O75367 (H2AY_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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. 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 an 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.20
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 SPOP. Part of a complex consisting of H2AFY, CUL3 and SPOP. Interacts with HDAC1 and HDAC2 By similarity.
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 component	Chromosome Nucleosome core Nucleus
Coding sequence diversity	Alternative splicing
Ligand	DNA-binding
Molecular function	Chromatin regulator
PTM	Isopeptide bond Methylation Phosphoprotein Ubl conjugation
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. Source: MGI nucleosome assembly Non-traceable author statement Ref.1. Source: UniProtKB
Cellular component	Barr body Inferred from direct assay. Source: MGI nucleosome Non-traceable author statement Ref.1. Source: UniProtKB
Molecular function	DNA binding Non-traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

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 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.1

PRO_0000055318

Regions

Domain

2 – 117

116

Histone H2A

Domain

184 – 370

187

Macro

Compositional bias

118 – 162

45

Lys-rich

Amino acid modifications

Modified residue

18

1

N6-methyllysine Ref.15

Modified residue

123

1

N6,N6-dimethyllysine Probable

Modified residue

129

1

Phosphothreonine Ref.13 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19

Modified residue

170

1

Phosphoserine Ref.17 Ref.18 Ref.19

Modified residue

173

1

Phosphoserine Ref.17 Ref.18 Ref.19

Modified residue

174

1

Phosphothreonine Ref.17

Modified residue

178

1

Phosphothreonine Ref.13 Ref.18

Cross-link

116

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate Ref.9

Cross-link

117

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate Ref.9

Natural variations

Alternative sequence

159

1

Missing in isoform 3.

VSP_038379

Alternative sequence

198 – 229

32

NLIHS…LKDDL → QVVQADIASIDSDAVVHPTN TDFYIGGEV in isoform 1.

VSP_002056

Experimental info

Sequence conflict

186

1

L → F in BAB14565. Ref.3

Sequence conflict

210

1

F → S in BAB14565. Ref.3

Sequence conflict

225

1

L → P in AAC33433. Ref.1

Sequence conflict

291

1

E → G in AAH95406. Ref.5

Secondary structure

1

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372

Helix Strand Turn

Details...

Helix

15 – 19

5

Helix

25 – 35

11

Beta strand

39 – 41

3

Helix

45 – 70

26

Beta strand

74 – 76

3

Helix

78 – 87

10

Helix

89 – 94

6

Turn

95 – 97

3

Beta strand

98 – 100

3

Helix

111 – 113

3

Beta strand

185 – 190

6

Beta strand

196 – 202

7

Helix

204 – 209

6

Beta strand

213 – 219

7

Helix

227 – 252

26

Beta strand

260 – 264

5

Beta strand

268 – 277

10

Helix

286 – 303

18

Beta strand

307 – 311

5

Helix

323 – 340

18

Beta strand

348 – 355

8

Helix

356 – 367

12

Sequences

	Sequence		Length	Mass (Da)
	Isoform 2 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 37DED989EF7E69DC	FASTA	372	39,617
	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
	Isoform 1 [UniParc]. Checksum: D21A4CE6C7AA3BB1	FASTA	369	39,184
	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 LFLGQKLQVV QADIASIDSD AVVHPTNTDF YIGGEVGNTL EKKGGKEFVE 250 260 270 280 290 300 AVLELRKKNG PLEVAGAAVS AGHGLPAKFV IHCNSPVWGA DKCEELLEKT VKNCLALADD 310 320 330 340 350 360 KKLKSIAFPS IGSGRNGFPK QTAAQLILKA ISSYFVSTMS SSIKTVYFVL FDSESIGIYV QEMAKLDAN
	Isoform 3 [UniParc]. Checksum: 54320BFD118454D1	FASTA	371	39,489
	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 QGEVSKAASA DSTTEGTPAD 190 200 210 220 230 240 GFTVLSTKSL FLGQKLNLIH SEISNLAGFE VEAIINPTNA DIDLKDDLGN TLEKKGGKEF 250 260 270 280 290 300 VEAVLELRKK NGPLEVAGAA VSAGHGLPAK FVIHCNSPVW GADKCEELLE KTVKNCLALA 310 320 330 340 350 360 DDKKLKSIAF PSIGSGRNGF PKQTAAQLIL KAISSYFVST MSSSIKTVYF VLFDSESIGI 370 YVQEMAKLDA N

References

	« Hide 'large scale' referencesShow '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: 9714746] [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: 9653160] [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. , 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] (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. , 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: 15372022] [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] (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: 12800201] [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: 9634239] [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: 12718888] [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: 16129414] [Abstract] Cited for: UBIQUITINATION AT LYS-116 AND LYS-117, 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: 15621527] [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: 15902274] [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: 15897469] [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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129 AND THR-178, MASS SPECTROMETRY. 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: 16428466] [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: 16210244] [Abstract] Cited for: METHYLATION AT LYS-18 AND LYS-123, PHOSPHORYLATION AT THR-129, 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: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129; SER-170; SER-173 AND THR-174, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129; SER-170; SER-173 AND THR-178, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"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 THR-129; SER-170 AND SER-173, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[20]	"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: 16107708] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-120 IN COMPLEX WITH THE NUCLEOSOME CORE PARTICLE, FUNCTION.
[21]	"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: 15965484] [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).
+	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.

IPI

IPI00059366.
IPI00304171.
IPI00744148.

RefSeq

NP_001035248.1. NM_001040158.1.
NP_004884.1. NM_004893.2.
NP_613075.1. NM_138609.2.
NP_613258.2. NM_138610.2.

UniGene

Hs.420272.
Hs.599225.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1U35	X-ray	3.00	C/G	1-120	[»]
1ZR3	X-ray	1.66	A/B/C/D	162-372	[»]
1ZR5	X-ray	2.92	A/B	161-372	[»]
2F8N	X-ray	2.90	G	1-119	[»]
2FXK	X-ray	2.54	A/B	162-372	[»]
3HSV	X-ray	1.43	M	172-186	[»]
3IID	X-ray	1.90	A	162-372	[»]
3IIF	X-ray	2.10	A/B/C	162-372	[»]
3IVB	X-ray	1.75	M	167-181	[»]

ProteinModelPortal

O75367.

SMR

O75367. Positions 10-117, 181-369.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-44283N.

IntAct

O75367. 2 interactions.

MINT

MINT-2866965.

STRING

O75367.

PTM databases

PhosphoSite

O75367.

2D gel databases

SWISS-2DPAGE

O75367.

Proteomic databases

PRIDE

O75367.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000510038; ENSP00000424971; ENSG00000113648.
ENST00000511689; ENSP00000423563; ENSG00000113648.

GeneID

9555.

KEGG

hsa:9555.

UCSC

uc003lam.1. human.
uc003lan.1. human.

Organism-specific databases

CTD

9555.

GeneCards

GC05M134669.

HGNC

HGNC:4740. H2AFY.

MIM

610054. gene.

neXtProt

NX_O75367.

PharmGKB

PA29117.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG11347.

HOVERGEN

HBG009342.

InParanoid

O75367.

OMA

ANDEELH.

OrthoDB

EOG4XH00N.

PhylomeDB

O75367.

Gene expression databases

ArrayExpress

O75367.

Bgee

O75367.

CleanEx

HS_H2AFY.

Genevestigator

O75367.

GermOnline

ENSG00000113648. 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

SM00506. A1pp. 1 hit.
SM00414. H2A. 1 hit.
[Graphical view]

SUPFAM

SSF47113. Histone-fold. 1 hit.

PROSITE

PS51154. MACRO. 1 hit.
[Graphical view]

ProtoNet

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Other

NextBio

35835.

PMAP-CutDB

O75367.

SOURCE

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Entry information

Entry name

H2AY_HUMAN

Accession

Primary (citable) accession number: O75367
Secondary accession number(s): O75377 , Q503A8, Q7Z5E3, Q96D41, Q9H8P3, Q9UP96

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 122 of the entry and version 4 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.