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P49450 (CENPA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone H3-like centromeric protein A
Alternative name(s):
Centromere autoantigen A
Centromere protein A
Short name=CENP-A
Gene names
Name:CENPA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length140 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Histone H3-like variant which exclusively replaces conventional H3 in the nucleosome core of centromeric chromatin at the inner plate of the kinetochore. Required for recruitment and assembly of kinetochore proteins, mitotic progression and chromosome segregation. May serve as an epigenetic mark that propagates centromere identity through replication and cell division. The CENPA-H4 heterotetramer can bind DNA by itself (in vitro). Ref.28 Ref.29

Subunit structure

Forms a nucleosome-like histone octamer containing two molecules each of H2A, H2B, CENPA and H4 assembled in one CENPA-H4 heterotetramer and two H2A-H2B heterodimers. Nucleosomes containing CENPA also contain histone H2A variants such as macroH2A H2AFY and H2A.Z/H2AFZ. The CENPA-H4 heterotetramer is more compact and structurally more rigid than corresponding H3-H4 heterotetramers. Heterotrimer composed of HJURP, CENPA and histone H4, where HJURP interacts with the dimer formed by CENPA and histone H4 and prevents tetramerization of CENPA and H4. Component of the CENPA-NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU. Interacts (via CATD domain) with HJURP; the interaction is direct and is required for its localization to centromeres. Interacts with CENPC, CENPN and CENPT; interaction is direct. Interacts directly with herpes virus HSV-1 ICP0 protein. Part of a centromere complex consisting of CENPA, CENPT and CENPW. Ref.6 Ref.8 Ref.13 Ref.15 Ref.19 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.28 Ref.29

Subcellular location

Nucleus. Chromosomecentromerekinetochore. Note: Localizes exclusively in the kinetochore domain of centromeres. Occupies a compact domain at the inner kinetochore plate stretching across 2 thirds of the length of the constriction but encompassing only one third of the constriction width and height. Ref.11 Ref.12 Ref.16 Ref.18 Ref.20 Ref.28

Domain

The CATD (CENPA targeting domain) region is responsible for the more compact structure of nucleosomes containing CENPA and is necessary and sufficient to mediate the localization into centromeres. Ref.13

Post-translational modification

Ubiquitinated Probable. Interaction with herpes virus HSV-1 ICP0 protein, leads to its degradation by the proteasome pathway. Ref.8

Phosphorylation of Ser-7 by AURKA and AURKB during prophase is required for localization of AURKA and AURKB at inner centromere and is essential for kinetochore function. Initial phosphorylation during prophase is mediated by AURKA and is maintained by AURKB.

Poly-ADP-ribosylated by PARP1 By similarity.

Miscellaneous

Antibodies against CENPA are present in sera from patients with autoimmune diseases that developed autoantibodies against centrosomal proteins.

Sequence similarities

Belongs to the histone H3 family.

Ontologies

Keywords
   Biological processHost-virus interaction
   Cellular componentCentromere
Chromosome
Kinetochore
Nucleosome core
Nucleus
   Coding sequence diversityAlternative splicing
   LigandDNA-binding
   PTMADP-ribosylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processCENP-A containing nucleosome assembly at centromere

Traceable author statement. Source: Reactome

establishment of mitotic spindle orientation

Inferred from mutant phenotype PubMed 19468067. Source: UniProtKB

kinetochore assembly

Inferred from direct assay PubMed 11682612. Source: BHF-UCL

mitotic cell cycle

Traceable author statement. Source: Reactome

nucleosome assembly

Traceable author statement. Source: Reactome

protein localization to chromosome, centromeric region

Inferred from direct assay PubMed 11682612. Source: BHF-UCL

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentchromosome, centromeric region

Inferred from direct assay PubMed 11084331. Source: MGI

condensed chromosome inner kinetochore

Inferred from electronic annotation. Source: Ensembl

condensed nuclear chromosome kinetochore

Inferred from direct assay PubMed 18195732. Source: BHF-UCL

condensed nuclear chromosome, centromeric region

Inferred from direct assay PubMed 11682612. Source: BHF-UCL

cytosol

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

nucleosome

Inferred from electronic annotation. Source: UniProtKB-KW

nucleus

Traceable author statement Ref.1. Source: ProtInc

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

chromatin binding

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HIST2H4BP628054EBI-1751979,EBI-302023
HJURPQ8NCD314EBI-1751979,EBI-719429

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P49450-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P49450-2)

The sequence of this isoform differs from the canonical sequence as follows:
     71-96: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 140140Histone H3-like centromeric protein A
PRO_0000221373

Regions

Region41 – 140100H3-like
Region75 – 11642CATD

Amino acid modifications

Modified residue71Phosphoserine; by AURKA and AURKB Ref.9 Ref.10 Ref.17
Modified residue171Phosphoserine Ref.21 Ref.27
Modified residue191Phosphoserine Ref.21 Ref.27
Modified residue271Phosphoserine Ref.21 Ref.27

Natural variations

Alternative sequence71 – 9626Missing in isoform 2.
VSP_020430

Experimental info

Mutagenesis71S → A: Induces a delay at the terminal stage of cytokinesis and chromosome misalignment during mitosis due to a defect in kinetochore attachment to microtubules. Ref.9 Ref.10

Secondary structure

.......... 140
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 11A28FEB54486489

FASTA14015,991
        10         20         30         40         50         60 
MGPRRRSRKP EAPRRRSPSP TPTPGPSRRG PSLGASSHQH SRRRQGWLKE IRKLQKSTHL 

        70         80         90        100        110        120 
LIRKLPFSRL AREICVKFTR GVDFNWQAQA LLALQEAAEA FLVHLFEDAY LLTLHAGRVT 

       130        140 
LFPKDVQLAR RIRGLEEGLG 

« Hide

Isoform 2 [UniParc].

Checksum: 9E0DB58DBB95C1CF
Show »

FASTA11413,001

References

« Hide 'large scale' references
[1]"Human CENP-A contains a histone H3 related histone fold domain that is required for targeting to the centromere."
Sullivan K.F., Hechenberger M., Masri K.
J. Cell Biol. 127:581-592(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]"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. expand/collapse author list , 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].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Uterus.
[6]"Assembly of CENP-A into centromeric chromatin requires a cooperative array of nucleosomal DNA contact sites."
Shelby R.D., Vafa O., Sullivan K.F.
J. Cell Biol. 136:501-513(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33, SUBUNIT.
[7]"Autoepitopes on autoantigen centromere protein-A (CENP-A) are restricted to the N-terminal region, which has no homology with histone H3."
Muro Y., Azuma N., Onouchi H., Kunimatsu M., Tomita Y., Sasaki M., Sugimoto K.
Clin. Exp. Immunol. 120:218-223(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF AUTOANTIGENIC EPITOPES.
[8]"Degradation of nucleosome-associated centromeric histone H3-like protein CENP-A induced by herpes simplex virus type 1 protein ICP0."
Lomonte P., Sullivan K.F., Everett R.D.
J. Biol. Chem. 276:5829-5835(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, INTERACTION WITH HSV-1 ICP0.
[9]"CENP-A is phosphorylated by Aurora B kinase and plays an unexpected role in completion of cytokinesis."
Zeitlin S.G., Shelby R.D., Sullivan K.F.
J. Cell Biol. 155:1147-1157(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-7, MUTAGENESIS OF SER-7.
[10]"CENP-A phosphorylation by Aurora-A in prophase is required for enrichment of Aurora-B at inner centromeres and for kinetochore function."
Kunitoku N., Sasayama T., Marumoto T., Zhang D., Honda S., Kobayashi O., Hatakeyama K., Ushio Y., Saya H., Hirota T.
Dev. Cell 5:853-864(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-7, MUTAGENESIS OF SER-7.
[11]"Chromosome size and origin as determinants of the level of CENP-A incorporation into human centromeres."
Irvine D.V., Amor D.J., Perry J., Sirvent N., Pedeutour F., Choo K.H., Saffery R.
Chromosome Res. 12:805-815(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[12]"Centromeric chromatin exhibits a histone modification pattern that is distinct from both euchromatin and heterochromatin."
Sullivan B.A., Karpen G.H.
Nat. Struct. Mol. Biol. 11:1076-1083(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[13]"Structural determinants for generating centromeric chromatin."
Black B.E., Foltz D.R., Chakravarthy S., Luger K., Woods V.L. Jr., Cleveland D.W.
Nature 430:578-582(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, DOMAIN CATD.
[14]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"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 BY MASS SPECTROMETRY, IDENTIFICATION IN THE CENPA-NAC COMPLEX WITH CENPC; CENPH; CENPM; CENPN; CENPT AND CENPU.
[16]"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.
[17]"Aurora-C and Aurora-B share phosphorylation and regulation of CENP-A and Borealin during mitosis."
Slattery S.D., Moore R.V., Brinkley B.R., Hall R.M.
Cell Cycle 7:787-795(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-7.
[18]"Assembly of the inner kinetochore proteins CENP-A and CENP-B in living human cells."
Orthaus S., Biskup C., Hoffmann B., Hoischen C., Ohndorf S., Benndorf K., Diekmann S.
ChemBioChem 9:77-92(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[19]"Live-cell imaging reveals sustained centromere binding of CENP-T via CENP-A and CENP-B."
Hellwig D., Muench S., Orthaus S., Hoischen C., Hemmerich P., Diekmann S.
J. Biophotonics 1:245-254(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CENPT.
[20]"Three-dimensional localization of CENP-A suggests a complex higher order structure of centromeric chromatin."
Marshall O.J., Marshall A.T., Choo K.H.A.
J. Cell Biol. 183:1193-1202(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[21]"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-17; SER-19 AND SER-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"Centromere-specific assembly of CENP-A nucleosomes is mediated by HJURP."
Foltz D.R., Jansen L.E.T., Bailey A.O., Yates J.R. III, Bassett E.A., Wood S., Black B.E., Cleveland D.W.
Cell 137:472-484(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HJURP.
[23]"HJURP is a cell-cycle-dependent maintenance and deposition factor of CENP-A at centromeres."
Dunleavy E.M., Roche D., Tagami H., Lacoste N., Ray-Gallet D., Nakamura Y., Daigo Y., Nakatani Y., Almouzni-Pettinotti G.
Cell 137:485-497(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HJURP.
[24]"Cancer-upregulated gene 2 (CUG2), a new component of centromere complex, is required for kinetochore function."
Kim H., Lee M., Lee S., Park B., Koh W., Lee D.J., Lim D.S., Lee S.
Mol. Cells 27:697-701(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN COMPLEX WITH CENPT AND CENPW.
[25]"Centromere assembly requires the direct recognition of CENP-A nucleosomes by CENP-N."
Carroll C.W., Silva M.C.C., Godek K.M., Jansen L.E.T., Straight A.F.
Nat. Cell Biol. 11:896-902(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CENPN.
[26]"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: INTERACTION WITH CENPC.
[27]"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-17; SER-19 AND SER-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"The structure of (CENP-A-H4)(2) reveals physical features that mark centromeres."
Sekulic N., Bassett E.A., Rogers D.J., Black B.E.
Nature 467:347-351(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
[29]"Structure of a CENP-A-histone H4 heterodimer in complex with chaperone HJURP."
Hu H., Liu Y., Wang M., Fang J., Huang H., Yang N., Li Y., Wang J., Yao X., Shi Y., Li G., Xu R.M.
Genes Dev. 25:901-906(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH HJURP AND HISTONE H4, FUNCTION, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U14518 mRNA. Translation: AAA57416.1.
BT007246 mRNA. Translation: AAP35910.1.
AC011740 Genomic DNA. Translation: AAX93267.1.
CH471053 Genomic DNA. Translation: EAX00669.1.
CH471053 Genomic DNA. Translation: EAX00670.1.
BC000881 mRNA. Translation: AAH00881.1.
BC002703 mRNA. Translation: AAH02703.1.
U82609 Genomic DNA. Translation: AAB47505.1.
PIRI38855.
RefSeqNP_001035891.1. NM_001042426.1.
NP_001800.1. NM_001809.3.
UniGeneHs.1594.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3AN2X-ray3.60A/E1-140[»]
3NQJX-ray2.10A60-140[»]
3NQUX-ray2.50A1-140[»]
3R45X-ray2.60A1-140[»]
ProteinModelPortalP49450.
SMRP49450. Positions 46-134.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107487. 67 interactions.
DIPDIP-52297N.
IntActP49450. 9 interactions.
MINTMINT-4720873.
STRING9606.ENSP00000336868.

PTM databases

PhosphoSiteP49450.

Polymorphism databases

DMDM1345726.

Proteomic databases

PaxDbP49450.
PRIDEP49450.

Protocols and materials databases

DNASU1058.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000233505; ENSP00000233505; ENSG00000115163. [P49450-2]
ENST00000335756; ENSP00000336868; ENSG00000115163. [P49450-1]
GeneID1058.
KEGGhsa:1058.
UCSCuc002rhr.3. human. [P49450-1]
uc002rhs.3. human. [P49450-2]

Organism-specific databases

CTD1058.
GeneCardsGC02P026988.
HGNCHGNC:1851. CENPA.
HPACAB008371.
MIM117139. gene.
neXtProtNX_P49450.
PharmGKBPA26396.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2036.
HOGENOMHOG000155290.
HOVERGENHBG001172.
InParanoidP49450.
KOK11495.
OMALVREICV.
OrthoDBEOG7KSXC2.
PhylomeDBP49450.
TreeFamTF354293.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

ArrayExpressP49450.
BgeeP49450.
CleanExHS_CENPA.
GenevestigatorP49450.

Family and domain databases

Gene3D1.10.20.10. 1 hit.
InterProIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR000164. Histone_H3.
[Graphical view]
PANTHERPTHR11426. PTHR11426. 1 hit.
PfamPF00125. Histone. 1 hit.
[Graphical view]
PRINTSPR00622. HISTONEH3.
SMARTSM00428. H3. 1 hit.
[Graphical view]
SUPFAMSSF47113. SSF47113. 1 hit.
PROSITEPS00959. HISTONE_H3_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP49450.
GeneWikiCENPA.
GenomeRNAi1058.
NextBio4426.
PROP49450.
SOURCESearch...

Entry information

Entry nameCENPA_HUMAN
AccessionPrimary (citable) accession number: P49450
Secondary accession number(s): D6W544, Q53T74, Q9BVW2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: April 16, 2014
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM