Cdkn1b
entrez
12576
canonical
uniprot
P46414
canonical
ensembl
ENSMUSG00000003031
resolver
ensp
ENSMUSP00000003115
resolver
ensp
ENSMUSP00000065832
resolver
ensp
ENSMUSP00000145056
resolver
enst
ENSMUST00000003115
resolver
enst
ENSMUST00000067327
resolver
enst
ENSMUST00000204807
resolver
genesymbol
Cdkn1b
resolver
uniprot
Q8BG74
resolver
uniprot_entry
CDN1B_MOUSE
resolver
uniprot_sec
Q8BG74
resolver
amino_acid_sequence
MSNVRVSNGSPSLERMDARQAEHPKPSACRNLFGPVNHEELTRDLEKHCRDMEEASQRKWNFDFQNHKPLEGRYEWQEVERGSLPEFYYRPPRPPKSACKVLAQESQDVSGSRQAVPLIGSQANSEDRHLVDQMPDSSDNPAGLAEQCPGMRKRPAAEDSSSQNKRANRTEENVSDGSPNAGTVEQTPKKPGLRRQT
uniprot
proteins
function
FUNCTION: Important regulator of cell cycle progression (PubMed:12972555, PubMed:8033213). Inhibits the kinase activity of CDK2 bound to cyclin A, but has little inhibitory activity on CDK2 bound to SPDYA (By similarity). Involved in G1 arrest. Potent inhibitor of cyclin E- and cyclin A-CDK2 complexes (PubMed:8033213). Forms a complex with cyclin type D-CDK4 complexes and is involved in the assembly, stability, and modulation of CCND1-CDK4 complex activation. Acts either as an inhibitor or an activator of cyclin type D-CDK4 complexes depending on its phosphorylation state and/or stoichiometry. {ECO:0000250|UniProtKB:P46527, ECO:0000269|PubMed:12093740, ECO:0000269|PubMed:12972555, ECO:0000269|PubMed:15528185, ECO:0000269|PubMed:20228253, ECO:0000269|PubMed:8033213, ECO:0000269|PubMed:9399644}.
uniprot
proteins
mass_dalton
22193
uniprot
proteins
mutagenesis
MUTAGEN 10; /note="S->A: Loss of phosphorylation in G(0) phase. No change in cMYC-induced CDK2-mediated phosphorylation. Rapid dissociation from the cyclin E/CDK2 complex after induction by cMYC. Loss of protein stability in G(0) phase. No change in protein stability at S-phase."; /evidence="ECO:0000269|PubMed:15528185, ECO:0000269|PubMed:9399644"; MUTAGEN 90; /note="R->G: Loss of interaction with NUP50. No cyclin E-mediated degradation of phosphorylated p27KIP1."; /evidence="ECO:0000269|PubMed:10811608"; MUTAGEN 187; /note="T->E: Loss of cMyc-induced CDK2-mediated phosphorylation. Rapid dissociation from the cyclin E/CDK2 complex after induction by c-Myc."; /evidence="ECO:0000269|PubMed:9399644"; MUTAGEN 187; /note="T->V: Loss of cMYC-induced CDK2-mediated phosphorylation Dissociates very slowly from the cyclin E/CDK2 complex after induction by cMYC. Cell cycle arrest."; /evidence="ECO:0000269|PubMed:9399644
uniprot
proteins
post_translational_modification
PTM: Phosphorylated; phosphorylation occurs on serine, threonine and tyrosine residues. Phosphorylation on Ser-10 is the major site of phosphorylation in resting cells, takes place at the G(0)-G(1) phase and leads to protein stability. Phosphorylation on other sites is greatly enhanced by mitogens, growth factors, MYC and in certain cancer cell lines. The phosphorylated form found in the cytoplasm is inactivate. Phosphorylation on Thr-197 is required for interaction with 14-3-3 proteins. Phosphorylation on Thr-187, by CDK1 and CDK2 leads to protein ubiquitination and proteasomal degradation. Tyrosine phosphorylation promotes this process. Phosphorylation by PKB/AKT1 can be suppressed by LY294002, an inhibitor of the catalytic subunit of PI3K. Phosphorylation on Tyr-88 and Tyr-89 has no effect on binding CDK2, but is required for binding CDK4. Dephosphorylated on tyrosine residues by G-CSF (By similarity). Dephosphorylated on Thr-187 by PPM1H, leading to CDKN1B stability (By similarity). {ECO:0000250|UniProtKB:P46527}.; PTM: Ubiquitinated; in the cytoplasm by the KPC complex (composed of RNF123/KPC1 and UBAC1/KPC2) and, in the nucleus, by SCF(SKP2). The latter requires prior phosphorylation on Thr-187. Ubiquitinated; by a TRIM21-containing SCF(SKP2)-like complex; leads to its degradation (By similarity). {ECO:0000250}.; PTM: Subject to degradation in the lysosome. Interaction with SNX6 promotes lysosomal degradation.
uniprot
proteins
protein_family
CDI family
uniprot
proteins
pubmed
10086358
uniprot
proteins
pubmed
10811608
uniprot
proteins
pubmed
12093740
uniprot
proteins
pubmed
12972555
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15528185
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19767775
uniprot
proteins
pubmed
20228253
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23707388
uniprot
proteins
pubmed
8033212
uniprot
proteins
pubmed
8033213
uniprot
proteins
pubmed
8534916
uniprot
proteins
pubmed
9399644
uniprot
proteins
sequence_length
197
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Endosome {ECO:0000269|PubMed:20228253}. Note=Nuclear and cytoplasmic in quiescent cells. AKT- or RSK-mediated phosphorylation on Thr-197, binds 14-3-3, translocates to the cytoplasm and promotes cell cycle progression. Mitogen-activated UHMK1 phosphorylation on Ser-10 also results in translocation to the cytoplasm and cell cycle progression. Phosphorylation on Ser-10 facilitates nuclear export. Translocates to the nucleus on phosphorylation of Tyr-88 and Tyr-89 (By similarity). Colocalizes at the endosome with SNX6; this leads to lysosomal degradation (PubMed:20228253). {ECO:0000250, ECO:0000269|PubMed:20228253}.
uniprot
proteins