Cdkn2a
entrez
12578
canonical
uniprot
P51480
canonical
uniprot
Q64364
canonical
ensembl
ENSMUSG00000044303
resolver
ensp
ENSMUSP00000061847
resolver
ensp
ENSMUSP00000102748
resolver
genesymbol
Cdkn2a
resolver
genesymbol_syn
P16ink4a
resolver
uniprot
A2ANM1
resolver
uniprot
A2ANM2
resolver
uniprot
O89088
resolver
uniprot
P97510
resolver
uniprot
P97937
resolver
uniprot
Q4U255
resolver
uniprot
Q6PEA2
resolver
uniprot
Q78E39
resolver
uniprot
Q78E57
resolver
uniprot
Q792X7
resolver
uniprot
Q9QWH6
resolver
uniprot
Q9QWH7
resolver
uniprot
Q9QWH8
resolver
uniprot
Q9QXC7
resolver
uniprot
Q9R051
resolver
uniprot_entry
ARF_MOUSE
resolver
uniprot_entry
CDN2A_MOUSE
resolver
uniprot_sec
A2ANM1
resolver
uniprot_sec
A2ANM2
resolver
uniprot_sec
O89088
resolver
uniprot_sec
P97510
resolver
uniprot_sec
P97937
resolver
uniprot_sec
Q4U255
resolver
uniprot_sec
Q6PEA2
resolver
uniprot_sec
Q78E39
resolver
uniprot_sec
Q78E57
resolver
uniprot_sec
Q792X7
resolver
uniprot_sec
Q9QWH6
resolver
uniprot_sec
Q9QWH7
resolver
uniprot_sec
Q9QWH8
resolver
uniprot_sec
Q9QXC7
resolver
uniprot_sec
Q9R051
resolver
amino_acid_sequence
MESAADRLARAAAQGRVHDVRALLEAGVSPNAPNSFGRTPIQVMMMGNVHVAALLLNYGADSNCEDPTTFSRPVHDAAREGFLDTLVVLHGSGARLDVRDAWGRLPLDLAQERGHQDIVRYLRSAGCSLCSAGWSLCTAGNVAQTDGHSFSSSTPRALELRGQSQEQS
uniprot
proteins
amino_acid_sequence
MGRRFLVTVRIQRAGRPLQERVFLVKFVRSRRPRTASCALAFVNMLLRLERILRRGPHRNPGPGDDDGQRSRSSSSAQLRCRFELRGPHYLLPPGARRSAGRLPGHAGGAARVRGSAGCARCLGSPAARLGPRAGTSRHRAIFAFRWVLFVFRWVVFVYRWERRPDRRA
uniprot
proteins
function
FUNCTION: Acts as a negative regulator of the proliferation of normal cells by interacting strongly with CDK4 and CDK6. This inhibits their ability to interact with cyclins D and to phosphorylate the retinoblastoma protein.
uniprot
proteins
function
FUNCTION: Capable of inducing cell cycle arrest in G1 and G2 phases (PubMed:8521522, PubMed:9393858). Acts as a tumor suppressor (PubMed:15601844, PubMed:17936562, PubMed:8521522, PubMed:9393858). Binds to MDM2 and blocks its nucleocytoplasmic shuttling by sequestering it in the nucleolus (PubMed:10359817, PubMed:9529248). This inhibits the oncogenic action of MDM2 by blocking MDM2-induced degradation of p53 and enhancing p53-dependent transactivation and apoptosis (PubMed:10359817). Also induces G2 arrest and apoptosis in a p53-independent manner by preventing the activation of cyclin B1/CDC2 complexes (PubMed:15361884). Binds to BCL6 and down-regulates BCL6-induced transcriptional repression (PubMed:15567177). Binds to E2F1 and MYC and blocks their transcriptional activator activity but has no effect on MYC transcriptional repression (By similarity). Binds to TOP1/TOPOI and stimulates its activity (By similarity). This complex binds to rRNA gene promoters and may play a role in rRNA transcription and/or maturation (By similarity). Interacts with NPM1/B23 and promotes its polyubiquitination and degradation, thus inhibiting rRNA processing (By similarity). Plays a role in inhibiting ribosome biogenesis, perhaps by binding to the nucleolar localization sequence of transcription termination factor TTF1, and thereby preventing nucleolar localization of TTF1 (PubMed:20513429). Interacts with COMMD1 and promotes its 'Lys63'-linked polyubiquitination (By similarity). Interacts with UBE2I/UBC9 and enhances sumoylation of a number of its binding partners including MDM2 and E2F1 (By similarity). Binds to HUWE1 and represses its ubiquitin ligase activity (By similarity). May play a role in controlling cell proliferation and apoptosis during mammary gland development (By similarity). {ECO:0000250|UniProtKB:Q8N726, ECO:0000269|PubMed:10359817, ECO:0000269|PubMed:15361884, ECO:0000269|PubMed:15567177, ECO:0000269|PubMed:15601844, ECO:0000269|PubMed:17936562, ECO:0000269|PubMed:20513429, ECO:0000269|PubMed:8521522, ECO:0000269|PubMed:9393858, ECO:0000269|PubMed:9529248}.; FUNCTION: [Isoform smARF]: May be involved in regulation of autophagy and caspase-independent cell death; the short-lived mitochondrial isoform is stabilized by C1QBP. {ECO:0000269|PubMed:16713577}.
uniprot
proteins
mass_dalton
17941
uniprot
proteins
mass_dalton
19238
uniprot
proteins
mutagenesis
MUTAGEN 64; /note="C->G,R: No effect on activity."; /evidence="ECO:0000269|PubMed:9012842"; MUTAGEN 76; /note="D->N: Loss of activity."; /evidence="ECO:0000269|PubMed:9012842"; MUTAGEN 84..85; /note="Missing: Loss of activity."; /evidence="ECO:0000269|PubMed:9012842
uniprot
proteins
mutagenesis
MUTAGEN 85; /note="L->P,R: No effect on activity."; /evidence="ECO:0000269|PubMed:9012842"; MUTAGEN 93; /note="P->S: No effect on activity."; /evidence="ECO:0000269|PubMed:9012842"; MUTAGEN 97; /note="R->Q: No effect on activity."; /evidence="ECO:0000269|PubMed:9012842"; MUTAGEN 105..106; /note="Missing: No effect on activity."; /evidence="ECO:0000269|PubMed:9012842"; MUTAGEN 120; /note="A->T: No effect on activity."; /evidence="ECO:0000269|PubMed:9012842
uniprot
proteins
post_translational_modification
PTM: Phosphorylation seems to increase interaction with CDK4. {ECO:0000250}.
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated in normal cells by TRIP12 via the ubiquitin fusion degradation (UFD) pathway, a process that mediates ubiquitination at the N-terminus, regardless of the absence of lysine residues. Ubiquitination leads to its proteasomal degradation. In cancer cells, however, TRIP12 is located in a different cell compartment, preventing ubiquitination and degradation. {ECO:0000250|UniProtKB:Q8N726}.
uniprot
proteins
protein_family
CDKN2 cyclin-dependent kinase inhibitor family
uniprot
proteins
pubmed
10097151
uniprot
proteins
pubmed
10359817
uniprot
proteins
pubmed
10753221
uniprot
proteins
pubmed
10898794
uniprot
proteins
pubmed
11327858
uniprot
proteins
pubmed
12154087
uniprot
proteins
pubmed
15105443
uniprot
proteins
pubmed
15361884
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15567177
uniprot
proteins
pubmed
15601844
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16713577
uniprot
proteins
pubmed
17110379
uniprot
proteins
pubmed
17486078
uniprot
proteins
pubmed
17546045
uniprot
proteins
pubmed
17936562
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
20513429
uniprot
proteins
pubmed
7651726
uniprot
proteins
pubmed
8521522
uniprot
proteins
pubmed
9012842
uniprot
proteins
pubmed
9021155
uniprot
proteins
pubmed
9178896
uniprot
proteins
pubmed
9393858
uniprot
proteins
pubmed
9482902
uniprot
proteins
pubmed
9529248
uniprot
proteins
pubmed
9667743
uniprot
proteins
sequence_length
168
uniprot
proteins
sequence_length
169
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q8N726, ECO:0000269|PubMed:10359817, ECO:0000269|PubMed:15567177, ECO:0000269|PubMed:15601844, ECO:0000269|PubMed:8521522, ECO:0000305|PubMed:20513429}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q8N726, ECO:0000305|PubMed:20513429}.; SUBCELLULAR LOCATION: [Isoform smARF]: Mitochondrion {ECO:0000269|PubMed:16713577}.
uniprot
proteins