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Core histone macro-H2A.1 (Histone macroH2A1) (mH2A1) (Histone H2A.y) (H2A/y) (Medulloblastoma antigen MU-MB-50.205)

 H2AY_HUMAN              Reviewed;         372 AA.
O75367; O75377; Q503A8; Q7Z5E3; Q96D41; Q9H8P3; Q9UP96;
24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
25-OCT-2017, entry version 183.
RecName: Full=Core histone macro-H2A.1;
Short=Histone macroH2A1;
Short=mH2A1;
AltName: Full=Histone H2A.y;
Short=H2A/y;
AltName: Full=Medulloblastoma antigen MU-MB-50.205;
Name=H2AFY; Synonyms=MACROH2A1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
TISSUE=Liver;
PubMed=9714746; DOI=10.1016/S0167-4781(98)00098-0;
Lee Y., Hong M., Kim J.W., Hong Y.M., Choe Y.-K., Chang S.Y.,
Lee K.S., Choe I.S.;
"Isolation of cDNA clones encoding human histone macroH2A1 subtypes.";
Biochim. Biophys. Acta 1399:73-77(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=Umbilical cord blood;
PubMed=9653160; DOI=10.1073/pnas.95.14.8175;
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.;
"Identification of genes expressed in human CD34(+) hematopoietic
stem/progenitor cells by expressed sequence tags and efficient full-
length cDNA cloning.";
Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Ovary;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
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.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Bone marrow, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 6-372 (ISOFORM 3).
TISSUE=Medulloblastoma;
PubMed=12800201; DOI=10.1002/ijc.11208;
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.;
"Novel tumor antigens identified by autologous antibody screening of
childhood medulloblastoma cDNA libraries.";
Int. J. Cancer 106:244-251(2003).
[7]
SUBCELLULAR LOCATION.
PubMed=9634239; DOI=10.1038/31275;
Costanzi C., Pehrson J.R.;
"Histone macroH2A1 is concentrated in the inactive X chromosome of
female mammals.";
Nature 393:599-601(1998).
[8]
FUNCTION.
PubMed=12718888; DOI=10.1016/S1097-2765(03)00100-X;
Angelov D., Molla A., Perche P.-Y., Hans F., Cote J., Khochbin S.,
Bouvet P., Dimitrov S.;
"The histone variant macroH2A interferes with transcription factor
binding and SWI/SNF nucleosome remodeling.";
Mol. Cell 11:1033-1041(2003).
[9]
UBIQUITINATION AT LYS-116 AND LYS-117, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=16129414; DOI=10.1016/j.bbrc.2005.08.046;
Ogawa Y., Ono T., Wakata Y., Okawa K., Tagami H., Shibahara K.;
"Histone variant macroH2A1.2 is mono-ubiquitinated at its histone
domain.";
Biochem. Biophys. Res. Commun. 336:204-209(2005).
[10]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15621527; DOI=10.1016/j.devcel.2004.10.019;
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.;
"Formation of MacroH2A-containing senescence-associated
heterochromatin foci and senescence driven by ASF1a and HIRA.";
Dev. Cell 8:19-30(2005).
[11]
FUNCTION, AND BINDING OF THE MACRO DOMAIN TO ADP-RIBOSE (ISOFORM 1).
PubMed=15902274; DOI=10.1038/sj.emboj.7600664;
Karras G.I., Kustatscher G., Buhecha H.R., Allen M.D., Pugieux C.,
Sait F., Bycroft M., Ladurner A.G.;
"The macro domain is an ADP-ribose binding module.";
EMBO J. 24:1911-1920(2005).
[12]
IDENTIFICATION IN A COMPLEX WITH CULLIN3 AND SPOP, UBIQUITINATION,
SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=15897469; DOI=10.1073/pnas.0408918102;
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.;
"Stable X chromosome inactivation involves the PRC1 Polycomb complex
and requires histone MACROH2A1 and the CULLIN3/SPOP ubiquitin E3
ligase.";
Proc. Natl. Acad. Sci. U.S.A. 102:7635-7640(2005).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129 AND THR-178, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[14]
FUNCTION.
PubMed=16428466; DOI=10.1128/MCB.26.3.1156-1164.2006;
Doyen C.-M., An W., Angelov D., Bondarenko V., Mietton F.,
Studitsky V.M., Hamiche A., Roeder R.G., Bouvet P., Dimitrov S.;
"Mechanism of polymerase II transcription repression by the histone
variant macroH2A.";
Mol. Cell. Biol. 26:1156-1164(2006).
[15]
METHYLATION AT LYS-18 AND LYS-123, PHOSPHORYLATION AT THR-129, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16210244; DOI=10.1074/mcp.M500285-MCP200;
Chu F., Nusinow D.A., Chalkley R.J., Plath K., Panning B.,
Burlingame A.L.;
"Mapping post-translational modifications of the histone variant
MacroH2A1 using tandem mass spectrometry.";
Mol. Cell. Proteomics 5:194-203(2006).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17924679; DOI=10.1021/pr070152u;
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"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.";
J. Proteome Res. 6:4150-4162(2007).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170 AND THR-178, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129; SER-170; SER-173
AND THR-178, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129 AND THR-178, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129 AND SER-170, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[22]
FUNCTION (ISOFORMS 1 AND 2), AND ALTERNATIVE SPLICING (ISOFORMS 1 AND
2).
PubMed=23022728; DOI=10.1038/nsmb.2390;
Dardenne E., Pierredon S., Driouch K., Gratadou L., Lacroix-Triki M.,
Espinoza M.P., Zonta E., Germann S., Mortada H., Villemin J.P.,
Dutertre M., Lidereau R., Vagner S., Auboeuf D.;
"Splicing switch of an epigenetic regulator by RNA helicases promotes
tumor-cell invasiveness.";
Nat. Struct. Mol. Biol. 19:1139-1146(2012).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129; SER-170; SER-173
AND THR-178, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[24]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-123; LYS-167; LYS-189 AND
LYS-323, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[25]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-120 IN COMPLEX WITH THE
NUCLEOSOME CORE PARTICLE, AND FUNCTION.
PubMed=16107708; DOI=10.1128/MCB.25.17.7616-7624.2005;
Chakravarthy S., Gundimella S.K., Caron C., Perche P.-Y.,
Pehrson J.R., Khochbin S., Luger K.;
"Structural characterization of the histone variant macroH2A.";
Mol. Cell. Biol. 25:7616-7624(2005).
[26]
X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS) OF 162-372 (ISOFORM 1), X-RAY
CRYSTALLOGRAPHY (2.92 ANGSTROMS) OF 161-372 (ISOFORM 2), AND BINDING
TO ADP-RIBOSE AND O-ACETYL-ADP-RIBOSE (ISOFORM 1).
PubMed=15965484; DOI=10.1038/nsmb956;
Kustatscher G., Hothorn M., Pugieux C., Scheffzek K., Ladurner A.G.;
"Splicing regulates NAD metabolite binding to histone macroH2A.";
Nat. Struct. Mol. Biol. 12:624-625(2005).
[27]
X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS) OF 172-186 IN COMPLEXES WITH
SPOP, SUBUNIT, AND UBIQUITINATION.
PubMed=19818708; DOI=10.1016/j.molcel.2009.09.022;
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.;
"Structures of SPOP-substrate complexes: insights into molecular
architectures of BTB-Cul3 ubiquitin ligases.";
Mol. Cell 36:39-50(2009).
-!- FUNCTION: Variant histone H2A which replaces conventional H2A in a
subset of nucleosomes where it represses transcription
(PubMed:12718888, PubMed:15621527, PubMed:16428466). 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 (PubMed:15897469). Inhibits the binding of
transcription factors, including NF-kappa-B, and interferes with
the activity of remodeling SWI/SNF complexes (PubMed:12718888,
PubMed:16428466). Inhibits histone acetylation by EP300 and
recruits class I HDACs, which induces a hypoacetylated state of
chromatin (PubMed:16428466, PubMed:16107708).
{ECO:0000269|PubMed:12718888, ECO:0000269|PubMed:15621527,
ECO:0000269|PubMed:15897469, ECO:0000269|PubMed:16107708,
ECO:0000269|PubMed:16428466}.
-!- FUNCTION: Isoform 1: Binds ADP-ribose and O-acetyl-ADP-ribose, and
may be involved in ADP-ribose-mediated chromatin modulation
(PubMed:15902274). Increases the expression of genes involved in
redox metabolism, including SOD3 (PubMed:23022728).
{ECO:0000269|PubMed:15902274, ECO:0000269|PubMed:23022728}.
-!- FUNCTION: Isoform 2: Represses SOD3 gene expression.
{ECO:0000269|PubMed:23022728}.
-!- SUBUNIT: 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. {ECO:0000250,
ECO:0000269|PubMed:15897469, ECO:0000269|PubMed:16107708,
ECO:0000269|PubMed:19818708}.
-!- INTERACTION:
P46100:ATRX; NbExp=2; IntAct=EBI-6249599, EBI-396461;
P04626:ERBB2; NbExp=6; IntAct=EBI-2868511, EBI-641062;
A1L162:ERICH2; NbExp=5; IntAct=EBI-2868511, EBI-2682520;
P61244:MAX; NbExp=2; IntAct=EBI-2868511, EBI-751711;
O95271:TNKS; NbExp=6; IntAct=EBI-6249599, EBI-1105254;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15621527,
ECO:0000269|PubMed:15897469, ECO:0000269|PubMed:9634239}.
Chromosome {ECO:0000269|PubMed:15621527,
ECO:0000269|PubMed:15897469, ECO:0000269|PubMed:9634239}.
Note=Enriched in inactive X chromosome chromatin and in
senescence-associated heterochromatin.
{ECO:0000269|PubMed:15621527, ECO:0000269|PubMed:15897469,
ECO:0000269|PubMed:9634239}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=2; Synonyms=mH2A1.2 {ECO:0000303|PubMed:23022728};
IsoId=O75367-1; Sequence=Displayed;
Note=The preferential expression of isoform 2 over that of
isoform 1 requires the presence of DDX5/DDX17.
{ECO:0000269|PubMed:23022728};
Name=1; Synonyms=mH2A1.1 {ECO:0000303|PubMed:23022728};
IsoId=O75367-2; Sequence=VSP_002056;
Note=Specifically binds ADP-ribose and O-acetyl-ADP-ribose.
Important residues for binding are Asp-203, Gly-224, Gly-314 and
Phe-348. Preferentially expressed over isoform 2 in the absence
of DDX5/DDX17. {ECO:0000269|PubMed:15902274,
ECO:0000269|PubMed:23022728};
Name=3;
IsoId=O75367-3; Sequence=VSP_038379;
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:9714746}.
-!- PTM: 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.
{ECO:0000269|PubMed:15897469, ECO:0000269|PubMed:16129414,
ECO:0000269|PubMed:19818708}.
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EMBL; AF041483; AAC33433.1; -; mRNA.
EMBL; AF044286; AAC33434.1; -; mRNA.
EMBL; AF054174; AAC39908.1; -; mRNA.
EMBL; AK023409; BAB14565.1; -; mRNA.
EMBL; AC026691; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC013331; AAH13331.1; -; mRNA.
EMBL; BC095406; AAH95406.1; -; mRNA.
EMBL; AY134746; AAN08620.1; -; mRNA.
CCDS; CCDS4183.1; -. [O75367-3]
CCDS; CCDS4184.1; -. [O75367-2]
CCDS; CCDS4185.1; -. [O75367-1]
RefSeq; NP_001035248.1; NM_001040158.1. [O75367-3]
RefSeq; NP_004884.1; NM_004893.2. [O75367-3]
RefSeq; NP_613075.1; NM_138609.2. [O75367-2]
RefSeq; NP_613258.2; NM_138610.2. [O75367-1]
RefSeq; XP_011542031.1; XM_011543729.2. [O75367-1]
RefSeq; XP_011542032.1; XM_011543730.2. [O75367-3]
UniGene; Hs.420272; -.
UniGene; Hs.599225; -.
PDB; 1U35; X-ray; 3.00 A; C/G=1-120.
PDB; 1ZR3; X-ray; 1.66 A; A/B/C/D=162-372.
PDB; 1ZR5; X-ray; 2.92 A; A/B=161-372.
PDB; 2F8N; X-ray; 2.90 A; G=1-120.
PDB; 2FXK; X-ray; 2.54 A; A/B=162-372.
PDB; 3HQH; X-ray; 2.30 A; M=167-181.
PDB; 3HSV; X-ray; 1.43 A; M=172-186.
PDB; 3IID; X-ray; 1.90 A; A=162-372.
PDB; 3IIF; X-ray; 2.10 A; A/B/C=162-372.
PDB; 3IVB; X-ray; 1.75 A; M=167-181.
PDB; 5IIT; X-ray; 2.13 A; A/B/C/D=181-369.
PDB; 5LNC; X-ray; 3.29 A; A/B=182-369.
PDBsum; 1U35; -.
PDBsum; 1ZR3; -.
PDBsum; 1ZR5; -.
PDBsum; 2F8N; -.
PDBsum; 2FXK; -.
PDBsum; 3HQH; -.
PDBsum; 3HSV; -.
PDBsum; 3IID; -.
PDBsum; 3IIF; -.
PDBsum; 3IVB; -.
PDBsum; 5IIT; -.
PDBsum; 5LNC; -.
ProteinModelPortal; O75367; -.
SMR; O75367; -.
BioGrid; 114927; 86.
CORUM; O75367; -.
DIP; DIP-44283N; -.
ELM; O75367; -.
IntAct; O75367; 29.
MINT; MINT-2866965; -.
STRING; 9606.ENSP00000423563; -.
iPTMnet; O75367; -.
PhosphoSitePlus; O75367; -.
SwissPalm; O75367; -.
BioMuta; H2AFY; -.
SWISS-2DPAGE; O75367; -.
EPD; O75367; -.
MaxQB; O75367; -.
PaxDb; O75367; -.
PeptideAtlas; O75367; -.
PRIDE; O75367; -.
TopDownProteomics; O75367-1; -. [O75367-1]
TopDownProteomics; O75367-2; -. [O75367-2]
DNASU; 9555; -.
Ensembl; ENST00000304332; ENSP00000302572; ENSG00000113648. [O75367-3]
Ensembl; ENST00000312469; ENSP00000310169; ENSG00000113648. [O75367-2]
Ensembl; ENST00000510038; ENSP00000424971; ENSG00000113648. [O75367-1]
Ensembl; ENST00000511689; ENSP00000423563; ENSG00000113648. [O75367-1]
GeneID; 9555; -.
KEGG; hsa:9555; -.
UCSC; uc003lam.2; human. [O75367-1]
CTD; 9555; -.
DisGeNET; 9555; -.
EuPathDB; HostDB:ENSG00000113648.16; -.
GeneCards; H2AFY; -.
HGNC; HGNC:4740; H2AFY.
HPA; HPA041189; -.
HPA; HPA050962; -.
MIM; 610054; gene.
neXtProt; NX_O75367; -.
OpenTargets; ENSG00000113648; -.
PharmGKB; PA29117; -.
eggNOG; ENOG410IV3A; Eukaryota.
eggNOG; KOG1756; Eukaryota.
eggNOG; KOG2633; Eukaryota.
eggNOG; COG2110; LUCA.
eggNOG; COG5262; LUCA.
GeneTree; ENSGT00900000140854; -.
HOVERGEN; HBG009342; -.
InParanoid; O75367; -.
KO; K11251; -.
OMA; HCNSPIW; -.
OrthoDB; EOG091G0XGD; -.
PhylomeDB; O75367; -.
TreeFam; TF332276; -.
ChiTaRS; H2AFY; human.
EvolutionaryTrace; O75367; -.
GeneWiki; H2AFY; -.
GenomeRNAi; 9555; -.
PMAP-CutDB; O75367; -.
PRO; PR:O75367; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000113648; -.
CleanEx; HS_H2AFY; -.
ExpressionAtlas; O75367; baseline and differential.
Genevisible; O75367; HS.
GO; GO:0001740; C:Barr body; IDA:UniProtKB.
GO; GO:0000793; C:condensed chromosome; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; IDA:UniProtKB.
GO; GO:0000228; C:nuclear chromosome; IDA:UniProtKB.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IDA:BHF-UCL.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0000786; C:nucleosome; NAS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005721; C:pericentric heterochromatin; IDA:BHF-UCL.
GO; GO:0001739; C:sex chromatin; TAS:BHF-UCL.
GO; GO:0031490; F:chromatin DNA binding; IDA:UniProtKB.
GO; GO:0001046; F:core promoter sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
GO; GO:0010385; F:double-stranded methylated DNA binding; IDA:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0031492; F:nucleosomal DNA binding; IDA:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0030291; F:protein serine/threonine kinase inhibitor activity; IMP:UniProtKB.
GO; GO:0000182; F:rDNA binding; IDA:UniProtKB.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0006342; P:chromatin silencing; IBA:GO_Central.
GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
GO; GO:0007549; P:dosage compensation; IDA:MGI.
GO; GO:0071169; P:establishment of protein localization to chromatin; IMP:UniProtKB.
GO; GO:1902750; P:negative regulation of cell cycle G2/M phase transition; IMP:UniProtKB.
GO; GO:0045814; P:negative regulation of gene expression, epigenetic; IMP:UniProtKB.
GO; GO:0061086; P:negative regulation of histone H3-K27 methylation; IMP:UniProtKB.
GO; GO:0051572; P:negative regulation of histone H3-K4 methylation; IMP:UniProtKB.
GO; GO:0033128; P:negative regulation of histone phosphorylation; IMP:UniProtKB.
GO; GO:1904815; P:negative regulation of protein localization to chromosome, telomeric region; IDA:BHF-UCL.
GO; GO:0071901; P:negative regulation of protein serine/threonine kinase activity; IMP:UniProtKB.
GO; GO:1902883; P:negative regulation of response to oxidative stress; IMP:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:1901837; P:negative regulation of transcription of nuclear large rRNA transcript from RNA polymerase I promoter; IMP:UniProtKB.
GO; GO:0006334; P:nucleosome assembly; NAS:UniProtKB.
GO; GO:0045815; P:positive regulation of gene expression, epigenetic; IMP:UniProtKB.
GO; GO:0045618; P:positive regulation of keratinocyte differentiation; IMP:UniProtKB.
GO; GO:0034184; P:positive regulation of maintenance of mitotic sister chromatid cohesion; IDA:BHF-UCL.
GO; GO:1902884; P:positive regulation of response to oxidative stress; IMP:UniProtKB.
GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:UniProtKB.
GO; GO:0019216; P:regulation of lipid metabolic process; IMP:UniProtKB.
GO; GO:1902882; P:regulation of response to oxidative stress; IMP:UniProtKB.
CDD; cd00074; H2A; 1.
CDD; cd02904; Macro_H2A_like; 1.
InterPro; IPR021171; Core_histone_macro-H2A.
InterPro; IPR009072; Histone-fold.
InterPro; IPR002119; Histone_H2A.
InterPro; IPR007125; Histone_H2A/H2B/H3.
InterPro; IPR032454; Histone_H2A_C.
InterPro; IPR002589; Macro_dom.
InterPro; IPR035796; Macro_H2A.
Pfam; PF00125; Histone; 1.
Pfam; PF16211; Histone_H2A_C; 1.
Pfam; PF01661; Macro; 1.
PIRSF; PIRSF037942; Core_histone_macro-H2A; 1.
PRINTS; PR00620; HISTONEH2A.
SMART; SM00506; A1pp; 1.
SMART; SM00414; H2A; 1.
SUPFAM; SSF47113; SSF47113; 1.
PROSITE; PS51154; MACRO; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Chromatin regulator;
Chromosome; Complete proteome; DNA-binding; Isopeptide bond;
Methylation; Nucleosome core; Nucleus; Phosphoprotein;
Reference proteome; Ubl conjugation.
CHAIN 1 372 Core histone macro-H2A.1.
/FTId=PRO_0000055318.
DOMAIN 2 117 Histone H2A.
DOMAIN 184 370 Macro. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
COMPBIAS 118 162 Lys-rich.
MOD_RES 18 18 N6-methyllysine.
{ECO:0000269|PubMed:16210244}.
MOD_RES 116 116 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q9QZQ8}.
MOD_RES 123 123 N6,N6-dimethyllysine; alternate.
{ECO:0000305|PubMed:16210244}.
MOD_RES 123 123 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q9QZQ8}.
MOD_RES 129 129 Phosphothreonine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:16210244}.
MOD_RES 170 170 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 173 173 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 178 178 Phosphothreonine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
CROSSLNK 116 116 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate. {ECO:0000269|PubMed:16129414}.
CROSSLNK 117 117 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:16129414}.
CROSSLNK 123 123 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 167 167 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 189 189 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 323 323 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 159 159 Missing (in isoform 3).
{ECO:0000303|PubMed:12800201,
ECO:0000303|PubMed:9653160}.
/FTId=VSP_038379.
VAR_SEQ 198 229 NLIHSEISNLAGFEVEAIINPTNADIDLKDDL -> QVVQA
DIASIDSDAVVHPTNTDFYIGGEV (in isoform 1).
{ECO:0000303|PubMed:9714746}.
/FTId=VSP_002056.
CONFLICT 186 186 L -> F (in Ref. 3; BAB14565).
{ECO:0000305}.
CONFLICT 210 210 F -> S (in Ref. 3; BAB14565).
{ECO:0000305}.
CONFLICT 225 225 L -> P (in Ref. 1; AAC33433).
{ECO:0000305}.
CONFLICT 291 291 E -> G (in Ref. 5; AAH95406).
{ECO:0000305}.
HELIX 15 19 {ECO:0000244|PDB:2F8N}.
HELIX 25 35 {ECO:0000244|PDB:2F8N}.
STRAND 36 38 {ECO:0000244|PDB:2F8N}.
STRAND 39 41 {ECO:0000244|PDB:1U35}.
HELIX 44 70 {ECO:0000244|PDB:2F8N}.
STRAND 74 76 {ECO:0000244|PDB:2F8N}.
HELIX 78 86 {ECO:0000244|PDB:2F8N}.
HELIX 89 94 {ECO:0000244|PDB:2F8N}.
TURN 95 97 {ECO:0000244|PDB:2F8N}.
STRAND 98 100 {ECO:0000244|PDB:2F8N}.
HELIX 111 113 {ECO:0000244|PDB:2F8N}.
STRAND 174 177 {ECO:0000244|PDB:3IVB}.
STRAND 185 190 {ECO:0000244|PDB:1ZR3}.
STRAND 196 202 {ECO:0000244|PDB:1ZR3}.
HELIX 204 209 {ECO:0000244|PDB:1ZR5}.
STRAND 213 219 {ECO:0000244|PDB:1ZR3}.
HELIX 227 252 {ECO:0000244|PDB:1ZR3}.
STRAND 260 264 {ECO:0000244|PDB:1ZR3}.
STRAND 268 277 {ECO:0000244|PDB:1ZR3}.
HELIX 286 303 {ECO:0000244|PDB:1ZR3}.
STRAND 307 311 {ECO:0000244|PDB:1ZR3}.
STRAND 315 319 {ECO:0000244|PDB:2FXK}.
HELIX 323 340 {ECO:0000244|PDB:1ZR3}.
STRAND 341 343 {ECO:0000244|PDB:1ZR5}.
STRAND 348 355 {ECO:0000244|PDB:1ZR3}.
HELIX 356 367 {ECO:0000244|PDB:1ZR3}.
SEQUENCE 372 AA; 39617 MW; 37DED989EF7E69DC CRC64;
MSSRGGKKKS TKTSRSAKAG VIFPVGRMLR YIKKGHPKYR IGVGAPVYMA AVLEYLTAEI
LELAGNAARD NKKGRVTPRH ILLAVANDEE LNQLLKGVTI ASGGVLPNIH PELLAKKRGS
KGKLEAIITP PPAKKAKSPS QKKPVSKKAG GKKGARKSKK KQGEVSKAAS ADSTTEGTPA
DGFTVLSTKS LFLGQKLNLI HSEISNLAGF EVEAIINPTN ADIDLKDDLG NTLEKKGGKE
FVEAVLELRK KNGPLEVAGA AVSAGHGLPA KFVIHCNSPV WGADKCEELL EKTVKNCLAL
ADDKKLKSIA FPSIGSGRNG FPKQTAAQLI LKAISSYFVS TMSSSIKTVY FVLFDSESIG
IYVQEMAKLD AN


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