Relation Results

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-174840	Ser101	GSHRDQGsSALSGVG	Homo sapiens	Leukemia Cell
pmid	sentence
21750978	We identified four novelikarosphosphorylation sites that are phosphorylated by ck2 kinase. / ck2-mediated phosphorylation inhibits ikaros' localization to pc-hc / hyperphosphorylation of ikaros promotes its degradation by the ubiquitin/proteasome pathway

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-174844	Ser13	GQDMSQVsGKESPPV	Homo sapiens	Leukemia Cell
pmid	sentence
21750978	We identified four novelikarosphosphorylation sites that are phosphorylated by ck2 kinase. / ck2-mediated phosphorylation inhibits ikaros' localization to pc-hc / hyperphosphorylation of ikaros promotes its degradation by the ubiquitin/proteasome pathway

Identifier	Residue	Sequence	Organism
SIGNOR-174848	Ser295	LSDTPYDsSASYEKE	Homo sapiens
pmid	sentence
21750978	We identified four novelikarosphosphorylation sites that are phosphorylated by ck2 kinase. / ck2-mediated phosphorylation inhibits ikaros' localization to pc-hc / hyperphosphorylation of ikaros promotes its degradation by the ubiquitin/proteasome pathway / these results suggest that ck2 kinase directly phosphorylates amino acids 13, 23, 63, 101 and 294 in vivo

Identifier	Residue	Sequence	Organism
SIGNOR-174852	Ser63	NVKVETQsDEENGRA	Homo sapiens
pmid	sentence
21750978	We identified four novelikarosphosphorylation sites that are phosphorylated by ck2 kinase. / ck2-mediated phosphorylation inhibits ikaros' localization to pc-hc / hyperphosphorylation of ikaros promotes its degradation by the ubiquitin/proteasome pathway / these results suggest that ck2 kinase directly phosphorylates amino acids 13, 23, 63, 101 and 294 in vivo

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-174856	Thr23	ESPPVSDtPDEGDEP	Homo sapiens	Leukemia Cell
pmid	sentence
21750978	We identified four novelikarosphosphorylation sites that are phosphorylated by ck2 kinase. / ck2-mediated phosphorylation inhibits ikaros' localization to pc-hc / hyperphosphorylation of ikaros promotes its degradation by the ubiquitin/proteasome pathway

Publications:

5

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-251056	Ser1085	RQRLAVSsRGENLVH	in vitro
pmid	sentence
11298324	Interaction of CD163 with the regulatory subunit of casein kinase II (CKII) and dependence of CD163 signaling on CKII and protein kinase C. \| Inhibition studies using specific kinase inhibitors reveal that both CKII and PKC are involved in the CD163 signaling mechanism resulting in the secretion of proinflammatory cytokines.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-275752	Ser1112	VPIAVGEsDFENLNT	Homo sapiens	Neuron
pmid	sentence
19064667	We found that the ankyrin-binding motif of Na(v)1.2 that determines channel concentration at the AIS depends on a glutamate residue (E1111), but also on several serine residues (S1112, S1124, and S1126). We showed that phosphorylation of these residues by protein kinase CK2 (CK2) regulates Na(v) channel interaction with ankyrins. \| inhibition of CK2 activity reduced sodium channel accumulation at the AIS of neurons. In conclusion, CK2 contributes to sodium channel organization by regulating their interaction with ankyrin G.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-275756	Ser1124	LNTEEFSsESDMEES	Homo sapiens	Neuron
pmid	sentence
19064667	We found that the ankyrin-binding motif of Na(v)1.2 that determines channel concentration at the AIS depends on a glutamate residue (E1111), but also on several serine residues (S1112, S1124, and S1126). We showed that phosphorylation of these residues by protein kinase CK2 (CK2) regulates Na(v) channel interaction with ankyrins. \| inhibition of CK2 activity reduced sodium channel accumulation at the AIS of neurons. In conclusion, CK2 contributes to sodium channel organization by regulating their interaction with ankyrin G.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-275760	Ser1126	TEEFSSEsDMEESKE	Homo sapiens	Neuron
pmid	sentence
19064667	We found that the ankyrin-binding motif of Na(v)1.2 that determines channel concentration at the AIS depends on a glutamate residue (E1111), but also on several serine residues (S1112, S1124, and S1126). We showed that phosphorylation of these residues by protein kinase CK2 (CK2) regulates Na(v) channel interaction with ankyrins. \| inhibition of CK2 activity reduced sodium channel accumulation at the AIS of neurons. In conclusion, CK2 contributes to sodium channel organization by regulating their interaction with ankyrin G.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-251055	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-263115	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	Organism	Cell Line
SIGNOR-251068	Ser174	DKENGSVsSSETPPP	Homo sapiens	U2-OS Cell
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.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251069	Ser389	LKEAEEEsSGGEEED	Homo sapiens	U2-OS Cell
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.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251070	Ser390	KEAEEESsGGEEEDE	Homo sapiens	U2-OS Cell
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:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-251062	Ser2	sSSEEVSW	Homo sapiens
pmid	sentence
1939094	Phosphorylation of the beta subunit of casein kinase II in human A431 cells. Identification of the autophosphorylation site \| Cleavage of the beta subunit, that had been autophosphorylated in vitro, at tryptophan 9 and tryptophan 12 using N-chlorosuccinimide demonstrated that the autophosphorylation site is located near the amino terminus of the protein, most likely at serine 2 and serine 3.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251057	Ser203	APAPDEGsDLFYDDY	Homo sapiens	HeLa Cell
pmid	sentence
11546811	CDC34 is specifically phosphorylated in vitro by recombinant CK2 and HeLa nuclear extract at five sites within the carboxyl-terminal 36 amino acids of CDC34. \| 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-251058	Ser222	EVEEEADsCFGDDED	Homo sapiens	HeLa Cell
pmid	sentence
11546811	CDC34 is specifically phosphorylated in vitro by recombinant CK2 and HeLa nuclear extract at five sites within the carboxyl-terminal 36 amino acids of CDC34. \| 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-251059	Ser231	FGDDEDDsGTEES	Homo sapiens	HeLa Cell
pmid	sentence
11546811	CDC34 is specifically phosphorylated in vitro by recombinant CK2 and HeLa nuclear extract at five sites within the carboxyl-terminal 36 amino acids of CDC34. \| 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-251060	Ser236	DDSGTEEs	Homo sapiens
pmid	sentence
12037680	CDC34 is specifically phosphorylated in vitro by recombinant CK2 and HeLa nuclear extract at five sites within the carboxyl-terminal 36 amino acids of CDC34. \| 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-251061	Thr233	DDEDDSGtEES	Homo sapiens	HeLa Cell
pmid	sentence
11546811	CDC34 is specifically phosphorylated in vitro by recombinant CK2 and HeLa nuclear extract at five sites within the carboxyl-terminal 36 amino acids of CDC34. \| 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	Cell Line
SIGNOR-29462	Ser209	QAASNFKsPVKTIR	Homo sapiens	Lymphoma Cell
pmid	sentence
7578274	In cells, the casein kinase ii beta-subunit is phosphorylated at an autophosphorylation site and at a site (ser-209) that is maximally phosphorylated in mitotic cells. These studies provide strong biochemical evidence that p34cdc2 is the enzyme that phosphorylates ser-209 on the beta-subunit of ckii in mitotic cells.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-251071	Ser214	LLSASQLsAEEEEEK	in vitro
pmid	sentence
10327653	Using two-dimensional tryptic phosphopeptide mapping and purified protein kinases, we demonstrate that Hoxb-6 is phosphorylated in vitro by casein kinase II and cAMP-dependent protein kinase. The casein kinase II phosphorylation site was mapped to serine-214.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276424	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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-275744	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-275745	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
SIGNOR-251072	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-251073	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-251074	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-251077	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-251075	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-251076	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	Cell Line
SIGNOR-251065	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-251066	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
SIGNOR-251067	Thr112	EGMQIPStQFDAAHP	Homo sapiens
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:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251079	Ser408	DYTTGGEsCDELEED	Homo sapiens	ECV-304 Cell
pmid	sentence
12804768	Mutagenesis of serine 407 to alanine resulted in reduced ability of the kinase to phosphorylate occludin. The threonine 403 to alanine mutant had a smaller effect but the double mutant (T403/S407A) was even less phosphorylated than either of the single mutants. These data are consistent with the claim that CK2 is the kinase in brain extracts responsible for phosphorylation of occludin.

Identifier	Residue	Sequence	Organism
SIGNOR-251080	Thr404	HYETDYTtGGESCDE	Homo sapiens
pmid	sentence
12804768	Mutagenesis of serine 407 to alanine resulted in reduced ability of the kinase to phosphorylate occludin. The threonine 403 to alanine mutant had a smaller effect but the double mutant (T403/S407A) was even less phosphorylated than either of the single mutants. These data are consistent with the claim that CK2 is the kinase in brain extracts responsible for phosphorylation of occludin.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-265270	Ser574	EEVSDKGsDSEEEET	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-265268	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-265272	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-251063	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-251064	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	Cell Line
SIGNOR-251078	Ser6	sQMDITDI	Homo sapiens	NALM-6 Cell
pmid	sentence
8943850	Taken together, these data indicate that CD10/NEP is itself phosphorylated by CKII and that CD10/NEP co-associates with additional tyrosine phosphoproteins including lyn.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251053	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-251054	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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273636	Ser825	KSGYHDDsDEDLLE	Mus musculus	AML-12 Cell
pmid	sentence
25805502	Phosphorylation of Ser-825 is required for insulin to induce Sort1 in AML12 cells. LC-MS/MS analysis further revealed that serine phosphorylation of Sort1 protein was required for insulin induction of Sort1 in a casein kinase 2-dependent manner and that inhibition of PI3K signaling or prevention of Sort1 phosphorylation accelerated proteasome-dependent Sort1 degradation.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-200806	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-251082	Ser942	EEEDELEsGDQEDED	in vitro
pmid	sentence
10931861	Phosphorylation is mediated by casein kinase II (CKII) or a CKII-like kinase. \| Serine 941 in the Acidic Domain of p115 Is Essential for Reassembly of Golgi Cisternae

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251081	Thr10	DVEDGEEtCALASHS	Homo sapiens	HeLa Cell
pmid	sentence
12748192	In the present study, we show the evidence that CKBBP1 is phosphorylated on threonine residue at position 10 by CKII in vitro and in vivo. Most importantly, disruption of this phosphorylation in CKBBP1 results in accumulation of IκBα and p27Kip1 in HeLa cells and inhibits cell proliferation that appears to be linked to defects in G1/S transition.

Publications:

1

Organism:

Homo Sapiens

Name	CSNK2B View Modifications
Full Name	Casein kinase II subunit beta
Synonyms	CK II beta, Phosvitin, Protein G5a \| CK2N, G5A
Primary ID	P67870
Links	- -
Type	protein
Relations	48
Function	Regulatory subunit of casein kinase II/CK2. As part of the kinase complex regulates the basal catalytic activity of the alpha subunit a constitutively active serine/threonine-protein kinase that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine (PubMed:11239457, PubMed:16818610). Participates in Wnt signaling (By similarity).

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