Q9P0M6 (H2AW_HUMAN) 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:	MACROH2A2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	372 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	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. Ref.6
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.1 Ref.2 Ref.6
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
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW dosage compensation Inferred from direct assay Ref.1. Source: MGI nucleosome assembly Inferred from electronic annotation. Source: InterPro
Cellular component	Barr body Inferred from direct assay 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

Initiator methionine

1

1

Removed By similarity

Chain

2 – 372

371

Core histone macro-H2A.2

PRO_0000055320

Regions

Domain

2 – 117

116

Histone H2A

Domain

184 – 370

187

Macro

Compositional bias

118 – 161

44

Lys-rich

Amino acid modifications

Modified residue

12

1

N6-acetyllysine Ref.8

Modified residue

129

1

Phosphoserine Ref.7

Secondary structure

1

.

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372

Helix Strand Turn

Details...

Beta strand

184 – 190

7

Beta strand

196 – 201

6

Helix

204 – 206

3

Beta strand

216 – 219

4

Helix

232 – 235

4

Helix

240 – 251

12

Beta strand

260 – 264

5

Beta strand

270 – 277

8

Helix

286 – 303

18

Beta strand

307 – 311

5

Helix

323 – 340

18

Beta strand

348 – 353

6

Turn

356 – 358

3

Helix

362 – 367

6

Sequences

	Sequence		Length	Mass (Da)
	Q9P0M6 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: C4B35CD156031AF1	FASTA	372	40,058
	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 PPEKRGRKAT SGKKGGKKSK AAKPRTSKKS KPKDSDKEGT SNSTSEDGPG 190 200 210 220 230 240 DGFTILSSKS LVLGQKLSLT QSDISHIGSM RVEGIVHPTT AEIDLKEDIG KALEKAGGKE 250 260 270 280 290 300 FLETVKELRK SQGPLEVAEA AVSQSSGLAA KFVIHCHIPQ WGSDKCEEQL EETIKNCLSA 310 320 330 340 350 360 AEDKKLKSVA FPPFPSGRNC FPKQTAAQVT LKAISAHFDD SSASSLKNVY FLLFDSESIG 370 IYVQEMAKLD AK

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: 11331621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
[2]	"MACROH2A2, a new member of the MACROH2A core histone family." Costanzi C., Pehrson J.R. J. Biol. Chem. 276:21776-21784(2001) [PubMed: 11262398] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed: 15164054] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Uterus.
[6]	"Formation of MacroH2A-containing senescence-associated heterochromatin foci and senescence driven by ASF1a and HIRA." Zhang R., Poustovoitov M.V., Ye X., Santos H.A., Chen W., Daganzo S.M., Erzberger J.P., Serebriiskii I.G., Canutescu A.A., Dunbrack R.L., Pehrson J.R., Berger J.M., Kaufman P.D., Adams P.D. Dev. Cell 8:19-30(2005) [PubMed: 15621527] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[7]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[8]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-12, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF336304 mRNA. Translation: AAK52471.1.
AF151534 mRNA. Translation: AAF72101.1.
AK022776 mRNA. Translation: BAB14239.1.
AL731540 Genomic DNA. Translation: CAI13683.1.
BC016172 mRNA. Translation: AAH16172.1.

IPI

IPI00220994.

RefSeq

NP_061119.1. NM_018649.2.

UniGene

Hs.499953.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2XD7	X-ray	2.09	A/B/C/D	177-369	[»]

ProteinModelPortal

Q9P0M6.

SMR

Q9P0M6. Positions 12-117, 177-369.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48563N.

IntAct

Q9P0M6. 1 interaction.

STRING

Q9P0M6.

PTM databases

PhosphoSite

Q9P0M6.

Polymorphism databases

DMDM

12585260.

Proteomic databases

PRIDE

Q9P0M6.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000373255; ENSP00000362352; ENSG00000099284.

GeneID

55506.

KEGG

hsa:55506.

UCSC

uc001jqm.1. human.

Organism-specific databases

CTD

55506.

GeneCards

GC10P071812.

H-InvDB

HIX0008890.

HGNC

HGNC:14453. H2AFY2.

HPA

HPA035865.

neXtProt

NX_Q9P0M6.

PharmGKB

PA29118.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG07040.

GeneTree

ENSGT00540000069960.

HOGENOM

HBG715905.

HOVERGEN

HBG009342.

InParanoid

Q9P0M6.

OMA

GAKGKSE.

OrthoDB

EOG4CNQRG.

PhylomeDB

Q9P0M6.

Gene expression databases

ArrayExpress

Q9P0M6.

Bgee

Q9P0M6.

CleanEx

HS_H2AFY2.

Genevestigator

Q9P0M6.

GermOnline

ENSG00000099284. Homo sapiens.

Family and domain databases

InterPro

IPR002589. A1pp.
IPR021171. Core_histone_macro-H2A.
IPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR002119. Histone_H2A.
[Graphical view]

Gene3D

G3DSA:1.10.20.10. Histone-fold. 1 hit.

KO

K11251.

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

59903.

Entry information

Entry name

H2AW_HUMAN

Accession

Primary (citable) accession number: Q9P0M6
Secondary accession number(s): Q5SQT2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 105 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.