CENPC_MOUSE
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 03-AUG-2022, entry version 144.
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).
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).
CC {ECO:0000250|UniProtKB:Q03188, ECO:0000269|PubMed:25533956}.
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}.
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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 ComplexPortal; CPX-5704; Kinetochore CCAN complex.
DR IntAct; P49452; 167.
DR MINT; P49452; -.
DR STRING; 10090.ENSMUSP00000031170; -.
DR iPTMnet; P49452; -.
DR PhosphoSitePlus; P49452; -.
DR EPD; P49452; -.
DR jPOST; P49452; -.
DR MaxQB; P49452; -.
DR PaxDb; P49452; -.
DR PeptideAtlas; P49452; -.
DR PRIDE; P49452; -.
DR ProteomicsDB; 280059; -.
DR Antibodypedia; 6105; 239 antibodies from 31 providers.
DR DNASU; 12617; -.
DR Ensembl; ENSMUST00000031170; ENSMUSP00000031170; ENSMUSG00000029253.
DR GeneID; 12617; -.
DR KEGG; mmu:12617; -.
DR UCSC; uc008xxc.2; mouse.
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; NFEDKDI; -.
DR OrthoDB; 215502at2759; -.
DR PhylomeDB; P49452; -.
DR TreeFam; TF101132; -.
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; 17 hits in 110 CRISPR screens.
DR PRO; PR:P49452; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P49452; protein.
DR Bgee; ENSMUSG00000029253; Expressed in pharyngeal arch 2 and 250 other tissues.
DR Genevisible; P49452; MM.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:MGI.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0030496; C:midbody; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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:MGI.
DR GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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 GO; GO:0051455; P:monopolar spindle attachment to meiosis I kinetochore; IBA:GO_Central.
DR Gene3D; 2.60.120.10; -; 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; PTHR16684; 2.
DR Pfam; PF11699; CENP-C_C; 1.
DR Pfam; PF15620; CENP-C_mid; 1.
DR Pfam; PF15622; CENP_C_N; 2.
DR SUPFAM; SSF51182; SSF51182; 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..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..510
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..542
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..643
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
