ID H2AY_HUMAN Reviewed; 369 AA. AC O75367; O75377; Q503A8; Q7Z5E3; Q96D41; Q9H8P3; Q9UP96; DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 12-OCT-2022, sequence version 5. DT 04-NOV-2026, entry version 235. DE RecName: Full=Core histone macro-H2A.1; DE Short=Histone macroH2A1; DE Short=mH2A1; DE AltName: Full=Histone H2A.y; DE Short=H2A/y; DE AltName: Full=Medulloblastoma antigen MU-MB-50.205; GN Name=MACROH2A1 {ECO:0000312|HGNC:HGNC:4740}; GN Synonyms=H2AFY {ECO:0000312|HGNC:HGNC:4740}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY. RC TISSUE=Liver; RX PubMed=9714746; DOI=10.1016/s0167-4781(98)00098-0; RA Lee Y., Hong M., Kim J.W., Hong Y.M., Choe Y.-K., Chang S.Y., Lee K.S., RA Choe I.S.; RT "Isolation of cDNA clones encoding human histone macroH2A1 subtypes."; RL Biochim. Biophys. Acta 1399:73-77(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC TISSUE=Umbilical cord blood; RX PubMed=9653160; DOI=10.1073/pnas.95.14.8175; RA Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H., RA He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H., RA Wang Y.-X., Chen S.-J., Chen Z.; RT "Identification of genes expressed in human CD34(+) hematopoietic RT stem/progenitor cells by expressed sequence tags and efficient full-length RT cDNA cloning."; RL Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Ovary; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Bone marrow, and Placenta; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-369 (ISOFORM 3). RC TISSUE=Medulloblastoma; RX PubMed=12800201; DOI=10.1002/ijc.11208; RA Behrends U., Schneider I., Roessler S., Frauenknecht H., Golbeck A., RA Lechner B., Eigenstetter G., Zobywalski C., Mueller-Weihrich S., RA Graubner U., Schmid I., Sackerer D., Spaeth M., Goetz C., Prantl F., RA Asmuss H.-P., Bise K., Mautner J.; RT "Novel tumor antigens identified by autologous antibody screening of RT childhood medulloblastoma cDNA libraries."; RL Int. J. Cancer 106:244-251(2003). RN [7] RP SUBCELLULAR LOCATION. RX PubMed=9634239; DOI=10.1038/31275; RA Costanzi C., Pehrson J.R.; RT "Histone macroH2A1 is concentrated in the inactive X chromosome of female RT mammals."; RL Nature 393:599-601(1998). RN [8] RP FUNCTION. RX PubMed=12718888; DOI=10.1016/s1097-2765(03)00100-x; RA Angelov D., Molla A., Perche P.-Y., Hans F., Cote J., Khochbin S., RA Bouvet P., Dimitrov S.; RT "The histone variant macroH2A interferes with transcription factor binding RT and SWI/SNF nucleosome remodeling."; RL Mol. Cell 11:1033-1041(2003). RN [9] RP UBIQUITINATION AT LYS-116 AND LYS-117, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=16129414; DOI=10.1016/j.bbrc.2005.08.046; RA Ogawa Y., Ono T., Wakata Y., Okawa K., Tagami H., Shibahara K.; RT "Histone variant macroH2A1.2 is mono-ubiquitinated at its histone domain."; RL Biochem. Biophys. Res. Commun. 336:204-209(2005). RN [10] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=15621527; DOI=10.1016/j.devcel.2004.10.019; RA Zhang R., Poustovoitov M.V., Ye X., Santos H.A., Chen W., Daganzo S.M., RA Erzberger J.P., Serebriiskii I.G., Canutescu A.A., Dunbrack R.L., RA Pehrson J.R., Berger J.M., Kaufman P.D., Adams P.D.; RT "Formation of MacroH2A-containing senescence-associated heterochromatin RT foci and senescence driven by ASF1a and HIRA."; RL Dev. Cell 8:19-30(2005). RN [11] RP FUNCTION, AND BINDING OF THE MACRO DOMAIN TO ADP-RIBOSE (ISOFORM 1). RX PubMed=15902274; DOI=10.1038/sj.emboj.7600664; RA Karras G.I., Kustatscher G., Buhecha H.R., Allen M.D., Pugieux C., Sait F., RA Bycroft M., Ladurner A.G.; RT "The macro domain is an ADP-ribose binding module."; RL EMBO J. 24:1911-1920(2005). RN [12] RP IDENTIFICATION IN A COMPLEX WITH CULLIN3 AND SPOP, UBIQUITINATION, RP SUBCELLULAR LOCATION, AND FUNCTION. RX PubMed=15897469; DOI=10.1073/pnas.0408918102; RA Hernandez-Munoz I., Lund A.H., van der Stoop P., Boutsma E., Muijrers I., RA Verhoeven E., Nusinow D.A., Panning B., Marahrens Y., van Lohuizen M.; RT "Stable X chromosome inactivation involves the PRC1 Polycomb complex and RT requires histone MACROH2A1 and the CULLIN3/SPOP ubiquitin E3 ligase."; RL Proc. Natl. Acad. Sci. U.S.A. 102:7635-7640(2005). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129 AND THR-178, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [14] RP FUNCTION. RX PubMed=16428466; DOI=10.1128/mcb.26.3.1156-1164.2006; RA Doyen C.-M., An W., Angelov D., Bondarenko V., Mietton F., Studitsky V.M., RA Hamiche A., Roeder R.G., Bouvet P., Dimitrov S.; RT "Mechanism of polymerase II transcription repression by the histone variant RT macroH2A."; RL Mol. Cell. Biol. 26:1156-1164(2006). RN [15] RP METHYLATION AT LYS-18 AND LYS-123, PHOSPHORYLATION AT THR-129, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=16210244; DOI=10.1074/mcp.m500285-mcp200; RA Chu F., Nusinow D.A., Chalkley R.J., Plath K., Panning B., Burlingame A.L.; RT "Mapping post-translational modifications of the histone variant MacroH2A1 RT using tandem mass spectrometry."; RL Mol. Cell. Proteomics 5:194-203(2006). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17924679; DOI=10.1021/pr070152u; RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells RT and high confident phosphopeptide identification by cross-validation of RT MS/MS and MS/MS/MS spectra."; RL J. Proteome Res. 6:4150-4162(2007). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170 AND THR-178, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129; SER-170; SER-173 AND RP THR-178, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129 AND THR-178, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [21] RP SUBCELLULAR LOCATION. RX PubMed=21211722; DOI=10.1016/j.molcel.2010.12.008; RA Mehrotra P.V., Ahel D., Ryan D.P., Weston R., Wiechens N., Kraehenbuehl R., RA Owen-Hughes T., Ahel I.; RT "DNA repair factor APLF is a histone chaperone."; RL Mol. Cell 41:46-55(2011). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129 AND SER-170, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [23] RP FUNCTION (ISOFORMS 1 AND 2), AND ALTERNATIVE SPLICING (ISOFORMS 1 AND 2). RX PubMed=23022728; DOI=10.1038/nsmb.2390; RA Dardenne E., Pierredon S., Driouch K., Gratadou L., Lacroix-Triki M., RA Espinoza M.P., Zonta E., Germann S., Mortada H., Villemin J.P., RA Dutertre M., Lidereau R., Vagner S., Auboeuf D.; RT "Splicing switch of an epigenetic regulator by RNA helicases promotes RT tumor-cell invasiveness."; RL Nat. Struct. Mol. Biol. 19:1139-1146(2012). RN [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129; SER-170; SER-173 AND RP THR-178, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [25] RP LACK OF ADP-RIBOSE GLYCOHYDROLASE ACTIVITY. RX PubMed=23474714; DOI=10.1038/nsmb.2521; RA Rosenthal F., Feijs K.L., Frugier E., Bonalli M., Forst A.H., Imhof R., RA Winkler H.C., Fischer D., Caflisch A., Hassa P.O., Luescher B., RA Hottiger M.O.; RT "Macrodomain-containing proteins are new mono-ADP-ribosylhydrolases."; RL Nat. Struct. Mol. Biol. 20:502-507(2013). RN [26] RP SUBCELLULAR LOCATION. RX PubMed=29905837; DOI=10.1093/nar/gky507; RA Corbeski I., Dolinar K., Wienk H., Boelens R., van Ingen H.; RT "DNA repair factor APLF acts as a H2A-H2B histone chaperone through binding RT its DNA interaction surface."; RL Nucleic Acids Res. 46:7138-7152(2018). RN [27] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-123; LYS-167; LYS-189 AND RP LYS-320, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [28] RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH THE NUCLEOSOME CORE PARTICLE, AND RP FUNCTION. RX PubMed=16107708; DOI=10.1128/mcb.25.17.7616-7624.2005; RA Chakravarthy S., Gundimella S.K., Caron C., Perche P.-Y., Pehrson J.R., RA Khochbin S., Luger K.; RT "Structural characterization of the histone variant macroH2A."; RL Mol. Cell. Biol. 25:7616-7624(2005). RN [29] RP X-RAY CRYSTALLOGRAPHY (ISOFORM 1), X-RAY CRYSTALLOGRAPHY (ISOFORM 2), AND RP BINDING TO ADP-RIBOSE AND O-ACETYL-ADP-RIBOSE (ISOFORM 1). RX PubMed=15965484; DOI=10.1038/nsmb956; RA Kustatscher G., Hothorn M., Pugieux C., Scheffzek K., Ladurner A.G.; RT "Splicing regulates NAD metabolite binding to histone macroH2A."; RL Nat. Struct. Mol. Biol. 12:624-625(2005). RN [30] RP X-RAY CRYSTALLOGRAPHY IN COMPLEXES WITH SPOP, SUBUNIT, AND UBIQUITINATION. RX PubMed=19818708; DOI=10.1016/j.molcel.2009.09.022; RA Zhuang M., Calabrese M.F., Liu J., Waddell M.B., Nourse A., Hammel M., RA Miller D.J., Walden H., Duda D.M., Seyedin S.N., Hoggard T., Harper J.W., RA White K.P., Schulman B.A.; RT "Structures of SPOP-substrate complexes: insights into molecular RT architectures of BTB-Cul3 ubiquitin ligases."; RL Mol. Cell 36:39-50(2009). CC -!- FUNCTION: Variant histone H2A which replaces conventional H2A in a CC subset of nucleosomes where it represses transcription CC (PubMed:12718888, PubMed:15621527, PubMed:16428466). Nucleosomes wrap CC and compact DNA into chromatin, limiting DNA accessibility to the CC cellular machineries which require DNA as a template (PubMed:15897469). CC Histones thereby play a central role in transcription regulation, DNA CC repair, DNA replication and chromosomal stability (PubMed:15897469). CC DNA accessibility is regulated via a complex set of post-translational CC modifications of histones, also called histone code, and nucleosome CC remodeling. Involved in stable X chromosome inactivation CC (PubMed:15897469). Inhibits the binding of transcription factors, CC including NF-kappa-B, and interferes with the activity of remodeling CC SWI/SNF complexes (PubMed:12718888, PubMed:16428466). Inhibits histone CC acetylation by EP300 and recruits class I HDACs, which induces a CC hypoacetylated state of chromatin (PubMed:16107708, PubMed:16428466). CC {ECO:0000269|PubMed:12718888, ECO:0000269|PubMed:15621527, CC ECO:0000269|PubMed:15897469, ECO:0000269|PubMed:16107708, CC ECO:0000269|PubMed:16428466}. CC -!- FUNCTION: [Isoform 1]: Isoform that specifically binds poly-ADP-ribose CC and O-acetyl-ADP-ribose and plays a key role in NAD(+) metabolism CC (PubMed:15902274). Able to bind to the ends of poly-ADP-ribose chains CC created by PARP1 and cap them (By similarity). This prevents PARP1 from CC further addition of ADP-ribose and thus limits the consumption of CC nuclear NAD(+), allowing the cell to maintain proper NAD(+) levels in CC both the nucleus and the mitochondria to promote proper mitochondrial CC respiration (By similarity). Increases the expression of genes involved CC in redox metabolism, including SOD3 (PubMed:23022728). CC {ECO:0000250|UniProtKB:Q9QZQ8, ECO:0000269|PubMed:15902274, CC ECO:0000269|PubMed:23022728}. CC -!- FUNCTION: [Isoform 2]: In contrast to isoform 1, does not bind poly- CC ADP-ribose (PubMed:15902274). Represses SOD3 gene expression CC (PubMed:23022728). {ECO:0000269|PubMed:15902274, CC ECO:0000269|PubMed:23022728}. CC -!- SUBUNIT: The nucleosome is a histone octamer containing two molecules CC each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and CC two H2A-H2B heterodimers. Interacts with HDAC1 and HDAC2 CC (PubMed:16107708). Interacts with SPOP (PubMed:15897469, CC PubMed:19818708). Part of a complex consisting of MACROH2A1, CUL3 and CC SPOP (PubMed:15897469, PubMed:19818708). {ECO:0000269|PubMed:15897469, CC ECO:0000269|PubMed:16107708, ECO:0000269|PubMed:19818708}. CC -!- SUBUNIT: [Isoform 1]: Interacts with PARP1. CC {ECO:0000250|UniProtKB:Q9QZQ8}. CC -!- INTERACTION: CC O75367; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-2868511, EBI-3867333; CC O75367; P04626: ERBB2; NbExp=6; IntAct=EBI-2868511, EBI-641062; CC O75367; A1L162: ERICH2; NbExp=6; IntAct=EBI-2868511, EBI-2682520; CC O75367; Q8N9E0: FAM133A; NbExp=3; IntAct=EBI-2868511, EBI-10268158; CC O75367; U3KQK0: H2BC15; NbExp=6; IntAct=EBI-2868511, EBI-12142839; CC O75367; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-2868511, EBI-10171774; CC O75367; P61244: MAX; NbExp=2; IntAct=EBI-2868511, EBI-751711; CC O75367; Q6ZUT1: NKAPD1; NbExp=3; IntAct=EBI-2868511, EBI-3920396; CC O75367; Q8N9Q2: SREK1IP1; NbExp=3; IntAct=EBI-2868511, EBI-10268630; CC O75367; Q12933: TRAF2; NbExp=3; IntAct=EBI-2868511, EBI-355744; CC O75367; Q12899: TRIM26; NbExp=3; IntAct=EBI-2868511, EBI-2341136; CC O75367; Q3SXR9: VCX2; NbExp=3; IntAct=EBI-2868511, EBI-11983741; CC O75367; Q969S3: ZNF622; NbExp=3; IntAct=EBI-2868511, EBI-2687480; CC O75367-2; P46100: ATRX; NbExp=2; IntAct=EBI-6249599, EBI-396461; CC O75367-2; O95271: TNKS; NbExp=6; IntAct=EBI-6249599, EBI-1105254; CC O75367-3; P04626: ERBB2; NbExp=3; IntAct=EBI-6250866, EBI-641062; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15621527, CC ECO:0000269|PubMed:15897469, ECO:0000269|PubMed:9634239}. Chromosome CC {ECO:0000269|PubMed:15621527, ECO:0000269|PubMed:15897469, CC ECO:0000269|PubMed:21211722, ECO:0000269|PubMed:29905837, CC ECO:0000269|PubMed:9634239}. Note=Enriched in inactive X chromosome CC chromatin and in senescence-associated heterochromatin CC (PubMed:15621527, PubMed:15897469, PubMed:9634239). Recruited to DNA CC damage sites in an APLF-dependent manner (PubMed:21211722, CC PubMed:29905837). {ECO:0000269|PubMed:15621527, CC ECO:0000269|PubMed:15897469, ECO:0000269|PubMed:21211722, CC ECO:0000269|PubMed:29905837, ECO:0000269|PubMed:9634239}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=mH2A1.1 {ECO:0000303|PubMed:23022728}; CC IsoId=O75367-2; Sequence=Displayed; CC Name=2; Synonyms=mH2A1.2 {ECO:0000303|PubMed:23022728}; CC IsoId=O75367-1; Sequence=VSP_061610; CC Name=3; CC IsoId=O75367-3; Sequence=VSP_061609, VSP_061610; CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9714746}. CC -!- DOMAIN: [Isoform 1]: The macro domain specifically binds poly-ADP- CC ribose. {ECO:0000269|PubMed:15902274}. CC -!- PTM: Monoubiquitinated at either Lys-116 or Lys-117. May also be CC polyubiquitinated. Ubiquitination is mediated by the CUL3/SPOP E3 CC complex and does not promote proteasomal degradation. Instead, it is CC required for enrichment in inactive X chromosome chromatin. CC {ECO:0000269|PubMed:15897469, ECO:0000269|PubMed:16129414, CC ECO:0000269|PubMed:19818708}. CC -!- MISCELLANEOUS: [Isoform 2]: The preferential expression of isoform 2 CC over that of isoform 1 requires the presence of DDX5/DDX17. CC {ECO:0000269|PubMed:23022728}. CC -!- MISCELLANEOUS: [Isoform 1]: Preferentially expressed over isoform 2 in CC the absence of DDX5/DDX17. {ECO:0000269|PubMed:23022728}. CC -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}. CC -!- CAUTION: [Isoform 1]: In contrast to other Macro-domain containing CC proteins, lacks ADP-ribose glycohydrolase activity. CC {ECO:0000269|PubMed:23474714}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF041483; AAC33433.1; -; mRNA. DR EMBL; AF044286; AAC33434.1; -; mRNA. DR EMBL; AF054174; AAC39908.1; -; mRNA. DR EMBL; AK023409; BAB14565.1; -; mRNA. DR EMBL; AC026691; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC013331; AAH13331.1; -; mRNA. DR EMBL; BC095406; AAH95406.1; -; mRNA. DR EMBL; AY134746; AAN08620.1; -; mRNA. DR CCDS; CCDS4183.1; -. [O75367-3] DR CCDS; CCDS4184.1; -. [O75367-2] DR CCDS; CCDS4185.1; -. [O75367-1] DR RefSeq; NP_001035248.1; NM_001040158.2. [O75367-3] DR RefSeq; NP_001387330.1; NM_001400401.1. [O75367-1] DR RefSeq; NP_001387331.1; NM_001400402.1. [O75367-1] DR RefSeq; NP_004884.1; NM_004893.3. [O75367-3] DR RefSeq; NP_613075.1; NM_138609.3. [O75367-2] DR RefSeq; NP_613258.2; NM_138610.3. [O75367-1] DR RefSeq; XP_011542032.1; XM_011543730.4. [O75367-3] DR RefSeq; XP_054209808.1; XM_054353833.1. [O75367-3] DR PDB; 1U35; X-ray; 3.00 A; C/G=1-120. DR PDB; 1ZR3; X-ray; 1.66 A; A/B/C/D=162-369. DR PDB; 1ZR5; X-ray; 2.92 A; A/B=161-369. DR PDB; 2F8N; X-ray; 2.90 A; G=1-120. DR PDB; 2FXK; X-ray; 2.54 A; A/B=162-369. DR PDB; 3HQH; X-ray; 2.30 A; M=167-181. DR PDB; 3HSV; X-ray; 1.43 A; M=171-186. DR PDB; 3IID; X-ray; 1.90 A; A=162-369. DR PDB; 3IIF; X-ray; 2.10 A; A/B/C=162-369. DR PDB; 3IVB; X-ray; 1.75 A; M=167-181. DR PDB; 5IIT; X-ray; 2.13 A; A/B/C/D=181-366. DR PDB; 5LNC; X-ray; 3.29 A; A/B=182-366. DR PDB; 7D3Y; X-ray; 3.11 A; A/B=181-369. DR PDB; 9PM0; EM; 2.90 A; A/E=1-161. DR AlphaFoldDB; O75367; -. DR EMDB; EMD-18699; -. DR EMDB; EMD-71726; -. DR MDRepo; O75367; -. DR SMR; O75367; -. DR BioGRID; 114927; 552. DR CORUM; O75367; -. DR DIP; DIP-44283N; -. DR ELM; O75367; -. DR FunCoup; O75367; 2183. DR IntAct; O75367; 183. DR NDEx; IQUERY-CP-MACROH2A1; 1 NDEx IQuery Curated Pathway. DR STRING; 9606.ENSP00000423563; -. DR GlyCosmos; O75367; 1 site, 2 glycans. DR GlyGen; O75367; 1 site, 2 O-linked glycans (1 site). DR iPTMnet; O75367; -. DR PhosphoSitePlus; O75367; -. DR SwissPalm; O75367; -. DR BioMuta; H2AFY; -. DR CPTAC; CPTAC-383; -. DR CPTAC; CPTAC-384; -. DR jPOST; O75367; -. DR MassIVE; O75367; -. DR PaxDb; 9606-ENSP00000423563; -. DR PeptideAtlas; O75367; -. DR PRIDE; O75367; -. DR ProteomicsDB; 49934; -. [O75367-1] DR ProteomicsDB; 49935; -. [O75367-2] DR ProteomicsDB; 49936; -. [O75367-3] DR Pumba; O75367; -. DR TopDownProteomics; O75367-1; -. [O75367-1] DR TopDownProteomics; O75367-2; -. [O75367-2] DR Antibodypedia; 26391; 279 antibodies from 35 providers. DR DNASU; 9555; -. DR Ensembl; ENST00000304332.8; ENSP00000302572.4; ENSG00000113648.18. [O75367-3] DR Ensembl; ENST00000312469.8; ENSP00000310169.4; ENSG00000113648.18. [O75367-2] DR Ensembl; ENST00000510038.1; ENSP00000424971.1; ENSG00000113648.18. [O75367-1] DR Ensembl; ENST00000511689.6; ENSP00000423563.1; ENSG00000113648.18. [O75367-1] DR Ensembl; ENST00000877621.1; ENSP00000547680.1; ENSG00000113648.18. [O75367-3] DR Ensembl; ENST00000877622.1; ENSP00000547681.1; ENSG00000113648.18. [O75367-1] DR Ensembl; ENST00000877623.1; ENSP00000547682.1; ENSG00000113648.18. [O75367-1] DR Ensembl; ENST00000877624.1; ENSP00000547683.1; ENSG00000113648.18. [O75367-3] DR Ensembl; ENST00000877627.1; ENSP00000547686.1; ENSG00000113648.18. [O75367-2] DR Ensembl; ENST00000923034.1; ENSP00000593093.1; ENSG00000113648.18. [O75367-3] DR Ensembl; ENST00000923035.1; ENSP00000593094.1; ENSG00000113648.18. [O75367-3] DR Ensembl; ENST00000923036.1; ENSP00000593095.1; ENSG00000113648.18. [O75367-1] DR Ensembl; ENST00000953738.1; ENSP00000623797.1; ENSG00000113648.18. [O75367-3] DR Ensembl; ENST00000953740.1; ENSP00000623799.1; ENSG00000113648.18. [O75367-1] DR Ensembl; ENST00000953743.1; ENSP00000623802.1; ENSG00000113648.18. [O75367-2] DR Ensembl; ENST00000953746.1; ENSP00000623805.1; ENSG00000113648.18. [O75367-1] DR GeneID; 9555; -. DR KEGG; hsa:9555; -. DR MANE-Select; ENST00000511689.6; ENSP00000423563.1; NM_138610.3; NP_613258.2. [O75367-1] DR UCSC; uc003lam.2; human. [O75367-2] DR AGR; HGNC:4740; -. DR CTD; 9555; -. DR DisGeNET; 9555; -. DR GeneCards; MACROH2A1; -. DR HGNC; HGNC:4740; MACROH2A1. DR HPA; ENSG00000113648; Low tissue specificity. DR MalaCards; MACROH2A1; -. DR MIM; 610054; gene. DR OpenTargets; ENSG00000113648; -. DR Orphanet; 1275; Brachydactyly-elbow wrist dysplasia syndrome. DR VEuPathDB; HostDB:ENSG00000113648; -. DR eggNOG; KOG1756; Eukaryota. DR eggNOG; KOG2633; Eukaryota. DR GeneTree; ENSGT00940000159541; -. DR HOGENOM; CLU_062828_0_0_1; -. DR InParanoid; O75367; -. DR OrthoDB; 9421954at2759; -. DR PAN-GO; O75367; 6 GO annotations based on evolutionary models. DR PhylomeDB; O75367; -. DR PathwayCommons; O75367; -. DR SignaLink; O75367; -. DR SIGNOR; O75367; -. DR Agora; ENSG00000113648; -. DR BioGRID-ORCS; 9555; 7 hits in 1153 CRISPR screens. DR CD-CODE; 232F8A39; P-body. DR CD-CODE; 8C2F96ED; Centrosome. DR CD-CODE; 91857CE7; Nucleolus. DR ChiTaRS; H2AFY; human. DR EvolutionaryTrace; O75367; -. DR GeneWiki; H2AFY; -. DR GenomeRNAi; 9555; -. DR Pharos; O75367; Tbio. DR PRO; PR:O75367; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; O75367; protein. DR Bgee; ENSG00000113648; Expressed in epithelium of nasopharynx and 211 other cell types or tissues. DR ExpressionAtlas; O75367; baseline and differential. DR GO; GO:0001740; C:Barr body; IDA:UniProtKB. DR GO; GO:0000785; C:chromatin; IDA:UniProtKB. DR GO; GO:0005694; C:chromosome; EXP:UniProtKB. DR GO; GO:0000781; C:chromosome, telomeric region; HDA:BHF-UCL. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0000228; C:nuclear chromosome; IDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0000786; C:nucleosome; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; EXP:UniProtKB. DR GO; GO:0005721; C:pericentric heterochromatin; IDA:BHF-UCL. DR GO; GO:0001739; C:sex chromatin; TAS:BHF-UCL. DR GO; GO:0090734; C:site of DNA damage; IDA:UniProt. DR GO; GO:0072570; F:ADP-D-ribose binding; IDA:UniProtKB. DR GO; GO:0160002; F:ADP-D-ribose modification-dependent protein binding; ISS:UniProtKB. DR GO; GO:0031490; F:chromatin DNA binding; IDA:UniProtKB. DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB. DR GO; GO:0010385; F:double-stranded methylated DNA binding; IDA:UniProtKB. DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL. DR GO; GO:0031492; F:nucleosomal DNA binding; IDA:UniProtKB. DR GO; GO:0160004; F:poly-ADP-D-ribose modification-dependent protein binding; ISS:UniProt. DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB. DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro. DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB. DR GO; GO:0030291; F:protein serine/threonine kinase inhibitor activity; IMP:UniProtKB. DR GO; GO:0000182; F:rDNA binding; IDA:UniProtKB. DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:UniProtKB. DR GO; GO:0030527; F:structural constituent of chromatin; IDA:UniProt. DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB. DR GO; GO:0006281; P:DNA repair; IDA:UniProt. DR GO; GO:0009048; P:dosage compensation by inactivation of X chromosome; IDA:MGI. DR GO; GO:0040029; P:epigenetic regulation of gene expression; IMP:UniProtKB. DR GO; GO:0071169; P:establishment of protein localization to chromatin; IMP:UniProtKB. DR GO; GO:0031507; P:heterochromatin formation; IBA:GO_Central. DR GO; GO:1902750; P:negative regulation of cell cycle G2/M phase transition; IMP:UniProtKB. DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; IMP:UniProtKB. DR GO; GO:1904815; P:negative regulation of protein localization to chromosome, telomeric region; IDA:BHF-UCL. DR GO; GO:1902883; P:negative regulation of response to oxidative stress; IMP:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB. DR GO; GO:1901837; P:negative regulation of transcription of nucleolar large rRNA by RNA polymerase I; IMP:UniProtKB. DR GO; GO:0006334; P:nucleosome assembly; NAS:UniProtKB. DR GO; GO:1903226; P:positive regulation of endodermal cell differentiation; IMP:UniProtKB. DR GO; GO:0045618; P:positive regulation of keratinocyte differentiation; IMP:UniProtKB. DR GO; GO:0034184; P:positive regulation of maintenance of mitotic sister chromatid cohesion; IDA:BHF-UCL. DR GO; GO:1902884; P:positive regulation of response to oxidative stress; IMP:UniProtKB. DR GO; GO:0019216; P:regulation of lipid metabolic process; IMP:UniProtKB. DR GO; GO:1902688; P:regulation of NAD metabolic process; ISS:UniProtKB. DR GO; GO:0002082; P:regulation of oxidative phosphorylation; ISS:UniProt. DR GO; GO:1902882; P:regulation of response to oxidative stress; IMP:UniProtKB. DR GO; GO:0045815; P:transcription initiation-coupled chromatin remodeling; IMP:UniProtKB. DR CDD; cd00074; HFD_H2A; 1. DR CDD; cd02904; Macro_H2A-like; 1. DR FunFam; 1.10.20.10:FF:000013; Core histone macro-H2A; 1. DR FunFam; 3.40.220.10:FF:000002; Core histone macro-H2A; 1. DR Gene3D; 1.10.20.10; Histone, subunit A; 1. DR Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1. DR InterPro; IPR021171; Core_histone_macro-H2A. DR InterPro; IPR007125; H2A/H2B/H3. DR InterPro; IPR061508; HFD_H2A. DR InterPro; IPR009072; Histone-fold. DR InterPro; IPR002119; Histone_H2A. DR InterPro; IPR032454; Histone_H2A_C. DR InterPro; IPR002589; Macro_dom. DR InterPro; IPR043472; Macro_dom-like. DR InterPro; IPR035796; Macro_H2A. DR PANTHER; PTHR23430; HISTONE H2A; 1. DR Pfam; PF00125; Histone; 1. DR Pfam; PF16211; Histone_H2A_C; 1. DR Pfam; PF01661; Macro; 1. DR PIRSF; PIRSF037942; Core_histone_macro-H2A; 1. DR PRINTS; PR00620; HISTONEH2A. DR SMART; SM00506; A1pp; 1. DR SMART; SM00414; H2A; 1. DR SUPFAM; SSF47113; Histone-fold; 1. DR SUPFAM; SSF52949; Macro domain-like; 1. DR PROSITE; PS51154; MACRO; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Chromatin regulator; KW Chromosome; DNA-binding; Isopeptide bond; Methylation; Nucleosome core; KW Nucleus; Phosphoprotein; Proteomics identification; Reference proteome; KW Ubl conjugation. FT CHAIN 1..369 FT /note="Core histone macro-H2A.1" FT /id="PRO_0000055318" FT DOMAIN 2..117 FT /note="Histone H2A" FT DOMAIN 184..367 FT /note="Macro" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490" FT REGION 128..180 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 144..160 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 203 FT /ligand="a glycoprotein" FT /ligand_id="ChEBI:CHEBI:17089" FT /ligand_part="poly[(1''->2')-ADP-alpha-D-ribose] group" FT /ligand_part_id="ChEBI:CHEBI:157741" FT /evidence="ECO:0000250|UniProtKB:A0A0D2UG83" FT BINDING 204 FT /ligand="a glycoprotein" FT /ligand_id="ChEBI:CHEBI:17089" FT /ligand_part="poly[(1''->2')-ADP-alpha-D-ribose] group" FT /ligand_part_id="ChEBI:CHEBI:157741" FT /evidence="ECO:0000250|UniProtKB:A0A0D2UG83" FT BINDING 226 FT /ligand="a glycoprotein" FT /ligand_id="ChEBI:CHEBI:17089" FT /ligand_part="poly[(1''->2')-ADP-alpha-D-ribose] group" FT /ligand_part_id="ChEBI:CHEBI:157741" FT /evidence="ECO:0000250|UniProtKB:A0A0D2UG83" FT BINDING 275 FT /ligand="a glycoprotein" FT /ligand_id="ChEBI:CHEBI:17089" FT /ligand_part="poly[(1''->2')-ADP-alpha-D-ribose] group" FT /ligand_part_id="ChEBI:CHEBI:157741" FT /evidence="ECO:0000250|UniProtKB:A0A0D2UG83" FT BINDING 312 FT /ligand="a glycoprotein" FT /ligand_id="ChEBI:CHEBI:17089" FT /ligand_part="poly[(1''->2')-ADP-alpha-D-ribose] group" FT /ligand_part_id="ChEBI:CHEBI:157741" FT /evidence="ECO:0000250|UniProtKB:A0A0D2UG83" FT BINDING 313 FT /ligand="a glycoprotein" FT /ligand_id="ChEBI:CHEBI:17089" FT /ligand_part="poly[(1''->2')-ADP-alpha-D-ribose] group" FT /ligand_part_id="ChEBI:CHEBI:157741" FT /evidence="ECO:0000250|UniProtKB:A0A0D2UG83" FT BINDING 314 FT /ligand="a glycoprotein" FT /ligand_id="ChEBI:CHEBI:17089" FT /ligand_part="poly[(1''->2')-ADP-alpha-D-ribose] group" FT /ligand_part_id="ChEBI:CHEBI:157741" FT /evidence="ECO:0000250|UniProtKB:A0A0D2UG83" FT BINDING 316 FT /ligand="a glycoprotein" FT /ligand_id="ChEBI:CHEBI:17089" FT /ligand_part="poly[(1''->2')-ADP-alpha-D-ribose] group" FT /ligand_part_id="ChEBI:CHEBI:157741" FT /evidence="ECO:0000250|UniProtKB:A0A0D2UG83" FT MOD_RES 7 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P0C0S5" FT MOD_RES 9 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P0C0S5" FT MOD_RES 18 FT /note="N6-methyllysine" FT /evidence="ECO:0000269|PubMed:16210244" FT MOD_RES 116 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9QZQ8" FT MOD_RES 123 FT /note="N6,N6-dimethyllysine; alternate" FT /evidence="ECO:0000305|PubMed:16210244" FT MOD_RES 123 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9QZQ8" FT MOD_RES 129 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:16210244, FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17924679, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 170 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 173 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 178 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT CROSSLNK 116 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin); alternate" FT /evidence="ECO:0000269|PubMed:16129414" FT CROSSLNK 117 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000269|PubMed:16129414" FT CROSSLNK 123 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 167 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 189 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 320 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 160 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:12800201, FT ECO:0000303|PubMed:9653160" FT /id="VSP_061609" FT VAR_SEQ 198..226 FT /note="QVVQADIASIDSDAVVHPTNTDFYIGGEV -> NLIHSEISNLAGFEVEAII FT NPTNADIDLKDDL (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:12800201, FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:9653160, ECO:0000303|PubMed:9714746" FT /id="VSP_061610" FT CONFLICT 186 FT /note="L -> F (in Ref. 3; BAB14565)" FT /evidence="ECO:0000305" FT CONFLICT 288 FT /note="E -> G (in Ref. 5; AAH95406)" FT /evidence="ECO:0000305" FT HELIX 15..19 FT /evidence="ECO:0007829|PDB:2F8N" FT HELIX 25..35 FT /evidence="ECO:0007829|PDB:2F8N" FT STRAND 36..38 FT /evidence="ECO:0007829|PDB:2F8N" FT STRAND 39..41 FT /evidence="ECO:0007829|PDB:1U35" FT HELIX 44..70 FT /evidence="ECO:0007829|PDB:2F8N" FT STRAND 74..76 FT /evidence="ECO:0007829|PDB:2F8N" FT HELIX 78..86 FT /evidence="ECO:0007829|PDB:2F8N" FT HELIX 89..94 FT /evidence="ECO:0007829|PDB:2F8N" FT TURN 95..97 FT /evidence="ECO:0007829|PDB:2F8N" FT STRAND 98..100 FT /evidence="ECO:0007829|PDB:2F8N" FT HELIX 111..113 FT /evidence="ECO:0007829|PDB:2F8N" FT STRAND 174..177 FT /evidence="ECO:0007829|PDB:3IVB" FT STRAND 185..190 FT /evidence="ECO:0007829|PDB:1ZR3" FT STRAND 196..202 FT /evidence="ECO:0007829|PDB:1ZR3" FT HELIX 204..206 FT /evidence="ECO:0007829|PDB:1ZR3" FT STRAND 210..216 FT /evidence="ECO:0007829|PDB:1ZR3" FT HELIX 224..249 FT /evidence="ECO:0007829|PDB:1ZR3" FT STRAND 257..261 FT /evidence="ECO:0007829|PDB:1ZR3" FT STRAND 265..274 FT /evidence="ECO:0007829|PDB:1ZR3" FT HELIX 283..300 FT /evidence="ECO:0007829|PDB:1ZR3" FT STRAND 304..308 FT /evidence="ECO:0007829|PDB:1ZR3" FT STRAND 312..316 FT /evidence="ECO:0007829|PDB:2FXK" FT HELIX 320..337 FT /evidence="ECO:0007829|PDB:1ZR3" FT STRAND 338..340 FT /evidence="ECO:0007829|PDB:1ZR5" FT STRAND 345..352 FT /evidence="ECO:0007829|PDB:1ZR3" FT HELIX 353..364 FT /evidence="ECO:0007829|PDB:1ZR3" SQ SEQUENCE 369 AA; 39184 MW; D21A4CE6C7AA3BB1 CRC64; MSSRGGKKKS TKTSRSAKAG VIFPVGRMLR YIKKGHPKYR IGVGAPVYMA AVLEYLTAEI LELAGNAARD NKKGRVTPRH ILLAVANDEE LNQLLKGVTI ASGGVLPNIH PELLAKKRGS KGKLEAIITP PPAKKAKSPS QKKPVSKKAG GKKGARKSKK KQGEVSKAAS ADSTTEGTPA DGFTVLSTKS LFLGQKLQVV QADIASIDSD AVVHPTNTDF YIGGEVGNTL EKKGGKEFVE AVLELRKKNG PLEVAGAAVS AGHGLPAKFV IHCNSPVWGA DKCEELLEKT VKNCLALADD KKLKSIAFPS IGSGRNGFPK QTAAQLILKA ISSYFVSTMS SSIKTVYFVL FDSESIGIYV QEMAKLDAN //