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Q9P0M6 (H2AW_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Core histone macro-H2A.2

Short name=Histone macroH2A2
Short name=mH2A2
Gene names
Name:H2AFY2
Synonyms:MACROH2A2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length372 AA.
Sequence statusComplete.
Protein existenceEvidence 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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 372372Core histone macro-H2A.2
PRO_0000055320

Regions

Domain2 – 117116Histone H2A
Domain184 – 370187Macro
Compositional bias118 – 16144Lys-rich

Secondary structure

......................... 372
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9P0M6 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: C4B35CD156031AF1

FASTA37240,058
        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 

« Hide

References

« Hide '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], 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
RefSeqNP_061119.1. NM_018649.2.
UniGeneHs.499953.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2XD7X-ray2.09A/B/C/D177-369[»]
ProteinModelPortalQ9P0M6.
SMRQ9P0M6. Positions 12-117, 177-369.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120686. 7 interactions.
DIPDIP-48563N.
IntActQ9P0M6. 1 interaction.
MINTMINT-6609507.
STRING9606.ENSP00000362352.

PTM databases

PhosphoSiteQ9P0M6.

Polymorphism databases

DMDM12585260.

Proteomic databases

PaxDbQ9P0M6.
PRIDEQ9P0M6.

Protocols and materials databases

DNASU55506.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000373255; ENSP00000362352; ENSG00000099284.
GeneID55506.
KEGGhsa:55506.
UCSCuc001jqm.3. human.

Organism-specific databases

CTD55506.
GeneCardsGC10P071812.
H-InvDBHIX0008890.
HGNCHGNC:14453. H2AFY2.
HPAHPA035865.
neXtProtNX_Q9P0M6.
PharmGKBPA29118.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2110.
HOGENOMHOG000234653.
HOVERGENHBG009342.
InParanoidQ9P0M6.
KOK11251.
OMAVEGIINP.
OrthoDBEOG71G9VP.
PhylomeDBQ9P0M6.
TreeFamTF332276.

Gene expression databases

ArrayExpressQ9P0M6.
BgeeQ9P0M6.
CleanExHS_H2AFY2.
GenevestigatorQ9P0M6.

Family and domain databases

Gene3D1.10.20.10. 1 hit.
InterProIPR021171. Core_histone_macro-H2A.
IPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR002119. Histone_H2A.
IPR002589. Macro_dom.
[Graphical view]
PfamPF00125. Histone. 1 hit.
PF01661. Macro. 1 hit.
[Graphical view]
PIRSFPIRSF037942. Core_histone_macro-H2A. 1 hit.
PRINTSPR00620. HISTONEH2A.
SMARTSM00414. H2A. 1 hit.
[Graphical view]
SUPFAMSSF47113. SSF47113. 1 hit.
PROSITEPS51154. MACRO. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSH2AFY2. human.
EvolutionaryTraceQ9P0M6.
GeneWikiH2AFY2.
GenomeRNAi55506.
NextBio59903.
PROQ9P0M6.

Entry information

Entry nameH2AW_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 124 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM