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A1A4R1

- H2A2C_BOVIN

UniProt

A1A4R1 - H2A2C_BOVIN

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Protein
Histone H2A type 2-C
Gene
HIST2H2AC
Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

Functioni

Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
Complete GO annotation...

GO - Biological processi

  1. nucleosome assembly Source: InterPro
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_209769. Meiotic recombination.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H2A type 2-C
Gene namesi
Name:HIST2H2AC
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. nucleosome Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 129128Histone H2A type 2-C
PRO_0000281917Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine By similarity
Modified residuei2 – 21Phosphoserine; by RPS6KA5 By similarity
Modified residuei4 – 41Citrulline; alternate By similarity
Modified residuei4 – 41Symmetric dimethylarginine; by PRMT5; alternate By similarity
Modified residuei6 – 61N6-acetyllysine By similarity
Modified residuei10 – 101N6-acetyllysine By similarity
Cross-linki14 – 14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-linki16 – 16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Modified residuei37 – 371N6-crotonyllysine By similarity
Modified residuei105 – 1051N5-methylglutamine By similarity
Modified residuei119 – 1191N6-crotonyllysine By similarity
Modified residuei120 – 1201N6-crotonyllysine; alternate By similarity
Cross-linki120 – 120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity
Modified residuei121 – 1211Phosphothreonine; by VPRBP By similarity
Modified residuei123 – 1231Phosphoserine By similarity
Modified residuei125 – 1251N6-crotonyllysine By similarity

Post-translational modificationi

Monoubiquitination of Lys-120 (H2AK119Ub) by RING1 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is involved in the initiation of both imprinted and random X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome chromatin. Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3 (H3K27me). H2AK119Ub by RNF2/RING2 can also be induced by ultraviolet and may be involved in DNA repair. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage. Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro. H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events By similarity.
Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1. Phosphorylation at Thr-121 (H2AT120ph) by VPRBP is present in the regulatory region of many tumor suppresor genes and down-regulates their transcription By similarity.
Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex By similarity.
Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage By similarity.
Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes By similarity.

Keywords - PTMi

Acetylation, Citrullination, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiA1A4R1.
PRIDEiA1A4R1.

Interactioni

Subunit structurei

The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000052035.

Structurei

3D structure databases

ProteinModelPortaliA1A4R1.
SMRiA1A4R1. Positions 14-119.

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H2A family.

Phylogenomic databases

eggNOGiCOG5262.
HOGENOMiHOG000234652.
HOVERGENiHBG009342.
InParanoidiA1A4R1.
KOiK11251.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR002119. Histone_H2A.
[Graphical view]
PfamiPF00125. Histone. 1 hit.
[Graphical view]
PRINTSiPR00620. HISTONEH2A.
SMARTiSM00414. H2A. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS00046. HISTONE_H2A. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

A1A4R1-1 [UniParc]FASTAAdd to Basket

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MSGRGKQGGK ARAKAKSRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV    50
YMAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGK 100
VTIAQGGVLP NIQAVLLPKK TESHKAKSK 129
Length:129
Mass (Da):13,988
Last modified:January 23, 2007 - v1
Checksum:i358AE20D1C531724
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC126824 mRNA. Translation: AAI26825.1.
RefSeqiNP_001075189.1. NM_001081720.2.
UniGeneiBt.12047.

Genome annotation databases

GeneIDi513666.
KEGGibta:513666.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC126824 mRNA. Translation: AAI26825.1 .
RefSeqi NP_001075189.1. NM_001081720.2.
UniGenei Bt.12047.

3D structure databases

ProteinModelPortali A1A4R1.
SMRi A1A4R1. Positions 14-119.
ModBasei Search...

Protein-protein interaction databases

STRINGi 9913.ENSBTAP00000052035.

Proteomic databases

PaxDbi A1A4R1.
PRIDEi A1A4R1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 513666.
KEGGi bta:513666.

Organism-specific databases

CTDi 8338.

Phylogenomic databases

eggNOGi COG5262.
HOGENOMi HOG000234652.
HOVERGENi HBG009342.
InParanoidi A1A4R1.
KOi K11251.

Enzyme and pathway databases

Reactomei REACT_209769. Meiotic recombination.

Miscellaneous databases

NextBioi 20870973.

Family and domain databases

Gene3Di 1.10.20.10. 1 hit.
InterProi IPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR002119. Histone_H2A.
[Graphical view ]
Pfami PF00125. Histone. 1 hit.
[Graphical view ]
PRINTSi PR00620. HISTONEH2A.
SMARTi SM00414. H2A. 1 hit.
[Graphical view ]
SUPFAMi SSF47113. SSF47113. 1 hit.
PROSITEi PS00046. HISTONE_H2A. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. NIH - Mammalian Gene Collection (MGC) project
    Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Fetal lung.

Entry informationi

Entry nameiH2A2C_BOVIN
AccessioniPrimary (citable) accession number: A1A4R1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 55 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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