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 24-JAN-2024, entry version 155. 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; 10090-ENSMUSP00000128828; -. DR PeptideAtlas; P49919; -. DR ProteomicsDB; 281356; -. [P49919-1] DR ProteomicsDB; 281357; -. [P49919-2] DR Antibodypedia; 972; 1300 antibodies from 41 providers. DR DNASU; 12577; -. DR Ensembl; ENSMUST00000037287.8; ENSMUSP00000037302.7; ENSMUSG00000037664.14. [P49919-2] DR Ensembl; ENSMUST00000167912.9; ENSMUSP00000128828.2; ENSMUSG00000037664.14. [P49919-1] DR GeneID; 12577; -. DR KEGG; mmu:12577; -. DR UCSC; uc009kpd.2; mouse. [P49919-1] DR AGR; MGI:104564; -. 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; 2900553at2759; -. DR TreeFam; TF101111; -. DR Reactome; R-MMU-69231; Cyclin D associated events in G1. DR BioGRID-ORCS; 12577; 0 hits in 78 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 266 other cell types or tissues. DR ExpressionAtlas; P49919; baseline and differential. 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:0140678; F:molecular function inhibitor activity; ISO:MGI. 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: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:0045892; P:negative regulation of DNA-templated transcription; ISO:MGI. DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; 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:0042551; P:neuron maturation; IMP:MGI. DR GO; GO:0001890; P:placenta development; IMP:MGI. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; 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; p27; 1. DR InterPro; IPR003175; CDI_dom. DR InterPro; IPR044898; CDI_dom_sf. DR PANTHER; PTHR10265; CYCLIN-DEPENDENT KINASE INHIBITOR 1; 1. DR PANTHER; PTHR10265:SF44; CYCLIN-DEPENDENT KINASE INHIBITOR 1C; 1. DR Pfam; PF02234; CDI; 1. DR Genevisible; P49919; MM. 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 //