Skip Header

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

P04908

- H2A1B_HUMAN

UniProt

P04908 - H2A1B_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 1-B/E

Gene

HIST1H2AB

more
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
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_169185. DNA Damage/Telomere Stress Induced Senescence.
REACT_169436. Oxidative Stress Induced Senescence.
REACT_172610. HATs acetylate histones.
REACT_172744. Condensation of Prophase Chromosomes.
REACT_200753. formation of the beta-catenin:TCF transactivating complex.
REACT_200808. PRC2 methylates histones and DNA.
REACT_200827. SIRT1 negatively regulates rRNA Expression.
REACT_200856. NoRC negatively regulates rRNA expression.
REACT_2204. RNA Polymerase I Chain Elongation.
REACT_22186. Deposition of new CENPA-containing nucleosomes at the centromere.
REACT_2232. RNA Polymerase I Promoter Opening.
REACT_27271. Meiotic recombination.
REACT_75792. Meiotic synapsis.
REACT_75925. Amyloids.
REACT_7963. Packaging Of Telomere Ends.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H2A type 1-B/E
Alternative name(s):
Histone H2A.2
Histone H2A/a
Histone H2A/m
Gene namesi
Name:HIST1H2AB
Synonyms:H2AFM
AND
Name:HIST1H2AE
Synonyms:H2AFA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:4734. HIST1H2AB.
HGNC:4724. HIST1H2AE.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProtKB
  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

PharmGKBiPA29111.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 130129Histone H2A type 1-B/EPRO_0000055237Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine3 Publications
Modified residuei2 – 21Phosphoserine; by RPS6KA52 Publications
Modified residuei4 – 41Citrulline; alternate1 Publication
Modified residuei4 – 41Symmetric dimethylarginine; by PRMT5; alternateBy similarity
Modified residuei6 – 61N6-acetyllysineBy 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 residuei37 – 371N6-crotonyllysine1 Publication
Modified residuei105 – 1051N5-methylglutamine1 Publication
Modified residuei119 – 1191N6-crotonyllysine1 Publication
Modified residuei120 – 1201N6-crotonyllysine; alternate1 Publication
Cross-linki120 – 120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate3 Publications
Modified residuei121 – 1211Phosphothreonine; by VPRBP2 Publications
Modified residuei126 – 1261N6-crotonyllysine1 Publication

Post-translational modificationi

Deiminated on Arg-4 in granulocytes upon calcium entry.
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.10 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.6 Publications
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
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.1 Publication

Keywords - PTMi

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

Proteomic databases

PaxDbiP04908.
PRIDEiP04908.

PTM databases

PhosphoSiteiP04908.

Expressioni

Gene expression databases

BgeeiP04908.
CleanExiHS_HIST1H2AB.
HS_HIST1H2AE.
ExpressionAtlasiP04908. differential.
GenevestigatoriP04908.

Organism-specific databases

HPAiCAB011483.
CAB012242.

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

BioGridi109266. 16 interactions.
113931. 33 interactions.
DIPiDIP-44197N.
IntActiP04908. 26 interactions.
MINTiMINT-1139478.
STRINGi9606.ENSP00000259791.

Structurei

Secondary structure

1
130
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi18 – 225
Helixi28 – 369
Turni37 – 393
Beta strandi42 – 443
Helixi47 – 7327
Beta strandi77 – 793
Helixi81 – 899
Helixi92 – 976
Turni98 – 1003
Beta strandi101 – 1033
Helixi114 – 1163

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CV5X-ray2.50C/G1-130[»]
3A6NX-ray2.70C/G1-130[»]
3AFAX-ray2.50C/G1-130[»]
3AN2X-ray3.60C/G1-130[»]
3AV1X-ray2.50C/G1-130[»]
3AV2X-ray2.80C/G1-130[»]
3AYWX-ray2.90C/G1-130[»]
3AZEX-ray3.00C/G1-130[»]
3AZFX-ray2.70C/G1-130[»]
3AZGX-ray2.40C/G1-130[»]
3AZHX-ray3.49C/G1-130[»]
3AZIX-ray2.70C/G1-130[»]
3AZJX-ray2.89C/G1-130[»]
3AZKX-ray3.20C/G1-130[»]
3AZLX-ray2.70C/G1-130[»]
3AZMX-ray2.89C/G1-130[»]
3AZNX-ray3.00C/G1-130[»]
3W96X-ray3.00C/G11-130[»]
3W97X-ray3.20C/G1-130[»]
3W98X-ray3.42C/G1-130[»]
3W99X-ray3.00C/G1-130[»]
3WKJX-ray2.80C/G1-130[»]
ProteinModelPortaliP04908.
SMRiP04908. Positions 12-119.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04908.

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H2A family.Curated

Phylogenomic databases

eggNOGiCOG5262.
HOGENOMiHOG000234652.
HOVERGENiHBG009342.
InParanoidiP04908.
KOiK11251.
OMAiTKNAQSR.
OrthoDBiEOG7M0NTR.
PhylomeDBiP04908.
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.

P04908-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSGRGKQGGK ARAKAKTRSS RAGLQFPVGR VHRLLRKGNY SERVGAGAPV
60 70 80 90 100
YLAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGR
110 120 130
VTIAQGGVLP NIQAVLLPKK TESHHKAKGK
Length:130
Mass (Da):14,135
Last modified:January 23, 2007 - v2
Checksum:i9CFE6184B2CC89F5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti38 – 392GN → AH in CAA24951. (PubMed:6647026)Curated

Mass spectrometryi

Molecular mass is 14037.9 Da from positions 2 - 130. Determined by ESI. Monoisotopic with N-acetylserine.1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X00089 Genomic DNA. Translation: CAA24951.1.
M60752 Genomic DNA. Translation: AAA63191.1.
Z83741 Genomic DNA. Translation: CAB06036.1.
AY131983 Genomic DNA. Translation: AAN59964.1.
AY131986 Genomic DNA. Translation: AAN59967.1.
AL031777 Genomic DNA. Translation: CAB39192.1.
BC093836 mRNA. Translation: AAH93836.1.
BC093862 mRNA. Translation: AAH93862.1.
CCDSiCCDS4574.1.
CCDS4595.1.
PIRiB26318. HSHUA5.
G40335.
RefSeqiNP_003504.2. NM_003513.2.
NP_066390.1. NM_021052.2.
UniGeneiHs.121017.
Hs.248174.

Genome annotation databases

EnsembliENST00000303910; ENSP00000303373; ENSG00000277075.
ENST00000615868; ENSP00000483842; ENSG00000278463.
GeneIDi3012.
8335.
KEGGihsa:3012.
hsa:8335.
UCSCiuc003nft.1. human.

Polymorphism databases

DMDMi124028530.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X00089 Genomic DNA. Translation: CAA24951.1 .
M60752 Genomic DNA. Translation: AAA63191.1 .
Z83741 Genomic DNA. Translation: CAB06036.1 .
AY131983 Genomic DNA. Translation: AAN59964.1 .
AY131986 Genomic DNA. Translation: AAN59967.1 .
AL031777 Genomic DNA. Translation: CAB39192.1 .
BC093836 mRNA. Translation: AAH93836.1 .
BC093862 mRNA. Translation: AAH93862.1 .
CCDSi CCDS4574.1.
CCDS4595.1.
PIRi B26318. HSHUA5.
G40335.
RefSeqi NP_003504.2. NM_003513.2.
NP_066390.1. NM_021052.2.
UniGenei Hs.121017.
Hs.248174.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2CV5 X-ray 2.50 C/G 1-130 [» ]
3A6N X-ray 2.70 C/G 1-130 [» ]
3AFA X-ray 2.50 C/G 1-130 [» ]
3AN2 X-ray 3.60 C/G 1-130 [» ]
3AV1 X-ray 2.50 C/G 1-130 [» ]
3AV2 X-ray 2.80 C/G 1-130 [» ]
3AYW X-ray 2.90 C/G 1-130 [» ]
3AZE X-ray 3.00 C/G 1-130 [» ]
3AZF X-ray 2.70 C/G 1-130 [» ]
3AZG X-ray 2.40 C/G 1-130 [» ]
3AZH X-ray 3.49 C/G 1-130 [» ]
3AZI X-ray 2.70 C/G 1-130 [» ]
3AZJ X-ray 2.89 C/G 1-130 [» ]
3AZK X-ray 3.20 C/G 1-130 [» ]
3AZL X-ray 2.70 C/G 1-130 [» ]
3AZM X-ray 2.89 C/G 1-130 [» ]
3AZN X-ray 3.00 C/G 1-130 [» ]
3W96 X-ray 3.00 C/G 11-130 [» ]
3W97 X-ray 3.20 C/G 1-130 [» ]
3W98 X-ray 3.42 C/G 1-130 [» ]
3W99 X-ray 3.00 C/G 1-130 [» ]
3WKJ X-ray 2.80 C/G 1-130 [» ]
ProteinModelPortali P04908.
SMRi P04908. Positions 12-119.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109266. 16 interactions.
113931. 33 interactions.
DIPi DIP-44197N.
IntActi P04908. 26 interactions.
MINTi MINT-1139478.
STRINGi 9606.ENSP00000259791.

PTM databases

PhosphoSitei P04908.

Polymorphism databases

DMDMi 124028530.

Proteomic databases

PaxDbi P04908.
PRIDEi P04908.

Protocols and materials databases

DNASUi 3012.
8335.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000303910 ; ENSP00000303373 ; ENSG00000277075 .
ENST00000615868 ; ENSP00000483842 ; ENSG00000278463 .
GeneIDi 3012.
8335.
KEGGi hsa:3012.
hsa:8335.
UCSCi uc003nft.1. human.

Organism-specific databases

CTDi 3012.
8335.
GeneCardsi GC06M026033.
GC06P026295.
HGNCi HGNC:4734. HIST1H2AB.
HGNC:4724. HIST1H2AE.
HPAi CAB011483.
CAB012242.
MIMi 602786. gene.
602795. gene.
neXtProti NX_P04908.
PharmGKBi PA29111.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5262.
HOGENOMi HOG000234652.
HOVERGENi HBG009342.
InParanoidi P04908.
KOi K11251.
OMAi TKNAQSR.
OrthoDBi EOG7M0NTR.
PhylomeDBi P04908.
TreeFami TF300137.

Enzyme and pathway databases

Reactomei REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_169185. DNA Damage/Telomere Stress Induced Senescence.
REACT_169436. Oxidative Stress Induced Senescence.
REACT_172610. HATs acetylate histones.
REACT_172744. Condensation of Prophase Chromosomes.
REACT_200753. formation of the beta-catenin:TCF transactivating complex.
REACT_200808. PRC2 methylates histones and DNA.
REACT_200827. SIRT1 negatively regulates rRNA Expression.
REACT_200856. NoRC negatively regulates rRNA expression.
REACT_2204. RNA Polymerase I Chain Elongation.
REACT_22186. Deposition of new CENPA-containing nucleosomes at the centromere.
REACT_2232. RNA Polymerase I Promoter Opening.
REACT_27271. Meiotic recombination.
REACT_75792. Meiotic synapsis.
REACT_75925. Amyloids.
REACT_7963. Packaging Of Telomere Ends.

Miscellaneous databases

EvolutionaryTracei P04908.
GeneWikii HIST1H2AB.
HIST1H2AE.
NextBioi 11940.
PROi P04908.
SOURCEi Search...

Gene expression databases

Bgeei P04908.
CleanExi HS_HIST1H2AB.
HS_HIST1H2AE.
ExpressionAtlasi P04908. differential.
Genevestigatori P04908.

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 primary structure and expression of four cloned human histone genes."
    Zhong R., Roeder R.G., Heintz N.
    Nucleic Acids Res. 11:7409-7425(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H2AB).
  2. "Isolation and characterization of two human H1 histone genes within clusters of core histone genes."
    Albig W., Kardalinou E., Drabent B., Zimmer A., Doenecke D.
    Genomics 10:940-948(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H2AE).
  3. "The human histone gene cluster at the D6S105 locus."
    Albig W., Doenecke D.
    Hum. Genet. 101:284-294(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H2AE).
  4. "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] (HIST1H2AB AND HIST1H2AE).
  5. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (HIST1H2AE).
    Tissue: Liver.
  7. "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.
  8. "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.
  9. "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.
  10. "Global regulation of post-translational modifications on core histones."
    Galasinski S.C., Louie D.F., Gloor K.K., Resing K.A., Ahn N.G.
    J. Biol. Chem. 277:2579-2588(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT SER-2, ACETYLATION AT SER-2.
  11. "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.
  12. "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.
  13. Cited for: UBIQUITINATION AT LYS-120.
  14. "Precise characterization of human histones in the H2A gene family by top down mass spectrometry."
    Boyne M.T. II, Pesavento J.J., Mizzen C.A., Kelleher N.L.
    J. Proteome Res. 5:248-253(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY, ACETYLATION AT SER-2.
  15. "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.
  16. "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.
  17. Cited for: UBIQUITINATION.
  18. "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.
  19. "Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification."
    Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., Buchou T., Cheng Z., Rousseaux S., Rajagopal N., Lu Z., Ye Z., Zhu Q., Wysocka J., Ye Y., Khochbin S., Ren B., Zhao Y.
    Cell 146:1016-1028(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: CROTONYLATION AT LYS-37; LYS-119; LYS-120 AND LYS-126.
  20. "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.
  21. "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.
  22. "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.
  23. "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.

Entry informationi

Entry nameiH2A1B_HUMAN
AccessioniPrimary (citable) accession number: P04908
Secondary accession number(s): P28001, Q76P63
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 153 of the entry and version 2 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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