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Protein

Histone H2A type 2-B

Gene

HIST2H2AB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciZFISH:G66-33449-MONOMER.
ReactomeiR-HSA-3214815. HDACs deacetylate histones.
R-HSA-3214847. HATs acetylate histones.
R-HSA-3214858. RMTs methylate histone arginines.
R-HSA-5689603. UCH proteinases.
R-HSA-5689880. Ub-specific processing proteases.
R-HSA-5689901. Metalloprotease DUBs.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H2A type 2-B
Gene namesi
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:20508. HIST2H2AB.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • nuclear chromatin Source: GO_Central
  • nucleosome Source: UniProtKB-KW
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi2S → A: Blocks the inhibition of transcription by RPS6KA5/MSK1. 1 Publication1

Organism-specific databases

OpenTargetsiENSG00000184270.
PharmGKBiPA134884141.

Polymorphism and mutation databases

BioMutaiHIST2H2AB.
DMDMi74750623.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00002275052 – 130Histone H2A type 2-BAdd BLAST129

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserine1 Publication1
Modified residuei2Phosphoserine; by RPS6KA51 Publication1
Modified residuei4Citrulline; alternate1 Publication1
Modified residuei4Symmetric dimethylarginine; by PRMT5; alternateBy similarity1
Cross-linki14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
Cross-linki16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
Modified residuei37N6-crotonyllysine1 Publication1
Modified residuei105N5-methylglutamine1 Publication1
Modified residuei119N6-crotonyllysine1 Publication1
Modified residuei120N6-crotonyllysine; alternate1 Publication1
Cross-linki120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate4 Publications
Modified residuei121Phosphothreonine; by VPRBP2 Publications1

Post-translational modificationi

Deiminated on Arg-4 in granulocytes upon calcium entry.1 Publication
Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM27 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. Monoubiquitination of Lys-120 (H2AK119Ub) by TRIM27 may promote transformation of cells in a number of breast cancers (PubMed:25470042). 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.11 Publications
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.4 Publications
Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage.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 (PubMed:24352239).1 Publication
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.1 Publication

Keywords - PTMi

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

Proteomic databases

EPDiQ8IUE6.
MaxQBiQ8IUE6.
PaxDbiQ8IUE6.
PeptideAtlasiQ8IUE6.
PRIDEiQ8IUE6.
TopDownProteomicsiQ8IUE6.

PTM databases

iPTMnetiQ8IUE6.
PhosphoSitePlusiQ8IUE6.
SwissPalmiQ8IUE6.

Expressioni

Gene expression databases

BgeeiENSG00000184270.
CleanExiHS_HIST2H2AB.

Organism-specific databases

HPAiCAB011483.
HPA041189.

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

BioGridi130469. 56 interactors.
IntActiQ8IUE6. 3 interactors.
MINTiMINT-2809410.
STRINGi9606.ENSP00000332790.

Structurei

3D structure databases

ProteinModelPortaliQ8IUE6.
SMRiQ8IUE6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H2A family.Curated

Phylogenomic databases

eggNOGiKOG1756. Eukaryota.
COG5262. LUCA.
GeneTreeiENSGT00760000118934.
HOGENOMiHOG000234652.
HOVERGENiHBG009342.
InParanoidiQ8IUE6.
KOiK11251.
OMAiAVEFEMS.
OrthoDBiEOG091G0XGD.
PhylomeDBiQ8IUE6.
TreeFamiTF300137.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR002119. Histone_H2A.
IPR007125. Histone_H2A/H2B/H3.
IPR032454. Histone_H2A_C.
IPR032458. Histone_H2A_CS.
[Graphical view]
PfamiPF00125. Histone. 1 hit.
PF16211. Histone_H2A_C. 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.

Q8IUE6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGRGKQGGK ARAKAKSRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV
60 70 80 90 100
YLAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAVRN DEELNKLLGG
110 120 130
VTIAQGGVLP NIQAVLLPKK TESHKPGKNK
Length:130
Mass (Da):13,995
Last modified:January 23, 2007 - v3
Checksum:i87932FEA853F5E93
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03580253A → T in a breast cancer sample; somatic mutation. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY131972 Genomic DNA. Translation: AAN59958.1.
AL591493 Genomic DNA. Translation: CAI12570.1.
CCDSiCCDS938.1.
RefSeqiNP_778235.1. NM_175065.2.
UniGeneiHs.664173.

Genome annotation databases

EnsembliENST00000331128; ENSP00000332790; ENSG00000184270.
GeneIDi317772.
KEGGihsa:317772.
UCSCiuc001ete.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY131972 Genomic DNA. Translation: AAN59958.1.
AL591493 Genomic DNA. Translation: CAI12570.1.
CCDSiCCDS938.1.
RefSeqiNP_778235.1. NM_175065.2.
UniGeneiHs.664173.

3D structure databases

ProteinModelPortaliQ8IUE6.
SMRiQ8IUE6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi130469. 56 interactors.
IntActiQ8IUE6. 3 interactors.
MINTiMINT-2809410.
STRINGi9606.ENSP00000332790.

PTM databases

iPTMnetiQ8IUE6.
PhosphoSitePlusiQ8IUE6.
SwissPalmiQ8IUE6.

Polymorphism and mutation databases

BioMutaiHIST2H2AB.
DMDMi74750623.

Proteomic databases

EPDiQ8IUE6.
MaxQBiQ8IUE6.
PaxDbiQ8IUE6.
PeptideAtlasiQ8IUE6.
PRIDEiQ8IUE6.
TopDownProteomicsiQ8IUE6.

Protocols and materials databases

DNASUi317772.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000331128; ENSP00000332790; ENSG00000184270.
GeneIDi317772.
KEGGihsa:317772.
UCSCiuc001ete.4. human.

Organism-specific databases

CTDi317772.
GeneCardsiHIST2H2AB.
HGNCiHGNC:20508. HIST2H2AB.
HPAiCAB011483.
HPA041189.
MIMi615014. gene.
neXtProtiNX_Q8IUE6.
OpenTargetsiENSG00000184270.
PharmGKBiPA134884141.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1756. Eukaryota.
COG5262. LUCA.
GeneTreeiENSGT00760000118934.
HOGENOMiHOG000234652.
HOVERGENiHBG009342.
InParanoidiQ8IUE6.
KOiK11251.
OMAiAVEFEMS.
OrthoDBiEOG091G0XGD.
PhylomeDBiQ8IUE6.
TreeFamiTF300137.

Enzyme and pathway databases

BioCyciZFISH:G66-33449-MONOMER.
ReactomeiR-HSA-3214815. HDACs deacetylate histones.
R-HSA-3214847. HATs acetylate histones.
R-HSA-3214858. RMTs methylate histone arginines.
R-HSA-5689603. UCH proteinases.
R-HSA-5689880. Ub-specific processing proteases.
R-HSA-5689901. Metalloprotease DUBs.

Miscellaneous databases

GeneWikiiHIST2H2AB.
GenomeRNAii317772.
PROiQ8IUE6.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000184270.
CleanExiHS_HIST2H2AB.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR002119. Histone_H2A.
IPR007125. Histone_H2A/H2B/H3.
IPR032454. Histone_H2A_C.
IPR032458. Histone_H2A_CS.
[Graphical view]
PfamiPF00125. Histone. 1 hit.
PF16211. Histone_H2A_C. 1 hit.
[Graphical view]
PRINTSiPR00620. HISTONEH2A.
SMARTiSM00414. H2A. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS00046. HISTONE_H2A. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiH2A2B_HUMAN
AccessioniPrimary (citable) accession number: Q8IUE6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 125 of the entry and version 3 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.