| + |
CDK6 | up-regulates 
phosphorylation
|
CDKN1B |
0.85 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-140401 |
Ser10 |
NVRVSNGsPSLERMD |
Homo sapiens |
|
| pmid |
sentence |
| 16160006 |
Phosphorylation on ser-10 is the major site of phosphorylation in resting cells, takes place at the g(0)-g1 phase and leads to protein stability.p27(kip1) was phosphorylated by v-cyclin-cdk6 predominantly on ser10, which enhances its cytoplasmic localization. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia |
| + |
CDK6 |
phosphorylation
|
RBL2 |
0.667 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-104711 |
Ser1035 |
NMDAPPLsPYPFVRT |
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 11157749 |
We now identify 22 in vivo phosphorylation sites of p130, targeted by diverse kinases, and present evidence for three cyclin-dependent kinase 4(6) [cdk4(6)] specific phosphorylations, which appear critical for controlling the growth-restraining activity of p130. all three residues selectively targeted by cdk4(6), t401 (n-terminus), s672 (spacer region) and s1035 (c-terminus) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-104715 |
Ser672 |
TLYDRYSsPPASTTR |
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 11157749 |
We now identify 22 in vivo phosphorylation sites of p130, targeted by diverse kinases, and present evidence for three cyclin-dependent kinase 4(6) [cdk4(6)] specific phosphorylations, which appear critical for controlling the growth-restraining activity of p130. all three residues selectively targeted by cdk4(6), t401 (n-terminus), s672 (spacer region) and s1035 (c-terminus) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-104719 |
Thr401 |
SKALRIStPLTGVRY |
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 11157749 |
We now identify 22 in vivo phosphorylation sites of p130, targeted by diverse kinases, and present evidence for three cyclin-dependent kinase 4(6) [cdk4(6)] specific phosphorylations, which appear critical for controlling the growth-restraining activity of p130. all three residues selectively targeted by cdk4(6), t401 (n-terminus), s672 (spacer region) and s1035 (c-terminus) |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
CDK6 | down-regulates activity 
phosphorylation
|
CDKN1A |
0.859 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-144832 |
Ser130 |
SGEQAEGsPGGPGDS |
Homo sapiens |
|
| pmid |
sentence |
| 16508017 |
Here, we show that p21cip1 is associated with k cyclin both in overexpression models and in primary effusion lymphoma cells and is a substrate of the k cyclin/cdk6 complex, resulting in phosphorylation of p21cip1 on serine 130. This phosphoform of p21cip1 appeared unable to associate with cdk2 in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia |
| + |
CDK6 | up-regulates
phosphorylation
|
RUNX1 |
0.598 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-169326 |
Ser21 |
TPPSTALsPGKMSEA |
Homo sapiens |
|
| pmid |
sentence |
| 21059642 |
Phosphorylation of runx1 on ser-303 by cdks leads its ubiquitin-mediated degradation during g2/m (19). We developed additional evidence that cdks phosphorylate ser-303 and found that ser-48 and ser-424 are also substrates of cdk1/cyclin b and cdk6/cyclin d3. Moreover, we demonstrated that phosphorylation of ser-48, ser-303, and ser-424 strengthens the ability of runx1 to activate transcription and to stimulate proliferation of the ba/f3 hematopoietic cell line (20). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138953 |
Ser249 |
DTRQIQPsPPWSYDQ |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 16046550 |
We have identified four phosphorylation sites on aml1c that are necessary for transcriptional activity of aml1c in k562 and 293t cells (27).4 mutation of these four sites (serine 276, serine 293, serine 303, and threonine 300) to alanine abolishes transcriptional activation, whereas mutation of these sites to aspartic acid (which mimics phosphorylation) results in a hyperactive protein. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138957 |
Ser266 |
QYLGSIAsPSVHPAT |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 16046550 |
We have identified four phosphorylation sites on aml1c that are necessary for transcriptional activity of aml1c in k562 and 293t cells (27).4 mutation of these four sites (serine 276, serine 293, serine 303, and threonine 300) to alanine abolishes transcriptional activation, whereas mutation of these sites to aspartic acid (which mimics phosphorylation) results in a hyperactive protein. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-169330 |
Ser397 |
SMVGGERsPPRILPP |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 21059642 |
Phosphorylation of runx1 on ser-303 by cdks leads its ubiquitin-mediated degradation during g2/m (19). We developed additional evidence that cdks phosphorylate ser-303 and found that ser-48 and ser-424 are also substrates of cdk1/cyclin b and cdk6/cyclin d3. Moreover, we demonstrated that phosphorylation of ser-48, ser-303, and ser-424 strengthens the ability of runx1 to activate transcription and to stimulate proliferation of the ba/f3 hematopoietic cell line (20). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138965 |
Thr273 |
SPSVHPAtPISPGRA |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 16046550 |
We have identified four phosphorylation sites on aml1c that are necessary for transcriptional activity of aml1c in k562 and 293t cells (27).4 mutation of these four sites (serine 276, serine 293, serine 303, and threonine 300) to alanine abolishes transcriptional activation, whereas mutation of these sites to aspartic acid (which mimics phosphorylation) results in a hyperactive protein. |
|
| Publications: |
5 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, Onco-fusion proteins in AML |
| + |
CDK6 | up-regulates activity
phosphorylation
|
RUNX1 |
0.598 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-169334 |
Ser276 |
VHPATPIsPGRASGM |
Homo sapiens |
|
| pmid |
sentence |
| 21059642 |
Phosphorylation of runx1 on ser-303 by cdks leads its ubiquitin-mediated degradation during g2/m (19). We developed additional evidence that cdks phosphorylate ser-303 and found that ser-48 and ser-424 are also substrates of cdk1/cyclin b and cdk6/cyclin d3. Moreover, we demonstrated that phosphorylation of ser-48, ser-303, and ser-424 strengthens the ability of runx1 to activate transcription and to stimulate proliferation of the ba/f3 hematopoietic cell line (20). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138961 |
Ser276 |
VHPATPIsPGRASGM |
Homo sapiens |
|
| pmid |
sentence |
| 16046550 |
We have identified four phosphorylation sites on aml1c that are necessary for transcriptional activity of aml1c in k562 and 293t cells (27).4 mutation of these four sites (serine 276, serine 293, serine 303, and threonine 300) to alanine abolishes transcriptional activation, whereas mutation of these sites to aspartic acid (which mimics phosphorylation) results in a hyperactive protein. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, Onco-fusion proteins in AML |
| + |
CDK6 | down-regulates
phosphorylation
|
RB1 |
0.761 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-135189 |
Ser811 |
IYISPLKsPYKISEG |
Homo sapiens |
|
| pmid |
sentence |
| 15809340 |
Phosphorylated by cdk6 and cdk4, and subsequently by cdk2 at ser-567 in g1, thereby releasing e2f1 which is then able to activate cell growth. Here we show that although these cdks phosphorylate multiple residues in prb, they do so with different residue selectivities in vitro;thr821 and thr826 are preferentially phosphorylated by cdk6 and cdk4, respectively. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK6 | down-regulates
phosphorylation
|
CDKN1B |
0.85 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-140405 |
Thr187 |
NAGSVEQtPKKPGLR |
Homo sapiens |
B-lymphocyte, Lymphoma Cell |
| pmid |
sentence |
| 16160006 |
Phosphorylation on thr-187, by cdk2 leads to protein ubiquitination and proteasomal degradationp27(kip1) was phosphorylated by v-cyclin-cdk6 predominantly on ser10, which enhances its cytoplasmic localization. Interestingly, upon reactivation of kshv lytic cycle, v-cyclin-cdk6 phosphorylated p27(kip1) on thr187, which resulted in down-regulation of p27(kip1) protein levels. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia |
| + |
CDK6 | down-regulates
phosphorylation
|
PRDX1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-87113 |
Thr90 |
CHLAWVNtPKKQGGL |
Homo sapiens |
|
| pmid |
sentence |
| 11986303 |
Peroxiredoxin (prx) i is a member of the peroxiredoxin family of peroxidases and contains a consensus site (thr(90)-pro-lys-lys) for phosphorylation by cyclin-dependent kinases (cdks). This protein has now been shown to be phosphorylated specifically on thr(90) by several cdks, including cdc2, in vitro. Phosphorylation of prx i on thr(90) reduced the peroxidase activity of this protein by 80%.Prx i was also phosphorylated, with an efficiency similar to that observed with cdc2, when incubated in vitro with cdk2, cdk4, or cdk6 that had been immunoprecipitated from hela cell lysates with specific antibodies (data not shown). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDC25A | up-regulates activity
dephosphorylation
|
CDK6 |
0.693 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267569 |
Tyr24 |
AEIGEGAyGKVFKAR |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 23429262 |
Invalidation of CDK4 has no impact by itself on the cell proliferation, but invalidation of CDC25A prevents the dephosphorylation of CDK6 (Y24) and CDK4 (Y17) residues, and impedes their association with CCNDs. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK6 | form complex 
binding
|
CyclinD3/CDK6 |
0.933 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273028 |
|
|
|
|
| pmid |
sentence |
| 8114739 |
Here, we show that the human PLSTIRE gene product is a novel cyclin-dependent kinase, cdk6. The cdk6 kinase is associated with cyclins D1, D2, and D3 in lysates of human cells and is activated by coexpression with D-type cyclins in Sf9 insect cells. |
|
| Publications: |
1 |
| + |
CDKN2A | down-regulates
binding
|
CDK6 |
0.866 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-44557 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8891723 |
The first group, including p16ink4a, p15ink4b,p18ink4cand p19ink4d, is specific for the g1 cdks,cdk4and cdk6, inhibiting the kinase activity of cyclin d/cdk4-cdk6 complexes on prb. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-140412 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16161044 |
In addition, cytoplasmic p16 bound cyclin dependent kinase (cdk)4/6, potentially indicating that p16 could have a function in the cytoplasm. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, Onco-fusion proteins in AML |
| + |
palbociclib | down-regulates
chemical inhibition
|
CDK6 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-205707 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NUP98 Fusion | up-regulates quantity by expression 
transcriptional regulation
|
CDK6 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261505 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32344427 |
NUP98-fusion proteins directly regulate leukemia-associated gene expression programs in AML. CDK6 expression is under direct transcriptional control of NUP98-fusions and NUP98-fusion AML is particularly sensitive to CDK6 inhibition. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, Onco-fusion proteins in AML |
| + |
CDKN2C | down-regulates
binding
|
CDK6 |
0.875 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-44601 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8891723 |
The first group, including p16ink4a, p15ink4b,p18ink4cand p19ink4d, is specific for the g1 cdks,cdk4and cdk6, inhibiting the kinase activity of cyclin d/cdk4-cdk6 complexes on prb. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDKN1A | down-regulates
binding
|
CDK6 |
0.859 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-30030 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 7626805 |
P21cip1 is a cyclin-dependent kinase (cdk) inhibitor that is transcriptionally activated by p53 in response to dna damage.We Have explored the interaction of p21 with the currently known cdks. p21 effectively inhibits cdk2, cdk3, cdk4, and cdk6 kinases |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia |
| + |
4-(2,6-dichlorobenzamido)-N-(piperidin-4-yl)-pyrazole-3-carboxamide | down-regulates
chemical inhibition
|
CDK6 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-189996 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK6 | form complex
binding
|
CyclinD1/CDK6 |
0.95 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250681 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8114739 |
Here, we show that the human PLSTIRE gene product is a novel cyclin-dependent kinase, cdk6. The cdk6 kinase is associated with cyclins D1, D2, and D3 in lysates of human cells and is activated by coexpression with D-type cyclins in Sf9 insect cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MYC | up-regulates quantity by expression
transcriptional regulation
|
CDK6 |
0.466 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-102737 |
|
|
Homo sapiens |
Leukemia Cell |
| pmid |
sentence |
| 12835716 |
The degradation of c-myc protein decreases the expression of the cell cycle regulators cdk4 and cdk6, which reversibly slows down the cell cycle. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia |
| + |
alvocidib | down-regulates
chemical inhibition
|
CDK6 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-192385 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
alvocidib hydrochloride | down-regulates
chemical inhibition
|
CDK6 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-192470 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SAAL1 | up-regulates quantity by expression
post transcriptional regulation
|
CDK6 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260386 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30513680 |
This study was performed to elucidate the molecular function of the synoviocyte proliferation-associated in collagen-induced arthritis (CIA) 1/serum amyloid A-like 1 (SPACIA1/SAAL1) in mice CIA, an animal model of rheumatoid arthritis (RA), and human RA-synovial fibroblasts (RASFs). Expression levels of cdk6, but not cdk4, which are D-type cyclin partners, were downregulated by SPACIA1/SAAL1 siRNA at the post-transcriptional level. The CDK6, expression of which is up-regulated by the SPACIA1/SAAL1 expression, might be a critical factor in the exacerbation of CIA. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
CDK6
- 
- 