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P49450

- CENPA_HUMAN

UniProt

P49450 - CENPA_HUMAN

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Protein
Histone H3-like centromeric protein A
Gene
CENPA
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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).2 Publications

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. chromatin binding Source: ProtInc
  3. protein binding Source: UniProtKB

GO - Biological processi

  1. centromere-specific nucleosome assembly Source: Reactome
  2. establishment of mitotic spindle orientation Source: UniProtKB
  3. kinetochore assembly Source: BHF-UCL
  4. mitotic cell cycle Source: Reactome
  5. nucleosome assembly Source: Reactome
  6. protein localization to chromosome, centromeric region Source: BHF-UCL
  7. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_22186. Deposition of new CENPA-containing nucleosomes at the centromere.
REACT_682. Mitotic Prometaphase.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H3-like centromeric protein A
Alternative name(s):
Centromere autoantigen A
Centromere protein A
Short name:
CENP-A
Gene namesi
Name:CENPA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:1851. CENPA.

Subcellular locationi

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.6 Publications

GO - Cellular componenti

  1. chromosome, centromeric region Source: MGI
  2. condensed chromosome inner kinetochore Source: Ensembl
  3. condensed nuclear chromosome kinetochore Source: BHF-UCL
  4. condensed nuclear chromosome, centromeric region Source: BHF-UCL
  5. cytosol Source: Reactome
  6. nucleoplasm Source: Reactome
  7. nucleosome Source: UniProtKB-KW
  8. nucleus Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Kinetochore, Nucleosome core, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi7 – 71S → A: Induces a delay at the terminal stage of cytokinesis and chromosome misalignment during mitosis due to a defect in kinetochore attachment to microtubules. 2 Publications

Organism-specific databases

PharmGKBiPA26396.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 140140Histone H3-like centromeric protein A
PRO_0000221373Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei7 – 71Phosphoserine; by AURKA and AURKB3 Publications
Modified residuei17 – 171Phosphoserine2 Publications
Modified residuei19 – 191Phosphoserine2 Publications
Modified residuei27 – 271Phosphoserine2 Publications

Post-translational modificationi

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

Keywords - PTMi

ADP-ribosylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP49450.
PRIDEiP49450.

PTM databases

PhosphoSiteiP49450.

Expressioni

Gene expression databases

ArrayExpressiP49450.
BgeeiP49450.
CleanExiHS_CENPA.
GenevestigatoriP49450.

Organism-specific databases

HPAiCAB008371.

Interactioni

Subunit structurei

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.12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HIST2H4BP628054EBI-1751979,EBI-302023
HJURPQ8NCD314EBI-1751979,EBI-719429

Protein-protein interaction databases

BioGridi107487. 67 interactions.
DIPiDIP-52297N.
IntActiP49450. 9 interactions.
MINTiMINT-4720873.
STRINGi9606.ENSP00000336868.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi64 – 7916
Beta strandi85 – 873
Helixi88 – 11528
Beta strandi119 – 1213
Helixi123 – 13311

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3AN2X-ray3.60A/E1-140[»]
3NQJX-ray2.10A60-140[»]
3NQUX-ray2.50A1-140[»]
3R45X-ray2.60A1-140[»]
ProteinModelPortaliP49450.
SMRiP49450. Positions 46-134.

Miscellaneous databases

EvolutionaryTraceiP49450.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni41 – 140100H3-like
Add
BLAST
Regioni75 – 11642CATD
Add
BLAST

Domaini

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.1 Publication

Sequence similaritiesi

Belongs to the histone H3 family.

Phylogenomic databases

eggNOGiCOG2036.
HOGENOMiHOG000155290.
HOVERGENiHBG001172.
InParanoidiP49450.
KOiK11495.
OMAiLVREICV.
OrthoDBiEOG7KSXC2.
PhylomeDBiP49450.
TreeFamiTF354293.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR000164. Histone_H3.
[Graphical view]
PANTHERiPTHR11426. PTHR11426. 1 hit.
PfamiPF00125. Histone. 1 hit.
[Graphical view]
PRINTSiPR00622. HISTONEH3.
SMARTiSM00428. H3. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS00959. HISTONE_H3_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P49450-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MGPRRRSRKP EAPRRRSPSP TPTPGPSRRG PSLGASSHQH SRRRQGWLKE    50
IRKLQKSTHL LIRKLPFSRL AREICVKFTR GVDFNWQAQA LLALQEAAEA 100
FLVHLFEDAY LLTLHAGRVT LFPKDVQLAR RIRGLEEGLG 140
Length:140
Mass (Da):15,991
Last modified:February 1, 1996 - v1
Checksum:i11A28FEB54486489
GO
Isoform 2 (identifier: P49450-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     71-96: Missing.

Note: No experimental confirmation available.

Show »
Length:114
Mass (Da):13,001
Checksum:i9E0DB58DBB95C1CF
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei71 – 9626Missing in isoform 2.
VSP_020430Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS1729.1. [P49450-1]
CCDS42662.1. [P49450-2]
PIRiI38855.
RefSeqiNP_001035891.1. NM_001042426.1. [P49450-2]
NP_001800.1. NM_001809.3. [P49450-1]
UniGeneiHs.1594.

Genome annotation databases

EnsembliENST00000233505; ENSP00000233505; ENSG00000115163. [P49450-2]
ENST00000335756; ENSP00000336868; ENSG00000115163. [P49450-1]
GeneIDi1058.
KEGGihsa:1058.
UCSCiuc002rhr.3. human. [P49450-1]
uc002rhs.3. human. [P49450-2]

Polymorphism databases

DMDMi1345726.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS1729.1. [P49450-1 ]
CCDS42662.1. [P49450-2 ]
PIRi I38855.
RefSeqi NP_001035891.1. NM_001042426.1. [P49450-2 ]
NP_001800.1. NM_001809.3. [P49450-1 ]
UniGenei Hs.1594.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P49450.
SMRi P49450. Positions 46-134.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107487. 67 interactions.
DIPi DIP-52297N.
IntActi P49450. 9 interactions.
MINTi MINT-4720873.
STRINGi 9606.ENSP00000336868.

PTM databases

PhosphoSitei P49450.

Polymorphism databases

DMDMi 1345726.

Proteomic databases

PaxDbi P49450.
PRIDEi P49450.

Protocols and materials databases

DNASUi 1058.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000233505 ; ENSP00000233505 ; ENSG00000115163 . [P49450-2 ]
ENST00000335756 ; ENSP00000336868 ; ENSG00000115163 . [P49450-1 ]
GeneIDi 1058.
KEGGi hsa:1058.
UCSCi uc002rhr.3. human. [P49450-1 ]
uc002rhs.3. human. [P49450-2 ]

Organism-specific databases

CTDi 1058.
GeneCardsi GC02P026988.
HGNCi HGNC:1851. CENPA.
HPAi CAB008371.
MIMi 117139. gene.
neXtProti NX_P49450.
PharmGKBi PA26396.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2036.
HOGENOMi HOG000155290.
HOVERGENi HBG001172.
InParanoidi P49450.
KOi K11495.
OMAi LVREICV.
OrthoDBi EOG7KSXC2.
PhylomeDBi P49450.
TreeFami TF354293.

Enzyme and pathway databases

Reactomei REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_22186. Deposition of new CENPA-containing nucleosomes at the centromere.
REACT_682. Mitotic Prometaphase.

Miscellaneous databases

EvolutionaryTracei P49450.
GeneWikii CENPA.
GenomeRNAii 1058.
NextBioi 4426.
PROi P49450.
SOURCEi Search...

Gene expression databases

ArrayExpressi P49450.
Bgeei P49450.
CleanExi HS_CENPA.
Genevestigatori P49450.

Family and domain databases

Gene3Di 1.10.20.10. 1 hit.
InterProi IPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR000164. Histone_H3.
[Graphical view ]
PANTHERi PTHR11426. PTHR11426. 1 hit.
Pfami PF00125. Histone. 1 hit.
[Graphical view ]
PRINTSi PR00622. HISTONEH3.
SMARTi SM00428. H3. 1 hit.
[Graphical view ]
SUPFAMi SSF47113. SSF47113. 1 hit.
PROSITEi PS00959. HISTONE_H3_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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.

Entry informationi

Entry nameiCENPA_HUMAN
AccessioniPrimary (citable) accession number: P49450
Secondary accession number(s): D6W544, Q53T74, Q9BVW2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: September 3, 2014
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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