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P22752

- H2A1_MOUSE

UniProt

P22752 - H2A1_MOUSE

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Protein
Histone H2A type 1
Gene
Hist1h2ab
Hist1h2ac
Hist1h2ad
Hist1h2ae
Hist1h2ag
Hist1h2ai
more..
Hist1h2an
Hist1h2ao less..
Organism
Mus musculus (Mouse)
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_198626. Meiotic synapsis.
REACT_200667. NoRC negatively regulates rRNA expression.
REACT_214440. NoRC negatively regulates rRNA expression.
REACT_226917. HATs acetylate histones.
REACT_27235. Meiotic Recombination.
REACT_75800. Meiotic Synapsis.

Names & Taxonomyi

Organism-specific databases

Protein namesi
Recommended name:
Histone H2A type 1
Gene namesi
Name:Hist1h2ab
AND
Name:Hist1h2ac
AND
Name:Hist1h2ad
AND
Name:Hist1h2ae
AND
Name:Hist1h2ag
AND
Name:Hist1h2ai
AND
Name:Hist1h2an
AND
Name:Hist1h2ao
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 13
MGIiMGI:2448306. Hist1h2ab.
MGI:2448287. Hist1h2ac.
MGI:2448289. Hist1h2ad.
MGI:2448290. Hist1h2ae.
MGI:2448293. Hist1h2ag.
MGI:2448457. Hist1h2ai.
MGI:2448300. Hist1h2an.
MGI:2448302. Hist1h2ao.

Subcellular locationi

GO - Cellular componenti

  1. nucleosome Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 130129Histone H2A type 1
PRO_0000055231Add
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 By similarity
Modified residuei4 – 41Symmetric dimethylarginine; by PRMT5; alternate1 Publication
Modified residuei6 – 61N6-acetyllysine1 Publication
Cross-linki14 – 14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-linki16 – 16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Modified residuei37 – 371N6-crotonyllysine1 Publication
Modified residuei105 – 1051N5-methylglutamine1 Publication
Modified residuei119 – 1191N6-crotonyllysine1 Publication
Modified residuei120 – 1201N6-crotonyllysine; alternate By similarity
Cross-linki120 – 120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate2 Publications
Modified residuei121 – 1211Phosphothreonine; by VPRBP By similarity
Modified residuei126 – 1261N6-crotonyllysine By similarity

Post-translational modificationi

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 By similarity. 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. H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events.2 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 By similarity.1 Publication
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 By similarity.
Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage.
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

PaxDbiP22752.
PRIDEiP22752.

PTM databases

PhosphoSiteiP22752.

Expressioni

Gene expression databases

ArrayExpressiP22752.
BgeeiP22752.
CleanExiMM_HIST1H2AB.
MM_HIST1H2AC.
MM_HIST1H2AD.
MM_HIST1H2AE.
MM_HIST1H2AG.
MM_HIST1H2AI.
MM_HIST1H2AN.
MM_HIST1H2AO.
GenevestigatoriP22752.

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

BioGridi235110. 4 interactions.
IntActiP22752. 6 interactions.
MINTiMINT-1173009.
STRINGi10090.ENSMUSP00000088285.

Structurei

3D structure databases

ProteinModelPortaliP22752.
SMRiP22752. Positions 12-119.

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H2A family.

Phylogenomic databases

eggNOGiCOG5262.
GeneTreeiENSGT00730000110388.
HOGENOMiHOG000234652.
HOVERGENiHBG009342.
InParanoidiP22752.
KOiK11251.
OMAiFISFAVM.
OrthoDBiEOG7M0NTR.
PhylomeDBiP22752.
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.

P22752-1 [UniParc]FASTAAdd to Basket

« Hide

MSGRGKQGGK ARAKAKTRSS RAGLQFPVGR VHRLLRKGNY SERVGAGAPV    50
YLAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGR 100
VTIAQGGVLP NIQAVLLPKK TESHHKAKGK 130
Length:130
Mass (Da):14,135
Last modified:January 23, 2007 - v3
Checksum:i9CFE6184B2CC89F5
GO

Sequence cautioni

The sequence CAA29291.1 differs from that shown. Reason: Several sequencing errors.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91G → C in AAA37763. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X05862 Genomic DNA. Translation: CAA29291.1. Sequence problems.
M33988 Genomic DNA. Translation: AAA37763.1.
M37736 Genomic DNA. Translation: AAA37809.1.
U62669 Genomic DNA. Translation: AAB04761.1.
AY158909 Genomic DNA. Translation: AAO06220.1.
AY158912 Genomic DNA. Translation: AAO06222.1.
AY158913 Genomic DNA. Translation: AAO06223.1.
AY158915 Genomic DNA. Translation: AAO06225.1.
AY158917 Genomic DNA. Translation: AAO06227.1.
AY158918 Genomic DNA. Translation: AAO06228.1.
AY158919 Genomic DNA. Translation: AAO06229.1.
AY158920 Genomic DNA. Translation: AAO06230.1.
AK028026 mRNA. Translation: BAC25706.1.
AK033518 mRNA. Translation: BAC28337.1.
AK145443 mRNA. Translation: BAE26439.1.
AK146846 mRNA. Translation: BAE27477.1.
AL589651 Genomic DNA. Translation: CAI24114.1.
AL589879 Genomic DNA. Translation: CAI25463.1.
AL589879 Genomic DNA. Translation: CAI25466.1.
AL590388 Genomic DNA. Translation: CAI25841.1.
AL590614 Genomic DNA. Translation: CAI26129.1.
AL592149 Genomic DNA. Translation: CAI24893.1.
BC058544 mRNA. Translation: AAH58544.1.
BC062251 mRNA. Translation: AAH62251.1.
BC065803 mRNA. Translation: AAH65803.1.
BC076498 mRNA. Translation: AAH76498.1.
BC090402 mRNA. Translation: AAH90402.1.
BC099406 mRNA. Translation: AAH99406.1.
BC110626 mRNA. Translation: AAI10627.1.
BC116373 mRNA. Translation: AAI16374.1.
BC117110 mRNA. Translation: AAI17111.1.
BC119295 mRNA. Translation: AAI19296.1.
BC119297 mRNA. Translation: AAI19298.1.
BC127164 mRNA. Translation: AAI27165.1.
BC133661 mRNA. Translation: AAI33662.1.
CCDSiCCDS26288.1.
CCDS26297.1.
CCDS26301.1.
CCDS26307.1.
CCDS26348.1.
CCDS26351.1.
CCDS26356.1.
CCDS26364.1.
CCDS49214.1.
PIRiJH0303.
S04152.
RefSeqiNP_001171015.1. NM_001177544.2.
NP_783591.2. NM_175660.3.
NP_835489.1. NM_178182.2.
NP_835491.1. NM_178184.2.
NP_835492.1. NM_178185.2.
NP_835493.1. NM_178186.3.
NP_835494.1. NM_178187.4.
NP_835495.1. NM_178188.4.
NP_835496.1. NM_178189.5.
UniGeneiMm.14767.
Mm.250564.
Mm.261665.
Mm.261973.
Mm.263165.
Mm.390553.
Mm.422826.
Mm.423402.

Genome annotation databases

EnsembliENSMUST00000070124; ENSMUSP00000088285; ENSMUSG00000071516.
ENSMUST00000078369; ENSMUSP00000077477; ENSMUSG00000061615.
ENSMUST00000081342; ENSMUSP00000080088; ENSMUSG00000094777.
ENSMUST00000090776; ENSMUSP00000088281; ENSMUSG00000071478.
ENSMUST00000091741; ENSMUSP00000089335; ENSMUSG00000069301.
ENSMUST00000091745; ENSMUSP00000089339; ENSMUSG00000094248.
ENSMUST00000091751; ENSMUSP00000089345; ENSMUSG00000069309.
ENSMUST00000102969; ENSMUSP00000100034; ENSMUSG00000069272.
ENSMUST00000171127; ENSMUSP00000127684; ENSMUSG00000069270.
GeneIDi319164.
319165.
319166.
319167.
319170.
319171.
319172.
319191.
665433.
KEGGimmu:319164.
mmu:319165.
mmu:319166.
mmu:319167.
mmu:319170.
mmu:319171.
mmu:319172.
mmu:319191.
mmu:665433.
UCSCiuc007prb.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X05862 Genomic DNA. Translation: CAA29291.1 . Sequence problems.
M33988 Genomic DNA. Translation: AAA37763.1 .
M37736 Genomic DNA. Translation: AAA37809.1 .
U62669 Genomic DNA. Translation: AAB04761.1 .
AY158909 Genomic DNA. Translation: AAO06220.1 .
AY158912 Genomic DNA. Translation: AAO06222.1 .
AY158913 Genomic DNA. Translation: AAO06223.1 .
AY158915 Genomic DNA. Translation: AAO06225.1 .
AY158917 Genomic DNA. Translation: AAO06227.1 .
AY158918 Genomic DNA. Translation: AAO06228.1 .
AY158919 Genomic DNA. Translation: AAO06229.1 .
AY158920 Genomic DNA. Translation: AAO06230.1 .
AK028026 mRNA. Translation: BAC25706.1 .
AK033518 mRNA. Translation: BAC28337.1 .
AK145443 mRNA. Translation: BAE26439.1 .
AK146846 mRNA. Translation: BAE27477.1 .
AL589651 Genomic DNA. Translation: CAI24114.1 .
AL589879 Genomic DNA. Translation: CAI25463.1 .
AL589879 Genomic DNA. Translation: CAI25466.1 .
AL590388 Genomic DNA. Translation: CAI25841.1 .
AL590614 Genomic DNA. Translation: CAI26129.1 .
AL592149 Genomic DNA. Translation: CAI24893.1 .
BC058544 mRNA. Translation: AAH58544.1 .
BC062251 mRNA. Translation: AAH62251.1 .
BC065803 mRNA. Translation: AAH65803.1 .
BC076498 mRNA. Translation: AAH76498.1 .
BC090402 mRNA. Translation: AAH90402.1 .
BC099406 mRNA. Translation: AAH99406.1 .
BC110626 mRNA. Translation: AAI10627.1 .
BC116373 mRNA. Translation: AAI16374.1 .
BC117110 mRNA. Translation: AAI17111.1 .
BC119295 mRNA. Translation: AAI19296.1 .
BC119297 mRNA. Translation: AAI19298.1 .
BC127164 mRNA. Translation: AAI27165.1 .
BC133661 mRNA. Translation: AAI33662.1 .
CCDSi CCDS26288.1.
CCDS26297.1.
CCDS26301.1.
CCDS26307.1.
CCDS26348.1.
CCDS26351.1.
CCDS26356.1.
CCDS26364.1.
CCDS49214.1.
PIRi JH0303.
S04152.
RefSeqi NP_001171015.1. NM_001177544.2.
NP_783591.2. NM_175660.3.
NP_835489.1. NM_178182.2.
NP_835491.1. NM_178184.2.
NP_835492.1. NM_178185.2.
NP_835493.1. NM_178186.3.
NP_835494.1. NM_178187.4.
NP_835495.1. NM_178188.4.
NP_835496.1. NM_178189.5.
UniGenei Mm.14767.
Mm.250564.
Mm.261665.
Mm.261973.
Mm.263165.
Mm.390553.
Mm.422826.
Mm.423402.

3D structure databases

ProteinModelPortali P22752.
SMRi P22752. Positions 12-119.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 235110. 4 interactions.
IntActi P22752. 6 interactions.
MINTi MINT-1173009.
STRINGi 10090.ENSMUSP00000088285.

PTM databases

PhosphoSitei P22752.

Proteomic databases

PaxDbi P22752.
PRIDEi P22752.

Protocols and materials databases

DNASUi 319172.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000070124 ; ENSMUSP00000088285 ; ENSMUSG00000071516 .
ENSMUST00000078369 ; ENSMUSP00000077477 ; ENSMUSG00000061615 .
ENSMUST00000081342 ; ENSMUSP00000080088 ; ENSMUSG00000094777 .
ENSMUST00000090776 ; ENSMUSP00000088281 ; ENSMUSG00000071478 .
ENSMUST00000091741 ; ENSMUSP00000089335 ; ENSMUSG00000069301 .
ENSMUST00000091745 ; ENSMUSP00000089339 ; ENSMUSG00000094248 .
ENSMUST00000091751 ; ENSMUSP00000089345 ; ENSMUSG00000069309 .
ENSMUST00000102969 ; ENSMUSP00000100034 ; ENSMUSG00000069272 .
ENSMUST00000171127 ; ENSMUSP00000127684 ; ENSMUSG00000069270 .
GeneIDi 319164.
319165.
319166.
319167.
319170.
319171.
319172.
319191.
665433.
KEGGi mmu:319164.
mmu:319165.
mmu:319166.
mmu:319167.
mmu:319170.
mmu:319171.
mmu:319172.
mmu:319191.
mmu:665433.
UCSCi uc007prb.1. mouse.

Organism-specific databases

CTDi 3012.
3013.
319170.
319171.
665433.
8329.
8334.
8335.
8969.
MGIi MGI:2448306. Hist1h2ab.
MGI:2448287. Hist1h2ac.
MGI:2448289. Hist1h2ad.
MGI:2448290. Hist1h2ae.
MGI:2448293. Hist1h2ag.
MGI:2448457. Hist1h2ai.
MGI:2448300. Hist1h2an.
MGI:2448302. Hist1h2ao.

Phylogenomic databases

eggNOGi COG5262.
GeneTreei ENSGT00730000110388.
HOGENOMi HOG000234652.
HOVERGENi HBG009342.
InParanoidi P22752.
KOi K11251.
OMAi FISFAVM.
OrthoDBi EOG7M0NTR.
PhylomeDBi P22752.
TreeFami TF300137.

Enzyme and pathway databases

Reactomei REACT_198626. Meiotic synapsis.
REACT_200667. NoRC negatively regulates rRNA expression.
REACT_214440. NoRC negatively regulates rRNA expression.
REACT_226917. HATs acetylate histones.
REACT_27235. Meiotic Recombination.
REACT_75800. Meiotic Synapsis.

Miscellaneous databases

NextBioi 394244.
SOURCEi Search...

Gene expression databases

ArrayExpressi P22752.
Bgeei P22752.
CleanExi MM_HIST1H2AB.
MM_HIST1H2AC.
MM_HIST1H2AD.
MM_HIST1H2AE.
MM_HIST1H2AG.
MM_HIST1H2AI.
MM_HIST1H2AN.
MM_HIST1H2AO.
Genevestigatori P22752.

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. "Mouse histone H2A and H2B genes: four functional genes and a pseudogene undergoing gene conversion with a closely linked functional gene."
    Liu T.-J., Liu L., Marzluff W.F.
    Nucleic Acids Res. 15:3023-3039(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Structure of a mouse histone-encoding gene cluster."
    Gruber A., Streit A., Reist M., Benninger P., Boehni R., Schuemperli D.
    Gene 95:303-304(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "A genomic clone encoding a novel proliferation-dependent histone H2A.1 mRNA enriched in the poly(A)+ fraction."
    Fecker L., Ekblom P., Kurkinen M., Ekblom M.
    Mol. Cell. Biol. 10:2848-2854(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Characterization of the mouse histone gene cluster on chromosome 13: 45 histone genes in three patches spread over 1Mb."
    Wang Z.-F., Krasikov T., Frey M.R., Wang J., Matera A.G., Marzluff W.F.
    Genome Res. 6:688-701(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: C57BL/6J.
  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].
  6. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Colon and Heart.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  8. "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].
    Strain: C57BL/6, C57BL/6J and FVB/N.
    Tissue: Brain, Mammary tumor, Placenta and Thymus.
  9. "Quantitative determination of histone modification. H2A acetylation and phosphorylation."
    Pantazis P., Bonner W.M.
    J. Biol. Chem. 256:4669-4675(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-2, ACETYLATION AT SER-2 AND LYS-6.
  10. "Polycomb group proteins Ring1A/B link ubiquitylation of histone H2A to heritable gene silencing and X inactivation."
    de Napoles M., Mermoud J.E., Wakao R., Tang Y.A., Endoh M., Appanah R., Nesterova T.B., Silva J., Otte A.P., Vidal M., Koseki H., Brockdorff N.
    Dev. Cell 7:663-676(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION AT LYS-120.
  11. "Ring1b-mediated H2A ubiquitination associates with inactive X chromosomes and is involved in initiation of X inactivation."
    Fang J., Chen T., Chadwick B., Li E., Zhang Y.
    J. Biol. Chem. 279:52812-52815(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION AT LYS-120.
  12. "Blimp1 associates with Prmt5 and directs histone arginine methylation in mouse germ cells."
    Ancelin K., Lange U.C., Hajkova P., Schneider R., Bannister A.J., Kouzarides T., Surani M.A.
    Nat. Cell Biol. 8:623-630(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT ARG-4.
  13. "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 AND LYS-119.
  14. "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_MOUSE
AccessioniPrimary (citable) accession number: P22752
Secondary accession number(s): P10812, Q149U0, Q5SZZ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 144 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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