Q03188 (CENPC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Centromere protein C 1
Short name=CENP-C 1

Alternative name(s):
Centromere autoantigen C
Interphase centromere complex protein 7

Gene names

Name:	CENPC1
Synonyms:	CENPC, ICEN7

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	943 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. CENPC recruits DNA methylation and DNMT3B to both centromeric and pericentromeric satellite repeats and regulates the histone code in these regions. Ref.10 Ref.13
Subunit structure	Oligomer. Component of the CENPA-NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and MLF1IP/CENPU. The CENPA-NAC complex interacts with the CENPA-CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. Binds to DAXX. Interacts directly with CENPA. Ref.6 Ref.9 Ref.10
Subcellular location	Nucleus. Chromosome › centromere › kinetochore. Note: Localizes exclusively in the kinetochore domain of centromeres. Ref.7 Ref.10 Ref.13
Domain	The MIF2 homology domain II targets centromeres and binds the alpha satellite DNA in vivo. The MIF2 homology domain III can induce CENPC dimerization/oligomerization. Ref.9
Sequence similarities	Belongs to the CENPC family.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Centromere Chromosome Kinetochore Nucleus
Ligand	DNA-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW chromosome segregation Inferred from mutant phenotype Ref.13. Source: UniProtKB kinetochore assembly Inferred from mutant phenotype Ref.13. Source: UniProtKB mitotic prometaphase Traceable author statement. Source: Reactome
Cellular_component	centromeric heterochromatin Inferred from direct assay Ref.13. Source: UniProtKB condensed chromosome kinetochore Inferred from electronic annotation. Source: UniProtKB-SubCell condensed nuclear chromosome, centromeric region Inferred from direct assay PubMed 11682612. Source: BHF-UCL cytosol Traceable author statement. Source: Reactome kinetochore Inferred from direct assay Ref.13. Source: UniProtKB
Molecular_function	DNA binding Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 943	943	Centromere protein C 1		PRO_0000089474
Regions
	Region	737 – 759	23	MIF2 homology domain II
	Region	890 – 943	54	MIF2 homology domain III
	Motif	259 – 273	15	Nuclear localization signal Potential
	Motif	484 – 499	16	Nuclear localization signal Potential
	Motif	558 – 574	17	Nuclear localization signal Potential
	Motif	780 – 798	19	Nuclear localization signal Potential
Amino acid modifications
	Modified residue	96	1	Phosphoserine Ref.12
	Modified residue	130	1	Phosphothreonine Ref.12
	Modified residue	146	1	Phosphoserine Ref.11
	Modified residue	183	1	Phosphothreonine Ref.11
	Modified residue	189	1	Phosphoserine Ref.11
	Modified residue	225	1	Phosphoserine Ref.4 Ref.12 Ref.14
	Modified residue	261	1	Phosphoserine Ref.8
	Modified residue	316	1	Phosphoserine Ref.8
	Modified residue	439	1	Phosphoserine Ref.12 Ref.14
	Modified residue	538	1	Phosphoserine Ref.11 Ref.12
	Modified residue	709	1	Phosphoserine Ref.14
	Modified residue	710	1	Phosphoserine Ref.14
	Modified residue	734	1	Phosphothreonine Ref.12
	Modified residue	763	1	Phosphoserine Ref.11 Ref.12
	Modified residue	773	1	Phosphoserine Ref.8 Ref.11 Ref.12
Experimental info
	Sequence conflict	179	1	Q → K in AAA51974. Ref.1
	Sequence conflict	341	1	L → F in AAA51974. Ref.1
	Sequence conflict	389	1	G → D in AAA51974. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q03188 [UniParc]. Last modified May 18, 2010. Version 2. Checksum: 2AA5AF82BA88C809	FASTA	943	106,834
	10 20 30 40 50 60 MAASGLDHLK NGYRRRFCRP SRARDINTEQ GQNVLEILQD CFEEKSLAND FSTNSTKSVP 70 80 90 100 110 120 NSTRKIKDTC IQSPSKECQK SHPKSVPVSS KKKEASLQFV VEPSEATNRS VQAHEVHQKI 130 140 150 160 170 180 LATDVSSKNT PDSKKISSRN INDHHSEADE EFYLSVGSPS VLLDAKTSVS QNVIPSSAQK 190 200 210 220 230 240 RETYTFENSV NMLPSSTEVS VKTKKRLNFD DKVMLKKIEI DNKVSDEEDK TSEGQERKPS 250 260 270 280 290 300 GSSQNRIRDS EYEIQRQAKK SFSTLFLETV KRKSESSPIV RHAATAPPHS CPPDDTKLIE 310 320 330 340 350 360 DEFIIDESDQ SFASRSWITI PRKAGSLKQR TISPAESTAL LQGRKSREKH HNILPKTLAN 370 380 390 400 410 420 DKHSHKPHPV ETSQPSDKTV LDTSYALIGE TVNNYRSTKY EMYSKNAEKP SRSKRTIKQK 430 440 450 460 470 480 QRRKFMAKPA EEQLDVGQSK DENIHTSHIT QDEFQRNSDR NMEEHEEMGN DCVSKKQMPP 490 500 510 520 530 540 VGSKKSSTRK DKEESKKKRF SSESKNKLVP EEVTSTVTKS RRISRRPSDW WVVKSEESPV 550 560 570 580 590 600 YSNSSVRNEL PMHHNSSRKS TKKTNQSSKN IRKKTIPLKR QKTATKGNQR VQKFLNAEGS 610 620 630 640 650 660 GGIVGHDEIS RCSLSEPLES DEADLAKKKN LDCSRSTRSS KNEDNIMTAQ NVPLKPQTSG 670 680 690 700 710 720 YTCNIPTESN LDSGEHKTSV LEESGPSRLN NNYLMSGKND VDDEEVHGSS DDSKQSKVIP 730 740 750 760 770 780 KNRIHHKLVL PSNTPNVRRT KRTRLKPLEY WRGERIDYQG RPSGGFVISG VLSPDTISSK 790 800 810 820 830 840 RKAKENIGKV NKKSNKKRIC LDNDERKTNL MVNLGIPLGD PLQPTRVKDP ETREIILMDL 850 860 870 880 890 900 VRPQDTYQFF VKHGELKVYK TLDTPFFSTG KLILGPQEEK GKQHVGQDIL VFYVNFGDLL 910 920 930 940 CTLHETPYIL STGDSFYVPS GNYYNIKNLR NEESVLLFTQ IKR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"CENP-C, an autoantigen in scleroderma, is a component of the human inner kinetochore plate." Saitoh H., Tomkiel J., Cooke C.A., Ratrie H. III, Maurer M., Rothfield N.F., Earnshaw W.C. Cell 70:115-125(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Placenta.
[2]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Promoter characterization of centromere protein C reveals its participation in cell cycle regulation in late G1-phase and expression control by E2F-1, pRb, p107 and Sp-1." Poppe M., Botz J., Hahm B., Dobat K., Eickelbaum W., Paweletz N., Arand M., Knehr M. Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
[4]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[5]	"Comprehensive analysis of the ICEN (Interphase Centromere Complex) components enriched in the CENP-A chromatin of human cells." Izuta H., Ikeno M., Suzuki N., Tomonaga T., Nozaki N., Obuse C., Kisu Y., Goshima N., Nomura F., Nomura N., Yoda K. Genes Cells 11:673-684(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
[6]	"The human CENP-A centromeric nucleosome-associated complex." Foltz D.R., Jansen L.E.T., Black B.E., Bailey A.O., Yates J.R. III, Cleveland D.W. Nat. Cell Biol. 8:458-469(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE CENPA-NAC COMPLEX WITH CENPA; CENPH; CENPM; CENPN; CENPT AND CENPU.
[7]	"Co-localization of CENP-C and CENP-H to discontinuous domains of CENP-A chromatin at human neocentromeres." Alonso A., Fritz B., Hasson D., Abrusan G., Cheung F., Yoda K., Radlwimmer B., Ladurner A.G., Warburton P.E. Genome Biol. 8:R148.1-R148.19(2007) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[8]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261; SER-316 AND SER-773, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"The C-terminal domain of CENP-C displays multiple and critical functions for mammalian centromere formation." Trazzi S., Perini G., Bernardoni R., Zoli M., Reese J.C., Musacchio A., Della Valle G. PLoS ONE 4:E5832-E5832(2009) [PubMed] [Europe PMC] [Abstract] Cited for: DOMAIN, SUBUNIT, INTERACTION WITH CENPA.
[10]	"DNMT3B interacts with constitutive centromere protein CENP-C to modulate DNA methylation and the histone code at centromeric regions." Gopalakrishnan S., Sullivan B.A., Trazzi S., Della Valle G., Robertson K.D. Hum. Mol. Genet. 18:3178-3193(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DNMT3B.
[11]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146; THR-183; SER-189; SER-538; SER-763 AND SER-773, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96; THR-130; SER-225; SER-439; SER-538; THR-734; SER-763 AND SER-773, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"Induced ectopic kinetochore assembly bypasses the requirement for CENP-A nucleosomes." Gascoigne K.E., Takeuchi K., Suzuki A., Hori T., Fukagawa T., Cheeseman I.M. Cell 145:410-422(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[14]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225; SER-439; SER-709 AND SER-710, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M95724 mRNA. Translation: AAA51974.1. AC104806 Genomic DNA. No translation available. AC109356 Genomic DNA. No translation available. AF151723 Genomic DNA. Translation: AAF73191.1.
IPI	IPI00304885.
PIR	A42681.
RefSeq	NP_001803.2. NM_001812.2.
UniGene	Hs.479867.
3D structure databases
ProteinModelPortal	Q03188.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q03188. 10 interactions.
MINT	MINT-4786577.
STRING	9606.ENSP00000273853.
PTM databases
PhosphoSite	Q03188.
Polymorphism databases
DMDM	296434446.
Proteomic databases
PaxDb	Q03188.
PRIDE	Q03188.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000273853; ENSP00000273853; ENSG00000145241.
GeneID	1060.
KEGG	hsa:1060.
UCSC	uc003hdd.1. human.
Organism-specific databases
CTD	1060.
GeneCards	GC04M068341.
H-InvDB	HIX0024603.
HGNC	HGNC:1854. CENPC1.
HPA	HPA049740.
MIM	117141. gene.
neXtProt	NX_Q03188.
PharmGKB	PA26398.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG329217.
HOGENOM	HOG000090256.
HOVERGEN	HBG050891.
InParanoid	Q03188.
KO	K11497.
OMA	WITIPRK.
OrthoDB	EOG4JM7P0.
Enzyme and pathway databases
Reactome	REACT_115566. Cell Cycle. REACT_21300. Mitotic M-M/G1 phases.
Gene expression databases
ArrayExpress	Q03188.
Bgee	Q03188.
CleanEx	HS_CENPC1.
Genevestigator	Q03188.
GermOnline	ENSG00000145241. Homo sapiens.
Family and domain databases
Gene3D	2.60.120.10. 1 hit.
InterPro	IPR025974. Mif2/CENP-C_cupin. IPR014710. RmlC-like_jellyroll. IPR011051. RmlC_Cupin. [Graphical view]
Pfam	PF11699. Mif2. 1 hit. [Graphical view]
SUPFAM	SSF51182. RmlC_like_cupin. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	CENPC1. human.
GenomeRNAi	1060.
NextBio	4436.
SOURCE	Search...

Entry information

Entry name

CENPC_HUMAN

Accession

Primary (citable) accession number: Q03188
Secondary accession number(s): Q9P0M5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	May 18, 2010
Last modified:	May 1, 2013
This is version 109 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.