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P22752 (H2A1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone H2A type 1
Gene names
Name:Hist1h2ab
AND
Name:Hist1h2ac
AND
Name:Hist1h2ad
AND
Name:Hist1h2ae
AND
Name:Hist1h2ag
AND
Name:Hist1h2ai
AND
Name:Hist1h2an
AND
Name:Hist1h2ao
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length130 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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.

Subcellular location

Nucleus. Chromosome.

Post-translational modification

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. Ref.10 Ref.11

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. Ref.9

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. Ref.13

Sequence similarities

Belongs to the histone H2A family.

Sequence caution

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

Ontologies

Keywords
   Cellular componentChromosome
Nucleosome core
Nucleus
   LigandDNA-binding
   PTMAcetylation
Citrullination
Isopeptide bond
Methylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processnucleosome assembly

Inferred from electronic annotation. Source: InterPro

   Cellular_componentnucleosome

Inferred from electronic annotation. Source: UniProtKB-KW

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 130129Histone H2A type 1
PRO_0000055231

Amino acid modifications

Modified residue21N-acetylserine Ref.9
Modified residue21Phosphoserine; by RPS6KA5 Ref.9
Modified residue41Citrulline; alternate By similarity
Modified residue41Symmetric dimethylarginine; by PRMT5; alternate Ref.12
Modified residue61N6-acetyllysine Ref.9
Modified residue371N6-crotonyllysine Ref.13
Modified residue1051N5-methylglutamine Ref.14
Modified residue1191N6-crotonyllysine Ref.13
Modified residue1201N6-crotonyllysine; alternate By similarity
Modified residue1211Phosphothreonine; by VPRBP By similarity
Modified residue1261N6-crotonyllysine By similarity
Cross-link14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate Ref.10 Ref.11

Experimental info

Sequence conflict91G → C in AAA37763. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P22752 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 9CFE6184B2CC89F5

FASTA13014,135
        10         20         30         40         50         60 
MSGRGKQGGK ARAKAKTRSS RAGLQFPVGR VHRLLRKGNY SERVGAGAPV YLAAVLEYLT 

        70         80         90        100        110        120 
AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGR VTIAQGGVLP NIQAVLLPKK 

       130 
TESHHKAKGK 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS26288.1.
CCDS26297.1.
CCDS26301.1.
CCDS26307.1.
CCDS26348.1.
CCDS26351.1.
CCDS26356.1.
CCDS26364.1.
CCDS49214.1.
PIRJH0303.
S04152.
RefSeqNP_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.
UniGeneMm.14767.
Mm.250564.
Mm.261665.
Mm.261973.
Mm.263165.
Mm.390553.
Mm.422826.
Mm.423402.

3D structure databases

ProteinModelPortalP22752.
SMRP22752. Positions 12-119.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid235110. 4 interactions.
IntActP22752. 6 interactions.
MINTMINT-1173009.
STRING10090.ENSMUSP00000088285.

PTM databases

PhosphoSiteP22752.

Proteomic databases

PaxDbP22752.
PRIDEP22752.

Protocols and materials databases

DNASU319172.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000070124; 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.
GeneID319164.
319165.
319166.
319167.
319170.
319171.
319172.
319191.
665433.
KEGGmmu:319164.
mmu:319165.
mmu:319166.
mmu:319167.
mmu:319170.
mmu:319171.
mmu:319172.
mmu:319191.
mmu:665433.
UCSCuc007prb.1. mouse.

Organism-specific databases

CTD3012.
3013.
319170.
319171.
665433.
8329.
8334.
8335.
8969.
MGIMGI: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

eggNOGCOG5262.
GeneTreeENSGT00730000110388.
HOGENOMHOG000234652.
HOVERGENHBG009342.
InParanoidP22752.
KOK11251.
OMAFISFAVM.
OrthoDBEOG7M0NTR.
PhylomeDBP22752.
TreeFamTF300137.

Enzyme and pathway databases

ReactomeREACT_188804. Cell Cycle.
REACT_200794. Mus musculus biological processes.

Gene expression databases

ArrayExpressP22752.
BgeeP22752.
CleanExMM_HIST1H2AB.
MM_HIST1H2AC.
MM_HIST1H2AD.
MM_HIST1H2AE.
MM_HIST1H2AG.
MM_HIST1H2AI.
MM_HIST1H2AN.
MM_HIST1H2AO.
GenevestigatorP22752.

Family and domain databases

Gene3D1.10.20.10. 1 hit.
InterProIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR002119. Histone_H2A.
[Graphical view]
PfamPF00125. Histone. 1 hit.
[Graphical view]
PRINTSPR00620. HISTONEH2A.
SMARTSM00414. H2A. 1 hit.
[Graphical view]
SUPFAMSSF47113. SSF47113. 1 hit.
PROSITEPS00046. HISTONE_H2A. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio394244.
SOURCESearch...

Entry information

Entry nameH2A1_MOUSE
AccessionPrimary (citable) accession number: P22752
Secondary accession number(s): P10812, Q149U0, Q5SZZ2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 143 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot