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Protein

Histone H3-like centromeric protein A

Gene

Cenpa

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Histone H3-like nucleosomal protein that is specifically found in centromeric nucleosomes. Replaces conventional H3 in the nucleosome core of centromeric chromatin at the inner plate of the kinetochore. The presence of CENPA subtly modifies the nucleosome structure and the way DNA is wrapped around the nucleosome and gives rise to protruding DNA ends that are less well-ordered and rigid compared to nucleosomes containing histone H3. May serve as an epigenetic mark that propagates centromere identity through replication and cell division (By similarity). Required for recruitment and assembly of kinetochore proteins, and as a consequence required for progress through mitosis, chromosome segregation and cytokinesis (PubMed:27499292).By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2500257. Resolution of Sister Chromatid Cohesion.
R-MMU-5663220. RHO GTPases Activate Formins.
R-MMU-606279. Deposition of new CENPA-containing nucleosomes at the centromere.
R-MMU-68877. Mitotic Prometaphase.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H3-like centromeric protein A
Alternative name(s):
Centromere protein A
Short name:
CENP-A
Gene namesi
Name:Cenpa
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:88375. Cenpa.

Subcellular locationi

  • Nucleus By similarity
  • Chromosomecentromerekinetochore By similarity
  • Chromosomecentromere By similarity

  • 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. Phosphorylation at Ser-62 during early mitosis abolishes association with chromatin and centromeres and results in dispersed nuclear location.By similarity

GO - Cellular componenti

  • chromosome, centromeric region Source: MGI
  • condensed chromosome inner kinetochore Source: MGI
  • condensed nuclear chromosome, centromeric region Source: MGI
  • condensed nuclear chromosome kinetochore Source: MGI
  • nuclear nucleosome Source: MGI
  • nuclear pericentric heterochromatin Source: MGI
  • nucleosome Source: GO_Central
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Kinetochore, Nucleosome core, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002213742 – 134Histone H3-like centromeric protein AAdd BLAST133

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N,N,N-trimethylglycineBy similarity1
Modified residuei16PhosphoserineBy similarity1
Modified residuei22PhosphoserineBy similarity1
Modified residuei62PhosphoserineBy similarity1

Post-translational modificationi

Poly-ADP-ribosylated by PARP1.
Trimethylated by NTMT1 at the N-terminal glycine after cleavage of Met-1. Methylation is low before incorporation into nucleosomes and increases with cell cycle progression, with the highest levels in mitotic nucleosomes.By similarity
Phosphorylated by CDK1 at Ser-62 during early mitosis; this abolishes association with chromatin and centromeres, prevents interaction with HJURP and thereby prevents premature assembly of CENPA into centromeres. Dephosphorylated at Ser-62 by PPP1CA during late mitosis.By similarity

Keywords - PTMi

ADP-ribosylation, Methylation, Phosphoprotein

Proteomic databases

MaxQBiO35216.
PaxDbiO35216.
PeptideAtlasiO35216.
PRIDEiO35216.

PTM databases

iPTMnetiO35216.
PhosphoSitePlusiO35216.

Expressioni

Gene expression databases

BgeeiENSMUSG00000029177.
CleanExiMM_CENPA.
ExpressionAtlasiO35216. baseline and differential.
GenevisibleiO35216. MM.

Interactioni

Subunit structurei

Component of centromeric nucleosomes, where DNA is wrapped around a histone octamer core. The octamer contains two molecules each of H2A, H2B, CENPA and H4 assembled in one CENPA-H4 heterotetramer and two H2A-H2B heterodimers. CENPA modulates the DNA-binding characteristics of nucleosomes so that protruding DNA ends have higher flexibility than in nucleosomes containing conventional histone H3. Inhibits binding of histone H1 to nucleosomes, since histone H1 binds preferentially to rigid DNA linkers that protrude from nucleosomes. 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. Can assemble into nucleosomes that contain both CENPA and histone H3.3; these nucleosomes interact with a single CENPC chain. 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. Part of a centromere complex consisting of CENPA, CENPT and CENPW. Identified in centromere complexes containing histones H2A, H2B and H4, and at least CENPA, CENPB, CENPC, CENPT, CENPN, HJURP, SUPT16H, SSRP1 and RSF1. Can self-associate. The CENPA-H4 heterotetramer can bind DNA by itself (in vitro). Interacts with CDK1, PPP1CA and RBBP7.By similarity

Protein-protein interaction databases

IntActiO35216. 2 interactors.
MINTiMINT-237454.
STRINGi10090.ENSMUSP00000122831.

Structurei

3D structure databases

ProteinModelPortaliO35216.
SMRiO35216.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni34 – 48Important for flexibility of DNA ends that protrude from nucleosomesBy similarityAdd BLAST15
Regioni35 – 134H3-likeAdd BLAST100
Regioni69 – 110CATDAdd BLAST42

Domaini

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

Sequence similaritiesi

Belongs to the histone H3 family.Curated

Phylogenomic databases

eggNOGiKOG1745. Eukaryota.
COG2036. LUCA.
GeneTreeiENSGT00840000129844.
HOVERGENiHBG001172.
InParanoidiO35216.
KOiK11495.
OMAiHLLIRKY.
OrthoDBiEOG091G13T2.
PhylomeDBiO35216.
TreeFamiTF354293.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_H2A/H2B/H3.
IPR000164. Histone_H3/CENP-A.
[Graphical view]
PANTHERiPTHR11426. PTHR11426. 1 hit.
PfamiPF00125. Histone. 1 hit.
[Graphical view]
PRINTSiPR00622. HISTONEH3.
SMARTiSM00428. H3. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O35216-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGPRRKPQTP RRRPSSPAPG PSRQSSSVGS QTLRRRQKFM WLKEIKTLQK
60 70 80 90 100
STDLLFRKKP FSMVVREICE KFSRGVDFWW QAQALLALQE AAEAFLIHLF
110 120 130
EDAYLLSLHA GRVTLFPKDI QLTRRIRGFE GGLP
Length:134
Mass (Da):15,509
Last modified:January 1, 1998 - v1
Checksum:i0381FA6492E43C3D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF012709 mRNA. Translation: AAC39957.1.
AF012710 Genomic DNA. Translation: AAC39958.1.
AK010718 mRNA. Translation: BAB27140.1.
AK011399 mRNA. Translation: BAB27591.1.
AK053763 mRNA. Translation: BAC35512.1.
AK089033 mRNA. Translation: BAC40710.1.
BC011038 mRNA. Translation: AAH11038.1.
CCDSiCCDS19162.1.
RefSeqiNP_001289058.1. NM_001302129.1.
NP_001289059.1. NM_001302130.1.
NP_001289060.1. NM_001302131.1.
NP_001289061.1. NM_001302132.1.
NP_031707.1. NM_007681.3.
UniGeneiMm.290563.

Genome annotation databases

EnsembliENSMUST00000144742; ENSMUSP00000122831; ENSMUSG00000029177.
GeneIDi12615.
KEGGimmu:12615.
UCSCiuc008wvt.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF012709 mRNA. Translation: AAC39957.1.
AF012710 Genomic DNA. Translation: AAC39958.1.
AK010718 mRNA. Translation: BAB27140.1.
AK011399 mRNA. Translation: BAB27591.1.
AK053763 mRNA. Translation: BAC35512.1.
AK089033 mRNA. Translation: BAC40710.1.
BC011038 mRNA. Translation: AAH11038.1.
CCDSiCCDS19162.1.
RefSeqiNP_001289058.1. NM_001302129.1.
NP_001289059.1. NM_001302130.1.
NP_001289060.1. NM_001302131.1.
NP_001289061.1. NM_001302132.1.
NP_031707.1. NM_007681.3.
UniGeneiMm.290563.

3D structure databases

ProteinModelPortaliO35216.
SMRiO35216.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO35216. 2 interactors.
MINTiMINT-237454.
STRINGi10090.ENSMUSP00000122831.

PTM databases

iPTMnetiO35216.
PhosphoSitePlusiO35216.

Proteomic databases

MaxQBiO35216.
PaxDbiO35216.
PeptideAtlasiO35216.
PRIDEiO35216.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000144742; ENSMUSP00000122831; ENSMUSG00000029177.
GeneIDi12615.
KEGGimmu:12615.
UCSCiuc008wvt.2. mouse.

Organism-specific databases

CTDi1058.
MGIiMGI:88375. Cenpa.

Phylogenomic databases

eggNOGiKOG1745. Eukaryota.
COG2036. LUCA.
GeneTreeiENSGT00840000129844.
HOVERGENiHBG001172.
InParanoidiO35216.
KOiK11495.
OMAiHLLIRKY.
OrthoDBiEOG091G13T2.
PhylomeDBiO35216.
TreeFamiTF354293.

Enzyme and pathway databases

ReactomeiR-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2500257. Resolution of Sister Chromatid Cohesion.
R-MMU-5663220. RHO GTPases Activate Formins.
R-MMU-606279. Deposition of new CENPA-containing nucleosomes at the centromere.
R-MMU-68877. Mitotic Prometaphase.

Miscellaneous databases

PROiO35216.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000029177.
CleanExiMM_CENPA.
ExpressionAtlasiO35216. baseline and differential.
GenevisibleiO35216. MM.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_H2A/H2B/H3.
IPR000164. Histone_H3/CENP-A.
[Graphical view]
PANTHERiPTHR11426. PTHR11426. 1 hit.
PfamiPF00125. Histone. 1 hit.
[Graphical view]
PRINTSiPR00622. HISTONEH3.
SMARTiSM00428. H3. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiCENPA_MOUSE
AccessioniPrimary (citable) accession number: O35216
Secondary accession number(s): Q545C9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: November 30, 2016
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.