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O75367 (H2AY_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Core histone macro-H2A.1

Short name=Histone macroH2A1
Short name=mH2A1
Alternative name(s):
Histone H2A.y
Short name=H2A/y
Medulloblastoma antigen MU-MB-50.205
Gene names
Name:H2AFY
Synonyms:MACROH2A1
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. Involved in stable X chromosome inactivation. Inhibits the binding of transcription factors and interferes with the activity of remodeling SWI/SNF complexes. Inhibits histone acetylation by EP300 and recruits class I HDACs, which induces a hypoacetylated state of chromatin. In addition, isoform 1, but not isoform 2, binds ADP-ribose and O-acetyl-ADP-ribose, and may be involved in ADP-ribose-mediated chromatin modulation. Ref.8 Ref.10 Ref.12 Ref.14 Ref.22

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. Interacts with HDAC1 and HDAC2 By similarity. Interacts with SPOP. Part of a complex consisting of H2AFY, CUL3 and SPOP. Ref.12 Ref.24

Subcellular location

Nucleus. Chromosome. Note: Enriched in inactive X chromosome chromatin and in senescence-associated heterochromatin. Ref.7 Ref.10 Ref.12

Tissue specificity

Ubiquitous. Ref.1

Post-translational modification

Monoubiquitinated at either Lys-116 or Lys-117. May also be polyubiquitinated. Ubiquitination is mediated by the CUL3/SPOP E3 complex and does not promote proteasomal degradation. Instead, it is required for enrichment in inactive X chromosome chromatin.

Miscellaneous

The number of individuals with antibodies against this antigen is 2-fold higher in pediatric patients with cancer compared to healthy controls.

Sequence similarities

Contains 1 histone H2A domain.

Contains 1 Macro domain.

Ontologies

Keywords
   Cellular componentChromosome
Nucleosome core
Nucleus
   Coding sequence diversityAlternative splicing
   LigandDNA-binding
   Molecular functionChromatin regulator
   PTMAcetylation
Isopeptide bond
Methylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin modification

Inferred from electronic annotation. Source: UniProtKB-KW

dosage compensation

Inferred from direct assay PubMed 15053874. Source: MGI

establishment of protein localization to chromatin

Inferred from mutant phenotype PubMed 19734898. Source: UniProt

negative regulation of cell cycle G2/M phase transition

Inferred from mutant phenotype PubMed 22194607. Source: UniProt

negative regulation of gene expression, epigenetic

Inferred from mutant phenotype PubMed 19734898PubMed 24071584. Source: UniProt

negative regulation of histone phosphorylation

Inferred from mutant phenotype PubMed 22194607. Source: UniProt

negative regulation of protein serine/threonine kinase activity

Inferred from mutant phenotype PubMed 22194607. Source: UniProt

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 19734898. Source: UniProt

negative regulation of transcription of nuclear large rRNA transcript from RNA polymerase I promoter

Inferred from mutant phenotype PubMed 24071584. Source: UniProt

nucleosome assembly

Non-traceable author statement Ref.1. Source: UniProtKB

   Cellular_componentBarr body

Inferred from direct assay PubMed 11331621. Source: MGI

condensed chromosome

Inferred from electronic annotation. Source: Ensembl

nuclear chromatin

Inferred from direct assay PubMed 19734898PubMed 22194607PubMed 24071584. Source: UniProt

nucleolus

Inferred from direct assay PubMed 24071584. Source: UniProt

nucleosome

Non-traceable author statement Ref.1. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 21630459. Source: UniProt

sex chromatin

Traceable author statement PubMed 19486527. Source: BHF-UCL

   Molecular_functionDNA binding

Non-traceable author statement Ref.1. Source: UniProtKB

chromatin DNA binding

Inferred from direct assay PubMed 19734898PubMed 24071584. Source: UniProt

double-stranded methylated DNA binding

Inferred from direct assay PubMed 24071584. Source: UniProt

protein binding

Inferred from physical interaction PubMed 22589551. Source: IntAct

protein kinase binding

Inferred from physical interaction PubMed 22194607. Source: UniProt

protein serine/threonine kinase inhibitor activity

Inferred from mutant phenotype PubMed 22194607. Source: UniProt

rDNA binding

Inferred from direct assay PubMed 24071584. Source: UniProt

transcription regulatory region DNA binding

Inferred from direct assay PubMed 19734898. Source: UniProt

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ERBB2P046266EBI-2868511,EBI-641062

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 2 (identifier: O75367-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 1 (identifier: O75367-2)

The sequence of this isoform differs from the canonical sequence as follows:
     198-229: NLIHSEISNLAGFEVEAIINPTNADIDLKDDL → QVVQADIASIDSDAVVHPTNTDFYIGGEV
Note: Specifically binds ADP-ribose and O-acetyl-ADP-ribose. Important residues for binding are Asp-203, Gly-224, Gly-314 and Phe-348.
Isoform 3 (identifier: O75367-3)

The sequence of this isoform differs from the canonical sequence as follows:
     159-159: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 372372Core histone macro-H2A.1
PRO_0000055318

Regions

Domain2 – 117116Histone H2A
Domain184 – 370187Macro
Compositional bias118 – 16245Lys-rich

Amino acid modifications

Modified residue181N6-methyllysine Ref.15
Modified residue1161N6-acetyllysine; alternate By similarity
Modified residue1231N6,N6-dimethyllysine; alternate Probable
Modified residue1231N6-acetyllysine; alternate By similarity
Modified residue1291Phosphothreonine Ref.13 Ref.15 Ref.16 Ref.19 Ref.20 Ref.21
Modified residue1701Phosphoserine Ref.17 Ref.19 Ref.21
Modified residue1731Phosphoserine Ref.19
Modified residue1781Phosphothreonine Ref.13 Ref.17 Ref.19 Ref.20
Cross-link116Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate Ref.9
Cross-link117Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9

Natural variations

Alternative sequence1591Missing in isoform 3.
VSP_038379
Alternative sequence198 – 22932NLIHS…LKDDL → QVVQADIASIDSDAVVHPTN TDFYIGGEV in isoform 1.
VSP_002056

Experimental info

Sequence conflict1861L → F in BAB14565. Ref.3
Sequence conflict2101F → S in BAB14565. Ref.3
Sequence conflict2251L → P in AAC33433. Ref.1
Sequence conflict2911E → G in AAH95406. Ref.5

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 2 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 37DED989EF7E69DC

FASTA37239,617
        10         20         30         40         50         60 
MSSRGGKKKS TKTSRSAKAG VIFPVGRMLR YIKKGHPKYR IGVGAPVYMA AVLEYLTAEI 

        70         80         90        100        110        120 
LELAGNAARD NKKGRVTPRH ILLAVANDEE LNQLLKGVTI ASGGVLPNIH PELLAKKRGS 

       130        140        150        160        170        180 
KGKLEAIITP PPAKKAKSPS QKKPVSKKAG GKKGARKSKK KQGEVSKAAS ADSTTEGTPA 

       190        200        210        220        230        240 
DGFTVLSTKS LFLGQKLNLI HSEISNLAGF EVEAIINPTN ADIDLKDDLG NTLEKKGGKE 

       250        260        270        280        290        300 
FVEAVLELRK KNGPLEVAGA AVSAGHGLPA KFVIHCNSPV WGADKCEELL EKTVKNCLAL 

       310        320        330        340        350        360 
ADDKKLKSIA FPSIGSGRNG FPKQTAAQLI LKAISSYFVS TMSSSIKTVY FVLFDSESIG 

       370 
IYVQEMAKLD AN 

« Hide

Isoform 1 [UniParc].

Checksum: D21A4CE6C7AA3BB1
Show »

FASTA36939,184
Isoform 3 [UniParc].

Checksum: 54320BFD118454D1
Show »

FASTA37139,489

References

« Hide 'large scale' references
[1]"Isolation of cDNA clones encoding human histone macroH2A1 subtypes."
Lee Y., Hong M., Kim J.W., Hong Y.M., Choe Y.-K., Chang S.Y., Lee K.S., Choe I.S.
Biochim. Biophys. Acta 1399:73-77(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
Tissue: Liver.
[2]"Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning."
Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H., He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H., Wang Y.-X., Chen S.-J., Chen Z.
Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
Tissue: Umbilical cord blood.
[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] (ISOFORM 2).
Tissue: Ovary.
[4]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(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] (ISOFORM 2).
Tissue: Bone marrow and Placenta.
[6]"Novel tumor antigens identified by autologous antibody screening of childhood medulloblastoma cDNA libraries."
Behrends U., Schneider I., Roessler S., Frauenknecht H., Golbeck A., Lechner B., Eigenstetter G., Zobywalski C., Mueller-Weihrich S., Graubner U., Schmid I., Sackerer D., Spaeth M., Goetz C., Prantl F., Asmuss H.-P., Bise K., Mautner J.
Int. J. Cancer 106:244-251(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-372 (ISOFORM 3).
Tissue: Medulloblastoma.
[7]"Histone macroH2A1 is concentrated in the inactive X chromosome of female mammals."
Costanzi C., Pehrson J.R.
Nature 393:599-601(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[8]"The histone variant macroH2A interferes with transcription factor binding and SWI/SNF nucleosome remodeling."
Angelov D., Molla A., Perche P.-Y., Hans F., Cote J., Khochbin S., Bouvet P., Dimitrov S.
Mol. Cell 11:1033-1041(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Histone variant macroH2A1.2 is mono-ubiquitinated at its histone domain."
Ogawa Y., Ono T., Wakata Y., Okawa K., Tagami H., Shibahara K.
Biochem. Biophys. Res. Commun. 336:204-209(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION AT LYS-116 AND LYS-117, IDENTIFICATION BY MASS SPECTROMETRY.
[10]"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.
[11]"The macro domain is an ADP-ribose binding module."
Karras G.I., Kustatscher G., Buhecha H.R., Allen M.D., Pugieux C., Sait F., Bycroft M., Ladurner A.G.
EMBO J. 24:1911-1920(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: BINDING TO ADP-RIBOSE (ISOFORM 1).
[12]"Stable X chromosome inactivation involves the PRC1 Polycomb complex and requires histone MACROH2A1 and the CULLIN3/SPOP ubiquitin E3 ligase."
Hernandez-Munoz I., Lund A.H., van der Stoop P., Boutsma E., Muijrers I., Verhoeven E., Nusinow D.A., Panning B., Marahrens Y., van Lohuizen M.
Proc. Natl. Acad. Sci. U.S.A. 102:7635-7640(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH CULLIN3 AND SPOP, UBIQUITINATION, SUBCELLULAR LOCATION, FUNCTION.
[13]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129 AND THR-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Mechanism of polymerase II transcription repression by the histone variant macroH2A."
Doyen C.-M., An W., Angelov D., Bondarenko V., Mietton F., Studitsky V.M., Hamiche A., Roeder R.G., Bouvet P., Dimitrov S.
Mol. Cell. Biol. 26:1156-1164(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[15]"Mapping post-translational modifications of the histone variant MacroH2A1 using tandem mass spectrometry."
Chu F., Nusinow D.A., Chalkley R.J., Plath K., Panning B., Burlingame A.L.
Mol. Cell. Proteomics 5:194-203(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LYS-18 AND LYS-123, PHOSPHORYLATION AT THR-129, IDENTIFICATION BY MASS SPECTROMETRY.
[16]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170 AND THR-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"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].
[19]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129; SER-170; SER-173 AND THR-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[20]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129 AND THR-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129 AND SER-170, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"Structural characterization of the histone variant macroH2A."
Chakravarthy S., Gundimella S.K., Caron C., Perche P.-Y., Pehrson J.R., Khochbin S., Luger K.
Mol. Cell. Biol. 25:7616-7624(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-120 IN COMPLEX WITH THE NUCLEOSOME CORE PARTICLE, FUNCTION.
[23]"Splicing regulates NAD metabolite binding to histone macroH2A."
Kustatscher G., Hothorn M., Pugieux C., Scheffzek K., Ladurner A.G.
Nat. Struct. Mol. Biol. 12:624-625(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS) OF 162-372 (ISOFORM 1), X-RAY CRYSTALLOGRAPHY (2.92 ANGSTROMS) OF 161-372 (ISOFORM 2), BINDING TO ADP-RIBOSE AND O-ACETYL-ADP-RIBOSE (ISOFORM 1).
[24]"Structures of SPOP-substrate complexes: insights into molecular architectures of BTB-Cul3 ubiquitin ligases."
Zhuang M., Calabrese M.F., Liu J., Waddell M.B., Nourse A., Hammel M., Miller D.J., Walden H., Duda D.M., Seyedin S.N., Hoggard T., Harper J.W., White K.P., Schulman B.A.
Mol. Cell 36:39-50(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS) OF 172-186 IN COMPLEXES WITH SPOP, SUBUNIT, UBIQUITINATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF041483 mRNA. Translation: AAC33433.1.
AF044286 mRNA. Translation: AAC33434.1.
AF054174 mRNA. Translation: AAC39908.1.
AK023409 mRNA. Translation: BAB14565.1.
AC026691 Genomic DNA. No translation available.
BC013331 mRNA. Translation: AAH13331.1.
BC095406 mRNA. Translation: AAH95406.1.
AY134746 mRNA. Translation: AAN08620.1.
CCDSCCDS4183.1. [O75367-3]
CCDS4184.1. [O75367-2]
CCDS4185.1. [O75367-1]
RefSeqNP_001035248.1. NM_001040158.1. [O75367-3]
NP_004884.1. NM_004893.2. [O75367-3]
NP_613075.1. NM_138609.2. [O75367-2]
NP_613258.2. NM_138610.2. [O75367-1]
UniGeneHs.420272.
Hs.599225.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1U35X-ray3.00C/G1-120[»]
1ZR3X-ray1.66A/B/C/D162-372[»]
1ZR5X-ray2.92A/B161-372[»]
2F8NX-ray2.90G1-120[»]
2FXKX-ray2.54A/B162-372[»]
3HQHX-ray2.30M167-181[»]
3HSVX-ray1.43M172-186[»]
3IIDX-ray1.90A162-372[»]
3IIFX-ray2.10A/B/C162-372[»]
3IVBX-ray1.75M167-181[»]
ProteinModelPortalO75367.
SMRO75367. Positions 10-117, 181-369.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114927. 37 interactions.
DIPDIP-44283N.
IntActO75367. 6 interactions.
MINTMINT-2866965.
STRING9606.ENSP00000353806.

PTM databases

PhosphoSiteO75367.

2D gel databases

SWISS-2DPAGEO75367.

Proteomic databases

MaxQBO75367.
PaxDbO75367.
PRIDEO75367.

Protocols and materials databases

DNASU9555.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000304332; ENSP00000302572; ENSG00000113648. [O75367-3]
ENST00000312469; ENSP00000310169; ENSG00000113648. [O75367-2]
ENST00000510038; ENSP00000424971; ENSG00000113648. [O75367-1]
ENST00000511689; ENSP00000423563; ENSG00000113648. [O75367-1]
GeneID9555.
KEGGhsa:9555.
UCSCuc003lam.1. human. [O75367-1]
uc003lan.1. human. [O75367-2]
uc003lao.1. human. [O75367-3]

Organism-specific databases

CTD9555.
GeneCardsGC05M134669.
HGNCHGNC:4740. H2AFY.
MIM610054. gene.
neXtProtNX_O75367.
PharmGKBPA29117.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2110.
HOVERGENHBG009342.
InParanoidO75367.
KOK11251.
OMAQVVQADI.
OrthoDBEOG71G9VP.
PhylomeDBO75367.
TreeFamTF332276.

Gene expression databases

ArrayExpressO75367.
BgeeO75367.
CleanExHS_H2AFY.
GenevestigatorO75367.

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.
SMARTSM00506. A1pp. 1 hit.
SM00414. H2A. 1 hit.
[Graphical view]
SUPFAMSSF47113. SSF47113. 1 hit.
PROSITEPS51154. MACRO. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSH2AFY. human.
EvolutionaryTraceO75367.
GeneWikiH2AFY.
GenomeRNAi9555.
NextBio35835.
PMAP-CutDBO75367.
PROO75367.
SOURCESearch...

Entry information

Entry nameH2AY_HUMAN
AccessionPrimary (citable) accession number: O75367
Secondary accession number(s): O75377 expand/collapse secondary AC list , Q503A8, Q7Z5E3, Q96D41, Q9H8P3, Q9UP96
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 147 of the entry and version 4 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

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM