CDKN1A
entrez
1026
canonical
uniprot
P38936
canonical
ensembl
ENSG00000124762
resolver
ensp
ENSP00000244741
resolver
ensp
ENSP00000362815
resolver
ensp
ENSP00000384849
resolver
ensp
ENSP00000409259
resolver
ensp
ENSP00000482768
resolver
ensp
ENSP00000534258
resolver
ensp
ENSP00000534259
resolver
ensp
ENSP00000534260
resolver
ensp
ENSP00000534261
resolver
ensp
ENSP00000534262
resolver
ensp
ENSP00000534263
resolver
ensp
ENSP00000534264
resolver
ensp
ENSP00000534265
resolver
ensp
ENSP00000534266
resolver
ensp
ENSP00000581863
resolver
ensp
ENSP00000581864
resolver
ensp
ENSP00000581865
resolver
ensp
ENSP00000581866
resolver
ensp
ENSP00000581867
resolver
ensp
ENSP00000581868
resolver
ensp
ENSP00000581869
resolver
ensp
ENSP00000581870
resolver
ensp
ENSP00000581871
resolver
ensp
ENSP00000613163
resolver
ensp
ENSP00000613164
resolver
ensp
ENSP00000613165
resolver
ensp
ENSP00000613166
resolver
ensp
ENSP00000613167
resolver
ensp
ENSP00000613169
resolver
ensp
ENSP00000613170
resolver
ensp
ENSP00000613171
resolver
ensp
ENSP00000613172
resolver
ensp
ENSP00000613173
resolver
ensp
ENSP00000613174
resolver
ensp
ENSP00000613175
resolver
ensp
ENSP00000788643
resolver
enst
ENST00000244741
resolver
enst
ENST00000373711
resolver
enst
ENST00000405375
resolver
enst
ENST00000448526
resolver
enst
ENST00000615513
resolver
enst
ENST00000864199
resolver
enst
ENST00000864200
resolver
enst
ENST00000864201
resolver
enst
ENST00000864202
resolver
enst
ENST00000864203
resolver
enst
ENST00000864204
resolver
enst
ENST00000864205
resolver
enst
ENST00000864206
resolver
enst
ENST00000864207
resolver
enst
ENST00000911804
resolver
enst
ENST00000911805
resolver
enst
ENST00000911806
resolver
enst
ENST00000911807
resolver
enst
ENST00000911808
resolver
enst
ENST00000911809
resolver
enst
ENST00000911810
resolver
enst
ENST00000911811
resolver
enst
ENST00000911812
resolver
enst
ENST00000943104
resolver
enst
ENST00000943105
resolver
enst
ENST00000943106
resolver
enst
ENST00000943107
resolver
enst
ENST00000943108
resolver
enst
ENST00000943110
resolver
enst
ENST00000943111
resolver
enst
ENST00000943112
resolver
enst
ENST00000943113
resolver
enst
ENST00000943114
resolver
enst
ENST00000943115
resolver
enst
ENST00000943116
resolver
genesymbol
CDKN1A
resolver
genesymbol_syn
CAP20
resolver
genesymbol_syn
CDKN1
resolver
genesymbol_syn
CIP1
resolver
genesymbol_syn
MDA6
resolver
genesymbol_syn
PIC1
resolver
genesymbol_syn
SDI1
resolver
genesymbol_syn
WAF1
resolver
hgnc
HGNC:1784
resolver
uniprot
Q14010
resolver
uniprot
Q6FI05
resolver
uniprot
Q9BUT4
resolver
uniprot_entry
CDN1A_HUMAN
resolver
uniprot_sec
Q14010
resolver
uniprot_sec
Q6FI05
resolver
uniprot_sec
Q9BUT4
resolver
amino_acid_sequence
MSEPAGDVRQNPCGSKACRRLFGPVDSEQLSRDCDALMAGCIQEARERWNFDFVTETPLEGDFAWERVRGLGLPKLYLPTGPRRGRDELGGGRRPGTSPALLQGTAEEDHVDLSLSCTLVPRSGEQAEGSPGGPGDSQGRKRRQTSMTDFYHSKRRLIFSKRKP
uniprot
proteins
function
FUNCTION: Plays an important role in controlling cell cycle progression and DNA damage-induced G2 arrest (PubMed:9106657). 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 (By similarity). 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. Inhibits DNA synthesis by DNA polymerase delta by competing with POLD3 for PCNA binding (PubMed:11595739). 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 (By similarity). {ECO:0000250|UniProtKB:P39689, ECO:0000269|PubMed:11595739, ECO:0000269|PubMed:8242751, ECO:0000269|PubMed:9106657}.
uniprot
proteins
mass_dalton
18119
uniprot
proteins
mutagenesis
MUTAGEN 80; /note="T->A: Abolishes UV radiation-induced phosphorylation and subsequent degradation."; /evidence="ECO:0000269|PubMed:25329316"; MUTAGEN 114; /note="S->E: Phosphomimetic mutant, increases ubiquitination by the DCX(DTL) complex."; /evidence="ECO:0000269|PubMed:18794347"; MUTAGEN 144..150; /note="QTSMTDF->ATSATDA: Abolishes interaction with PCNA and subsequent degradation by the proteasome."; /evidence="ECO:0000269|PubMed:18794347"; MUTAGEN 145; /note="T->A: Reduces phosphorylation by Akt; no change in interaction with PCNA, CDK2 or CDK4; no change in subcellular location."; /evidence="ECO:0000269|PubMed:11463845"; MUTAGEN 145; /note="T->D: No interaction with PCNA; 59% inhibition of CDK2 binding; modest inhibition of CDK4 binding; no change in subcellular location."; /evidence="ECO:0000269|PubMed:11463845"; MUTAGEN 146; /note="S->A: No change in interaction with PCNA. Abolishes UV radiation-induced phosphorylation and subsequent degradation."; /evidence="ECO:0000269|PubMed:11463845, ECO:0000269|PubMed:25329316"; MUTAGEN 146; /note="S->D: Reduces interaction with PCNA."; /evidence="ECO:0000269|PubMed:11463845"; MUTAGEN 147..151; /note="MTDFY->ATDAAA: Abolishes interaction with PCNA and subsequent degradation by the proteasome."; /evidence="ECO:0000269|PubMed:18703516"; MUTAGEN 154..156; /note="KRR->AAA: Abolishes degradation by the proteasome without affecting the interaction with PCNA."; /evidence="ECO:0000269|PubMed:18703516"; MUTAGEN 154; /note="K->A: Loss of interaction with TRIM39."; /evidence="ECO:0000269|PubMed:23213251
uniprot
proteins
post_translational_modification
PTM: Phosphorylation of Thr-145 by Akt or of Ser-146 by PKC impairs binding to PCNA. Phosphorylation at Ser-114 by GSK3-beta enhances ubiquitination by the DCX(DTL) complex. Phosphorylation of Thr-145 by PIM2 enhances CDKN1A stability and inhibits cell proliferation. Phosphorylation of Thr-145 by PIM1 results in the relocation of CDKN1A to the cytoplasm and enhanced CDKN1A protein stability. UV radiation-induced phosphorylation at Thr-80 by LKB1 and at Ser-146 by NUAK1 leads to its degradation. {ECO:0000269|PubMed:10753973, ECO:0000269|PubMed:11463845, ECO:0000269|PubMed:12431783, ECO:0000269|PubMed:16982699, ECO:0000269|PubMed:18794347, ECO:0000269|PubMed:20307683, 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. {ECO:0000269|PubMed:15226418, ECO:0000269|PubMed:23213251}.; PTM: Acetylation leads to protein stability. Acetylated in vitro on Lys-141, Lys-154, Lys-161 and Lys-163. Deacetylation by HDAC1 is prevented by competitive binding of C10orf90/FATS to HDAC1 (By similarity). {ECO:0000250}.
uniprot
proteins
protein_family
CDI family
uniprot
proteins
pubmed
10753973
uniprot
proteins
pubmed
11350925
uniprot
proteins
pubmed
11463845
uniprot
proteins
pubmed
11595739
uniprot
proteins
pubmed
12431783
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
15226418
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15574338
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
16982699
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18703516
uniprot
proteins
pubmed
18794347
uniprot
proteins
pubmed
18794348
uniprot
proteins
pubmed
19054851
uniprot
proteins
pubmed
19332548
uniprot
proteins
pubmed
19445729
uniprot
proteins
pubmed
19536131
uniprot
proteins
pubmed
20307683
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23213251
uniprot
proteins
pubmed
23645206
uniprot
proteins
pubmed
25329316
uniprot
proteins
pubmed
7655464
uniprot
proteins
pubmed
7753561
uniprot
proteins
pubmed
8125163
uniprot
proteins
pubmed
8242751
uniprot
proteins
pubmed
8242752
uniprot
proteins
pubmed
8259214
uniprot
proteins
pubmed
8861913
uniprot
proteins
pubmed
9106657
uniprot
proteins
sequence_length
164
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11463845}. Nucleus {ECO:0000269|PubMed:11463845, ECO:0000269|PubMed:23213251}.
uniprot
proteins