Cdkn1a
entrez
12575
canonical
uniprot
P39689
canonical
ensembl
ENSMUSG00000023067
resolver
ensp
ENSMUSP00000023829
resolver
ensp
ENSMUSP00000112411
resolver
ensp
ENSMUSP00000113150
resolver
ensp
ENSMUSP00000156559
resolver
enst
ENSMUST00000023829
resolver
enst
ENSMUST00000119901
resolver
enst
ENSMUST00000122348
resolver
enst
ENSMUST00000233296
resolver
genesymbol
Cdkn1a
resolver
genesymbol_syn
Cip1
resolver
genesymbol_syn
Waf1
resolver
uniprot
Q564P6
resolver
uniprot_entry
CDN1A_MOUSE
resolver
uniprot_entry
Q564P6_MOUSE
resolver
amino_acid_sequence
MSNPGDVRPVPHRSKVCRCLFGPVDSEQLRRDCDALMAGCLQEARERWNFDFVTETPLEGNFVWERVRSLGLPKVYLSPGSRSRDDLGGDKRPSTSSALLQGPAPEDHVALSLSCTLVSERPEDSPGGPGTSQGRKRRQTSLTDFYHSKRRLVFCKRKP
uniprot
proteins
function
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). Plays an important role in controlling cell cycle progression and DNA damage-induced G2 arrest (By similarity). {ECO:0000250|UniProtKB:P38936, ECO:0000269|PubMed:25329316}.; FUNCTION: Plays an important role in controlling cell cycle progression and DNA damage-induced G2 arrest (PubMed:37178686). Involved in p53/TP53 mediated inhibition of cellular proliferation in response to DNA damage. Also involved in p53-independent DNA damage-induced G2 arrest mediated by CREB3L1 in astrocytes and osteoblasts (PubMed:37178686). 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). Negatively regulates the CDK4- and CDK6-driven phosphorylation of RB1 in keratinocytes, thereby resulting in the release of E2F1 and subsequent transcription of E2F1-driven G1/S phase promoting genes (PubMed:36689330). {ECO:0000250|UniProtKB:P38936, ECO:0000269|PubMed:25329316, ECO:0000269|PubMed:36689330, ECO:0000269|PubMed:37178686}.
uniprot
proteins
mass_dalton
17785
uniprot
proteins
post_translational_modification
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|UniProtKB:P38936}.; 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}.
uniprot
proteins
protein_family
CDI family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
20154723
uniprot
proteins
pubmed
25329316
uniprot
proteins
pubmed
36689330
uniprot
proteins
pubmed
37178686
uniprot
proteins
pubmed
7796420
uniprot
proteins
pubmed
8084607
uniprot
proteins
pubmed
8242752
uniprot
proteins
sequence_length
159
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:36689330}. Nucleus {ECO:0000269|PubMed:20154723, ECO:0000269|PubMed:36689330}.
uniprot
proteins