CDN1C_MOUSE
ID CDN1C_MOUSE Reviewed; 348 AA.
AC P49919; G3UW61;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Cyclin-dependent kinase inhibitor 1C;
DE AltName: Full=Cyclin-dependent kinase inhibitor p57;
DE AltName: Full=p57Kip2;
GN Name=Cdkn1c; Synonyms=Kip2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RX PubMed=7729683; DOI=10.1101/gad.9.6.639;
RA Lee M.-H., Reynisdottir I., Massague J.;
RT "Cloning of p57KIP2, a cyclin-dependent kinase inhibitor with unique domain
RT structure and tissue distribution.";
RL Genes Dev. 9:639-649(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 14-348.
RX PubMed=7729684; DOI=10.1101/gad.9.6.650;
RA Matsuoka S., Edwards M.C., Bai C., Parker S., Zhang P., Baldini A.,
RA Harper J.W., Elledge S.J.;
RT "p57KIP2, a structurally distinct member of the p21CIP1 Cdk inhibitor
RT family, is a candidate tumor suppressor gene.";
RL Genes Dev. 9:650-662(1995).
RN [5]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-109, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Potent tight-binding inhibitor of several G1 cyclin/CDK
CC complexes (cyclin E-CDK2, cyclin D2-CDK4, and cyclin A-CDK2) and, to
CC lesser extent, of the mitotic cyclin B-CDC2. Negative regulator of cell
CC proliferation. May play a role in maintenance of the non-proliferative
CC state throughout life.
CC -!- SUBUNIT: Interacts with PCNA. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=KIP2a; Synonyms=p57a;
CC IsoId=P49919-1; Sequence=Displayed;
CC Name=KIP2b; Synonyms=p57b;
CC IsoId=P49919-2; Sequence=VSP_000868;
CC -!- TISSUE SPECIFICITY: Expressed in the heart, brain, lung, skeletal
CC muscle, kidney, pancreas and testis. High levels are seen in the
CC placenta while low levels are seen in the liver.
CC -!- SIMILARITY: Belongs to the CDI family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U20553; AAC52186.1; -; mRNA.
DR EMBL; AC023248; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466531; EDL18208.1; -; Genomic_DNA.
DR EMBL; U22399; AAA85096.1; -; mRNA.
DR CCDS; CCDS22040.1; -. [P49919-2]
DR CCDS; CCDS52463.1; -. [P49919-1]
DR PIR; I49262; I49262.
DR RefSeq; NP_001155096.1; NM_001161624.1. [P49919-1]
DR RefSeq; NP_034006.3; NM_009876.4. [P49919-2]
DR RefSeq; XP_006508534.1; XM_006508471.3.
DR AlphaFoldDB; P49919; -.
DR BioGRID; 198653; 2.
DR ELM; P49919; -.
DR STRING; 10090.ENSMUSP00000128828; -.
DR iPTMnet; P49919; -.
DR PhosphoSitePlus; P49919; -.
DR MaxQB; P49919; -.
DR PaxDb; P49919; -.
DR PeptideAtlas; P49919; -.
DR PRIDE; P49919; -.
DR ProteomicsDB; 281356; -. [P49919-1]
DR ProteomicsDB; 281357; -. [P49919-2]
DR Antibodypedia; 972; 1164 antibodies from 41 providers.
DR DNASU; 12577; -.
DR Ensembl; ENSMUST00000037287; ENSMUSP00000037302; ENSMUSG00000037664. [P49919-2]
DR Ensembl; ENSMUST00000167912; ENSMUSP00000128828; ENSMUSG00000037664. [P49919-1]
DR GeneID; 12577; -.
DR KEGG; mmu:12577; -.
DR UCSC; uc009kpd.2; mouse. [P49919-1]
DR CTD; 1028; -.
DR MGI; MGI:104564; Cdkn1c.
DR VEuPathDB; HostDB:ENSMUSG00000037664; -.
DR eggNOG; KOG4743; Eukaryota.
DR GeneTree; ENSGT00940000162677; -.
DR HOGENOM; CLU_077692_0_0_1; -.
DR InParanoid; P49919; -.
DR OrthoDB; 1595421at2759; -.
DR TreeFam; TF101111; -.
DR Reactome; R-MMU-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-MMU-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-MMU-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-MMU-6804116; TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest.
DR Reactome; R-MMU-69202; Cyclin E associated events during G1/S transition.
DR Reactome; R-MMU-69231; Cyclin D associated events in G1.
DR Reactome; R-MMU-69563; p53-Dependent G1 DNA Damage Response.
DR Reactome; R-MMU-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR BioGRID-ORCS; 12577; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Cdkn1c; mouse.
DR PRO; PR:P49919; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P49919; protein.
DR Bgee; ENSMUSG00000037664; Expressed in humerus cartilage element and 263 other tissues.
DR ExpressionAtlas; P49919; baseline and differential.
DR Genevisible; P49919; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0004861; F:cyclin-dependent protein serine/threonine kinase inhibitor activity; IEA:InterPro.
DR GO; GO:0004860; F:protein kinase inhibitor activity; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0030325; P:adrenal gland development; IMP:MGI.
DR GO; GO:0007568; P:aging; IMP:MGI.
DR GO; GO:0043010; P:camera-type eye development; IMP:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0055123; P:digestive system development; IMP:MGI.
DR GO; GO:0060669; P:embryonic placenta morphogenesis; IMP:MGI.
DR GO; GO:0071514; P:genomic imprinting; IMP:MGI.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0030099; P:myeloid cell differentiation; IGI:MGI.
DR GO; GO:1904030; P:negative regulation of cyclin-dependent protein kinase activity; ISO:MGI.
DR GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISO:MGI.
DR GO; GO:0033673; P:negative regulation of kinase activity; ISO:MGI.
DR GO; GO:0045930; P:negative regulation of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0042326; P:negative regulation of phosphorylation; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0042551; P:neuron maturation; IMP:MGI.
DR GO; GO:0001890; P:placenta development; IMP:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; ISO:MGI.
DR GO; GO:0007096; P:regulation of exit from mitosis; IGI:MGI.
DR GO; GO:1902746; P:regulation of lens fiber cell differentiation; IGI:MGI.
DR GO; GO:0001501; P:skeletal system development; IMP:MGI.
DR GO; GO:0060065; P:uterus development; IMP:MGI.
DR Gene3D; 4.10.365.10; -; 1.
DR InterPro; IPR003175; CDI_dom.
DR InterPro; IPR044898; CDI_dom_sf.
DR InterPro; IPR029842; CDKN1C.
DR PANTHER; PTHR10265:SF44; PTHR10265:SF44; 1.
DR Pfam; PF02234; CDI; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Methylation; Nucleus;
KW Protein kinase inhibitor; Reference proteome.
FT CHAIN 1..348
FT /note="Cyclin-dependent kinase inhibitor 1C"
FT /id="PRO_0000190088"
FT REGION 115..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 309..312
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 146..160
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..270
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 109
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 1..13
FT /note="Missing (in isoform KIP2b)"
FT /evidence="ECO:0000305"
FT /id="VSP_000868"
FT CONFLICT 150..151
FT /note="EP -> DA (in Ref. 1; AAC52186)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 348 AA; 37372 MW; 100032B2F76BEC92 CRC64;
MGMSDVYLRS RTAMERLASS DTFPVIARSS ACRSLFGPVD HEELGRELRM RLAELNAEDQ
NRWDFNFQQD VPLRGPGRLQ WMEVDSESVP AFYRETVQVG RCRLQLGPRP PPVAVAVIPR
SGPPAGEAPD GLEEAPEQPP SAPASAVVAE PTPPATPAPA SDLTSDPIPE VTLVATSDPT
PDPIPDANPD VATRDGEEQV PEQVSEQGEE SGAEPGDELG TEPVSEQGEE QGAEPVEEKD
EEPEEEQGAE PVEEQGAEPV EEQNGEPVEE QDENQEQRGQ ELKDQPLSGI PGRPAPGTAA
ANANDFFAKR KRTAQENKAS NDVPPGCPSP NVAPGVGAVE QTPRKRLR
