CENPC_HUMAN
ID CENPC_HUMAN Reviewed; 943 AA.
AC Q03188; Q6PIR0; Q8IW27; Q9P0M5;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 184.
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;
DE AltName: Full=Interphase centromere complex protein 7;
GN Name=CENPC; Synonyms=CENPC1, ICEN7;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS PHE-341 AND ASP-389.
RC TISSUE=Placenta;
RX PubMed=1339310; DOI=10.1016/0092-8674(92)90538-n;
RA Saitoh H., Tomkiel J., Cooke C.A., Ratrie H. III, Maurer M.,
RA Rothfield N.F., Earnshaw W.C.;
RT "CENP-C, an autoantigen in scleroderma, is a component of the human inner
RT kinetochore plate.";
RL Cell 70:115-125(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PHE-341.
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT PHE-341.
RC TISSUE=Blood, and Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RA Poppe M., Botz J., Hahm B., Dobat K., Eickelbaum W., Paweletz N., Arand M.,
RA Knehr M.;
RT "Promoter characterization of centromere protein C reveals its
RT participation in cell cycle regulation in late G1-phase and expression
RT control by E2F-1, pRb, p107 and Sp-1.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH DAXX, AND SUBCELLULAR LOCATION.
RX PubMed=9645950; DOI=10.1242/jcs.111.14.2029;
RA Pluta A.F., Earnshaw W.C., Goldberg I.G.;
RT "Interphase-specific association of intrinsic centromere protein CENP-C
RT with HDaxx, a death domain-binding protein implicated in Fas-mediated cell
RT death.";
RL J. Cell Sci. 111:2029-2041(1998).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16716197; DOI=10.1111/j.1365-2443.2006.00969.x;
RA Izuta H., Ikeno M., Suzuki N., Tomonaga T., Nozaki N., Obuse C., Kisu Y.,
RA Goshima N., Nomura F., Nomura N., Yoda K.;
RT "Comprehensive analysis of the ICEN (Interphase Centromere Complex)
RT components enriched in the CENP-A chromatin of human cells.";
RL Genes Cells 11:673-684(2006).
RN [9]
RP IDENTIFICATION IN THE CENPA-NAC COMPLEX WITH CENPA; CENPH; CENPM; CENPN;
RP CENPT AND CENPU.
RX PubMed=16622419; DOI=10.1038/ncb1397;
RA Foltz D.R., Jansen L.E.T., Black B.E., Bailey A.O., Yates J.R. III,
RA Cleveland D.W.;
RT "The human CENP-A centromeric nucleosome-associated complex.";
RL Nat. Cell Biol. 8:458-469(2006).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=17651496; DOI=10.1186/gb-2007-8-7-r148;
RA Alonso A., Fritz B., Hasson D., Abrusan G., Cheung F., Yoda K.,
RA Radlwimmer B., Ladurner A.G., Warburton P.E.;
RT "Co-localization of CENP-C and CENP-H to discontinuous domains of CENP-A
RT chromatin at human neocentromeres.";
RL Genome Biol. 8:R148.1-R148.19(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261; SER-316 AND SER-773,
RP VARIANT [LARGE SCALE ANALYSIS] PHE-341, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP DOMAIN, SUBUNIT, AND INTERACTION WITH CENPA.
RX PubMed=19503796; DOI=10.1371/journal.pone.0005832;
RA Trazzi S., Perini G., Bernardoni R., Zoli M., Reese J.C., Musacchio A.,
RA Della Valle G.;
RT "The C-terminal domain of CENP-C displays multiple and critical functions
RT for mammalian centromere formation.";
RL PLoS ONE 4:E5832-E5832(2009).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH DNMT3B.
RX PubMed=19482874; DOI=10.1093/hmg/ddp256;
RA Gopalakrishnan S., Sullivan B.A., Trazzi S., Della Valle G.,
RA Robertson K.D.;
RT "DNMT3B interacts with constitutive centromere protein CENP-C to modulate
RT DNA methylation and the histone code at centromeric regions.";
RL Hum. Mol. Genet. 18:3178-3193(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146; THR-183; SER-189;
RP SER-538; SER-763 AND SER-773, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96; THR-130; SER-225;
RP SER-439; SER-538; THR-734; SER-763 AND SER-773, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21529714; DOI=10.1016/j.cell.2011.03.031;
RA Gascoigne K.E., Takeuchi K., Suzuki A., Hori T., Fukagawa T.,
RA Cheeseman I.M.;
RT "Induced ectopic kinetochore assembly bypasses the requirement for CENP-A
RT nucleosomes.";
RL Cell 145:410-422(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225; SER-439; SER-709 AND
RP SER-710, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73; THR-130; SER-316;
RP SER-333; SER-528; SER-538; SER-684 AND THR-734, VARIANT [LARGE SCALE
RP ANALYSIS] PHE-341, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP DEVELOPMENTAL STAGE.
RX PubMed=24522885; DOI=10.1098/rsob.130229;
RA Dornblut C., Quinn N., Monajambashi S., Prendergast L., van Vuuren C.,
RA Muench S., Deng W., Leonhardt H., Cardoso M.C., Hoischen C., Diekmann S.,
RA Sullivan K.F.;
RT "A CENP-S/X complex assembles at the centromere in S and G2 phases of the
RT human cell cycle.";
RL Open Biol. 4:130229-130229(2014).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-217, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [21]
RP SUBUNIT.
RX PubMed=27499292; DOI=10.1016/j.molcel.2016.06.023;
RA Roulland Y., Ouararhni K., Naidenov M., Ramos L., Shuaib M., Syed S.H.,
RA Lone I.N., Boopathi R., Fontaine E., Papai G., Tachiwana H., Gautier T.,
RA Skoufias D., Padmanabhan K., Bednar J., Kurumizaka H., Schultz P.,
RA Angelov D., Hamiche A., Dimitrov S.;
RT "The flexible ends of CENP-A nucleosome are required for mitotic
RT fidelity.";
RL Mol. Cell 63:674-685(2016).
RN [22]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-45; LYS-119; LYS-134; LYS-180;
RP LYS-212; LYS-238; LYS-260; LYS-271; LYS-273; LYS-297; LYS-440; LYS-534;
RP LYS-677; LYS-727 AND LYS-807, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
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:0000269|PubMed:19482874,
CC ECO:0000269|PubMed:21529714}.
CC -!- SUBUNIT: Oligomer. Component of the CENPA-NAC complex, at least
CC composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU
CC (PubMed:16622419). The CENPA-NAC complex interacts with the CENPA-CAD
CC complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR
CC and CENPS. Binds to DAXX (PubMed:9645950). Interacts with DNMT3B
CC (PubMed:19482874). Interacts directly with CENPA (PubMed:19503796).
CC Identified in a centromere complex containing histones H2A, H2B and H4,
CC and at least CENPA, CENPB, CENPC, CENPT, CENPN, HJURP, SUPT16H, SSRP1
CC and RSF1 (PubMed:27499292). Interacts with MEIKIN (By similarity).
CC {ECO:0000250|UniProtKB:P49452, ECO:0000269|PubMed:16622419,
CC ECO:0000269|PubMed:19482874, ECO:0000269|PubMed:19503796,
CC ECO:0000269|PubMed:27499292, ECO:0000269|PubMed:9645950}.
CC -!- INTERACTION:
CC Q03188; P49450: CENPA; NbExp=4; IntAct=EBI-295799, EBI-1751979;
CC Q03188; Q03188: CENPC; NbExp=4; IntAct=EBI-295799, EBI-295799;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17651496}.
CC Chromosome, centromere, kinetochore {ECO:0000269|PubMed:17651496,
CC ECO:0000269|PubMed:19482874, ECO:0000269|PubMed:21529714}. Chromosome,
CC centromere {ECO:0000269|PubMed:9645950}. Note=Localizes exclusively in
CC the kinetochore domain of centromeres. {ECO:0000269|PubMed:21529714}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q03188-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q03188-2; Sequence=VSP_057280, VSP_057281;
CC -!- DEVELOPMENTAL STAGE: Expression varies across the cell cycle, with high
CC levels in G2 phase (at the mRNA level). {ECO:0000269|PubMed:24522885}.
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:0000269|PubMed:19503796}.
CC -!- SIMILARITY: Belongs to the CENP-C/MIF2 family. {ECO:0000305}.
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DR EMBL; M95724; AAA51974.1; -; mRNA.
DR EMBL; AC104806; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC109356; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471057; EAX05545.1; -; Genomic_DNA.
DR EMBL; BC030695; AAH30695.1; -; mRNA.
DR EMBL; BC041117; AAH41117.1; -; mRNA.
DR EMBL; AF151723; AAF73191.1; -; Genomic_DNA.
DR CCDS; CCDS47063.1; -. [Q03188-1]
DR PIR; A42681; A42681.
DR RefSeq; NP_001803.2; NM_001812.2. [Q03188-1]
DR PDB; 5LSJ; X-ray; 3.25 A; P/Q=1-71.
DR PDB; 5LSK; X-ray; 3.50 A; P=1-71.
DR PDB; 6MUO; EM; 3.60 A; K/L=518-537.
DR PDB; 6MUP; EM; 3.50 A; K/L=518-537.
DR PDB; 6SE6; EM; 3.50 A; V=426-537.
DR PDB; 6SEE; EM; 4.20 A; V=426-537.
DR PDB; 6SEF; EM; 3.70 A; V=426-537.
DR PDBsum; 5LSJ; -.
DR PDBsum; 5LSK; -.
DR PDBsum; 6MUO; -.
DR PDBsum; 6MUP; -.
DR PDBsum; 6SE6; -.
DR PDBsum; 6SEE; -.
DR PDBsum; 6SEF; -.
DR AlphaFoldDB; Q03188; -.
DR SMR; Q03188; -.
DR BioGRID; 107489; 105.
DR ComplexPortal; CPX-5646; Kinetochore CCAN complex.
DR CORUM; Q03188; -.
DR IntAct; Q03188; 57.
DR MINT; Q03188; -.
DR STRING; 9606.ENSP00000273853; -.
DR iPTMnet; Q03188; -.
DR PhosphoSitePlus; Q03188; -.
DR BioMuta; CENPC; -.
DR DMDM; 296434446; -.
DR EPD; Q03188; -.
DR jPOST; Q03188; -.
DR MassIVE; Q03188; -.
DR MaxQB; Q03188; -.
DR PaxDb; Q03188; -.
DR PeptideAtlas; Q03188; -.
DR PRIDE; Q03188; -.
DR ProteomicsDB; 58203; -. [Q03188-1]
DR ProteomicsDB; 67172; -.
DR ABCD; Q03188; 1 sequenced antibody.
DR Antibodypedia; 6105; 239 antibodies from 31 providers.
DR DNASU; 1060; -.
DR Ensembl; ENST00000273853.11; ENSP00000273853.6; ENSG00000145241.11. [Q03188-1]
DR Ensembl; ENST00000506882.5; ENSP00000426078.1; ENSG00000145241.11. [Q03188-2]
DR GeneID; 1060; -.
DR KEGG; hsa:1060; -.
DR MANE-Select; ENST00000273853.11; ENSP00000273853.6; NM_001812.4; NP_001803.2.
DR UCSC; uc003hdd.2; human. [Q03188-1]
DR CTD; 1060; -.
DR DisGeNET; 1060; -.
DR GeneCards; CENPC; -.
DR HGNC; HGNC:1854; CENPC.
DR HPA; ENSG00000145241; Low tissue specificity.
DR MIM; 117141; gene.
DR neXtProt; NX_Q03188; -.
DR OpenTargets; ENSG00000145241; -.
DR PharmGKB; PA26398; -.
DR VEuPathDB; HostDB:ENSG00000145241; -.
DR eggNOG; ENOG502RYQH; Eukaryota.
DR GeneTree; ENSGT00390000016737; -.
DR HOGENOM; CLU_013594_0_0_1; -.
DR InParanoid; Q03188; -.
DR OMA; NFEDKDI; -.
DR OrthoDB; 215502at2759; -.
DR PhylomeDB; Q03188; -.
DR TreeFam; TF101132; -.
DR PathwayCommons; Q03188; -.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR SignaLink; Q03188; -.
DR SIGNOR; Q03188; -.
DR BioGRID-ORCS; 1060; 656 hits in 1057 CRISPR screens.
DR ChiTaRS; CENPC; human.
DR GeneWiki; CENPC1; -.
DR GenomeRNAi; 1060; -.
DR Pharos; Q03188; Tbio.
DR PRO; PR:Q03188; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q03188; protein.
DR Bgee; ENSG00000145241; Expressed in calcaneal tendon and 105 other tissues.
DR ExpressionAtlas; Q03188; baseline and differential.
DR Genevisible; Q03188; HS.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0030496; C:midbody; IDA:HPA.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:UniProtKB.
DR GO; GO:0019237; F:centromeric DNA binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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; IMP:UniProtKB.
DR GO; GO:0051382; P:kinetochore assembly; IMP:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; IMP: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; 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; SSF51182; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cell division; Centromere;
KW Chromosome; DNA-binding; Isopeptide bond; Kinetochore; Mitosis; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..943
FT /note="Centromere protein C"
FT /id="PRO_0000089474"
FT REGION 70..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..759
FT /note="MIF2 homology domain II"
FT REGION 890..943
FT /note="MIF2 homology domain III"
FT MOTIF 259..273
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 484..499
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 558..574
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 780..798
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 70..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..472
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..580
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..697
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..717
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 130
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 183
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49452"
FT MOD_RES 397
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49452"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 538
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 684
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 709
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 710
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 734
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 763
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 773
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT CROSSLNK 45
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 119
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 134
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 180
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 212
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 217
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297"
FT CROSSLNK 238
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 260
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 271
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 273
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 297
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 440
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 534
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 677
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 727
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 807
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 539..542
FT /note="PVYS -> CLKC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_057280"
FT VAR_SEQ 543..943
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_057281"
FT VARIANT 341
FT /note="L -> F (in dbSNP:rs11250)"
FT /evidence="ECO:0000269|PubMed:1339310,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT /id="VAR_069295"
FT VARIANT 389
FT /note="G -> D (in dbSNP:rs1056787)"
FT /evidence="ECO:0000269|PubMed:1339310"
FT /id="VAR_069296"
FT CONFLICT 179
FT /note="Q -> K (in Ref. 1; AAA51974)"
FT /evidence="ECO:0000305"
FT STRAND 528..531
FT /evidence="ECO:0007829|PDB:6SE6"
SQ SEQUENCE 943 AA; 106834 MW; 2AA5AF82BA88C809 CRC64;
MAASGLDHLK NGYRRRFCRP SRARDINTEQ GQNVLEILQD CFEEKSLAND FSTNSTKSVP
NSTRKIKDTC IQSPSKECQK SHPKSVPVSS KKKEASLQFV VEPSEATNRS VQAHEVHQKI
LATDVSSKNT PDSKKISSRN INDHHSEADE EFYLSVGSPS VLLDAKTSVS QNVIPSSAQK
RETYTFENSV NMLPSSTEVS VKTKKRLNFD DKVMLKKIEI DNKVSDEEDK TSEGQERKPS
GSSQNRIRDS EYEIQRQAKK SFSTLFLETV KRKSESSPIV RHAATAPPHS CPPDDTKLIE
DEFIIDESDQ SFASRSWITI PRKAGSLKQR TISPAESTAL LQGRKSREKH HNILPKTLAN
DKHSHKPHPV ETSQPSDKTV LDTSYALIGE TVNNYRSTKY EMYSKNAEKP SRSKRTIKQK
QRRKFMAKPA EEQLDVGQSK DENIHTSHIT QDEFQRNSDR NMEEHEEMGN DCVSKKQMPP
VGSKKSSTRK DKEESKKKRF SSESKNKLVP EEVTSTVTKS RRISRRPSDW WVVKSEESPV
YSNSSVRNEL PMHHNSSRKS TKKTNQSSKN IRKKTIPLKR QKTATKGNQR VQKFLNAEGS
GGIVGHDEIS RCSLSEPLES DEADLAKKKN LDCSRSTRSS KNEDNIMTAQ NVPLKPQTSG
YTCNIPTESN LDSGEHKTSV LEESGPSRLN NNYLMSGKND VDDEEVHGSS DDSKQSKVIP
KNRIHHKLVL PSNTPNVRRT KRTRLKPLEY WRGERIDYQG RPSGGFVISG VLSPDTISSK
RKAKENIGKV NKKSNKKRIC LDNDERKTNL MVNLGIPLGD PLQPTRVKDP ETREIILMDL
VRPQDTYQFF VKHGELKVYK TLDTPFFSTG KLILGPQEEK GKQHVGQDIL VFYVNFGDLL
CTLHETPYIL STGDSFYVPS GNYYNIKNLR NEESVLLFTQ IKR
