Type |
Details |
Score |
Publication |
First Author: |
Ye X |
Year: |
2003 |
Journal: |
Mol Cell Biol |
Title: |
The cyclin E/Cdk2 substrate p220(NPAT) is required for S-phase entry, histone gene expression, and Cajal body maintenance in human somatic cells. |
Volume: |
23 |
Issue: |
23 |
Pages: |
8586-600 |
|
•
•
•
•
•
|
Publication |
First Author: |
Chang KH |
Year: |
2012 |
Journal: |
J Cell Sci |
Title: |
Deregulated Cdk5 triggers aberrant activation of cell cycle kinases and phosphatases inducing neuronal death. |
Volume: |
125 |
Issue: |
Pt 21 |
Pages: |
5124-37 |
|
•
•
•
•
•
|
Publication |
First Author: |
Heijink AM |
Year: |
2015 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
A haploid genetic screen identifies the G1/S regulatory machinery as a determinant of Wee1 inhibitor sensitivity. |
Volume: |
112 |
Issue: |
49 |
Pages: |
15160-5 |
|
•
•
•
•
•
|
Publication |
First Author: |
Liu K |
Year: |
2017 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
Mutant p53 perturbs DNA replication checkpoint control through TopBP1 and Treslin. |
Volume: |
114 |
Issue: |
19 |
Pages: |
E3766-E3775 |
|
•
•
•
•
•
|
Publication |
First Author: |
Principe DR |
Year: |
2017 |
Journal: |
Oncogene |
Title: |
TGFβ engages MEK/ERK to differentially regulate benign and malignant pancreas cell function. |
Volume: |
36 |
Issue: |
30 |
Pages: |
4336-4348 |
|
•
•
•
•
•
|
Publication |
First Author: |
Su M |
Year: |
2015 |
Journal: |
Cell Death Differ |
Title: |
MicroRNA-221 inhibits autophagy and promotes heart failure by modulating the p27/CDK2/mTOR axis. |
Volume: |
22 |
Issue: |
6 |
Pages: |
986-99 |
|
•
•
•
•
•
|
Publication |
First Author: |
Caruso JA |
Year: |
2018 |
Journal: |
Cancer Res |
Title: |
Low-Molecular-Weight Cyclin E in Human Cancer: Cellular Consequences and Opportunities for Targeted Therapies. |
Volume: |
78 |
Issue: |
19 |
Pages: |
5481-5491 |
|
•
•
•
•
•
|
Publication |
First Author: |
Mukai S |
Year: |
2015 |
Journal: |
Sci Rep |
Title: |
Lats1 suppresses centrosome overduplication by modulating the stability of Cdc25B. |
Volume: |
5 |
|
Pages: |
16173 |
|
•
•
•
•
•
|
Publication |
First Author: |
Mahapatra K |
Year: |
2020 |
Journal: |
Biochim Biophys Acta Gen Subj |
Title: |
Assessment of cytotoxic and genotoxic potentials of a mononuclear Fe(II) Schiff base complex with photocatalytic activity in Trigonella. |
Volume: |
1864 |
Issue: |
3 |
Pages: |
129503 |
|
•
•
•
•
•
|
Publication |
First Author: |
Choi JY |
Year: |
2018 |
Journal: |
Lab Anim Res |
Title: |
Successful development of squamous cell carcinoma and hyperplasia in RGEN-mediated p27 KO mice after the treatment of DMBA and TPA. |
Volume: |
34 |
Issue: |
3 |
Pages: |
118-125 |
|
•
•
•
•
•
|
Publication |
First Author: |
Xia P |
Year: |
2020 |
Journal: |
J Biol Chem |
Title: |
Doxorubicin induces cardiomyocyte apoptosis and atrophy through cyclin-dependent kinase 2-mediated activation of forkhead box O1. |
Volume: |
295 |
Issue: |
13 |
Pages: |
4265-4276 |
|
•
•
•
•
•
|
Publication |
First Author: |
Li Q |
Year: |
2018 |
Journal: |
J Mol Histol |
Title: |
Methylation of Cdkn1c may be involved in the regulation of tooth development through cell cycle inhibition. |
Volume: |
49 |
Issue: |
5 |
Pages: |
459-469 |
|
•
•
•
•
•
|
Publication |
First Author: |
Yamamori T |
Year: |
2015 |
Journal: |
Mol Biol Cell |
Title: |
Inhibition of the mitochondrial fission protein dynamin-related protein 1 (Drp1) impairs mitochondrial fission and mitotic catastrophe after x-irradiation. |
Volume: |
26 |
Issue: |
25 |
Pages: |
4607-17 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
408
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
352
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
404
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
DeLeo AB |
Year: |
1979 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
Detection of a transformation-related antigen in chemically induced sarcomas and other transformed cells of the mouse. |
Volume: |
76 |
Issue: |
5 |
Pages: |
2420-4 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
407
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
350
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
35
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
324
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
170
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
408
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
300
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
114
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
403
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
407
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
403
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
165
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
404
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
352
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
408
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Zilfou JT |
Year: |
2009 |
Journal: |
Cold Spring Harb Perspect Biol |
Title: |
Tumor suppressive functions of p53. |
Volume: |
1 |
Issue: |
5 |
Pages: |
a001883 |
|
•
•
•
•
•
|
Publication |
First Author: |
Smith ND |
Year: |
2003 |
Journal: |
J Urol |
Title: |
The p53 tumor suppressor gene and nuclear protein: basic science review and relevance in the management of bladder cancer. |
Volume: |
169 |
Issue: |
4 |
Pages: |
1219-28 |
|
•
•
•
•
•
|
Publication |
First Author: |
Oren M |
Year: |
1992 |
Journal: |
FASEB J |
Title: |
p53: the ultimate tumor suppressor gene? |
Volume: |
6 |
Issue: |
13 |
Pages: |
3169-76 |
|
•
•
•
•
•
|
Publication |
First Author: |
Crawford LV |
Year: |
1984 |
Journal: |
Mol Biol Med |
Title: |
The cellular protein p53 in human tumours. |
Volume: |
2 |
Issue: |
4 |
Pages: |
261-72 |
|
•
•
•
•
•
|
Publication |
First Author: |
Belyi VA |
Year: |
2009 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
One billion years of p53/p63/p73 evolution. |
Volume: |
106 |
Issue: |
42 |
Pages: |
17609-10 |
|
•
•
•
•
•
|
Publication |
First Author: |
Levine AJ |
Year: |
2009 |
Journal: |
Nat Rev Cancer |
Title: |
The first 30 years of p53: growing ever more complex. |
Volume: |
9 |
Issue: |
10 |
Pages: |
749-58 |
|
•
•
•
•
•
|
Publication |
First Author: |
Reich NC |
Year: |
1982 |
Journal: |
Virology |
Title: |
Specific interaction of the SV40 T antigen-cellular p53 protein complex with SV40 DNA. |
Volume: |
117 |
Issue: |
1 |
Pages: |
286-90 |
|
•
•
•
•
•
|
Publication |
First Author: |
Thomas R |
Year: |
1983 |
Journal: |
Virology |
Title: |
Characterization of human p53 antigens employing primate specific monoclonal antibodies. |
Volume: |
131 |
Issue: |
2 |
Pages: |
502-17 |
|
•
•
•
•
•
|
Publication |
First Author: |
Brandt T |
Year: |
2009 |
Journal: |
BMC Genomics |
Title: |
Conservation of DNA-binding specificity and oligomerisation properties within the p53 family. |
Volume: |
10 |
|
Pages: |
628 |
|
•
•
•
•
•
|
Publication |
First Author: |
Jiang M |
Year: |
2009 |
Journal: |
FEBS Lett |
Title: |
Cyclin Y, a novel membrane-associated cyclin, interacts with PFTK1. |
Volume: |
583 |
Issue: |
13 |
Pages: |
2171-8 |
|
•
•
•
•
•
|
Publication |
First Author: |
Davidson G |
Year: |
2009 |
Journal: |
Dev Cell |
Title: |
Cell cycle control of wnt receptor activation. |
Volume: |
17 |
Issue: |
6 |
Pages: |
788-99 |
|
•
•
•
•
•
|
Publication |
First Author: |
Kaffman A |
Year: |
1994 |
Journal: |
Science |
Title: |
Phosphorylation of the transcription factor PHO4 by a cyclin-CDK complex, PHO80-PHO85. |
Volume: |
263 |
Issue: |
5150 |
Pages: |
1153-6 |
|
•
•
•
•
•
|
Publication |
First Author: |
Levine K |
Year: |
1995 |
Journal: |
Prog Cell Cycle Res |
Title: |
The CLN gene family: central regulators of cell cycle Start in budding yeast. |
Volume: |
1 |
|
Pages: |
101-14 |
|
•
•
•
•
•
|
Publication |
First Author: |
Bhaduri S |
Year: |
2015 |
Journal: |
Curr Biol |
Title: |
A docking interface in the cyclin Cln2 promotes multi-site phosphorylation of substrates and timely cell-cycle entry. |
Volume: |
25 |
Issue: |
3 |
Pages: |
316-25 |
|
•
•
•
•
•
|
Publication |
First Author: |
Jeffrey PD |
Year: |
2000 |
Journal: |
Genes Dev |
Title: |
Structural basis of inhibition of CDK-cyclin complexes by INK4 inhibitors. |
Volume: |
14 |
Issue: |
24 |
Pages: |
3115-25 |
|
•
•
•
•
•
|
Publication |
First Author: |
Schulze-Gahmen U |
Year: |
1999 |
Journal: |
Structure |
Title: |
Crystal structure of a viral cyclin, a positive regulator of cyclin-dependent kinase 6. |
Volume: |
7 |
Issue: |
3 |
Pages: |
245-54 |
|
•
•
•
•
•
|
Publication |
First Author: |
Ko LJ |
Year: |
1997 |
Journal: |
Mol Cell Biol |
Title: |
p53 is phosphorylated by CDK7-cyclin H in a p36MAT1-dependent manner. |
Volume: |
17 |
Issue: |
12 |
Pages: |
7220-9 |
|
•
•
•
•
•
|
Publication |
First Author: |
Schneider E |
Year: |
1998 |
Journal: |
Oncogene |
Title: |
Regulation of CAK kinase activity by p53. |
Volume: |
17 |
Issue: |
21 |
Pages: |
2733-41 |
|
•
•
•
•
•
|
Publication |
First Author: |
Larochelle S |
Year: |
2006 |
Journal: |
Nat Struct Mol Biol |
Title: |
Dichotomous but stringent substrate selection by the dual-function Cdk7 complex revealed by chemical genetics. |
Volume: |
13 |
Issue: |
1 |
Pages: |
55-62 |
|
•
•
•
•
•
|
Publication |
First Author: |
Deshmukh AS |
Year: |
2016 |
Journal: |
Sci Rep |
Title: |
Cdk7 mediates RPB1-driven mRNA synthesis in Toxoplasma gondii. |
Volume: |
6 |
|
Pages: |
35288 |
|
•
•
•
•
•
|
Publication |
First Author: |
Devos M |
Year: |
2015 |
Journal: |
Mol Cell Biol |
Title: |
Fission yeast Cdk7 controls gene expression through both its CAK and C-terminal domain kinase activities. |
Volume: |
35 |
Issue: |
9 |
Pages: |
1480-90 |
|
•
•
•
•
•
|
Publication |
First Author: |
Kaldis P |
Year: |
1996 |
Journal: |
Cell |
Title: |
The Cdk-activating kinase (CAK) from budding yeast. |
Volume: |
86 |
Issue: |
4 |
Pages: |
553-64 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
Cyclins are eukaryotic proteins that play an active role in controlling nuclear cell division cycles [], and regulate cyclin dependent kinases (CDKs). Cyclins, together with the p34 (cdc2) or cdk2 kinases, form the Maturation Promoting Factor (MPF). There are two main groups of cyclins, G1/S cyclins, which are essential for the control of the cell cycle at the G1/S (start) transition, and G2/M cyclins, which are essential for the control of the cell cycle at the G2/M (mitosis) transition. G2/M cyclins accumulate steadily during G2 and are abruptly destroyed as cells exit from mitosis (at the end of the M-phase). In most species, there are multiple forms of G1 and G2 cyclins. For example, in vertebrates, there are two G2 cyclins, A and B, and at least three G1 cyclins, C, D, and E.Cyclin homologues have been found in various viruses, including Saimiriine herpesvirus 2 (Herpesvirus saimiri) and Human herpesvirus 8 (HHV-8) (Kaposi's sarcoma-associated herpesvirus). These viral homologues differ from their cellular counterparts in that the viral proteins have gained new functions and eliminated others to harness the cell and benefit the virus [].Cyclins contain two domains of similar all-α fold, of which this entry is associated with the N-terminal domain. |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
Cyclins are eukaryotic proteins that play an active role in controlling nuclear cell division cycles [], and regulate cyclin dependent kinases (CDKs). Cyclins, together with the p34 (cdc2) or cdk2 kinases, form the Maturation Promoting Factor (MPF). There are two main groups of cyclins, G1/S cyclins, which are essential for the control of the cell cycle at the G1/S (start) transition, and G2/M cyclins, which are essential for the control of the cell cycle at the G2/M (mitosis) transition. G2/M cyclins accumulate steadily during G2 and are abruptly destroyed as cells exit from mitosis (at the end of the M-phase). In most species, there are multiple forms of G1 and G2 cyclins. For example, in vertebrates, there are two G2 cyclins, A and B, and at least three G1 cyclins, C, D, and E.Cyclin homologues have been found in various viruses, including Saimiriine herpesvirus 2 (Herpesvirus saimiri) and Human herpesvirus 8 (HHV-8) (Kaposi's sarcoma-associated herpesvirus). These viral homologues differ from their cellular counterparts in that the viral proteins have gained new functions and eliminated others to harness the cell and benefit the virus [].This is the C-terminal domain of cyclins. |
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•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
This entry represents a G1-class of cyclins which has so far only been identified in fungi [, ]. These proteins are important for the control of the cell cycle at the G1/S transition and interact with the cdc2 protein kinase.Cyclins are eukaryotic proteins that play an active role in controlling nuclear cell division cycles [], and regulate cyclin dependent kinases (CDKs). Cyclins, together with the p34 (cdc2) or cdk2 kinases, form the Maturation Promoting Factor (MPF). There are two main groups of cyclins, G1/S cyclins, which are essential for the control of the cell cycle at the G1/S (start) transition, and G2/M cyclins, which are essential for the control of the cell cycle at the G2/M (mitosis) transition. G2/M cyclins accumulate steadily during G2 and are abruptly destroyed as cells exit from mitosis (at the end of the M-phase). In most species, there are multiple forms of G1 and G2 cyclins. For example, in vertebrates, there are two G2 cyclins, A and B, and at least three G1 cyclins, C, D, and E.Cyclin homologues have been found in various viruses, including Saimiriine herpesvirus 2 (Herpesvirus saimiri) and Human herpesvirus 8 (HHV-8) (Kaposi's sarcoma-associated herpesvirus). These viral homologues differ from their cellular counterparts in that the viral proteins have gained new functions and eliminated others to harness the cell and benefit the virus []. |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
Cyclins are eukaryotic proteins that play an active role in controlling nuclear cell division cycles [], and regulate cyclin dependent kinases (CDKs). Cyclins, together with the p34 (cdc2) or cdk2 kinases, form the Maturation Promoting Factor (MPF). There are two main groups of cyclins, G1/S cyclins, which are essential for the control of the cell cycle at the G1/S (start) transition, and G2/M cyclins, which are essential for the control of the cell cycle at the G2/M (mitosis) transition. G2/M cyclins accumulate steadily during G2 and are abruptly destroyed as cells exit from mitosis (at the end of the M-phase). In most species, there are multiple forms of G1 and G2 cyclins. For example, in vertebrates, there are two G2 cyclins, A and B, and at least three G1 cyclins, C, D, and E.Cyclin homologues have been found in various viruses, including Saimiriine herpesvirus 2 (Herpesvirus saimiri) and Human herpesvirus 8 (HHV-8) (Kaposi's sarcoma-associated herpesvirus). These viral homologues differ from their cellular counterparts in that the viral proteins have gained new functions and eliminated others to harness the cell and benefit the virus []. |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
Cyclins are eukaryotic proteins that play an active role in controlling nuclear cell division cycles [], and regulate cyclin dependent kinases (CDKs). Cyclins, together with the p34 (cdc2) or cdk2 kinases, form the Maturation Promoting Factor (MPF). There are two main groups of cyclins, G1/S cyclins, which are essential for the control of the cell cycle at the G1/S (start) transition, and G2/M cyclins, which are essential for the control of the cell cycle at the G2/M (mitosis) transition. G2/M cyclins accumulate steadily during G2 and are abruptly destroyed as cells exit from mitosis (at the end of the M-phase). In most species, there are multiple forms of G1 and G2 cyclins. For example, in vertebrates, there are two G2 cyclins, A and B, and at least three G1 cyclins, C, D, and E.Cyclin homologues have been found in various viruses, includingSaimiriine herpesvirus 2 (Herpesvirus saimiri) and Human herpesvirus 8 (HHV-8) (Kaposi's sarcoma-associated herpesvirus). These viral homologues differ from their cellular counterparts in that the viral proteins have gained new functions and eliminated others to harness the cell and benefit the virus [].This entry includes cyclin PHO80 and other cyclins that partner with the cyclin-dependent kinase (CDK) PHO85. The PHO80/PHO85 cyclin-cdk complex is used for a regulatory process other than cell-cycle control []. This entry also includes other PHO80-like cyclins that are involved in the cell-cycle control. They belong to the P/U family and interact preferentially with CDKA1 []. |
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•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
Cyclins are eukaryotic proteins that play an active role in controlling nuclear cell division cycles [], and regulate cyclin dependent kinases (CDKs). Cyclins, together with the p34 (cdc2) or cdk2 kinases, form the Maturation Promoting Factor (MPF). There are two main groups of cyclins, G1/S cyclins, which are essential for the control of the cell cycle at the G1/S (start) transition, and G2/M cyclins, which are essential for the control of the cell cycle at the G2/M (mitosis) transition. G2/M cyclins accumulate steadily during G2 and are abruptly destroyed as cells exit from mitosis (at the end of the M-phase). In most species, there are multiple forms of G1 and G2 cyclins. For example, in vertebrates, there are two G2 cyclins, A and B, and at least three G1 cyclins, C, D, and E.Cyclin homologues have been found in various viruses, including Saimiriine herpesvirus 2 (Herpesvirus saimiri) and Human herpesvirus 8 (HHV-8) (Kaposi's sarcoma-associated herpesvirus). These viral homologues differ from their cellular counterparts in that the viral proteins have gained new functions and eliminated others to harness the cell and benefit the virus [].This group represents a predicted cyclin found in epsilon-retroviruses, including walleye epidermal hyperplasia virus and walleye dermal sarcoma virus (WDSV). |
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•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
Cyclins are eukaryotic proteins that play an active role in controlling nuclear cell division cycles [], and regulate cyclin dependent kinases (CDKs). Cyclins, together with the p34 (cdc2) or cdk2 kinases, form the Maturation Promoting Factor (MPF). There are two main groups of cyclins, G1/S cyclins, which are essential for the control of the cell cycle at the G1/S (start) transition, and G2/M cyclins, which are essential for the control of the cell cycle at the G2/M (mitosis) transition. G2/M cyclins accumulate steadily during G2 and are abruptly destroyed as cells exit from mitosis (at the end of the M-phase). In most species, there are multiple forms of G1 and G2 cyclins. For example, in vertebrates, there are two G2 cyclins, A and B, and at least three G1 cyclins, C, D, and E.Cyclin homologues have been found in various viruses, including Saimiriine herpesvirus 2 (Herpesvirus saimiri) and Human herpesvirus 8 (HHV-8) (Kaposi's sarcoma-associated herpesvirus). These viral homologues differ from their cellular counterparts in that the viral proteins have gained new functions and eliminated others to harness the cell and benefit the virus [].This group represents cyclin Y (also known as cyclin X) and related cyclins. Cyclin Y is a positive regulatory subunit of the cyclin-dependent kinase CDK14/PFTK1. Cyclin Y acts as a cell-cycle regulator of Wnt signaling pathway during G2/M phase by recruiting CDK14/PFTK1 to the plasma membrane and promoting phosphorylation of LRP6, leading to the activation of the Wnt signaling pathway [, ]. |
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•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
Cyclins are eukaryotic proteins that play an active role in controlling nuclear cell division cycles [], and regulate cyclin dependent kinases (CDKs). Cyclins, together with the p34 (cdc2) or cdk2 kinases, form the Maturation Promoting Factor (MPF). There are two main groups of cyclins, G1/S cyclins, which are essential for the control of the cell cycle at the G1/S (start) transition, and G2/M cyclins, which are essential for the control of the cell cycle at the G2/M (mitosis) transition. G2/M cyclins accumulate steadily during G2 and are abruptly destroyed as cells exit from mitosis (at the end of the M-phase). In most species, there are multiple forms of G1 and G2 cyclins. For example, in vertebrates, there are two G2 cyclins, A and B, and at least three G1 cyclins, C, D, and E.Cyclin homologues have been found in various viruses, including Saimiriine herpesvirus 2 (Herpesvirus saimiri) and Human herpesvirus 8 (HHV-8) (Kaposi's sarcoma-associated herpesvirus). These viral homologues differ from their cellular counterparts in that the viral proteins have gained new functions and eliminated others to harness the cell and benefit the virus [].This group represents a viral cyclin. |
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Protein Domain |
Type: |
Domain |
Description: |
Cyclins are eukaryotic proteins that play an active role in controlling nuclear cell division cycles [], and regulate cyclin dependent kinases (CDKs). Cyclins, together with the p34 (cdc2) or cdk2 kinases, form the Maturation Promoting Factor (MPF). Thereare two main groups of cyclins, G1/S cyclins, which are essential for the control of the cell cycle at the G1/S (start) transition, and G2/M cyclins, which are essential for the control of the cell cycle at the G2/M (mitosis) transition. G2/M cyclins accumulate steadily during G2 and are abruptly destroyed as cells exit from mitosis (at the end of the M-phase). In most species, there are multiple forms of G1 and G2 cyclins. For example, in vertebrates, there are two G2 cyclins, A and B, and at least three G1 cyclins, C, D, and E.Cyclin homologues have been found in various viruses, including Saimiriine herpesvirus 2 (Herpesvirus saimiri) and Human herpesvirus 8 (HHV-8) (Kaposi's sarcoma-associated herpesvirus). These viral homologues differ from their cellular counterparts in that the viral proteins have gained new functions and eliminated others to harness the cell and benefit the virus [].This domain adopts a secondary structure consisting of a five α-helix cyclin fold. Interaction with cyclin dependent kinases (CDKs) at a PSTAIRE sequence motif within the catalytic cleft of CDK results in the regulation of CDK activity []. |
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Protein Domain |
Type: |
Domain |
Description: |
Cyclins are eukaryotic proteins that play an active role in controlling nuclear cell division cycles [], and regulate cyclin dependent kinases (CDKs). Cyclins, together with the p34 (cdc2) or cdk2 kinases, form the Maturation Promoting Factor (MPF). There are two main groups of cyclins, G1/S cyclins, which are essential for the control of the cell cycle at the G1/S (start) transition, and G2/M cyclins, which are essential for the control of the cell cycle at the G2/M (mitosis) transition. G2/M cyclins accumulate steadily during G2 and are abruptly destroyed as cells exit from mitosis (at the end of the M-phase). In most species, there are multiple forms of G1 and G2 cyclins. For example, in vertebrates, there are two G2 cyclins, A and B, and at least three G1 cyclins, C, D, and E.Cyclin homologues have been found in various viruses, including Saimiriine herpesvirus 2 (Herpesvirus saimiri) and Human herpesvirus 8 (HHV-8) (Kaposi's sarcoma-associated herpesvirus). These viral homologues differ from their cellular counterparts in that the viral proteins have gained new functions and eliminated others to harness the cell and benefit the virus [].This entry represents a domain found in a family of viral cyclins that specifically activate CDK6 of host cells to a very high degree []. This domain adopts a helical structure consisting of five α-helices, with one helix surrounded by the others. |
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Protein Domain |
Type: |
Family |
Description: |
Cyclin-dependent kinase 7 (CDK7) is a serine/threonine kinase involved in cell cycle control and in RNA polymerase II-mediated RNA transcription. It is activated by binding to a cyclin; binding to a different cyclin and phosphorylation of another kinase progresses the cell cycle. CDK7 binds cyclin-B and phosphorylates CDK1 during G2-M transition, and phosphorylates CDK2 and binds to cyclins during G1-S transition [, ]. CDK7 phosphorylates and activates p53 following DNA damage [], but CDK7 is then inactivated by p53, which arrests the cell cycle, allowing the cell to recover or undergo apoptosis []. CDK7 is also the catalytic subunit of the CDK-activating kinase (CAK) complex, which also contains cyclin-H (CCNH) and MAT1 [, ]. In turn, the CAK associates with the core-TFIIH to form the TFIIH basal transcription factor [].This entry includes CDK7 from animals, Kin28 from budding yeasts and Crk1 (also known as Mcs6) from fission yeasts. S. pombe possesses two CAKs, the nonessential Csk1 and the essential Mcs6 kinases, corresponding to the yeast Cak1 and the metazoan CDK7, respectively. Mcs6 modulates gene expression through both its CAK and CTD kinase activities []. Kin28 is the closest homologue of CDK7 from budding yeasts. It forms a complex with Ccl1 and Tfb3. This complex associate with TFIIH for transcription regulating activity, but does not display CAK activity []. Instead, Cak1, a single-subunit kinase distantly related to Cdk, catalyzes Cdk activation at both transitions of the budding yeast cell cycle []. |
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Protein Domain |
Type: |
Domain |
Description: |
P53 is a tumor suppressor gene product; mutations in p53 or lack of expression are found associated with a large fraction of all human cancers. P53 is activated by DNA damage and acts as a regulator of gene expression that ultimatively blocks progression through the cell cycle. P53 binds to DNA as a tetrameric transcription factor. In its inactive form, p53 is bound to the ring finger protein Mdm2, which promotes its ubiquitinylation and subsequent proteosomal degradation. Phosphorylation of p53 disrupts the Mdm2-p53 complex, while the stable and active p53 binds to regulatory regions of its target genes, such as the cyclin-kinase inhibitor p21, which complexes and inactivates cdk2 and other cyclin complexes [, , , , , , , , , ].This domain is found in p53 transcription factors, where it is responsible for DNA-binding. The DNA-binding domain acts to clamp, or in the case of TonEBP, encircle the DNA target in order to stabilise the protein-DNA complex []. Protein interactions may also serve to stabilise the protein-DNA complex, for example in the STAT-1 dimer the SH2 (Src homology 2) domain in each monomer is coupled to the DNA-binding domain to increase stability []. The DNA-binding domain consists of a β-sandwich formed of 9 strands in 2 sheets with a Greek-key topology. This structure is found in many transcription factors, often within the DNA-binding domain. |
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Publication |
First Author: |
Galderisi U |
Year: |
2003 |
Journal: |
Oncogene |
Title: |
Cell cycle regulation and neural differentiation. |
Volume: |
22 |
Issue: |
33 |
Pages: |
5208-19 |
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•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
344
 |
Fragment?: |
false |
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•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
377
 |
Fragment?: |
false |
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•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
341
 |
Fragment?: |
false |
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•
•
•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
294
 |
Fragment?: |
false |
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•
•
•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
377
 |
Fragment?: |
false |
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•
•
•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
291
 |
Fragment?: |
false |
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•
•
•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
171
 |
Fragment?: |
true |
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•
•
•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
272
 |
Fragment?: |
true |
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•
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•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
294
 |
Fragment?: |
false |
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•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
114
 |
Fragment?: |
true |
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•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
344
 |
Fragment?: |
false |
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•
•
•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
367
 |
Fragment?: |
false |
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•
•
•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
344
 |
Fragment?: |
false |
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•
•
•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
344
 |
Fragment?: |
false |
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•
•
•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
294
 |
Fragment?: |
false |
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•
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•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
172
 |
Fragment?: |
true |
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•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
148
 |
Fragment?: |
true |
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•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
294
 |
Fragment?: |
false |
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•
•
•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
344
 |
Fragment?: |
false |
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•
•
•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
2498
 |
Fragment?: |
false |
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•
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•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
377
 |
Fragment?: |
false |
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•
•
•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
294
 |
Fragment?: |
false |
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•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
81
 |
Fragment?: |
true |
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•
•
•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
294
 |
Fragment?: |
false |
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Publication |
First Author: |
Nasmyth K |
Year: |
1996 |
Journal: |
Science |
Title: |
Viewpoint: putting the cell cycle in order. |
Volume: |
274 |
Issue: |
5293 |
Pages: |
1643-5 |
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Publication |
First Author: |
Duncker BP |
Year: |
2003 |
Journal: |
Mutat Res |
Title: |
Cdc7 kinases (DDKs) and checkpoint responses: lessons from two yeasts. |
Volume: |
532 |
Issue: |
1-2 |
Pages: |
21-7 |
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Publication |
First Author: |
Hardy CF |
Year: |
1996 |
Journal: |
Mol Cell Biol |
Title: |
A novel role for Cdc5p in DNA replication. |
Volume: |
16 |
Issue: |
12 |
Pages: |
6775-82 |
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Publication |
First Author: |
Dowell SJ |
Year: |
1994 |
Journal: |
Science |
Title: |
Interaction of Dbf4, the Cdc7 protein kinase regulatory subunit, with yeast replication origins in vivo. |
Volume: |
265 |
Issue: |
5176 |
Pages: |
1243-6 |
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Publication |
First Author: |
Matsuoka M |
Year: |
1994 |
Journal: |
Mol Cell Biol |
Title: |
Activation of cyclin-dependent kinase 4 (cdk4) by mouse MO15-associated kinase. |
Volume: |
14 |
Issue: |
11 |
Pages: |
7265-75 |
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Publication |
First Author: |
Cheng N |
Year: |
2008 |
Journal: |
PLoS One |
Title: |
p27 deficiency cooperates with Bcl-2 but not Bax to promote T-cell lymphoma. |
Volume: |
3 |
Issue: |
4 |
Pages: |
e1911 |
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Publication |
First Author: |
Short JD |
Year: |
2008 |
Journal: |
Cancer Res |
Title: |
AMP-activated protein kinase signaling results in cytoplasmic sequestration of p27. |
Volume: |
68 |
Issue: |
16 |
Pages: |
6496-506 |
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Publication |
First Author: |
Tateishi Y |
Year: |
2012 |
Journal: |
Biochem Biophys Res Commun |
Title: |
Development of mice without Cip/Kip CDK inhibitors. |
Volume: |
427 |
Issue: |
2 |
Pages: |
285-92 |
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Publication |
First Author: |
Franklin DS |
Year: |
2000 |
Journal: |
Mol Cell Biol |
Title: |
Functional collaboration between different cyclin-dependent kinase inhibitors suppresses tumor growth with distinct tissue specificity. |
Volume: |
20 |
Issue: |
16 |
Pages: |
6147-58 |
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