ID CENPC_MOUSE Reviewed; 906 AA. AC P49452; B9EK81; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 04-NOV-2026, entry version 163. DE RecName: Full=Centromere protein C; DE Short=CENP-C; DE AltName: Full=Centromere autoantigen C; DE AltName: Full=Centromere protein C 1; DE Short=CENP-C 1; GN Name=Cenpc; Synonyms=Cenpc1; 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 STRAIN=SWR/J; RX PubMed=7959789; DOI=10.1006/geno.1994.1342; RA McKay S., Thomson E., Cooke H.; RT "Sequence homologies and linkage group conservation of the human and mouse RT Cenpc genes."; RL Genomics 22:36-40(1994). RN [2] 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 AND SER-363, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Spleen; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [5] RP INTERACTION WITH MEIKIN. RX PubMed=25533956; DOI=10.1038/nature14097; RA Kim J., Ishiguro K., Nambu A., Akiyoshi B., Yokobayashi S., Kagami A., RA Ishiguro T., Pendas A.M., Takeda N., Sakakibara Y., Kitajima T.S., RA Tanno Y., Sakuno T., Watanabe Y.; RT "Meikin is a conserved regulator of meiosis-I-specific kinetochore RT function."; RL Nature 517:466-471(2015). RN [6] RP INTERACTION WITH FBX047. RX PubMed=39244596; DOI=10.1038/s42003-024-06782-6; RA Ma A., Yang Y., Cao L., Chen L., Zhang J.V.; RT "FBXO47 regulates centromere pairing as key component of centromeric SCF E3 RT ligase in mouse spermatocytes."; RL Commun. Biol. 7:1099-1099(2024). CC -!- FUNCTION: Component of the CENPA-NAC (nucleosome-associated) complex, a CC complex that plays a central role in assembly of kinetochore proteins, CC mitotic progression and chromosome segregation. The CENPA-NAC complex CC recruits the CENPA-CAD (nucleosome distal) complex and may be involved CC in incorporation of newly synthesized CENPA into centromeres. CENPC CC recruits DNA methylation and DNMT3B to both centromeric and CC pericentromeric satellite repeats and regulates the histone code in CC these regions. {ECO:0000250|UniProtKB:Q03188}. CC -!- SUBUNIT: Oligomer. Component of the CENPA-NAC complex, at least CC composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU. The CC CENPA-NAC complex interacts with the CENPA-CAD complex, composed of CC CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. Binds to CC DAXX. Interacts with DNMT3B. Interacts directly with CENPA. Identified CC in a centromere complex containing histones H2A, H2B and H4, and at CC least CENPA, CENPB, CENPC, CENPT, CENPN, HJURP, SUPT16H, SSRP1 and RSF1 CC (By similarity). Interacts with MEIKIN (PubMed:25533956). Interacts CC with FBX047 (PubMed:39244596). {ECO:0000250|UniProtKB:Q03188, CC ECO:0000269|PubMed:25533956, ECO:0000269|PubMed:39244596}. CC -!- INTERACTION: CC P49452; Q5F2C3: Meikin; NbExp=5; IntAct=EBI-1186252, EBI-20739301; CC P49452; O08586: Pten; NbExp=2; IntAct=EBI-1186252, EBI-1186266; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q03188}. CC Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q03188}. CC Chromosome, centromere {ECO:0000250|UniProtKB:Q03188}. Note=Localizes CC exclusively in the kinetochore domain of centromeres. CC {ECO:0000250|UniProtKB:Q03188}. CC -!- DOMAIN: The MIF2 homology domain II targets centromeres and binds the CC alpha satellite DNA in vivo. The MIF2 homology domain III can induce CC CENPC dimerization/oligomerization. {ECO:0000250|UniProtKB:Q03188}. CC -!- SIMILARITY: Belongs to the CENP-C/MIF2 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; U03113; AAC04314.1; -; mRNA. DR EMBL; CH466524; EDL37951.1; -; Genomic_DNA. DR EMBL; BC150700; AAI50701.1; -; mRNA. DR CCDS; CCDS39123.1; -. DR PIR; A54654; A54654. DR RefSeq; NP_001332831.1; NM_001345902.1. DR RefSeq; NP_001332832.1; NM_001345903.1. DR RefSeq; NP_001332833.1; NM_001345904.1. DR RefSeq; NP_031709.2; NM_007683.4. DR AlphaFoldDB; P49452; -. DR SMR; P49452; -. DR BioGRID; 198676; 3. DR ComplexPortal; CPX-5704; Kinetochore CCAN complex. DR FunCoup; P49452; 2313. DR IntAct; P49452; 167. DR STRING; 10090.ENSMUSP00000031170; -. DR iPTMnet; P49452; -. DR PhosphoSitePlus; P49452; -. DR jPOST; P49452; -. DR PaxDb; 10090-ENSMUSP00000031170; -. DR PeptideAtlas; P49452; -. DR ProteomicsDB; 280059; -. DR Pumba; P49452; -. DR Antibodypedia; 6105; 269 antibodies from 35 providers. DR DNASU; 12617; -. DR Ensembl; ENSMUST00000031170.10; ENSMUSP00000031170.9; ENSMUSG00000029253.13. DR GeneID; 12617; -. DR KEGG; mmu:12617; -. DR UCSC; uc008xxc.2; mouse. DR AGR; MGI:99700; -. DR CTD; 12617; -. DR MGI; MGI:99700; Cenpc1. DR VEuPathDB; HostDB:ENSMUSG00000029253; -. DR eggNOG; ENOG502RYQH; Eukaryota. DR GeneTree; ENSGT00390000016737; -. DR HOGENOM; CLU_013594_0_0_1; -. DR InParanoid; P49452; -. DR OMA; AASGLXQ; -. DR OrthoDB; 1939643at2759; -. DR PhylomeDB; P49452; -. DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal. DR Reactome; R-MMU-2467813; Separation of Sister Chromatids. DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion. DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins. DR Reactome; R-MMU-606279; Deposition of new CENPA-containing nucleosomes at the centromere. DR Reactome; R-MMU-68877; Mitotic Prometaphase. DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation. DR BioGRID-ORCS; 12617; 18 hits in 116 CRISPR screens. DR PRO; PR:P49452; -. DR Proteomes; UP000000589; Chromosome 5. DR RNAct; P49452; protein. DR Bgee; ENSMUSG00000029253; Expressed in pharyngeal arch 2 and 253 other cell types or tissues. DR GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:MGI. DR GO; GO:0000939; C:inner kinetochore; ISO:GO_Central. DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB. DR GO; GO:0016604; C:nuclear body; ISO:GO_Central. DR GO; GO:0005654; C:nucleoplasm; ISO:GO_Central. DR GO; GO:0005634; C:nucleus; ISO:GO_Central. DR GO; GO:0005721; C:pericentric heterochromatin; IDA:MGI. DR GO; GO:0019237; F:centromeric DNA binding; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; ISO:GO_Central. DR GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; IBA:GO_Central. DR GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB. DR GO; GO:0051382; P:kinetochore assembly; ISS:UniProtKB. DR GO; GO:0000278; P:mitotic cell cycle; ISS:UniProtKB. DR FunFam; 2.60.120.10:FF:000033; Centromere protein C 1; 1. DR Gene3D; 2.60.120.10; Jelly Rolls; 1. DR InterPro; IPR028386; CENP-C/Mif2/cnp3. DR InterPro; IPR028931; CENP-C_mid. DR InterPro; IPR028052; CENP-C_N_dom. DR InterPro; IPR025974; Mif2/CENP-C_cupin. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR011051; RmlC_Cupin_sf. DR PANTHER; PTHR16684; CENTROMERE PROTEIN C; 1. DR PANTHER; PTHR16684:SF11; CENTROMERE PROTEIN C; 1. DR Pfam; PF11699; CENP-C_C; 1. DR Pfam; PF15620; CENP-C_mid; 1. DR Pfam; PF15622; CENP_C_N; 1. DR SUPFAM; SSF51182; RmlC-like cupins; 1. PE 1: Evidence at protein level; KW Cell cycle; Cell division; Centromere; Chromosome; DNA-binding; KW Isopeptide bond; Kinetochore; Mitosis; Nucleus; Phosphoprotein; KW Reference proteome; Ubl conjugation. FT CHAIN 1..906 FT /note="Centromere protein C" FT /id="PRO_0000089475" FT REGION 56..115 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 141..169 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 197..224 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 294..320 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 341..596 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 623..671 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 702..724 FT /note="MIF2 homology domain II" FT /evidence="ECO:0000250" FT REGION 853..906 FT /note="MIF2 homology domain III" FT /evidence="ECO:0000250" FT MOTIF 228..242 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT MOTIF 449..466 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT MOTIF 525..540 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT MOTIF 744..762 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT COMPBIAS 56..74 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 87..96 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 97..108 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 202..212 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 402..424 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 426..450 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 465..474 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 481..494 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 496..512 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 523..546 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 626..637 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 71 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q03188" FT MOD_RES 94 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q03188" FT MOD_RES 302 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q03188" FT MOD_RES 344 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 363 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 404 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q03188" FT MOD_RES 495 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q03188" FT MOD_RES 505 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q03188" FT MOD_RES 647 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q03188" FT MOD_RES 673 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q03188" FT MOD_RES 728 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q03188" FT MOD_RES 737 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q03188" FT CROSSLNK 150 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q03188" FT CROSSLNK 182 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q03188" FT CROSSLNK 229 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q03188" FT CROSSLNK 240 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q03188" FT CROSSLNK 242 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q03188" FT CROSSLNK 266 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q03188" FT CROSSLNK 501 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q03188" FT CROSSLNK 640 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q03188" FT CROSSLNK 692 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q03188" FT CROSSLNK 770 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q03188" FT CONFLICT 3 FT /note="S -> M (in Ref. 1; AAC04314)" FT /evidence="ECO:0000305" FT CONFLICT 185 FT /note="L -> S (in Ref. 1; AAC04314)" FT /evidence="ECO:0000305" FT CONFLICT 418 FT /note="K -> T (in Ref. 1; AAC04314)" FT /evidence="ECO:0000305" FT CONFLICT 450 FT /note="K -> R (in Ref. 1; AAC04314)" FT /evidence="ECO:0000305" FT CONFLICT 488 FT /note="C -> R (in Ref. 1; AAC04314)" FT /evidence="ECO:0000305" SQ SEQUENCE 906 AA; 102154 MW; 0DCFE76496B33946 CRC64; MASFHLDHLK NYHRRYCRSS RAPNIHTKKG QNMLEILQDC FEDQSKASFL DDFTESLTSS TQKKKANYSQ SSSKKCPESH SKPVPVSSRT GEASLQASAE PSEAAGGSVQ ANEVHHGASD ELDLCVGSPV VLLDANVNTL QKAASPAGQK RVASVSRSPV DRQASNKNIS FKTRKRLNFE DKVTLSTAET ENSVLQVEDN LSKGQEGTSS EITQKRDDLS SDVQSRSKKN FSELFLETVK RKSKSSSVVR HTAAVPFSPP PPSDMKLLED EFIIDRSDRS FSSRLWVMIP SKDRHLSAHK PSPENTALLQ GKKSREKSHS LSAMTFARNT QSDKAHPIEE AQLSVEENPA TTCTDELEND CRSPENKMQS ETAKTPPAWE RTTKQSQRRV SKPKAAEELR KGQSSWENSN VSNTGQDKLQ INSKRNMKDC EEVRNEPNPK KQKPALENKK KTNSTQTNKE KSGKKFFSGG SKNKFVPKKV TLTSRRSCRI SQRPSEWWRV KSDESSVDRN PSKENNSPVV YPNKKKQTKR NHVSKRAGKK PGSSKRQKTE MSPRVQKSLN VKDSGGTVSG HDDTSRSQRK PLKIIEADPT QKSLAISRPK RGCKYRNNVM TSPNVHLKSH TEEYTSKTQM ESASNSEMSK RSVWEESGPS RFKNYEMPGS SNSEMGDEQD QKSLHFTTRS FNMVPDKKLH HKLVLPSNSP NVRRSNRIRL KPLEYWRGER VDYQESSSGQ LVLEIISPSS VPTKIKAQRN LGKVNKKVTK KPTHLNSHEK AKMELPLDMR LGDPFQATLA KDPETAELVP MDLIRPRDTY RFFVEQHGLK VFKTLDTIYF STGKLVLGPY EEKGKQHVGQ DILVFYVNFG DLLCTLHETP YKLTTGDSFY VPSGNHYNIK NLLNVESSLL FTQIKR //