| Type |
Details |
Score |
| UniProt Feature |
| Begin: |
186 |
| Description: |
Phosphothreonine; by CDK1 |
| Type: |
modified residue |
| End: |
186 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
764 |
| Description: |
Phosphoserine; by CDK1 |
| Type: |
modified residue |
| End: |
764 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
246 |
| Description: |
Phosphoserine; by CDK1 |
| Type: |
modified residue |
| End: |
246 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
275 |
| Description: |
Phosphothreonine; by CDK1 |
| Type: |
modified residue |
| End: |
275 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
2085 |
| Description: |
Phosphothreonine; by CDK1 |
| Type: |
modified residue |
| End: |
2085 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
1997 |
| Description: |
Phosphothreonine; by CDK1 |
| Type: |
modified residue |
| End: |
1997 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
2069 |
| Description: |
Phosphoserine; by CDK1 |
| Type: |
modified residue |
| End: |
2069 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
2516 |
| Description: |
Phosphothreonine; by CDK1 |
| Type: |
modified residue |
| End: |
2516 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
537 |
| Description: |
Phosphoserine; by CDK1 |
| Type: |
modified residue |
| End: |
537 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
470 |
| Description: |
Phosphothreonine; by CDK1 |
| Type: |
modified residue |
| End: |
470 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
728 |
| Description: |
Phosphoserine; by CDK1 |
| Type: |
modified residue |
| End: |
728 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
608 |
| Description: |
Phosphothreonine; by CDK1 |
| Type: |
modified residue |
| End: |
608 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
172 |
| Description: |
Phosphoserine; by CDK1 |
| Type: |
modified residue |
| End: |
172 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
172 |
| Description: |
Phosphoserine; by CDK1 |
| Type: |
modified residue |
| End: |
172 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
382 |
| Description: |
Phosphoserine; by CDK1 |
| Type: |
modified residue |
| End: |
382 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
29 |
| Description: |
Phosphoserine; by CDK1 |
| Type: |
modified residue |
| End: |
29 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
1380 |
| Description: |
Phosphothreonine; by CDK1 |
| Type: |
modified residue |
| End: |
1380 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
1375 |
| Description: |
Phosphothreonine; by CDK1 |
| Type: |
modified residue |
| End: |
1375 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
172 |
| Description: |
Phosphoserine; by CDK1 |
| Type: |
modified residue |
| End: |
172 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
172 |
| Description: |
Phosphoserine; by CDK1 |
| Type: |
modified residue |
| End: |
172 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
172 |
| Description: |
Phosphoserine; by CDK1 |
| Type: |
modified residue |
| End: |
172 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
278 |
| Description: |
Phosphothreonine; by CDK1 |
| Type: |
modified residue |
| End: |
278 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
274 |
| Description: |
Phosphoserine; by CDK1 |
| Type: |
modified residue |
| End: |
274 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
71 |
| Description: |
Phosphoserine; by CDK1 |
| Type: |
modified residue |
| End: |
71 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
62 |
| Description: |
Phosphothreonine; by CDK1 |
| Type: |
modified residue |
| End: |
62 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
172 |
| Description: |
Phosphoserine; by CDK1 |
| Type: |
modified residue |
| End: |
172 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
261 |
| Description: |
Phosphoserine; by CDK1 |
| Type: |
modified residue |
| End: |
261 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
257 |
| Description: |
Phosphoserine; by CDK1 |
| Type: |
modified residue |
| End: |
257 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
265 |
| Description: |
Phosphoserine; by CDK1 |
| Type: |
modified residue |
| End: |
265 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
639 |
| Description: |
Phosphoserine; by CDK1 |
| Type: |
modified residue |
| End: |
639 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
123 |
| Description: |
Phosphoserine; by CDK1 |
| Type: |
modified residue |
| End: |
123 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
172 |
| Description: |
Phosphoserine; by CDK1 |
| Type: |
modified residue |
| End: |
172 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
172 |
| Description: |
Phosphoserine; by CDK1 |
| Type: |
modified residue |
| End: |
172 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
265 |
| Description: |
Phosphoserine; by CDK1 |
| Type: |
modified residue |
| End: |
265 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
4546 |
| Description: |
Phosphothreonine; by CDK1 |
| Type: |
modified residue |
| End: |
4546 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
33 |
| Description: |
Phosphoserine; by CDK1 |
| Type: |
modified residue |
| End: |
33 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
84 |
| Description: |
Phosphoserine; by CDK1 |
| Type: |
modified residue |
| End: |
84 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
473 |
| Description: |
Phosphoserine; by CDK1 |
| Type: |
modified residue |
| End: |
473 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
242 |
| Description: |
Phosphoserine; by CDK1 |
| Type: |
modified residue |
| End: |
242 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Nishiyama T |
| Year: |
2013 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
Aurora B and Cdk1 mediate Wapl activation and release of acetylated cohesin from chromosomes by phosphorylating Sororin. |
| Volume: |
110 |
| Issue: |
33 |
| Pages: |
13404-9 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
3214 |
| Description: |
Phosphoserine; by CDK1 and CDK2 |
| Type: |
modified residue |
| End: |
3214 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
34 |
| Description: |
Phosphothreonine; by CDK1 and CDK15 |
| Type: |
modified residue |
| End: |
34 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
164 |
| Description: |
Phosphoserine; by CDK1 and CDK2 |
| Type: |
modified residue |
| End: |
164 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
291 |
| Description: |
Phosphoserine; by CDK1 and PKB |
| Type: |
modified residue |
| End: |
291 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
345 |
| Description: |
Phosphothreonine; by CDK1 and CDK2 |
| Type: |
modified residue |
| End: |
345 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
90 |
| Description: |
Phosphoserine; by CDK1 and CDK9 |
| Type: |
modified residue |
| End: |
90 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
198 |
| Description: |
Phosphothreonine; by CDK1 and CDK2 |
| Type: |
modified residue |
| End: |
198 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
463 |
| Description: |
Phosphothreonine; by CDK1 and CDK2 |
| Type: |
modified residue |
| End: |
463 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
358 |
| Description: |
Phosphoserine; by MAPK13 and CDK1 |
| Type: |
modified residue |
| End: |
358 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
528 |
| Description: |
Phosphoserine; by CDK1 and CDK2 |
| Type: |
modified residue |
| End: |
528 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
245 |
| Description: |
Phosphothreonine; by CDK1 and MAPK1 |
| Type: |
modified residue |
| End: |
245 |
|
•
•
•
•
•
|
| Interaction Experiment |
| Description: |
Filamin a regulates neural progenitor proliferation and cortical size through Wee1-dependent Cdk1 phosphorylation. |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
187 |
| Description: |
Phosphothreonine; by PKB/AKT1, CDK1 and CDK2 |
| Type: |
modified residue |
| End: |
187 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
312 |
| Description: |
Phosphoserine; by AURKA, CDK1 and CDK2 |
| Type: |
modified residue |
| End: |
312 |
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
645 |
| Description: |
Phosphoserine; by CDK5, MAPK1 and CDK1 |
| Type: |
modified residue |
| End: |
645 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Zhong L |
| Year: |
2020 |
| Journal: |
Cell Discov |
| Title: |
Phosphorylation of cGAS by CDK1 impairs self-DNA sensing in mitosis. |
| Volume: |
6 |
|
| Pages: |
26 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Peng Y |
| Year: |
2008 |
| Journal: |
Dev Cell |
| Title: |
The cyclin-dependent kinase Cdk1 directly regulates vacuole inheritance. |
| Volume: |
15 |
| Issue: |
3 |
| Pages: |
478-85 |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
297
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Satyanarayana A |
| Year: |
2008 |
| Journal: |
Mol Biol Cell |
| Title: |
p21 Inhibits Cdk1 in the absence of Cdk2 to maintain the G1/S phase DNA damage checkpoint. |
| Volume: |
19 |
| Issue: |
1 |
| Pages: |
65-77 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Seldin L |
| Year: |
2013 |
| Journal: |
Mol Biol Cell |
| Title: |
NuMA localization, stability, and function in spindle orientation involve 4.1 and Cdk1 interactions. |
| Volume: |
24 |
| Issue: |
23 |
| Pages: |
3651-62 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Chou HY |
| Year: |
2011 |
| Journal: |
Cell Cycle |
| Title: |
Phosphorylation of NuSAP by Cdk1 regulates its interaction with microtubules in mitosis. |
| Volume: |
10 |
| Issue: |
23 |
| Pages: |
4083-9 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Althoff F |
| Year: |
2009 |
| Journal: |
Dev Biol |
| Title: |
Drosophila Cyclin J is a mitotically stable Cdk1 partner without essential functions. |
| Volume: |
333 |
| Issue: |
2 |
| Pages: |
263-72 |
|
•
•
•
•
•
|
| HT Experiment |
|
| Experiment Type: |
RNA-Seq |
| Study Type: |
WT vs. Mutant |
| Source: |
GEO |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Löffler H |
| Year: |
2011 |
| Journal: |
Cancer Res |
| Title: |
Cep63 recruits Cdk1 to the centrosome: implications for regulation of mitotic entry, centrosome amplification, and genome maintenance. |
| Volume: |
71 |
| Issue: |
6 |
| Pages: |
2129-39 |
|
•
•
•
•
•
|
| Allele |
| Name: |
eukaryotic translation initiation factor 4E binding protein 1; targeted mutation 2.1, Patrick Moore |
| Allele Type: |
Targeted |
|
|
•
•
•
•
•
|
| Strain |
| Attribute String: |
coisogenic, endonuclease-mediated mutation, mutant strain |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
234
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
233
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Grundt K |
| Year: |
2004 |
| Journal: |
Biochem Biophys Res Commun |
| Title: |
Characterisation of the NUCKS gene on human chromosome 1q32.1 and the presence of a homologous gene in different species. |
| Volume: |
323 |
| Issue: |
3 |
| Pages: |
796-801 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Members of this vertebrate family of proteins are targets for phosphorylation by CDK1 and casein kinase [, ]. They are also phosphorylated upon DNA damage, probably by ATM or ATR []. |
|
•
•
•
•
•
|
| Publication |
| First Author: |
He Y |
| Year: |
2015 |
| Journal: |
Biomed Pharmacother |
| Title: |
The tumor-suppressor gene LZTS1 suppresses hepatocellular carcinoma proliferation by impairing PI3K/Akt pathway. |
| Volume: |
76 |
|
| Pages: |
141-6 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Wang XX |
| Year: |
2015 |
| Journal: |
Pathol Oncol Res |
| Title: |
Loss of Leucine Zipper Putative Tumor Suppressor 1 (LZTS1) Expression Contributes to Lymph Node Metastasis of Breast Invasive Micropapillary Carcinoma. |
| Volume: |
21 |
| Issue: |
4 |
| Pages: |
1021-6 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Xu Z |
| Year: |
2014 |
| Journal: |
Biochem Biophys Res Commun |
| Title: |
miR-214 promotes the proliferation and invasion of osteosarcoma cells through direct suppression of LZTS1. |
| Volume: |
449 |
| Issue: |
2 |
| Pages: |
190-5 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Leucine zipper putative tumor suppressor 1 (LZTS1, FEZ1) plays a role in mitosis []. It is associated with assembled microtubules and is involved in the stabilization of active p34CDC2 (Cdk1) []. LZTS1 plays an important role in ensuring proper Cdk1 activity during M phase. By maintaining high levels of Cdk1 activity, it prevents chromosomes missegregation []. LZTS1 plays an important role in human carcinogenesis [, , ]. |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Shimada M |
| Year: |
2008 |
| Journal: |
Cell |
| Title: |
Chk1 is a histone H3 threonine 11 kinase that regulates DNA damage-induced transcriptional repression. |
| Volume: |
132 |
| Issue: |
2 |
| Pages: |
221-32 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Hu J |
| Year: |
2014 |
| Journal: |
Hum Mol Genet |
| Title: |
Formin 1 and filamin B physically interact to coordinate chondrocyte proliferation and differentiation in the growth plate. |
| Volume: |
23 |
| Issue: |
17 |
| Pages: |
4663-73 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Filamin family consists of Filamin-A (FLN-A), Filamin-B (FLN-B) and Filamin-C (FLN-C). They are a group of actin binding proteins that may be involved in actin microfilaments organisation [].This entry represents filamin B, which transduces signals from various membrane receptors and intracellular proteins onto the actin cytoskeleton []. In humans it regulates chondrocyte proliferation and differentiation through Cdk1 signalling []. |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Porter LA |
| Year: |
2003 |
| Journal: |
Mol Biol Cell |
| Title: |
Spy1 interacts with p27Kip1 to allow G1/S progression. |
| Volume: |
14 |
| Issue: |
9 |
| Pages: |
3664-74 |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
310
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
268
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
173
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
236
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
172
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
115
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
309
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
173
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
231
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
339
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
283
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Publication |
| First Author: |
McAndrew CW |
| Year: |
2007 |
| Journal: |
Cell Cycle |
| Title: |
Spy1 enhances phosphorylation and degradation of the cell cycle inhibitor p27. |
| Volume: |
6 |
| Issue: |
15 |
| Pages: |
1937-45 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
McGrath DA |
| Year: |
2017 |
| Journal: |
EMBO J |
| Title: |
Structural basis of divergent cyclin-dependent kinase activation by Spy1/RINGO proteins. |
| Volume: |
36 |
| Issue: |
15 |
| Pages: |
2251-2262 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Byeon IJ |
| Year: |
2005 |
| Journal: |
Nat Struct Mol Biol |
| Title: |
Sequential phosphorylation and multisite interactions characterize specific target recognition by the FHA domain of Ki67. |
| Volume: |
12 |
| Issue: |
11 |
| Pages: |
987-93 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Speedy (Spy1, also known as RINGO A) is a cell cycle regulatory protein which binds and activates CDK1 and CDK2 [], protein kinases that allows progression through G1/S phase and further replication events. Spy1 activates CDK2 inducing a conformational change of the CDK2 T-loop that avoids its phosphorylation []. Spy1 expression overcomes a p27-induced cell cycle arrest to allow for DNA synthesis, so cell cycle progression occurs due to an interaction between Spy1 and p27 []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
This entry represents eukaryotic proteins that contain a domain of approximately 40 amino acids in length. These proteins are found in association with . There are two conserved sequence motifs: TPVCTP and LERRKS. This domain is found on the human nucleolar protein hNIFK. It binds to the fork-head-associated domain of human Ki67. High-affinity binding requires sequential phosphorylation by two kinases, CDK1 and GSK3, yielding pThr238, pThr234 and pSer230. This interaction is involved in cell cycle regulation []. |
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| HT Experiment |
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| Experiment Type: |
RNA-Seq |
| Study Type: |
WT vs. Mutant |
| Source: |
GEO |
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| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
599
 |
| Fragment?: |
false |
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| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
598
 |
| Fragment?: |
true |
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| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
599
 |
| Fragment?: |
false |
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| Publication |
| First Author: |
Ishii H |
| Year: |
2001 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
FEZ1/LZTS1 gene at 8p22 suppresses cancer cell growth and regulates mitosis. |
| Volume: |
98 |
| Issue: |
18 |
| Pages: |
10374-9 |
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| Publication |
| First Author: |
Vecchione A |
| Year: |
2007 |
| Journal: |
Cell Div |
| Title: |
Fez1/Lzts1 a new mitotic regulator implicated in cancer development. |
| Volume: |
2 |
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| Pages: |
24 |
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