P22752 (H2A1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	130 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	The chromatin-associated form is phosphorylated on Thr-121 during mitosis By similarity. Ref.9 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 is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1 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 component	Chromosome Nucleosome core Nucleus
Ligand	DNA-binding
PTM	Acetylation Citrullination Isopeptide bond Methylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	nucleosome assembly Inferred from electronic annotation. Source: InterPro
Cellular_component	nucleosome Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 130	129	Histone H2A type 1		PRO_0000055231
Amino acid modifications
	Modified residue	2	1	N-acetylserine Ref.9
	Modified residue	2	1	Phosphoserine; by RPS6KA5 Ref.9
	Modified residue	4	1	Citrulline; alternate By similarity
	Modified residue	4	1	Symmetric dimethylarginine; by PRMT5; alternate Probable
	Modified residue	6	1	N6-acetyllysine Ref.9
	Modified residue	37	1	N6-crotonyl-L-lysine Ref.13
	Modified residue	119	1	N6-crotonyl-L-lysine Ref.13
	Modified residue	120	1	N6-crotonyl-L-lysine; alternate By similarity
	Modified residue	126	1	N6-crotonyl-L-lysine By similarity
	Cross-link	14		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
	Cross-link	16		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
	Cross-link	120		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate Ref.10 Ref.11
Experimental info
	Sequence conflict	9	1	G → C in AAA37763. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P22752 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 9CFE6184B2CC89F5	FASTA	130	14,135
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
+	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.
IPI	IPI00265761.
PIR	JH0303. S04152.
RefSeq	NP_001171015.1. NM_001177544.1. NP_783591.2. NM_175660.2. NP_835489.1. NM_178182.1. NP_835491.1. NM_178184.1. NP_835492.1. NM_178185.1. NP_835493.1. NM_178186.2. NP_835494.1. NM_178187.3. NP_835495.1. NM_178188.3. NP_835496.1. NM_178189.4.
UniGene	Mm.14767. Mm.250564. Mm.261665. Mm.261973. Mm.263165. Mm.377877. Mm.390553. Mm.422826. Mm.423402.
3D structure databases
ProteinModelPortal	P22752.
ModBase	Search...
Protein-protein interaction databases
IntAct	P22752. 2 interactions.
MINT	MINT-1173009.
STRING	10090.ENSMUSP00000088285.
PTM databases
PhosphoSite	P22752.
Proteomic databases
PaxDb	P22752.
PRIDE	P22752.
Protocols and materials databases
DNASU	319172.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	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.
GeneID	319164. 319165. 319166. 319167. 319170. 319171. 319172. 319191. 665433.
KEGG	mmu:319164. mmu:319165. mmu:319166. mmu:319167. mmu:319170. mmu:319171. mmu:319172. mmu:319191. mmu:665433.
Organism-specific databases
CTD	3012. 3013. 319170. 319171. 665433. 8329. 8334. 8335. 8969.
MGI	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
eggNOG	COG5262.
GeneTree	ENSGT00690000101712.
HOGENOM	HOG000234652.
HOVERGEN	HBG009342.
InParanoid	P22752.
KO	K11251.
OMA	QEESEAH.
Enzyme and pathway databases
Reactome	REACT_118161. Cell Cycle. REACT_120463. Meiosis. REACT_27235. Meiotic Recombination (mouse). REACT_75800. Meiotic Synapsis (mouse).
Gene expression databases
ArrayExpress	P22752.
Bgee	P22752.
CleanEx	MM_HIST1H2AB. MM_HIST1H2AC. MM_HIST1H2AD. MM_HIST1H2AE. MM_HIST1H2AG. MM_HIST1H2AI. MM_HIST1H2AN. MM_HIST1H2AO.
Genevestigator	P22752.
GermOnline	ENSMUSG00000060262. Mus musculus. ENSMUSG00000061615. Mus musculus. ENSMUSG00000069270. Mus musculus. ENSMUSG00000069272. Mus musculus. ENSMUSG00000069301. Mus musculus. ENSMUSG00000069304. Mus musculus. ENSMUSG00000069309. Mus musculus. ENSMUSG00000071516. Mus musculus.
Family and domain databases
Gene3D	1.10.20.10. 1 hit.
InterPro	IPR009072. Histone-fold. IPR007125. Histone_core_D. IPR002119. Histone_H2A. [Graphical view]
Pfam	PF00125. Histone. 1 hit. [Graphical view]
PRINTS	PR00620. HISTONEH2A.
SMART	SM00414. H2A. 1 hit. [Graphical view]
SUPFAM	SSF47113. Histone-fold. 1 hit.
PROSITE	PS00046. HISTONE_H2A. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	394244.
SOURCE	Search...

Entry information

Entry name

H2A1_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 131 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program