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.

P0C0S8

- H2A1_HUMAN

UniProt

P0C0S8 - H2A1_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
Gene
HIST1H2AG, H2AFP
HIST1H2AI, H2AFC
HIST1H2AK, H2AFD
HIST1H2AL, H2AFI
HIST1H2AM, H2AFN less..
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
  2. enzyme binding Source: UniProtKB
  3. protein binding Source: IntAct
Complete GO annotation...

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

Organism-specific databases

Protein namesi
Recommended name:
Histone H2A type 1
Short name:
H2A.1
Alternative name(s):
Histone H2A/p
Gene namesi
Synonyms:H2AFP
AND
Synonyms:H2AFC
AND
Synonyms:H2AFD
AND
Synonyms:H2AFI
AND
Synonyms:H2AFN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6
HGNCiHGNC:4737. HIST1H2AG.
HGNC:4725. HIST1H2AI.
HGNC:4726. HIST1H2AK.
HGNC:4730. HIST1H2AL.
HGNC:4735. HIST1H2AM.

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

PharmGKBiPA29114.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 130129Histone H2A type 1
PRO_0000055235Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine3 Publications
Modified residuei2 – 21Phosphoserine; by RPS6KA52 Publications
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 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.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.3 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 (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

MaxQBiP0C0S8.
PRIDEiP0C0S8.

PTM databases

PhosphoSiteiP0C0S8.

Expressioni

Gene expression databases

ArrayExpressiP0C0S8.
BgeeiP0C0S8.
CleanExiHS_HIST1H2AG.
HS_HIST1H2AI.
HS_HIST1H2AK.
HS_HIST1H2AL.
HS_HIST1H2AM.
GenevestigatoriP0C0S8.

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
Q9DUM33EBI-1390628,EBI-7971837From a different organism.
IL33O957603EBI-1390628,EBI-724057
YWHAZP631042EBI-1390628,EBI-347088

Protein-protein interaction databases

BioGridi113925. 8 interactions.
113926. 9 interactions.
113928. 9 interactions.
113932. 10 interactions.
114459. 14 interactions.
DIPiDIP-39638N.
IntActiP0C0S8. 20 interactions.
MINTiMINT-1519720.
STRINGi9606.ENSP00000330307.

Structurei

3D structure databases

ProteinModelPortaliP0C0S8.
SMRiP0C0S8. Positions 14-119.

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H2A family.

Phylogenomic databases

HOGENOMiHOG000234652.
HOVERGENiHBG009342.
InParanoidiP0C0S8.
KOiK11251.
OMAiIAMSGRG.
OrthoDBiEOG7M0NTR.
PhylomeDBiP0C0S8.
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.

P0C0S8-1 [UniParc]FASTAAdd to Basket

« Hide

MSGRGKQGGK ARAKAKTRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV    50
YLAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGK 100
VTIAQGGVLP NIQAVLLPKK TESHHKAKGK 130
Length:130
Mass (Da):14,091
Last modified:January 23, 2007 - v2
Checksum:i48DD539793FE8256
GO

Mass spectrometryi

Molecular mass is 13993.9 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
Z83742 Genomic DNA. Translation: CAB06037.1.
Z83739 Genomic DNA. Translation: CAB06034.1.
X83549 Genomic DNA. Translation: CAA58539.1.
X57138 Genomic DNA. Translation: CAA40417.1.
L19778 mRNA. Translation: AAC24466.1.
AY131987 Genomic DNA. Translation: AAN59968.1.
AY131989 Genomic DNA. Translation: AAN59970.1.
AY131991 Genomic DNA. Translation: AAN59972.1.
AY131992 Genomic DNA. Translation: AAN59973.1.
AY131993 Genomic DNA. Translation: AAN59974.1.
Z98744 Genomic DNA. Translation: CAB11417.1.
Z98744 Genomic DNA. Translation: CAD24073.1.
Z98744 Genomic DNA. Translation: CAD24077.1.
AL009179 Genomic DNA. Translation: CAA15669.1.
AL021807 Genomic DNA. Translation: CAA16948.1.
BC016677 mRNA. Translation: AAH16677.1.
BC069306 mRNA. Translation: AAH69306.1.
BC104199 mRNA. Translation: AAI04200.1.
BC104198 mRNA. Translation: AAI04199.1.
BC105129 mRNA. Translation: AAI05130.1.
BC112072 mRNA. Translation: AAI12073.1.
BC112254 mRNA. Translation: AAI12255.1.
BC112256 mRNA. Translation: AAI12257.1.
CCDSiCCDS4619.1.
CCDS4626.1.
CCDS4632.1.
CCDS4634.1.
CCDS4639.1.
PIRiB56624. HSHUA1.
RefSeqiNP_003500.1. NM_003509.2.
NP_003501.1. NM_003510.2.
NP_003502.1. NM_003511.2.
NP_003505.1. NM_003514.2.
NP_066408.1. NM_021064.4.
UniGeneiHs.134999.
Hs.233568.
Hs.51011.
Hs.534035.
Hs.734717.

Genome annotation databases

EnsembliENST00000330180; ENSP00000330307; ENSG00000184348.
ENST00000357320; ENSP00000349873; ENSG00000198374.
ENST00000358739; ENSP00000351589; ENSG00000196747.
ENST00000359193; ENSP00000352119; ENSG00000196787.
ENST00000359611; ENSP00000352627; ENSG00000233224.
GeneIDi8329.
8330.
8332.
8336.
8969.
KEGGihsa:8329.
hsa:8330.
hsa:8332.
hsa:8336.
hsa:8969.
UCSCiuc003niw.3. human.

Polymorphism databases

DMDMi83288406.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z83742 Genomic DNA. Translation: CAB06037.1 .
Z83739 Genomic DNA. Translation: CAB06034.1 .
X83549 Genomic DNA. Translation: CAA58539.1 .
X57138 Genomic DNA. Translation: CAA40417.1 .
L19778 mRNA. Translation: AAC24466.1 .
AY131987 Genomic DNA. Translation: AAN59968.1 .
AY131989 Genomic DNA. Translation: AAN59970.1 .
AY131991 Genomic DNA. Translation: AAN59972.1 .
AY131992 Genomic DNA. Translation: AAN59973.1 .
AY131993 Genomic DNA. Translation: AAN59974.1 .
Z98744 Genomic DNA. Translation: CAB11417.1 .
Z98744 Genomic DNA. Translation: CAD24073.1 .
Z98744 Genomic DNA. Translation: CAD24077.1 .
AL009179 Genomic DNA. Translation: CAA15669.1 .
AL021807 Genomic DNA. Translation: CAA16948.1 .
BC016677 mRNA. Translation: AAH16677.1 .
BC069306 mRNA. Translation: AAH69306.1 .
BC104199 mRNA. Translation: AAI04200.1 .
BC104198 mRNA. Translation: AAI04199.1 .
BC105129 mRNA. Translation: AAI05130.1 .
BC112072 mRNA. Translation: AAI12073.1 .
BC112254 mRNA. Translation: AAI12255.1 .
BC112256 mRNA. Translation: AAI12257.1 .
CCDSi CCDS4619.1.
CCDS4626.1.
CCDS4632.1.
CCDS4634.1.
CCDS4639.1.
PIRi B56624. HSHUA1.
RefSeqi NP_003500.1. NM_003509.2.
NP_003501.1. NM_003510.2.
NP_003502.1. NM_003511.2.
NP_003505.1. NM_003514.2.
NP_066408.1. NM_021064.4.
UniGenei Hs.134999.
Hs.233568.
Hs.51011.
Hs.534035.
Hs.734717.

3D structure databases

ProteinModelPortali P0C0S8.
SMRi P0C0S8. Positions 14-119.
ModBasei Search...

Protein-protein interaction databases

BioGridi 113925. 8 interactions.
113926. 9 interactions.
113928. 9 interactions.
113932. 10 interactions.
114459. 14 interactions.
DIPi DIP-39638N.
IntActi P0C0S8. 20 interactions.
MINTi MINT-1519720.
STRINGi 9606.ENSP00000330307.

PTM databases

PhosphoSitei P0C0S8.

Polymorphism databases

DMDMi 83288406.

Proteomic databases

MaxQBi P0C0S8.
PRIDEi P0C0S8.

Protocols and materials databases

DNASUi 8329.
8330.
8332.
8969.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000330180 ; ENSP00000330307 ; ENSG00000184348 .
ENST00000357320 ; ENSP00000349873 ; ENSG00000198374 .
ENST00000358739 ; ENSP00000351589 ; ENSG00000196747 .
ENST00000359193 ; ENSP00000352119 ; ENSG00000196787 .
ENST00000359611 ; ENSP00000352627 ; ENSG00000233224 .
GeneIDi 8329.
8330.
8332.
8336.
8969.
KEGGi hsa:8329.
hsa:8330.
hsa:8332.
hsa:8336.
hsa:8969.
UCSCi uc003niw.3. human.

Organism-specific databases

CTDi 8329.
8330.
8332.
8336.
8969.
GeneCardsi GC06M027807.
GC06M027921.
GC06P027106.
GC06P027776.
GC06P027843.
H-InvDB HIX0200889.
HGNCi HGNC:4737. HIST1H2AG.
HGNC:4725. HIST1H2AI.
HGNC:4726. HIST1H2AK.
HGNC:4730. HIST1H2AL.
HGNC:4735. HIST1H2AM.
MIMi 602787. gene.
602788. gene.
602793. gene.
602796. gene.
615012. gene.
neXtProti NX_P0C0S8.
PharmGKBi PA29114.
GenAtlasi Search...

Phylogenomic databases

HOGENOMi HOG000234652.
HOVERGENi HBG009342.
InParanoidi P0C0S8.
KOi K11251.
OMAi IAMSGRG.
OrthoDBi EOG7M0NTR.
PhylomeDBi P0C0S8.
TreeFami TF300137.

Enzyme and pathway databases

Reactomei REACT_172610. HATs acetylate histones.

Miscellaneous databases

ChiTaRSi HIST1H2AM. human.
GeneWikii HIST1H2AG.
HIST1H2AI.
HIST1H2AK.
HIST1H2AL.
HIST1H2AM.
NextBioi 31190.
PROi P0C0S8.
SOURCEi Search...

Gene expression databases

ArrayExpressi P0C0S8.
Bgeei P0C0S8.
CleanExi HS_HIST1H2AG.
HS_HIST1H2AI.
HS_HIST1H2AK.
HS_HIST1H2AL.
HS_HIST1H2AM.
Genevestigatori P0C0S8.

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 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] (HIST1H2AI; HIST1H2AK AND HIST1H2AL).
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H2AI; HIST1H2AK AND HIST1H2AL).
  3. "A novel divergently transcribed human histone H2A/H2B gene pair."
    Dobner T., Wolf I., Mai B., Lipp M.
    DNA Seq. 1:409-413(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE (HIST1H2AM).
  4. "The relative expression of human histone H2A genes is similar in different types of proliferating cells."
    Mannironi C., Orr A., Hatch C., Pilch D., Ivanova V., Bonner W.
    DNA Cell Biol. 13:161-170(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE (HIST1H2AG).
  5. "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] (HIST1H2AG; HIST1H2AI; HIST1H2AK; HIST1H2AL AND HIST1H2AM).
  6. "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] (HIST1H2AI; HIST1H2AK; HIST1H2AL AND HIST1H2AM).
  7. "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].
    Tissue: Colon and Lymph.
  8. "Human spleen histone H2A. Isolation and four variant sequences."
    Hayashi T., Ohe Y., Hayashi H., Iwai K.
    J. Biochem. 88:27-34(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: AMINO-ACID COMPOSITION OF TRYPTIC PEPTIDES.
    Tissue: Spleen.
  9. "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.
  10. "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.
  11. "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.
  12. "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.
  13. "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.
  14. "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.
  15. Cited for: UBIQUITINATION AT LYS-120.
  16. "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.
  17. "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.
  18. "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.
  19. Cited for: UBIQUITINATION.
  20. "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.
  21. "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.
  22. "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.
  23. "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.
  24. "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.
  25. "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 nameiH2A1_HUMAN
AccessioniPrimary (citable) accession number: P0C0S8
Secondary accession number(s): P02261, Q2M1R2, Q76PA6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 99 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

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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi