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Cyclin-dependent kinase inhibitor 1 (CDK-interacting protein 1) (Melanoma differentiation-associated protein) (p21)

 CDN1A_MOUSE             Reviewed;         159 AA.
P39689;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
07-NOV-2018, entry version 162.
RecName: Full=Cyclin-dependent kinase inhibitor 1;
AltName: Full=CDK-interacting protein 1;
AltName: Full=Melanoma differentiation-associated protein;
AltName: Full=p21;
Name=Cdkn1a; Synonyms=Cip1, Waf1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BXSB; TISSUE=Spleen;
PubMed=8084607;
Huppi K., Siwarski D., Dosik J., Michieli P., Chedid M., Reed S.,
Mock B., Givol D., Mushinski J.F.;
"Molecular cloning, sequencing, chromosomal localization and
expression of mouse p21 (Waf1).";
Oncogene 9:3017-3020(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7796420;
El-Deiry W.S., Tokino T., Waldman T., Velculescu V.E., Oliner J.D.,
Burell M., Hill D.E., Rees J.L., Hamilton S.R., Kinzler K.W.,
Vogelstein B.;
"Topological control of p21WAF1/CIP1 expression in normal and
neoplastic tissues.";
Cancer Res. 55:2910-2919(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-143.
PubMed=8242752; DOI=10.1016/0092-8674(93)90500-P;
El-Deiry W.S., Tokino T., Velculescu V.E., Levy D.B., Parsons R.,
Trent J.M., Lin D., Mercer W.E., Kinzler K.W., Vogelstein B.;
"WAF1, a potential mediator of p53 tumor suppression.";
Cell 75:817-825(1993).
[5]
INTERACTION WITH HDAC1, SUBCELLULAR LOCATION, AND ACETYLATION.
PubMed=20154723; DOI=10.1038/onc.2010.19;
Li Z., Zhang Q., Mao J.H., Weise A., Mrasek K., Fan X., Zhang X.,
Liehr T., Lu K.H., Balmain A., Cai W.W.;
"An HDAC1-binding domain within FATS bridges p21 turnover to
radiation-induced tumorigenesis.";
Oncogene 29:2659-2671(2010).
[6]
FUNCTION, INTERACTION WITH STK11, AND PHOSPHORYLATION AT SER-78 AND
SER-141.
PubMed=25329316; DOI=10.1371/journal.pgen.1004721;
Esteve-Puig R., Gil R., Gonzalez-Sanchez E., Bech-Serra J.J.,
Grueso J., Hernandez-Losa J., Moline T., Canals F., Ferrer B.,
Cortes J., Bastian B., Cajal S.R.Y., Martin-Caballero J., Flores J.M.,
Vivancos A., Garcia-Patos V., Recio J.A.;
"A mouse model uncovers LKB1 as an UVB-induced DNA damage sensor
mediating CDKN1A (p21WAF1/CIP1) degradation.";
PLoS Genet. 10:E1004721-E1004721(2014).
-!- FUNCTION: May be involved in p53/TP53 mediated inhibition of
cellular proliferation in response to DNA damage. Binds to and
inhibits cyclin-dependent kinase activity, preventing
phosphorylation of critical cyclin-dependent kinase substrates and
blocking cell cycle progression. Functions in the nuclear
localization and assembly of cyclin D-CDK4 complex and promotes
its kinase activity towards RB1. At higher stoichiometric ratios,
inhibits the kinase activity of the cyclin D-CDK4 complex
(PubMed:25329316). Inhibits DNA synthesis by DNA polymerase delta
by competing with POLD3 for PCNA binding (By similarity).
{ECO:0000250|UniProtKB:P38936, ECO:0000269|PubMed:25329316}.
-!- SUBUNIT: Interacts with HDAC1; the interaction is prevented by
competitive binding of C10orf90/FATS to HDAC1 facilitating
acetylation and protein stabilization of CDKN1A/p21
(PubMed:20154723). Interacts with MKRN1. Interacts with PSMA3.
Interacts with PCNA. Component of the ternary complex, cyclin D-
CDK4-CDKN1A. Interacts (via its N-terminal domain) with CDK4; the
interaction promotes the assembly of the cyclin D-CDK4 complex,
its nuclear translocation and promotes the cyclin D-dependent
enzyme activity of CDK4. Binding to CDK2 leads to CDK2/cyclin E
inactivation at the G1-S phase DNA damage checkpoint, thereby
arresting cells at the G1-S transition during DNA repair.
Interacts with PIM1 (By similarity). Interacts with STK11
(PubMed:25329316). Interacts with NUAK1 (By similarity).
{ECO:0000250|UniProtKB:P38936, ECO:0000269|PubMed:20154723,
ECO:0000269|PubMed:25329316}.
-!- INTERACTION:
Q9Z111:Gadd45g; NbExp=2; IntAct=EBI-1174103, EBI-1173616;
P17918:Pcna; NbExp=2; IntAct=EBI-1174103, EBI-1173716;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000269|PubMed:20154723}.
-!- INDUCTION: By p53, mezerein (antileukemic compound) and interferon
beta.
-!- DOMAIN: The C-terminal is required for nuclear localization of the
cyclin D-CDK4 complex. {ECO:0000250}.
-!- DOMAIN: The PIP-box K+4 motif mediates both the interaction with
PCNA and the recruitment of the DCX(DTL) complex: while the PIP-
box interacts with PCNA, the presence of the K+4 submotif,
recruits the DCX(DTL) complex, leading to its ubiquitination.
{ECO:0000250}.
-!- PTM: Phosphorylation of Thr-140 or Ser-141 impairs binding to
PCNA. Phosphorylation at Ser-112 by GSK3-beta enhances
ubiquitination by the DCX(DTL) complex (By similarity).
Phosphorylation of Thr-140 by PIM2 enhances its stability and
inhibits cell proliferation. Phosphorylation of Thr-140 by PIM1
results in the relocation of CDKN1A to the cytoplasm and enhanced
CDKN1A protein stability. UV radiation-induced phosphorylation at
Ser-78 and Ser-141 by NUAK1 leads to its degradation.
{ECO:0000250|UniProtKB:P38936, ECO:0000269|PubMed:25329316}.
-!- PTM: Ubiquitinated by MKRN1; leading to polyubiquitination and 26S
proteasome-dependent degradation. Ubiquitinated by the DCX(DTL)
complex, also named CRL4(CDT2) complex, leading to its degradation
during S phase or following UV irradiation. Ubiquitination by the
DCX(DTL) complex is essential to control replication licensing and
is PCNA-dependent: interacts with PCNA via its PIP-box, while the
presence of the containing the 'K+4' motif in the PIP box, recruit
the DCX(DTL) complex, leading to its degradation. Ubiquitination
at Ser-2 leads to degradation by the proteasome pathway.
Ubiquitinated by RNF114; leading to proteasomal degradation (By
similarity). {ECO:0000250}.
-!- PTM: Acetylation leads to protein stability. Acetylated in vitro
on Lys-136, Lys-149, Lys-156 and Lys-158. Deacetylation by HDAC1
is prevented by competitive binding of C10orf90/FATS to HDAC1.
{ECO:0000269|PubMed:20154723}.
-!- SIMILARITY: Belongs to the CDI family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U09507; AAB60456.1; -; mRNA.
EMBL; U24173; AAC52220.1; -; mRNA.
EMBL; BC002043; AAH02043.1; -; mRNA.
CCDS; CCDS28591.1; -.
PIR; A49438; A49438.
PIR; I49023; I49023.
RefSeq; NP_001104569.1; NM_001111099.2.
RefSeq; NP_031695.1; NM_007669.5.
UniGene; Mm.195663; -.
ProteinModelPortal; P39689; -.
SMR; P39689; -.
BioGrid; 198651; 15.
CORUM; P39689; -.
DIP; DIP-24178N; -.
ELM; P39689; -.
IntAct; P39689; 4.
MINT; P39689; -.
STRING; 10090.ENSMUSP00000023829; -.
iPTMnet; P39689; -.
PhosphoSitePlus; P39689; -.
EPD; P39689; -.
PaxDb; P39689; -.
PeptideAtlas; P39689; -.
PRIDE; P39689; -.
Ensembl; ENSMUST00000023829; ENSMUSP00000023829; ENSMUSG00000023067.
Ensembl; ENSMUST00000119901; ENSMUSP00000113150; ENSMUSG00000023067.
Ensembl; ENSMUST00000122348; ENSMUSP00000112411; ENSMUSG00000023067.
GeneID; 12575; -.
KEGG; mmu:12575; -.
UCSC; uc008bsg.2; mouse.
CTD; 1026; -.
MGI; MGI:104556; Cdkn1a.
eggNOG; KOG4743; Eukaryota.
eggNOG; ENOG410XXN5; LUCA.
GeneTree; ENSGT00530000063588; -.
HOGENOM; HOG000285999; -.
HOVERGEN; HBG050868; -.
InParanoid; P39689; -.
KO; K06625; -.
OMA; LEGNFAW; -.
OrthoDB; EOG091G19PZ; -.
PhylomeDB; P39689; -.
TreeFam; TF101038; -.
Reactome; R-MMU-176408; Regulation of APC/C activators between G1/S and early anaphase.
Reactome; R-MMU-187577; SCF(Skp2)-mediated degradation of p27/p21.
Reactome; R-MMU-198323; AKT phosphorylates targets in the cytosol.
Reactome; R-MMU-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-MMU-2559586; DNA Damage/Telomere Stress Induced Senescence.
Reactome; R-MMU-6804116; TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest.
Reactome; R-MMU-69202; Cyclin E associated events during G1/S transition.
Reactome; R-MMU-69231; Cyclin D associated events in G1.
Reactome; R-MMU-69563; p53-Dependent G1 DNA Damage Response.
Reactome; R-MMU-69656; Cyclin A:Cdk2-associated events at S phase entry.
Reactome; R-MMU-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
ChiTaRS; Cdkn1a; mouse.
PRO; PR:P39689; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000023067; Expressed in 311 organ(s), highest expression level in stroma of bone marrow.
CleanEx; MM_CDKN1A; -.
ExpressionAtlas; P39689; baseline and differential.
Genevisible; P39689; MM.
GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IPI:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0016604; C:nuclear body; ISO:MGI.
GO; GO:0005730; C:nucleolus; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0070557; C:PCNA-p21 complex; ISS:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0030332; F:cyclin binding; IDA:MGI.
GO; GO:0019912; F:cyclin-dependent protein kinase activating kinase activity; ISO:MGI.
GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; ISO:MGI.
GO; GO:0004861; F:cyclin-dependent protein serine/threonine kinase inhibitor activity; IDA:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0004860; F:protein kinase inhibitor activity; ISO:MGI.
GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0007050; P:cell cycle arrest; IDA:MGI.
GO; GO:0034198; P:cellular response to amino acid starvation; IMP:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:MGI.
GO; GO:0031668; P:cellular response to extracellular stimulus; ISO:MGI.
GO; GO:0071480; P:cellular response to gamma radiation; IDA:MGI.
GO; GO:0071479; P:cellular response to ionizing radiation; ISO:MGI.
GO; GO:0071493; P:cellular response to UV-B; IDA:UniProtKB.
GO; GO:0090398; P:cellular senescence; ISO:MGI.
GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; ISO:MGI.
GO; GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; IDA:MGI.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISO:MGI.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISO:MGI.
GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IMP:MGI.
GO; GO:0071850; P:mitotic cell cycle arrest; IDA:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:MGI.
GO; GO:1904030; P:negative regulation of cyclin-dependent protein kinase activity; ISO:MGI.
GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:MGI.
GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; ISO:MGI.
GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
GO; GO:0042326; P:negative regulation of phosphorylation; ISO:MGI.
GO; GO:1904706; P:negative regulation of vascular smooth muscle cell proliferation; ISO:MGI.
GO; GO:0030890; P:positive regulation of B cell proliferation; IGI:MGI.
GO; GO:0010942; P:positive regulation of cell death; ISO:MGI.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISO:MGI.
GO; GO:0043068; P:positive regulation of programmed cell death; IMP:MGI.
GO; GO:0045860; P:positive regulation of protein kinase activity; ISO:MGI.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; ISO:MGI.
GO; GO:0051726; P:regulation of cell cycle; IDA:MGI.
GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IMP:MGI.
GO; GO:2000278; P:regulation of DNA biosynthetic process; IMP:MGI.
GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:MGI.
GO; GO:0033158; P:regulation of protein import into nucleus, translocation; IMP:MGI.
GO; GO:0009411; P:response to UV; IMP:MGI.
InterPro; IPR003175; CDI.
InterPro; IPR029841; CDKN1A_vertebrate.
PANTHER; PTHR10265; PTHR10265; 1.
PANTHER; PTHR10265:SF16; PTHR10265:SF16; 1.
Pfam; PF02234; CDI; 1.
1: Evidence at protein level;
Acetylation; Cell cycle; Complete proteome; Cytoplasm; Metal-binding;
Nucleus; Phosphoprotein; Protein kinase inhibitor; Reference proteome;
Ubl conjugation; Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P38936}.
CHAIN 2 159 Cyclin-dependent kinase inhibitor 1.
/FTId=PRO_0000190080.
ZN_FING 12 40 C4-type. {ECO:0000255}.
REGION 17 24 Required for binding cyclins.
{ECO:0000250}.
REGION 53 58 Required for binding CDKs. {ECO:0000250}.
MOTIF 135 159 PIP-box K+4 motif.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:P38936}.
MOD_RES 78 78 Phosphoserine; by NUAK1.
{ECO:0000269|PubMed:25329316}.
MOD_RES 112 112 Phosphoserine; by GSK3-beta.
{ECO:0000250|UniProtKB:P38936}.
MOD_RES 125 125 Phosphoserine.
{ECO:0000250|UniProtKB:P38936}.
MOD_RES 140 140 Phosphothreonine; by PKA, PKB/AKT1, PIM1
and PIM2. {ECO:0000250|UniProtKB:P38936}.
MOD_RES 141 141 Phosphoserine; by NUAK1.
{ECO:0000269|PubMed:25329316}.
CROSSLNK 2 2 Glycyl serine ester (Ser-Gly) (interchain
with G-Cter in ubiquitin). {ECO:0000250}.
CONFLICT 30 30 R -> S (in Ref. 4; no nucleotide entry).
{ECO:0000305}.
CONFLICT 56 57 TP -> RQ (in Ref. 4; no nucleotide
entry). {ECO:0000305}.
SEQUENCE 159 AA; 17785 MW; 37B7C22B9A2FD089 CRC64;
MSNPGDVRPV PHRSKVCRCL FGPVDSEQLR RDCDALMAGC LQEARERWNF DFVTETPLEG
NFVWERVRSL GLPKVYLSPG SRSRDDLGGD KRPSTSSALL QGPAPEDHVA LSLSCTLVSE
RPEDSPGGPG TSQGRKRRQT SLTDFYHSKR RLVFCKRKP


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