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Cyclin-dependent kinase inhibitor 2A (Cyclin-dependent kinase 4 inhibitor A) (CDK4I) (p16-INK4a) (p16) (p16-INK4)

 CDN2A_RAT               Reviewed;         159 AA.
Q9R0Z3;
11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
12-AUG-2020, entry version 118.
RecName: Full=Cyclin-dependent kinase inhibitor 2A {ECO:0000312|RGD:2323};
AltName: Full=Cyclin-dependent kinase 4 inhibitor A;
Short=CDK4I;
AltName: Full=p16-INK4a;
Short=p16;
Short=p16-INK4;
Name=Cdkn2a {ECO:0000312|EMBL:AAL76338.1, ECO:0000312|RGD:2323};
Synonyms=P16ink4a {ECO:0000250|UniProtKB:P51480};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Rattus.
NCBI_TaxID=10116;
[1] {ECO:0000305, ECO:0000312|EMBL:AAD48924.1}
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=Fischer 344/N; TISSUE=Lung {ECO:0000312|EMBL:AAD48924.1};
PubMed=9032263; DOI=10.1128/mcb.17.3.1366;
Swafford D.S., Middleton S.K., Palmisano W.A., Nikula K.J., Tesfaigzi J.,
Baylin S.B., Herman J.G., Belinsky S.A.;
"Frequent aberrant methylation of p16INK4a in primary rat lung tumors.";
Mol. Cell. Biol. 17:1366-1374(1997).
[2] {ECO:0000312|EMBL:AAL76338.1}
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=ACI/SegHsd {ECO:0000312|EMBL:AAL76338.1},
Brown Norway/SsNHsd {ECO:0000312|EMBL:AAT92510.1}, and
COP {ECO:0000312|EMBL:AAL76339.1};
TISSUE=Spleen {ECO:0000312|EMBL:AAL76338.1};
Buckles L.K., Shull J.D.;
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
-!- 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 (By similarity). {ECO:0000250|UniProtKB:P51480}.
-!- SUBUNIT: Heterodimer with CDK4 or CDK6. Predominamt P16 complexes
contained CDK6. Interacts with CDK4 (both 'T-172'-phosphorylated and
non-phosphorylated forms); the interaction inhibits cyclin D-CDK4
kinase activity. Interacts with ISCO2 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Comment=Isoform 1 and isoform tumor suppressor ARF arise due to the
use of two alternative first exons joined to a common exon 2 at the
same acceptor site but in different reading frames, resulting in two
completely different isoforms. {ECO:0000250|UniProtKB:P51480};
Name=1 {ECO:0000269|PubMed:9032263}; Synonyms=p16INK4a
{ECO:0000250|UniProtKB:P51480};
IsoId=Q9R0Z3-1; Sequence=Displayed;
Name=tumor suppressor ARF {ECO:0000305}; Synonyms=p19ARF {ECO:0000305};
IsoId=Q8QZZ9-1; Sequence=External;
-!- TISSUE SPECIFICITY: Expressed in spleen, liver and lung. Not detected
in kidney, colon, stomach or brain. {ECO:0000269|PubMed:9032263}.
-!- PTM: Phosphorylation seems to increase interaction with CDK4.
{ECO:0000250}.
-!- MISCELLANEOUS: Down-regulated in a number of tumor cell lines in
response to methylation of the CpG island in exon 1.
{ECO:0000269|PubMed:9032263}.
-!- SIMILARITY: Belongs to the CDKN2 cyclin-dependent kinase inhibitor
family. {ECO:0000255}.
-!- CAUTION: The proteins described here are encoded by the gene CDKN2A,
but are completely unrelated in terms of sequence and function to tumor
suppressor ARF (AC Q8QZZ9) which is encoded by the same gene.
{ECO:0000305}.
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EMBL; L81167; AAD48924.1; -; mRNA.
EMBL; AF474976; AAL76338.1; -; mRNA.
EMBL; AF474977; AAL76339.1; -; mRNA.
EMBL; AY679728; AAT92510.1; -; mRNA.
RefSeq; NP_113738.1; NM_031550.1. [Q9R0Z3-1]
SMR; Q9R0Z3; -.
STRING; 10116.ENSRNOP00000061040; -.
PaxDb; Q9R0Z3; -.
PRIDE; Q9R0Z3; -.
GeneID; 25163; -.
KEGG; rno:25163; -.
CTD; 1029; -.
RGD; 2323; Cdkn2a.
eggNOG; KOG0504; Eukaryota.
KO; K06621; -.
OrthoDB; 1435166at2759; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0001652; C:granular component; ISO:RGD.
GO; GO:0005739; C:mitochondrion; ISO:RGD.
GO; GO:0005730; C:nucleolus; ISO:RGD.
GO; GO:0005654; C:nucleoplasm; ISO:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0032991; C:protein-containing complex; ISO:RGD.
GO; GO:0035985; C:senescence-associated heterochromatin focus; ISO:RGD.
GO; GO:0004861; F:cyclin-dependent protein serine/threonine kinase inhibitor activity; ISO:RGD.
GO; GO:0097718; F:disordered domain specific binding; ISO:RGD.
GO; GO:0097371; F:MDM2/MDM4 family protein binding; ISO:RGD.
GO; GO:0051059; F:NF-kappaB binding; ISO:RGD.
GO; GO:0002039; F:p53 binding; ISO:RGD.
GO; GO:0019901; F:protein kinase binding; ISO:RGD.
GO; GO:0047485; F:protein N-terminus binding; ISO:RGD.
GO; GO:0019789; F:SUMO transferase activity; ISO:RGD.
GO; GO:0008134; F:transcription factor binding; ISO:RGD.
GO; GO:1990948; F:ubiquitin ligase inhibitor activity; ISO:RGD.
GO; GO:0055105; F:ubiquitin-protein transferase inhibitor activity; ISO:RGD.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:RGD.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:1990000; P:amyloid fibril formation; ISO:RGD.
GO; GO:0008637; P:apoptotic mitochondrial changes; ISO:RGD.
GO; GO:0000422; P:autophagy of mitochondrion; ISO:RGD.
GO; GO:0007569; P:cell aging; ISO:RGD.
GO; GO:0007050; P:cell cycle arrest; ISO:RGD.
GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD.
GO; GO:0070301; P:cellular response to hydrogen peroxide; ISO:RGD.
GO; GO:0090398; P:cellular senescence; ISO:RGD.
GO; GO:0021549; P:cerebellum development; IEP:RGD.
GO; GO:0008544; P:epidermis development; ISO:RGD.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISO:RGD.
GO; GO:0042593; P:glucose homeostasis; ISO:RGD.
GO; GO:0051882; P:mitochondrial depolarization; ISO:RGD.
GO; GO:0030889; P:negative regulation of B cell proliferation; ISO:RGD.
GO; GO:0045786; P:negative regulation of cell cycle; ISO:RGD.
GO; GO:0030308; P:negative regulation of cell growth; ISO:RGD.
GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
GO; GO:0001953; P:negative regulation of cell-matrix adhesion; ISO:RGD.
GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; ISO:RGD.
GO; GO:2000346; P:negative regulation of hepatocyte proliferation; IMP:RGD.
GO; GO:0033088; P:negative regulation of immature T cell proliferation in thymus; ISO:RGD.
GO; GO:0033600; P:negative regulation of mammary gland epithelial cell proliferation; ISO:RGD.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISO:RGD.
GO; GO:0042326; P:negative regulation of phosphorylation; ISO:RGD.
GO; GO:0032091; P:negative regulation of protein binding; ISO:RGD.
GO; GO:0006469; P:negative regulation of protein kinase activity; ISO:RGD.
GO; GO:2000435; P:negative regulation of protein neddylation; ISO:RGD.
GO; GO:1903051; P:negative regulation of proteolysis involved in cellular protein catabolic process; ISO:RGD.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
GO; GO:1904667; P:negative regulation of ubiquitin protein ligase activity; ISO:RGD.
GO; GO:2000059; P:negative regulation of ubiquitin-dependent protein catabolic process; ISO:RGD.
GO; GO:0051444; P:negative regulation of ubiquitin-protein transferase activity; ISO:RGD.
GO; GO:0022008; P:neurogenesis; IEP:RGD.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
GO; GO:0060058; P:positive regulation of apoptotic process involved in mammary gland involution; ISO:RGD.
GO; GO:0071158; P:positive regulation of cell cycle arrest; ISO:RGD.
GO; GO:2000774; P:positive regulation of cellular senescence; ISO:RGD.
GO; GO:0043517; P:positive regulation of DNA damage response, signal transduction by p53 class mediator; ISO:RGD.
GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:RGD.
GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
GO; GO:2000111; P:positive regulation of macrophage apoptotic process; ISO:RGD.
GO; GO:1900182; P:positive regulation of protein localization to nucleus; ISO:RGD.
GO; GO:0033235; P:positive regulation of protein sumoylation; ISO:RGD.
GO; GO:1901798; P:positive regulation of signal transduction by p53 class mediator; ISO:RGD.
GO; GO:0034393; P:positive regulation of smooth muscle cell apoptotic process; ISO:RGD.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
GO; GO:0031648; P:protein destabilization; ISO:RGD.
GO; GO:0070534; P:protein K63-linked ubiquitination; ISO:RGD.
GO; GO:0000209; P:protein polyubiquitination; ISO:RGD.
GO; GO:0050821; P:protein stabilization; ISO:RGD.
GO; GO:0007265; P:Ras protein signal transduction; ISO:RGD.
GO; GO:1902510; P:regulation of apoptotic DNA fragmentation; ISO:RGD.
GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; ISO:RGD.
GO; GO:0051090; P:regulation of DNA-binding transcription factor activity; ISO:RGD.
GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; ISO:RGD.
GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
GO; GO:0046822; P:regulation of nucleocytoplasmic transport; ISO:RGD.
GO; GO:0046825; P:regulation of protein export from nucleus; ISO:RGD.
GO; GO:0031647; P:regulation of protein stability; ISO:RGD.
GO; GO:1903214; P:regulation of protein targeting to mitochondrion; ISO:RGD.
GO; GO:0090399; P:replicative senescence; ISO:RGD.
GO; GO:0061771; P:response to caloric restriction; IEP:RGD.
GO; GO:0042493; P:response to drug; IDA:RGD.
GO; GO:0070542; P:response to fatty acid; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IDA:RGD.
GO; GO:0010033; P:response to organic substance; IEP:RGD.
GO; GO:0010243; P:response to organonitrogen compound; IDA:RGD.
GO; GO:0009651; P:response to salt stress; IEP:RGD.
GO; GO:0009303; P:rRNA transcription; ISO:RGD.
GO; GO:0035986; P:senescence-associated heterochromatin focus assembly; ISO:RGD.
GO; GO:0048103; P:somatic stem cell division; ISO:RGD.
GO; GO:0035019; P:somatic stem cell population maintenance; ISO:RGD.
Gene3D; 1.25.40.20; -; 1.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
SMART; SM00248; ANK; 4.
SUPFAM; SSF48403; SSF48403; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
2: Evidence at transcript level;
Alternative splicing; ANK repeat; Cell cycle; Cytoplasm; Nucleus;
Phosphoprotein; Reference proteome; Repeat; Tumor suppressor.
CHAIN 1..159
/note="Cyclin-dependent kinase inhibitor 2A"
/id="PRO_0000144179"
REPEAT 3..35
/note="ANK 1"
/evidence="ECO:0000255"
REPEAT 36..64
/note="ANK 2"
/evidence="ECO:0000255"
REPEAT 69..98
/note="ANK 3"
/evidence="ECO:0000255"
REPEAT 102..134
/note="ANK 4"
/evidence="ECO:0000255"
MOD_RES 143
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P42771"
SEQUENCE 159 AA; 17366 MW; 3C4CA920A1FEAEB6 CRC64;
MESSADRLAR AAALGREHEV RALLEAGASP NAPNTFGRTP IQVMMMGNVK VAALLLSYGA
DSNCEDPTTL SRPVHDAARE GFLDTLVVLH QAGARLDVRD AWGRLPLDLA LERGHHDVVR
YLRYLLSSAG NVSRVTDRHN FCSSTPRCLG LRGQPPKQR


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