SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8IUE6

- H2A2B_HUMAN

UniProt

Q8IUE6 - H2A2B_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Histone H2A type 2-B

Gene
HIST2H2AB
Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. DNA binding Source: UniProtKB-KW

GO - Biological processi

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

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_172610. HATs acetylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H2A type 2-B
Gene namesi
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:20508. HIST2H2AB.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. nucleosome Source: UniProtKB-KW
  3. nucleus Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2 – 21S → A: Blocks the inhibition of transcription by RPS6KA5/MSK1. 1 Publication

Organism-specific databases

PharmGKBiPA134884141.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 130129Histone H2A type 2-BPRO_0000227505Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei2 – 21Phosphoserine; by RPS6KA51 Publication
Modified residuei4 – 41Citrulline; alternate
Modified residuei4 – 41Symmetric dimethylarginine; by PRMT5; alternate By similarity
Modified residuei6 – 61N6-acetyllysine By similarity
Cross-linki14 – 14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
Cross-linki16 – 16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
Modified residuei105 – 1051N5-methylglutamine1 Publication
Cross-linki120 – 120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)3 Publications
Modified residuei121 – 1211Phosphothreonine; by VPRBP2 Publications

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.9 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.1 Publication
Deiminated on Arg-4 in granulocytes upon calcium entry.
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 (1 Publication).
Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage By similarity.

Keywords - PTMi

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

Proteomic databases

MaxQBiQ8IUE6.
PaxDbiQ8IUE6.
PeptideAtlasiQ8IUE6.
PRIDEiQ8IUE6.

PTM databases

PhosphoSiteiQ8IUE6.

Expressioni

Gene expression databases

BgeeiQ8IUE6.
CleanExiHS_HIST2H2AB.
GenevestigatoriQ8IUE6.

Organism-specific databases

HPAiHPA041189.

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. 15 interactions.
IntActiQ8IUE6. 3 interactions.
MINTiMINT-2809410.
STRINGi9606.ENSP00000332790.

Structurei

3D structure databases

ProteinModelPortaliQ8IUE6.
SMRiQ8IUE6. Positions 14-119.

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H2A family.

Phylogenomic databases

eggNOGiCOG5262.
HOGENOMiHOG000234652.
HOVERGENiHBG009342.
InParanoidiQ8IUE6.
KOiK11251.
OMAiKAGQKGD.
OrthoDBiEOG7M0NTR.
PhylomeDBiQ8IUE6.
TreeFamiTF300137.

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.

Q8IUE6-1 [UniParc]FASTAAdd to Basket

« Hide

MSGRGKQGGK ARAKAKSRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV    50
YLAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAVRN DEELNKLLGG 100
VTIAQGGVLP NIQAVLLPKK TESHKPGKNK 130
Length:130
Mass (Da):13,995
Last modified:January 23, 2007 - v3
Checksum:i87932FEA853F5E93
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti53 – 531A → T in a breast cancer sample; somatic mutation. 1 Publication
VAR_035802

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
ENST00000579360; ENSP00000462774; ENSG00000263965.
GeneIDi317772.
KEGGihsa:317772.
UCSCiuc001ete.3. human.

Polymorphism databases

DMDMi74750623.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY131972 Genomic DNA. Translation: AAN59958.1 .
AL591493 Genomic DNA. Translation: CAI12570.1 .
CCDSi CCDS938.1.
RefSeqi NP_778235.1. NM_175065.2.
UniGenei Hs.664173.

3D structure databases

ProteinModelPortali Q8IUE6.
SMRi Q8IUE6. Positions 14-119.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 130469. 15 interactions.
IntActi Q8IUE6. 3 interactions.
MINTi MINT-2809410.
STRINGi 9606.ENSP00000332790.

PTM databases

PhosphoSitei Q8IUE6.

Polymorphism databases

DMDMi 74750623.

Proteomic databases

MaxQBi Q8IUE6.
PaxDbi Q8IUE6.
PeptideAtlasi Q8IUE6.
PRIDEi Q8IUE6.

Protocols and materials databases

DNASUi 317772.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000331128 ; ENSP00000332790 ; ENSG00000184270 .
ENST00000579360 ; ENSP00000462774 ; ENSG00000263965 .
GeneIDi 317772.
KEGGi hsa:317772.
UCSCi uc001ete.3. human.

Organism-specific databases

CTDi 317772.
GeneCardsi GC01M149861.
HGNCi HGNC:20508. HIST2H2AB.
HPAi HPA041189.
MIMi 615014. gene.
neXtProti NX_Q8IUE6.
PharmGKBi PA134884141.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5262.
HOGENOMi HOG000234652.
HOVERGENi HBG009342.
InParanoidi Q8IUE6.
KOi K11251.
OMAi KAGQKGD.
OrthoDBi EOG7M0NTR.
PhylomeDBi Q8IUE6.
TreeFami TF300137.

Enzyme and pathway databases

Reactomei REACT_172610. HATs acetylate histones.

Miscellaneous databases

GeneWikii HIST2H2AB.
GenomeRNAii 317772.
NextBioi 96429.
PROi Q8IUE6.
SOURCEi Search...

Gene expression databases

Bgeei Q8IUE6.
CleanExi HS_HIST2H2AB.
Genevestigatori Q8IUE6.

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

« Hide 'large scale' publications
  1. "The human and mouse replication-dependent histone genes."
    Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.
    Genomics 80:487-498(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Nucleosomal histone kinase-1 phosphorylates H2A Thr 119 during mitosis in the early Drosophila embryo."
    Aihara H., Nakagawa T., Yasui K., Ohta T., Hirose S., Dhomae N., Takio K., Kaneko M., Takeshima Y., Muramatsu M., Ito T.
    Genes Dev. 18:877-888(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-121.
  4. "Phosphorylation of histone H2A inhibits transcription on chromatin templates."
    Zhang Y., Griffin K., Mondal N., Parvin J.D.
    J. Biol. Chem. 279:21866-21872(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-2, MUTAGENESIS OF SER-2.
  5. "Role of histone H2A ubiquitination in Polycomb silencing."
    Wang H., Wang L., Erdjument-Bromage H., Vidal M., Tempst P., Jones R.S., Zhang Y.
    Nature 431:873-878(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION AT LYS-120.
  6. "Deimination of histone H2A and H4 at arginine 3 in HL-60 granulocytes."
    Hagiwara T., Hidaka Y., Yamada M.
    Biochemistry 44:5827-5834(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT SER-2, CITRULLINATION AT ARG-4, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing."
    Cao R., Tsukada Y., Zhang Y.
    Mol. Cell 20:845-854(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION AT LYS-120.
  8. Cited for: UBIQUITINATION AT LYS-120.
  9. "RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins."
    Mailand N., Bekker-Jensen S., Faustrup H., Melander F., Bartek J., Lukas C., Lukas J.
    Cell 131:887-900(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION.
  10. "RNF8 transduces the DNA-damage signal via histone ubiquitylation and checkpoint protein assembly."
    Huen M.S.Y., Grant R., Manke I., Minn K., Yu X., Yaffe M.B., Chen J.
    Cell 131:901-914(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION.
  11. Cited for: UBIQUITINATION.
  12. "RNF168 binds and amplifies ubiquitin conjugates on damaged chromosomes to allow accumulation of repair proteins."
    Doil C., Mailand N., Bekker-Jensen S., Menard P., Larsen D.H., Pepperkok R., Ellenberg J., Panier S., Durocher D., Bartek J., Lukas J., Lukas C.
    Cell 136:435-446(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "RNF168 ubiquitinates K13-15 on H2A/H2AX to drive DNA Damage signaling."
    Mattiroli F., Vissers J.H., van Dijk W.J., Ikpa P., Citterio E., Vermeulen W., Marteijn J.A., Sixma T.K.
    Cell 150:1182-1195(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION AT LYS-14 AND LYS-16 BY RNF168.
  15. "A novel ubiquitin mark at the N-terminal tail of histone H2As targeted by RNF168 ubiquitin ligase."
    Gatti M., Pinato S., Maspero E., Soffientini P., Polo S., Penengo L.
    Cell Cycle 11:2538-2544(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION AT LYS-14 AND LYS-16 BY RNF168.
  16. "VprBP has intrinsic kinase activity targeting histone H2A and represses gene transcription."
    Kim K., Kim J.M., Kim J.S., Choi J., Lee Y.S., Neamati N., Song J.S., Heo K., An W.
    Mol. Cell 52:459-467(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-121.
  17. "Glutamine methylation in histone H2A is an RNA-polymerase-I-dedicated modification."
    Tessarz P., Santos-Rosa H., Robson S.C., Sylvestersen K.B., Nelson C.J., Nielsen M.L., Kouzarides T.
    Nature 505:564-568(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT GLN-105.
  18. Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-53.

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: September 3, 2014
This is version 104 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

External Data

Dasty 3

Similar proteinsi