifier	Residue	Sequence	Organism
SIGNOR-250886	Thr23	TQGDDWDtDPDFVND	Homo sapiens
pmid	sentence
10806407	The in vivo Ser/Thr phosphorylation of HS1 is enhanced by okadaic acid and reduced by specific inhibitors of casein kinase (CK)2. In vitro, HS1 is an excellent substrate for either CK2 alpha subunit alone (Km = 47 nM) or CK2 holoenzyme \| It is likely therefore that Thr16 and/or Thr23 account for the phosphate incorporated into HS1 threonyl residue(s) upon incubation with CK2.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-265086	Thr210	TSSSSDEtDVEGKPS	Homo sapiens	HeLa Cell
pmid	sentence
25064736	Phosphorylated Thr 210 in Treacle is the major interaction site for NBS1\|A purified GST fragment of this region was efficiently phosphorylated by CK2 in vitro (Supplementary Fig. 4; T-2) and this fragment pulled down the MRN complex from Hela nuclear extracts only when previously phosphorylated by CK2

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-241361	Thr23	ALGPFPDtQDDFLKW	Mus musculus	MEL Cell
pmid	sentence
9722526	Regulation of erythroid Krppel-like factor (EKLF) transcriptional activity by phosphorylation of a protein kinase casein kinase II site within its interaction domain. the transactivation capability of EKLF is augmented by co-transfection of CKIIalpha. in vitro assays demonstrate that CKIIalpha interacts with EKLF, and that the EKLF interaction domain is phosphorylated by CKII only at Thr-41

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-123713	Thr236	VEKFKDNtIPDKVKK	Homo sapiens
pmid	sentence
15064744	Inhibition of protein kinase ck2 enzyme activity in vivo resulted in an enhanced nuclear localization of cdc25c. Thus, phosphorylation of cdc25c at threonine 236 is an important signal for the retention of cdc25c in the cytoplasm

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-183158	Thr244	GEKRKREtDDEGEDD	Homo sapiens
pmid	sentence
19130553	Here, we are able to report that casein kinase 2 (ck2) phosphorylates april on residue threonine244 (thr(244)) and demonstrate that the ck2-specific inhibitor 4,5,6,7-tetrabromo-2-azabenzimidazole abolishes cd83 expression in activated jurkat t cells by interfering with the nucleocytoplasmic translocation of cd83 mrna

Identifier	Residue	Sequence	Organism
SIGNOR-151261	Thr244	GEKRKREtDDEGEDD	Homo sapiens
pmid	sentence
17178712	Here, we are able to report that casein kinase 2 (ck2) phosphorylates april on residue threonine244 (thr(244)) and demonstrate that the ck2-specific inhibitor 4,5,6,7-tetrabromo-2-azabenzimidazole abolishes cd83 expression in activated jurkat t cells by interfering with the nucleocytoplasmic translocation of cd83 mrna

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-197844	Thr249	WSLNKEDtSEQVVPV	Homo sapiens
pmid	sentence
22695718	Casein kinase 2_ regulates multidrug resistance-associated protein 1 function via phosphorylation of thr249. This study supports a model in which ck2_ potentiates mrp1 function via direct phosphorylation of thr249.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250969	Thr300	PPEEGTEtSGDSQLL	in vitro
pmid	sentence
16426576	CK2-dependent C-terminal phosphorylation at T300 directs the nuclear transport of TSPY protein

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-149314	Thr350	PEVKKEEtLLDLDFD	Homo sapiens	HeLa Cell
pmid	sentence
16945112	Amphiphysins interact directly with clathrin and have a function in clathrin-mediated synaptic vesicle recycling and clathrin-mediated endocytosis. The n-terminal domain of clathrin bound to unphosphorylated amphiphysin-1, but not to the phosphorylated protein. The assumption that casein kinase 2 phosphorylates amphiphysin-1 at t350 and t387 was corroborated by experiments showing that: casein kinase 2 phosphorylated these residues directly in vitro,. upon activation by nerve growth factor, casein kinase 2 phosphorylates amphiphysin-1 and thereby regulates the endocytosis of clathrin-coated vesicles via the interaction between clathrin and amphiphysin.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-149318	Thr387	LPWDLWTtSTDLVQP	Homo sapiens	HeLa Cell
pmid	sentence
16945112	Amphiphysins interact directly with clathrin and have a function in clathrin-mediated synaptic vesicle recycling and clathrin-mediated endocytosis. The n-terminal domain of clathrin bound to unphosphorylated amphiphysin-1, but not to the phosphorylated protein. The assumption that casein kinase 2 phosphorylates amphiphysin-1 at t350 and t387 was corroborated by experiments showing that: casein kinase 2 phosphorylated these residues directly in vitro,. upon activation by nerve growth factor, casein kinase 2 phosphorylates amphiphysin-1 and thereby regulates the endocytosis of clathrin-coated vesicles via the interaction between clathrin and amphiphysin.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250829	Thr382	EFDTNYAtDDDIVFE	in vitro
pmid	sentence
11877451	We found that arrestin-3 is constitutively phosphorylated at Thr-382 and becomes dephosphorylated upon beta(2)-adrenergic receptor activation in COS-1 cells. Casein kinase II (CKII) appears to be the major kinase mediating arrestin-3 phosphorylation, since 1) Thr-382 is contained within a canonical consensus sequence for CKII phosphorylation and 2) wild type arrestin-3 but not a T382A mutant is phosphorylated by CKII in vitro. \| However, additional analysis reveals that arrestin-3 phosphorylation may regulate formation of a large arrestin-3-containing protein complex.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273630	Thr410	MEIASQRtKEERSSQ	Homo sapiens	HEK-293 Cell
pmid	sentence
29384474	Casein kinase 2 (CK2) phosphorylates RIOK1 at T410, which stabilizes RIOK1 by antagonizing K411 methylation and impeding the recruitment of FBXO6 to RIOK1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-267666	Thr454	AAEAAPPtQEAQGET	Homo sapiens
pmid	sentence
24962073	CK2alphawas bound to DBC1 and phosphorylated DBC1. The phosphorylation of DBC1 by CK2alphawas evidenced by co-immunoprecipitation of CK2alphaand DBC1 in a GST pull-down assay, an in vitro kinase assay, and immunofluorescence staining. \|In our results, CK2alpha affected the\|These results suggest that DBC1 may be involved in the progression of gastric carcinoma by inducing the EMT and that it is closely associated with CK2alpha-mediated phosphorylation of DBC1. phosphorylation of Thr454 on DBC1

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-158319	Thr494	TEAVQDPtKVEAHVR	Homo sapiens
pmid	sentence
17932117	Our findings provide new insights into the biology of hprp3p and suggest that the loss of hprp3p phosphorylation at thr494 is a key step for initiating thr494met aberrant interactions within u4/u6 snrnp complex and that these are likely linked to the rp18 phenotype.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-187450	Thr51	GFSDEDNtWEPEENL	Homo sapiens
pmid	sentence
19657222	Two recent papers suggest that hp1 recruitment to damage sites, rather than its rapid mobilization, is the predominant behaviour exhibited by this protein. Our findings reconcile recent findings in a new model, wherein rapid hp1beta mobilization from dsbs is mediated by its phosphorylation on thr51 by ck2

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-266900	Thr531	NTTGSDNtDTEGS	Homo sapiens
pmid	sentence
17936701	PVHL serves as an adaptor that promotes the phosphorylation of the Card9 C terminus by CK2.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262290	Thr531	NTTGSDNtDTEGS	Homo sapiens	HeLa Cell
pmid	sentence
17936701	PVHL Acts as an Adaptor to Promote the Inhibitory Phosphorylation of the NF-κB Agonist Card9 by CK2

Identifier	Residue	Sequence	Organism
SIGNOR-269111	Thr533	TGSDNTDtEGS	Homo sapiens
pmid	sentence
17936701	PVHL serves as an adaptor that promotes the phosphorylation of the Card9 C terminus by CK2.

Identifier	Residue	Sequence	Organism
SIGNOR-257601	Thr533	TGSDNTDtEGS	Homo sapiens
pmid	sentence
17936701	PVHL Acts as an Adaptor to Promote the Inhibitory Phosphorylation of the NF-κB Agonist Card9 by CK2

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-158414	Thr531	NTTGSDNtDTEGS	Homo sapiens
pmid	sentence
17936701	Pvhl acts as an adaptor to promote the inhibitory phosphorylation of the nf-kappab agonist card9 by ck2. The card9 c terminus contains multiple serine and threonine residues that resemble ck2 phosphorylation sites. Mass spectrometry analysis of myc-card9 recovered from hela cells revealed that these sites, including t531 and t533, were phosphorylated in vivo

Identifier	Residue	Sequence	Organism
SIGNOR-158418	Thr533	TGSDNTDtEGS	Homo sapiens
pmid	sentence
17936701	Pvhl acts as an adaptor to promote the inhibitory phosphorylation of the nf-kappab agonist card9 by ck2. The card9 c terminus contains multiple serine and threonine residues that resemble ck2 phosphorylation sites. Mass spectrometry analysis of myc-card9 recovered from hela cells revealed that these sites, including t531 and t533, were phosphorylated in vivo

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250954	Thr579	GDGIHDDtAGGEEGE	Homo sapiens
pmid	sentence
9153193	Casein kinase II-mediated phosphorylation of the C terminus of Sp1 decreases its DNA binding activity. \| Mutation of a consensus CKII site at amino acid 579, within the second zinc finger, eliminates phosphorylation of this site and the CKII-mediated inhibition of Sp1 binding.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-265260	Thr61	ERRPESFtTPEGPKP	Homo sapiens
pmid	sentence
18490441	Phosphorylation of Thr61 is necessary for subsequent phosphorylation of Thr60 by CK2 in vitro. Inhibitors of CK2 also prevent degradation of SLBP at the end of S phase. Thus, phosphorylation of Thr61 by cyclin A/Cdk1 primes phosphorylation of Thr60 by CK2 and is responsible for initiating SLBP degradation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250970	Thr69	VTRGDVFtMPEDEYT	Mus musculus	NIH-3T3 Cell
pmid	sentence
9733784	Therefore, we expressed Vn in a baculovirus system and show (i) that the CKII phosphorylation of wt-Vn enhances the adhesion of bovine aorta endothelial cells; (ii) that the double mutant T50E/T57E (in which the neutral Thr residues are replaced by the negatively charged Glu residues considered analogs of Thr-P) has a significantly enhanced capacity to promote cell adhesion and to accelerate cell spreading when compared with either wild-type Vn or to the neutral T50A/T57A mutant

Identifier	Residue	Sequence	Organism
SIGNOR-250971	Thr76	TMPEDEYtVYDDGEE	Mus musculus
pmid	sentence
9733784	Therefore, we expressed Vn in a baculovirus system and show (i) that the CKII phosphorylation of wt-Vn enhances the adhesion of bovine aorta endothelial cells; (ii) that the double mutant T50E/T57E (in which the neutral Thr residues are replaced by the negatively charged Glu residues considered analogs of Thr-P) has a significantly enhanced capacity to promote cell adhesion and to accelerate cell spreading when compared with either wild-type Vn or to the neutral T50A/T57A mutant

Publications:

2

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-250891	Thr796	ESGLPQLtSYDCEVN	in vitro
pmid	sentence
17382325	These results implied that only Thr-796 was phosphorylated CK2.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Organism
SIGNOR-187209		Homo sapiens
pmid	sentence
19623618	Here, we identify ck1 and ck2 as major kinases that directly bind to and phosphorylate lef-1 inducing distinct, kinase-specific changes in the lef-1/dna complex.CK1-dependent phosphorylation inhibits, whereas ck2 activates lef-1/beta-catenin transcriptional activity in reporter gene assays.

Identifier	Residue	Organism
SIGNOR-134500		Homo sapiens
pmid	sentence
15747065	Here, we identify ck1 and ck2 as major kinases that directly bind to and phosphorylate lef-1 inducing distinct, kinase-specific changes in the lef-1/dna complex. Ck1-dependent phosphorylation inhibits, whereas ck2 activates lef-1/beta-catenin transcriptional activity in reporter gene assays.

Identifier	Residue	Organism
SIGNOR-23958		Homo sapiens
pmid	sentence
2861485	Here, we identify ck1 and ck2 as major kinases that directly bind to and phosphorylate lef-1 inducing distinct, kinase-specific changes in the lef-1/dna complex.CK1-dependent phosphorylation inhibits, whereas ck2 activates lef-1/beta-catenin transcriptional activity in reporter gene assays.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-192064		Homo sapiens
pmid	sentence
22975381	Ck2-mediated phosphorylation at ser392 of p53 was attenuated in the presence of recombinant twist1

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-265822		Homo sapiens	Glioblastoma Cell
pmid	sentence
19941816	We demonstrate here that egfr activation results in disruption of the complex of beta-catenin and alpha-catenin, thereby abrogating the inhibitory effect of alpha-catenin on beta-catenin transactivation via ck2alpha-dependent phosphorylation of alpha-catenin at s641.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-170525		Homo sapiens
pmid	sentence
21149568	We have identified a novel striated muscle-specific splice variant of the formin fhod3 that introduces a casein kinase 2 (ck2) phosphorylation site. The specific targeting of muscle fhod3 to the myofibrils in cardiomyocytes is abolished in phosphomutants or by the inhibition of ck2. Phosphorylation of muscle fhod3 also prevents its interaction with p62/sequestosome 1 and its recruitment to autophagosomes.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Muscle

Identifier	Residue	Organism	Cell Line
SIGNOR-273656		Homo sapiens	THP-1 Cell
pmid	sentence
29733298	Here, we show that somatic nuclear autoantigenic sperm protein (sNASP) binds to TRAF6 to prevent TRAF6 autoubiquitination in unstimulated macrophages. Following LPS stimulation, a complex consisting of sNASP, TRAF6, IRAK4, and casein kinase 2 (CK2) is formed. CK2 phosphorylates sNASP at serine 158, allowing sNASP to dissociate from TRAF6. Free TRAF6 is then autoubiquitinated, followed by activation of downstream signaling pathways.

Publications:

1

Organism:

Homo Sapiens

Pathways: