P49450 (CENPA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone H3-like centromeric protein A

Alternative name(s):
Centromere autoantigen A
Centromere protein A
Short name=CENP-A

Gene names

Name:

CENPA

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	140 AA.
Sequence status	Complete.
Protein existence	Evidence 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 MLF1IP/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. Chromosome › centromere › kinetochore. 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 process	Host-virus interaction
Cellular component	Centromere Chromosome Kinetochore Nucleosome core Nucleus
Coding sequence diversity	Alternative splicing
Ligand	DNA-binding
PTM	ADP-ribosylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	CENP-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 prometaphase Traceable author statement. Source: Reactome protein localization to chromosome, centromeric region Inferred from direct assay PubMed 11682612. Source: BHF-UCL virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	condensed chromosome inner kinetochore Inferred from electronic annotation. Source: Compara condensed nuclear chromosome kinetochore Inferred from direct assay PubMed 18195732. Source: BHF-UCL cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome nucleosome Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	DNA 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
HIST2H4B	P62805	4	EBI-1751979,EBI-302023
HJURP	Q8NCD3	14	EBI-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 140

140

Histone H3-like centromeric protein A

PRO_0000221373

Regions

Region

41 – 140

100

H3-like

Region

75 – 116

42

CATD

Amino acid modifications

Modified residue

7

1

Phosphoserine; by AURKA and AURKB Ref.9 Ref.10 Ref.17

Modified residue

17

1

Phosphoserine Ref.21 Ref.27

Modified residue

19

1

Phosphoserine Ref.21 Ref.27

Modified residue

27

1

Phosphoserine Ref.21 Ref.27

Natural variations

Alternative sequence

71 – 96

26

Missing in isoform 2.

VSP_020430

Experimental info

Mutagenesis

7

1

S → 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

1

.

.

.

.

.

.

.

.

.

.

140

Helix Strand Turn

Details...

Helix

64 – 79

16

Beta strand

85 – 87

3

Helix

88 – 115

28

Beta strand

119 – 121

3

Helix

123 – 133

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: 11A28FEB54486489	FASTA	140	15,991
	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
	Isoform 2 [UniParc]. Checksum: 9E0DB58DBB95C1CF	FASTA	114	13,001
	10 20 30 40 50 60 MGPRRRSRKP EAPRRRSPSP TPTPGPSRRG PSLGASSHQH SRRRQGWLKE IRKLQKSTHL 70 80 90 100 110 LIRKLPFSRL AAEAFLVHLF EDAYLLTLHA GRVTLFPKDV QLARRIRGLE EGLG

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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.

IPI

IPI00027152.
IPI00333218.

PIR

I38855.

RefSeq

NP_001035891.1. NM_001042426.1.
NP_001800.1. NM_001809.3.

UniGene

Hs.1594.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3AN2	X-ray	3.60	A/E	1-140	[»]
3NQJ	X-ray	2.10	A	60-140	[»]
3NQU	X-ray	2.50	A	1-140	[»]
3R45	X-ray	2.60	A	1-140	[»]

ProteinModelPortal

P49450.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-52297N.

IntAct

P49450. 9 interactions.

MINT

MINT-4720873.

STRING

9606.ENSP00000336868.

PTM databases

PhosphoSite

P49450.

Polymorphism databases

DMDM

1345726.

Proteomic databases

PaxDb

P49450.

PRIDE

P49450.

Protocols and materials databases

DNASU

1058.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000233505; ENSP00000233505; ENSG00000115163.
ENST00000335756; ENSP00000336868; ENSG00000115163.

GeneID

1058.

KEGG

hsa:1058.

UCSC

uc002rhr.3. human.
uc002rhs.3. human.

Organism-specific databases

CTD

1058.

GeneCards

GC02P026988.

HGNC

HGNC:1851. CENPA.

HPA

CAB008371.

MIM

117139. gene.

neXtProt

NX_P49450.

PharmGKB

PA26396.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2036.

HOGENOM

HOG000155290.

HOVERGEN

HBG001172.

InParanoid

P49450.

KO

K11495.

OMA

LVREICV.

OrthoDB

EOG4MPHRS.

Enzyme and pathway databases

Pathway_Interaction_DB

aurora_a_pathway. Aurora A signaling.
aurora_b_pathway. Aurora B signaling.
foxm1pathway. FOXM1 transcription factor network.

Reactome

REACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

ArrayExpress

P49450.

Bgee

P49450.

CleanEx

HS_CENPA.

Genevestigator

P49450.

GermOnline

ENSG00000115163. Homo sapiens.

Family and domain databases

Gene3D

1.10.20.10. 1 hit.

InterPro

IPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR000164. Histone_H3.
[Graphical view]

PANTHER

PTHR11426. PTHR11426. 1 hit.

Pfam

PF00125. Histone. 1 hit.
[Graphical view]

PRINTS

PR00622. HISTONEH3.

SMART

SM00428. H3. 1 hit.
[Graphical view]

SUPFAM

SSF47113. Histone-fold. 1 hit.

PROSITE

PS00959. HISTONE_H3_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P49450.

GenomeRNAi

1058.

NextBio

4426.

SOURCE

Search...

Entry information

Entry name

CENPA_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 129 of the entry and version 1 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.