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P20671

- H2A1D_HUMAN

UniProt

P20671 - H2A1D_HUMAN

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Protein

Histone H2A type 1-D

Gene

HIST1H2AD

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
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_228108. RMTs methylate histone arginines.
REACT_228222. HDACs deacetylate histones.
REACT_267652. DNA methylation.
REACT_267668. Transcriptional regulation by small RNAs.
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-D
Alternative name(s):
Histone H2A.3
Histone H2A/g
Gene namesi
Name:HIST1H2AD
Synonyms:H2AFG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:4729. HIST1H2AD.

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

PharmGKBiPA29106.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 130129Histone H2A type 1-DPRO_0000055234Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei2 – 21Phosphoserine; by RPS6KA5By similarity
Modified residuei4 – 41Citrulline1 Publication
Modified residuei4 – 41Symmetric dimethylarginine; by PRMT5; alternateBy 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.5 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

MaxQBiP20671.
PaxDbiP20671.
PRIDEiP20671.

Expressioni

Gene expression databases

CleanExiHS_HIST1H2AD.
GenevestigatoriP20671.

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

BioGridi109267. 24 interactions.
IntActiP20671. 19 interactions.
MINTiMINT-4589032.
STRINGi9606.ENSP00000341094.

Structurei

3D structure databases

ProteinModelPortaliP20671.
SMRiP20671. Positions 12-119.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H2A family.Curated

Phylogenomic databases

eggNOGiCOG5262.
GeneTreeiENSGT00760000118934.
HOGENOMiHOG000234652.
HOVERGENiHBG009342.
InParanoidiP20671.
KOiK11251.
OMAiTESHQKA.
OrthoDBiEOG7M0NTR.
PhylomeDBiP20671.
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.

P20671-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSGRGKQGGK ARAKAKTRSS RAGLQFPVGR VHRLLRKGNY SERVGAGAPV
60 70 80 90 100
YLAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGK
110 120 130
VTIAQGGVLP NIQAVLLPKK TESHHKAKGK
Length:130
Mass (Da):14,107
Last modified:January 23, 2007 - v2
Checksum:i48CE6184B2CC9164
GO

Mass spectrometryi

Molecular mass is 14009.9 Da from positions 2 - 130. Determined by ESI. Monoisotopic with N-acetylserine.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16495 Genomic DNA. Translation: CAA34511.1.
Z80776 Genomic DNA. Translation: CAB02538.1.
AY131985 Genomic DNA. Translation: AAN59966.1.
CR541970 mRNA. Translation: CAG46768.1.
CR541999 mRNA. Translation: CAG46796.1.
AL031777 Genomic DNA. Translation: CAB39197.1.
BC093807 mRNA. Translation: AAH93807.1.
BC093809 mRNA. Translation: AAH93809.1.
BC128035 mRNA. Translation: AAI28036.1.
CCDSiCCDS4591.1.
PIRiS06754.
RefSeqiNP_066409.1. NM_021065.3.
UniGeneiHs.626666.
Hs.679229.

Genome annotation databases

EnsembliENST00000341023; ENSP00000341094; ENSG00000196866.
GeneIDi3013.
KEGGihsa:3013.
UCSCiuc003ngw.4. human.

Polymorphism databases

DMDMi121978.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16495 Genomic DNA. Translation: CAA34511.1 .
Z80776 Genomic DNA. Translation: CAB02538.1 .
AY131985 Genomic DNA. Translation: AAN59966.1 .
CR541970 mRNA. Translation: CAG46768.1 .
CR541999 mRNA. Translation: CAG46796.1 .
AL031777 Genomic DNA. Translation: CAB39197.1 .
BC093807 mRNA. Translation: AAH93807.1 .
BC093809 mRNA. Translation: AAH93809.1 .
BC128035 mRNA. Translation: AAI28036.1 .
CCDSi CCDS4591.1.
PIRi S06754.
RefSeqi NP_066409.1. NM_021065.3.
UniGenei Hs.626666.
Hs.679229.

3D structure databases

ProteinModelPortali P20671.
SMRi P20671. Positions 12-119.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109267. 24 interactions.
IntActi P20671. 19 interactions.
MINTi MINT-4589032.
STRINGi 9606.ENSP00000341094.

Polymorphism databases

DMDMi 121978.

Proteomic databases

MaxQBi P20671.
PaxDbi P20671.
PRIDEi P20671.

Protocols and materials databases

DNASUi 3013.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000341023 ; ENSP00000341094 ; ENSG00000196866 .
GeneIDi 3013.
KEGGi hsa:3013.
UCSCi uc003ngw.4. human.

Organism-specific databases

CTDi 3013.
GeneCardsi GC06M026199.
HGNCi HGNC:4729. HIST1H2AD.
MIMi 602792. gene.
neXtProti NX_P20671.
PharmGKBi PA29106.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5262.
GeneTreei ENSGT00760000118934.
HOGENOMi HOG000234652.
HOVERGENi HBG009342.
InParanoidi P20671.
KOi K11251.
OMAi TESHQKA.
OrthoDBi EOG7M0NTR.
PhylomeDBi P20671.
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_228108. RMTs methylate histone arginines.
REACT_228222. HDACs deacetylate histones.
REACT_267652. DNA methylation.
REACT_267668. Transcriptional regulation by small RNAs.
REACT_27271. Meiotic recombination.
REACT_75792. Meiotic synapsis.
REACT_75925. Amyloids.
REACT_7963. Packaging Of Telomere Ends.

Miscellaneous databases

GeneWikii HIST1H2AD.
GenomeRNAii 3013.
NextBioi 11944.
PROi P20671.
SOURCEi Search...

Gene expression databases

CleanExi HS_HIST1H2AD.
Genevestigatori P20671.

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. "Nucleotide sequences of mouse histone genes H2A and H3.1."
    Kosciessa U., Doenecke D.
    Nucleic Acids Res. 17:8861-8861(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Human histone gene organization: nonregular arrangement within a large cluster."
    Albig W., Kioschis P., Poustka A., Meergans K., Doenecke D.
    Genomics 40:314-322(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "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].
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  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].
    Tissue: Lung.
  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. "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.
  11. "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.
  12. Cited for: UBIQUITINATION AT LYS-120.
  13. "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.
  14. "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.
  15. "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.
  16. Cited for: UBIQUITINATION.
  17. "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.
  18. "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.
  19. "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.
  20. "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.
  21. "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.
  22. "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 nameiH2A1D_HUMAN
AccessioniPrimary (citable) accession number: P20671
Secondary accession number(s): A0PK91, P57754, Q6FGY6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 145 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

Caution

Was originally thought to originate from mouse.1 Publication

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