Q8CCK0 (H2AW_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Core histone macro-H2A.2
Short name=Histone macroH2A2
Short name=mH2A2

Gene names

Name:	H2afy2
Synonyms:	H2afy3

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	372 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Variant histone H2A which replaces conventional H2A in a subset of nucleosomes where it represses transcription. 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. May be involved in stable X chromosome inactivation.
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.
Subcellular location	Nucleus. Chromosome. Note: Enriched in inactive X chromosome chromatin and in senescence-associated heterochromatin. Ref.4
Tissue specificity	Present in liver, kidney and adrenal gland (at protein level). In the liver, present in cells of the bile ducts and parenchymal cells, but not in hepatocytes. In the kidney, present in proximal and distal convoluted tubules and in glomeruli. Present at highest levels in the parietal layer of Bowman capsule. In the adrenal gland, present in the outer cells of the capsule. Ref.4
Sequence similarities	Contains 1 histone H2A domain. Contains 1 Macro domain.

Ontologies

Keywords
Cellular component	Chromosome Nucleosome core Nucleus
Ligand	DNA-binding
Molecular function	Chromatin regulator
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW dosage compensation Inferred from sequence alignment Ref.1. Source: MGI nucleosome assembly Inferred from electronic annotation. Source: InterPro
Cellular_component	Barr body Inferred from sequence alignment Ref.1. Source: MGI nucleosome Inferred from electronic annotation. Source: UniProtKB-KW
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
	Chain	1 – 372	372	Core histone macro-H2A.2		PRO_0000227906
Regions
	Domain	2 – 117	116	Histone H2A
	Domain	184 – 370	187	Macro
Experimental info
	Sequence conflict	90	1	E → D in BAC27963. Ref.2
	Sequence conflict	239	1	K → E in BAE38003. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q8CCK0 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 471E3CDCE28F4A1D	FASTA	372	40,092
	10 20 30 40 50 60 MSGRSGKKKM SKLSRSARAG VIFPVGRLMR YLKKGTFKYR ISVGAPVYMA AVIEYLAAEI 70 80 90 100 110 120 LELAGNAARD NKKARIAPRH ILLAVANDEE LNQLLKGVTI ASGGVLPRIH PELLAKKRGT 130 140 150 160 170 180 KGKSETILSP PPEKRGRKAA SGKKGGKKSK ATKPRTSKKS KAKDSDKEGT SNSTSEDGPG 190 200 210 220 230 240 DGFTILSSKS LVLGQKLSLT QSDISHIGSM RVEGIVHPTT AEIDLKEEIG KALEKAGGKE 250 260 270 280 290 300 FLETVKELRK SQGPLEVAEA AVSQSSGLAA KFVIHCHIPQ WGSDKCEEQL EETIKNCLSA 310 320 330 340 350 360 AEDKKLKSVA FPPFPSGRNC FPKQTAAQVT LKAISAHFDD SSSSSLKNVY FLLFDSESIG 370 IYVQEMAKLD TK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Histone H2A variants and the inactive X chromosome: identification of a second macroH2A variant." Chadwick B.P., Willard H.F. Hum. Mol. Genet. 10:1101-1113(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6J.
[2]	"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: Cerebellum.
[3]	"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. Tissue: Brain and Olfactory epithelium.
[4]	"MACROH2A2, a new member of the MACROH2A core histone family." Costanzi C., Pehrson J.R. J. Biol. Chem. 276:21776-21784(2001) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF336305 mRNA. Translation: AAK52472.1. AK032636 mRNA. Translation: BAC27963.1. AK165020 mRNA. Translation: BAE38003.1. BC045140 mRNA. Translation: AAH45140.1. BC046794 mRNA. Translation: AAH46794.1. BC107279 mRNA. Translation: AAI07280.1. BC107280 mRNA. Translation: AAI07281.1. BC127144 mRNA. Translation: AAI27145.1.
IPI	IPI00652934.
RefSeq	NP_996883.1. NM_207000.2.
UniGene	Mm.272870.
3D structure databases
ProteinModelPortal	Q8CCK0.
SMR	Q8CCK0. Positions 12-117, 177-369.
ModBase	Search...
PTM databases
PhosphoSite	Q8CCK0.
Proteomic databases
PaxDb	Q8CCK0.
PRIDE	Q8CCK0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000020283; ENSMUSP00000020283; ENSMUSG00000020086.
GeneID	404634.
KEGG	mmu:404634.
UCSC	uc007fgm.1. mouse.
Organism-specific databases
CTD	55506.
MGI	MGI:3037658. H2afy2.
Phylogenomic databases
eggNOG	COG2110.
GeneTree	ENSGT00690000101745.
HOGENOM	HOG000234653.
HOVERGEN	HBG009342.
InParanoid	A0JP36.
KO	K11251.
OMA	GAKGKSE.
OrthoDB	EOG4CNQRG.
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	Q8CCK0.
Bgee	Q8CCK0.
CleanEx	MM_H2AFY2.
Genevestigator	Q8CCK0.
GermOnline	ENSMUSG00000020086. Mus musculus.
Family and domain databases
Gene3D	1.10.20.10. 1 hit.
InterPro	IPR002589. A1pp. IPR021171. Core_histone_macro-H2A. IPR009072. Histone-fold. IPR007125. Histone_core_D. IPR002119. Histone_H2A. [Graphical view]
Pfam	PF00125. Histone. 1 hit. PF01661. Macro. 1 hit. [Graphical view]
PIRSF	PIRSF037942. Core_histone_macro-H2A. 1 hit.
PRINTS	PR00620. HISTONEH2A.
SMART	SM00414. H2A. 1 hit. [Graphical view]
SUPFAM	SSF47113. Histone-fold. 1 hit.
PROSITE	PS51154. MACRO. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	407104.
SOURCE	Search...

Entry information

Entry name

H2AW_MOUSE

Accession

Primary (citable) accession number: Q8CCK0
Secondary accession number(s): A0JP36, Q3TNT4, Q925I6

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 21, 2006
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 81 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program