ID H2AY_MOUSE Reviewed; 369 AA. AC Q9QZQ8; Q91VZ2; Q9QZQ7; DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 12-OCT-2022, sequence version 4. DT 24-JAN-2024, entry version 181. DE RecName: Full=Core histone macro-H2A.1; DE Short=Histone macroH2A1; DE Short=mH2A1; DE AltName: Full=H2A.y; DE AltName: Full=H2A/y; GN Name=Macroh2a1 {ECO:0000312|MGI:MGI:1349392}; GN Synonyms=H2afy {ECO:0000312|MGI:MGI:1349392}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF RP 197-229 (ISOFORM 1), AND TISSUE SPECIFICITY. RC STRAIN=129/SvEvTacfBr; RX PubMed=10471737; DOI=10.1093/nar/27.18.3685; RA Rasmussen T.P., Huang T., Mastrangelo M.-A., Loring J., Panning B., RA Jaenisch R.; RT "Messenger RNAs encoding mouse histone macroH2A1 isoforms are expressed at RT similar levels in male and female cells and result from alternative RT splicing."; RL Nucleic Acids Res. 27:3685-3689(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INTERACTION WITH SPOP. RC TISSUE=Brain; RX PubMed=12183056; DOI=10.1016/s0167-4889(02)00249-5; RA Takahashi I., Kameoka Y., Hashimoto K.; RT "MacroH2A1.2 binds the nuclear protein Spop."; RL Biochim. Biophys. Acta 1591:63-68(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=FVB/N; TISSUE=Mammary gland; 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 [4] 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 [5] RP TISSUE SPECIFICITY. RX PubMed=11262398; DOI=10.1074/jbc.m010919200; RA Costanzi C., Pehrson J.R.; RT "MACROH2A2, a new member of the MACROH2A core histone family."; RL J. Biol. Chem. 276:21776-21784(2001). RN [6] RP SUBCELLULAR LOCATION. RX PubMed=15564378; DOI=10.1242/jcs.01537; RA Grigoryev S.A., Nikitina T., Pehrson J.R., Singh P.B., Woodcock C.L.; RT "Dynamic relocation of epigenetic chromatin markers reveals an active role RT of constitutive heterochromatin in the transition from proliferation to RT quiescence."; RL J. Cell Sci. 117:6153-6162(2004). RN [7] RP INTERACTION WITH HDAC1 AND HDAC2, AND 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). RN [9] 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=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, RC Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [10] 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 [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-116 AND LYS-123, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [12] RP FUNCTION (ISOFORM 1), INTERACTION WITH PARP1 (ISOFORM 1), DOMAIN (ISOFORM RP 1), AND MUTAGENESIS OF GLY-224. RX PubMed=28991266; DOI=10.1038/nsmb.3481; RA Posavec Marjanovic M., Hurtado-Bages S., Lassi M., Valero V., RA Malinverni R., Delage H., Navarro M., Corujo D., Guberovic I., Douet J., RA Gama-Perez P., Garcia-Roves P.M., Ahel I., Ladurner A.G., Yanes O., RA Bouvet P., Suelves M., Teperino R., Pospisilik J.A., Buschbeck M.; RT "MacroH2A1.1 regulates mitochondrial respiration by limiting nuclear NAD+ RT consumption."; RL Nat. Struct. Mol. Biol. 24:902-910(2017). RN [13] RP FUNCTION (ISOFORM 1), AND DOMAIN (ISOFORM 1). RX PubMed=34887560; DOI=10.1038/s41594-021-00692-5; RA Guberovic I., Hurtado-Bages S., Rivera-Casas C., Knobloch G., RA Malinverni R., Valero V., Leger M.M., Garcia J., Basquin J., RA Gomez de Cedron M., Frigole-Vivas M., Cheema M.S., Perez A., Ausio J., RA Ramirez de Molina A., Salvatella X., Ruiz-Trillo I., Eirin-Lopez J.M., RA Ladurner A.G., Buschbeck M.; RT "Evolution of a histone variant involved in compartmental regulation of NAD RT metabolism."; RL Nat. Struct. Mol. Biol. 28:1009-1019(2021). CC -!- FUNCTION: Variant histone H2A which replaces conventional H2A in a CC subset of nucleosomes where it represses transcription (By similarity). CC Nucleosomes wrap and compact DNA into chromatin, limiting DNA CC accessibility to the cellular machineries which require DNA as a CC template (By similarity). Histones thereby play a central role in CC transcription regulation, DNA repair, DNA replication and chromosomal CC stability (By similarity). DNA accessibility is regulated via a complex CC set of post-translational modifications of histones, also called CC histone code, and nucleosome remodeling (By similarity). Involved in CC stable X chromosome inactivation (By similarity). Inhibits the binding CC of transcription factors, including NF-kappa-B, and interferes with the CC activity of remodeling SWI/SNF complexes (By similarity). Inhibits CC histone acetylation by EP300 and recruits class I HDACs, which induces CC a hypoacetylated state of chromatin (PubMed:16107708). CC {ECO:0000250|UniProtKB:O75367, ECO:0000269|PubMed:16107708}. 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:28991266, PubMed:34887560). Able to bind to the ends of poly- CC ADP-ribose chains created by PARP1 and cap them (PubMed:28991266). This CC prevents PARP1 from further addition of ADP-ribose and thus limits the CC consumption of nuclear NAD(+), allowing the cell to maintain proper CC NAD(+) levels in both the nucleus and the mitochondria to promote CC proper mitochondrial respiration (PubMed:28991266). Increases the CC expression of genes involved in redox metabolism, including SOD3 CC (PubMed:23022728). {ECO:0000269|PubMed:23022728, CC ECO:0000269|PubMed:28991266, ECO:0000269|PubMed:34887560}. CC -!- FUNCTION: [Isoform 2]: In contrast to isoform 1, does not bind poly- CC ADP-ribose (By similarity). Represses SOD3 gene expression CC (PubMed:23022728). {ECO:0000250|UniProtKB:O75367, 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. Interacts CC with SPOP. Part of a complex consisting of MACROH2A1, CUL3 and SPOP. CC {ECO:0000250|UniProtKB:O75367}. CC -!- SUBUNIT: [Isoform 1]: Interacts with PARP1. CC {ECO:0000269|PubMed:28991266}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15564378, CC ECO:0000269|PubMed:9634239}. Chromosome {ECO:0000269|PubMed:15564378, CC ECO:0000269|PubMed:9634239}. Note=Enriched in inactive X chromosome CC chromatin and in senescence-associated heterochromatin CC (PubMed:9634239). In quiescent lymphocytes, associated with centromeric CC constitutive heterochromatin (PubMed:15564378). Recruited to DNA damage CC sites in an APLF-dependent manner (By similarity). CC {ECO:0000250|UniProtKB:O75367, ECO:0000269|PubMed:15564378, CC ECO:0000269|PubMed:9634239}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=mH2A1.1 {ECO:0000303|PubMed:23022728}, macroH2A1.1 CC {ECO:0000303|PubMed:28991266}; CC IsoId=Q9QZQ8-2; Sequence=Displayed; CC Name=2; Synonyms=mH2A1.2 {ECO:0000303|PubMed:23022728}, macroH2A1.2 CC {ECO:0000303|PubMed:28991266}; CC IsoId=Q9QZQ8-1; Sequence=VSP_061611; CC -!- TISSUE SPECIFICITY: Widely expressed, with high levels in testis. CC Present in liver, kidney and adrenal gland (at protein level). In the CC liver, present in hepatocytes and at a lesser extent in cells of the CC bile ducts. In the kidney, expressed in proximal and distal convoluted CC tubules and in straight proximal tubules. In the adrenal gland, present CC in inner cells of the cortex and medulla. {ECO:0000269|PubMed:10471737, CC ECO:0000269|PubMed:11262398}. CC -!- DOMAIN: [Isoform 1]: The macro domain specifically binds poly-ADP- CC ribose (PubMed:28991266, PubMed:34887560). Binds poly-ADP-ribose with CC lower affinity compared to premetazoan macroH2A1.1 ortholog CC (PubMed:34887560). {ECO:0000269|PubMed:28991266, CC ECO:0000269|PubMed:34887560}. 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:0000250|UniProtKB:O75367}. CC -!- MISCELLANEOUS: [Isoform 2]: Major form. The preferential expression of CC isoform 2 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 --------------------------------------------------------------------------- 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; AF171080; AAD53745.1; -; mRNA. DR EMBL; AF171081; AAD53746.1; -; mRNA. DR EMBL; AB071988; BAB68541.1; -; mRNA. DR EMBL; BC006955; AAH06955.1; -; mRNA. DR CCDS; CCDS26557.1; -. [Q9QZQ8-1] DR CCDS; CCDS49278.1; -. [Q9QZQ8-2] DR RefSeq; NP_001152985.1; NM_001159513.1. DR RefSeq; NP_001152986.1; NM_001159514.1. [Q9QZQ8-2] DR RefSeq; NP_001152987.1; NM_001159515.1. DR RefSeq; NP_036145.1; NM_012015.2. [Q9QZQ8-1] DR AlphaFoldDB; Q9QZQ8; -. DR SMR; Q9QZQ8; -. DR BioGRID; 205061; 14. DR IntAct; Q9QZQ8; 8. DR MINT; Q9QZQ8; -. DR STRING; 10090.ENSMUSP00000016081; -. DR GlyGen; Q9QZQ8; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9QZQ8; -. DR PhosphoSitePlus; Q9QZQ8; -. DR SwissPalm; Q9QZQ8; -. DR EPD; Q9QZQ8; -. DR jPOST; Q9QZQ8; -. DR MaxQB; Q9QZQ8; -. DR PaxDb; 10090-ENSMUSP00000016081; -. DR PeptideAtlas; Q9QZQ8; -. DR ProteomicsDB; 270915; -. [Q9QZQ8-1] DR ProteomicsDB; 270916; -. [Q9QZQ8-2] DR Pumba; Q9QZQ8; -. DR Antibodypedia; 26391; 258 antibodies from 31 providers. DR DNASU; 26914; -. DR Ensembl; ENSMUST00000016081.13; ENSMUSP00000016081.7; ENSMUSG00000015937.16. [Q9QZQ8-1] DR Ensembl; ENSMUST00000045788.9; ENSMUSP00000038221.8; ENSMUSG00000015937.16. [Q9QZQ8-2] DR GeneID; 26914; -. DR KEGG; mmu:26914; -. DR UCSC; uc007qsf.2; mouse. [Q9QZQ8-2] DR UCSC; uc007qsg.2; mouse. [Q9QZQ8-2] DR AGR; MGI:1349392; -. DR CTD; 9555; -. DR MGI; MGI:1349392; Macroh2a1. DR VEuPathDB; HostDB:ENSMUSG00000015937; -. DR eggNOG; KOG1756; Eukaryota. DR eggNOG; KOG2633; Eukaryota. DR GeneTree; ENSGT00940000159541; -. DR HOGENOM; CLU_062828_0_0_1; -. DR InParanoid; Q9QZQ8; -. DR OMA; GHNFPAK; -. DR OrthoDB; 235643at2759; -. DR PhylomeDB; Q9QZQ8; -. DR TreeFam; TF332276; -. DR BioGRID-ORCS; 26914; 1 hit in 81 CRISPR screens. DR ChiTaRS; H2afy; mouse. DR PRO; PR:Q9QZQ8; -. DR Proteomes; UP000000589; Chromosome 13. DR RNAct; Q9QZQ8; Protein. DR Bgee; ENSMUSG00000015937; Expressed in saccule of membranous labyrinth and 283 other cell types or tissues. DR GO; GO:0001740; C:Barr body; ISO:MGI. DR GO; GO:0005813; C:centrosome; TAS:MGI. DR GO; GO:0000785; C:chromatin; ISO:MGI. DR GO; GO:0000793; C:condensed chromosome; IDA:MGI. DR GO; GO:0000228; C:nuclear chromosome; ISO:MGI. DR GO; GO:0005730; C:nucleolus; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0000786; C:nucleosome; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005721; C:pericentric heterochromatin; ISO:MGI. DR GO; GO:0090734; C:site of DNA damage; ISO:MGI. DR GO; GO:0072570; F:ADP-D-ribose binding; IDA:UniProtKB. DR GO; GO:0160002; F:ADP-D-ribose modification-dependent protein binding; IDA:UniProtKB. DR GO; GO:0003682; F:chromatin binding; IDA:MGI. DR GO; GO:0031490; F:chromatin DNA binding; ISO:MGI. DR GO; GO:0003677; F:DNA binding; IBA:GO_Central. DR GO; GO:0010385; F:double-stranded methylated DNA binding; ISO:MGI. DR GO; GO:0019899; F:enzyme binding; ISO:MGI. DR GO; GO:0031492; F:nucleosomal DNA binding; IDA:UniProtKB. DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:UniProtKB. DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro. DR GO; GO:0019901; F:protein kinase binding; ISO:MGI. DR GO; GO:0030291; F:protein serine/threonine kinase inhibitor activity; ISO:MGI. DR GO; GO:0000182; F:rDNA binding; ISO:MGI. DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI. DR GO; GO:0030527; F:structural constituent of chromatin; ISO:MGI. DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI. DR GO; GO:0006281; P:DNA repair; ISO:MGI. DR GO; GO:0040029; P:epigenetic regulation of gene expression; ISO:MGI. DR GO; GO:0071169; P:establishment of protein localization to chromatin; ISO:MGI. DR GO; GO:1902750; P:negative regulation of cell cycle G2/M phase transition; ISO:MGI. DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; ISO:MGI. DR GO; GO:1904815; P:negative regulation of protein localization to chromosome, telomeric region; ISO:MGI. 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; IGI:MGI. 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; IEA:InterPro. DR GO; GO:1903226; P:positive regulation of endodermal cell differentiation; ISO:MGI. DR GO; GO:0045618; P:positive regulation of keratinocyte differentiation; ISO:MGI. DR GO; GO:0034184; P:positive regulation of maintenance of mitotic sister chromatid cohesion; ISO:MGI. DR GO; GO:1902884; P:positive regulation of response to oxidative stress; IMP:UniProtKB. DR GO; GO:0019216; P:regulation of lipid metabolic process; ISO:MGI. DR GO; GO:1902688; P:regulation of NAD metabolic process; IDA:UniProtKB. DR GO; GO:0002082; P:regulation of oxidative phosphorylation; IDA:UniProt. DR GO; GO:1902882; P:regulation of response to oxidative stress; IMP:UniProtKB. DR GO; GO:0007549; P:sex-chromosome dosage compensation; ISO:MGI. DR GO; GO:0045815; P:transcription initiation-coupled chromatin remodeling; ISO:MGI. DR CDD; cd00074; H2A; 1. DR CDD; cd02904; Macro_H2A-like; 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; IPR009072; Histone-fold. DR InterPro; IPR002119; Histone_H2A. DR InterPro; IPR007125; Histone_H2A/H2B/H3. 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:SF20; CORE HISTONE MACRO-H2A.1; 1. 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. DR Genevisible; Q9QZQ8; MM. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Chromatin regulator; Chromosome; KW DNA-binding; Isopeptide bond; Methylation; Nucleosome core; Nucleus; KW Phosphoprotein; Reference proteome; Ubl conjugation. FT CHAIN 1..369 FT /note="Core histone macro-H2A.1" FT /id="PRO_0000227904" 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 140..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:0000250|UniProtKB:O75367" FT MOD_RES 116 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 123 FT /note="N6,N6-dimethyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:O75367" FT MOD_RES 123 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 129 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19144319, FT ECO:0007744|PubMed:21183079" FT MOD_RES 170 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 173 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 178 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT CROSSLNK 116 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin); alternate" FT /evidence="ECO:0000250|UniProtKB:O75367" FT CROSSLNK 117 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:O75367" FT CROSSLNK 123 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:O75367" FT CROSSLNK 167 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:O75367" FT CROSSLNK 189 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:O75367" FT CROSSLNK 320 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:O75367" FT VAR_SEQ 198..226 FT /note="QVVQADIASIDSDAVVHPTNTDFYTGGEV -> NLIHSEISNLAGFEVEAII FT NPTNADIDLKDDL (in isoform 2)" FT /id="VSP_061611" FT MUTAGEN 224 FT /note="G->E: Abolished ability to bind poly-ADP-ribose and FT inhibit PARP1." FT /evidence="ECO:0000269|PubMed:28991266" SQ SEQUENCE 369 AA; 39290 MW; 33F123DE5C9C46EC CRC64; MSSRGGKKKS TKTSRSAKAG VIFPVGRMLR YIKKGHPKYR IGVGAPVYMA AVLEYLTAEI LELAGNAARD NKKGRVTPRH ILLAVANDEE LNQLLKGVTI ASGGVLPNIH PELLAKKRGS KGKLEAIITP PPAKKAKSPS QKKPVAKKTG GKKGARKSKK KQGEVSKAAS ADSTTEGTPT DGFTVLSTKS LFLGQKLQVV QADIASIDSD AVVHPTNTDF YTGGEVGNTL EKKGGKEFVE AVLELRKKNG PLEVAGAAIS AGHGLPAKFV IHCNSPVWGA DKCEELLEKT VKNCLALADD RKLKSIAFPS IGSGRNGFPK QTAAQLILKA ISSYFVSTMS SSIKTVYFML FDSESIGIYV QEMAKLDAN //