Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Core histone macro-H2A.2

Gene

H2AFY2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  1. chromatin DNA binding Source: UniProtKB
  2. transcription regulatory region DNA binding Source: UniProtKB

GO - Biological processi

  1. brain development Source: UniProtKB
  2. chromatin modification Source: UniProtKB-KW
  3. dosage compensation Source: MGI
  4. establishment of protein localization to chromatin Source: UniProtKB
  5. negative regulation of gene expression, epigenetic Source: UniProtKB
  6. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  7. negative regulation of transcription of nuclear large rRNA transcript from RNA polymerase I promoter Source: UniProtKB
  8. nucleosome assembly Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Core histone macro-H2A.2
Short name:
Histone macroH2A2
Short name:
mH2A2
Gene namesi
Name:H2AFY2
Synonyms:MACROH2A2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:14453. H2AFY2.

Subcellular locationi

Nucleus. Chromosome
Note: Enriched in inactive X chromosome chromatin and in senescence-associated heterochromatin.

GO - Cellular componenti

  1. Barr body Source: MGI
  2. extracellular vesicular exosome Source: UniProtKB
  3. nuclear chromatin Source: UniProtKB
  4. nucleoplasm Source: HPA
  5. nucleosome Source: UniProtKB-KW
  6. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29118.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 372372Core histone macro-H2A.2PRO_0000055320Add
BLAST

Proteomic databases

MaxQBiQ9P0M6.
PaxDbiQ9P0M6.
PRIDEiQ9P0M6.

PTM databases

PhosphoSiteiQ9P0M6.

Expressioni

Gene expression databases

BgeeiQ9P0M6.
CleanExiHS_H2AFY2.
ExpressionAtlasiQ9P0M6. baseline and differential.
GenevestigatoriQ9P0M6.

Organism-specific databases

HPAiHPA035865.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

BioGridi120686. 13 interactions.
DIPiDIP-48563N.
IntActiQ9P0M6. 2 interactions.
MINTiMINT-6609507.
STRINGi9606.ENSP00000362352.

Structurei

Secondary structure

1
372
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi184 – 1907Combined sources
Beta strandi196 – 2016Combined sources
Helixi204 – 2096Combined sources
Beta strandi213 – 2197Combined sources
Helixi228 – 25124Combined sources
Beta strandi260 – 2645Combined sources
Beta strandi268 – 27710Combined sources
Helixi286 – 30318Combined sources
Beta strandi307 – 3115Combined sources
Helixi323 – 34018Combined sources
Beta strandi348 – 3536Combined sources
Helixi356 – 36712Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XD7X-ray2.09A/B/C/D177-369[»]
ProteinModelPortaliQ9P0M6.
SMRiQ9P0M6. Positions 12-117, 177-369.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9P0M6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 117116Histone H2AAdd
BLAST
Domaini184 – 370187MacroPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi118 – 16144Lys-richAdd
BLAST

Sequence similaritiesi

Contains 1 histone H2A domain.Curated
Contains 1 Macro domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG2110.
GeneTreeiENSGT00760000119217.
HOGENOMiHOG000234653.
HOVERGENiHBG009342.
InParanoidiQ9P0M6.
KOiK11251.
OMAiKVEGIVH.
OrthoDBiEOG71G9VP.
PhylomeDBiQ9P0M6.
TreeFamiTF332276.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR021171. Core_histone_macro-H2A.
IPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR002119. Histone_H2A.
IPR002589. Macro_dom.
[Graphical view]
PfamiPF00125. Histone. 1 hit.
PF01661. Macro. 1 hit.
[Graphical view]
PIRSFiPIRSF037942. Core_histone_macro-H2A. 1 hit.
PRINTSiPR00620. HISTONEH2A.
SMARTiSM00414. H2A. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS51154. MACRO. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9P0M6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSGRSGKKKM SKLSRSARAG VIFPVGRLMR YLKKGTFKYR ISVGAPVYMA
60 70 80 90 100
AVIEYLAAEI LELAGNAARD NKKARIAPRH ILLAVANDEE LNQLLKGVTI
110 120 130 140 150
ASGGVLPRIH PELLAKKRGT KGKSETILSP PPEKRGRKAT SGKKGGKKSK
160 170 180 190 200
AAKPRTSKKS KPKDSDKEGT SNSTSEDGPG DGFTILSSKS LVLGQKLSLT
210 220 230 240 250
QSDISHIGSM RVEGIVHPTT AEIDLKEDIG KALEKAGGKE FLETVKELRK
260 270 280 290 300
SQGPLEVAEA AVSQSSGLAA KFVIHCHIPQ WGSDKCEEQL EETIKNCLSA
310 320 330 340 350
AEDKKLKSVA FPPFPSGRNC FPKQTAAQVT LKAISAHFDD SSASSLKNVY
360 370
FLLFDSESIG IYVQEMAKLD AK
Length:372
Mass (Da):40,058
Last modified:January 23, 2007 - v3
Checksum:iC4B35CD156031AF1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS7296.1.
RefSeqiNP_061119.1. NM_018649.2.
UniGeneiHs.499953.

Genome annotation databases

EnsembliENST00000373255; ENSP00000362352; ENSG00000099284.
GeneIDi55506.
KEGGihsa:55506.
UCSCiuc001jqm.3. human.

Polymorphism databases

DMDMi12585260.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS7296.1.
RefSeqiNP_061119.1. NM_018649.2.
UniGeneiHs.499953.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XD7X-ray2.09A/B/C/D177-369[»]
ProteinModelPortaliQ9P0M6.
SMRiQ9P0M6. Positions 12-117, 177-369.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120686. 13 interactions.
DIPiDIP-48563N.
IntActiQ9P0M6. 2 interactions.
MINTiMINT-6609507.
STRINGi9606.ENSP00000362352.

PTM databases

PhosphoSiteiQ9P0M6.

Polymorphism databases

DMDMi12585260.

Proteomic databases

MaxQBiQ9P0M6.
PaxDbiQ9P0M6.
PRIDEiQ9P0M6.

Protocols and materials databases

DNASUi55506.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000373255; ENSP00000362352; ENSG00000099284.
GeneIDi55506.
KEGGihsa:55506.
UCSCiuc001jqm.3. human.

Organism-specific databases

CTDi55506.
GeneCardsiGC10P071812.
H-InvDBHIX0008890.
HGNCiHGNC:14453. H2AFY2.
HPAiHPA035865.
neXtProtiNX_Q9P0M6.
PharmGKBiPA29118.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2110.
GeneTreeiENSGT00760000119217.
HOGENOMiHOG000234653.
HOVERGENiHBG009342.
InParanoidiQ9P0M6.
KOiK11251.
OMAiKVEGIVH.
OrthoDBiEOG71G9VP.
PhylomeDBiQ9P0M6.
TreeFamiTF332276.

Miscellaneous databases

ChiTaRSiH2AFY2. human.
EvolutionaryTraceiQ9P0M6.
GeneWikiiH2AFY2.
GenomeRNAii55506.
NextBioi59903.
PROiQ9P0M6.

Gene expression databases

BgeeiQ9P0M6.
CleanExiHS_H2AFY2.
ExpressionAtlasiQ9P0M6. baseline and differential.
GenevestigatoriQ9P0M6.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR021171. Core_histone_macro-H2A.
IPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR002119. Histone_H2A.
IPR002589. Macro_dom.
[Graphical view]
PfamiPF00125. Histone. 1 hit.
PF01661. Macro. 1 hit.
[Graphical view]
PIRSFiPIRSF037942. Core_histone_macro-H2A. 1 hit.
PRINTSiPR00620. HISTONEH2A.
SMARTiSM00414. H2A. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS51154. MACRO. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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].

Entry informationi

Entry nameiH2AW_HUMAN
AccessioniPrimary (citable) accession number: Q9P0M6
Secondary accession number(s): Q5SQT2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: January 23, 2007
Last modified: February 4, 2015
This is version 132 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.