ID YETS2_HUMAN Reviewed; 1422 AA. AC Q9ULM3; A7E2B9; D3DNS9; Q641P6; Q9NW96; DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 10-JAN-2006, sequence version 2. DT 27-MAR-2024, entry version 166. DE RecName: Full=YEATS domain-containing protein 2 {ECO:0000305}; GN Name=YEATS2 {ECO:0000312|HGNC:HGNC:25489}; GN Synonyms=KIAA1197 {ECO:0000303|PubMed:10574462}; 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 [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=10574462; DOI=10.1093/dnares/6.5.337; RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XV. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 6:337-345(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=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 [5] RP FUNCTION, AND IDENTIFICATION IN ATAC COMPLEX. RX PubMed=18838386; DOI=10.1074/jbc.m806936200; RA Wang Y.L., Faiola F., Xu M., Pan S., Martinez E.; RT "Human ATAC Is a GCN5/PCAF-containing acetylase complex with a novel NC2- RT like histone fold module that interacts with the TATA-binding protein."; RL J. Biol. Chem. 283:33808-33815(2008). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, AND IDENTIFICATION BY RP 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 [7] 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 [8] RP FUNCTION, AND IDENTIFICATION IN ATAC COMPLEX. RX PubMed=19103755; DOI=10.1128/mcb.01599-08; RA Guelman S., Kozuka K., Mao Y., Pham V., Solloway M.J., Wang J., Wu J., RA Lill J.R., Zha J.; RT "The double-histone-acetyltransferase complex ATAC is essential for RT mammalian development."; RL Mol. Cell. Biol. 29:1176-1188(2009). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-536, AND IDENTIFICATION BY RP 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-447; SER-463; SER-465; RP SER-471; SER-473; SER-575 AND SER-627, AND IDENTIFICATION BY MASS RP 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-447 AND SER-536, 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; THR-407; SER-447; RP SER-465; SER-473; SER-536; SER-575; SER-627 AND THR-1219, AND RP 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-478, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [14] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1110, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [15] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-592 AND LYS-1110, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033; RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., RA Vertegaal A.C.; RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."; RL Cell Rep. 10:1778-1791(2015). RN [16] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-9; LYS-113; LYS-189; LYS-370; RP LYS-487; LYS-552; LYS-592; LYS-649; LYS-773; LYS-923; LYS-1110; LYS-1130; RP LYS-1222 AND LYS-1285, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [17] RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 201-332 IN COMPLEX WITH H3K27CR RP PEPTIDE, FUNCTION, DOMAIN, AND MUTAGENESIS OF HIS-259; SER-261; TYR-262; RP TRP-282; GLU-284; PHE-285 AND TYR-313. RX PubMed=27103431; DOI=10.1038/cr.2016.49; RA Zhao D., Guan H., Zhao S., Mi W., Wen H., Li Y., Zhao Y., Allis C.D., RA Shi X., Li H.; RT "YEATS2 is a selective histone crotonylation reader."; RL Cell Res. 26:629-632(2016). RN [18] RP INVOLVEMENT IN FAME4. RX PubMed=22713812; DOI=10.1038/ejhg.2012.133; RA Yeetong P., Ausavarat S., Bhidayasiri R., Piravej K., Pasutharnchat N., RA Desudchit T., Chunharas C., Loplumlert J., Limotai C., Suphapeetiporn K., RA Shotelersuk V.; RT "A newly identified locus for benign adult familial myoclonic epilepsy on RT chromosome 3q26.32-3q28."; RL Eur. J. Hum. Genet. 21:225-228(2013). RN [19] RP INVOLVEMENT IN FAME4. RX PubMed=31539032; DOI=10.1093/brain/awz267; RA Yeetong P., Pongpanich M., Srichomthong C., Assawapitaksakul A., RA Shotelersuk V., Tantirukdham N., Chunharas C., Suphapeetiporn K., RA Shotelersuk V.; RT "TTTCA repeat insertions in an intron of YEATS2 in benign adult familial RT myoclonic epilepsy type 4."; RL Brain 142:3360-3366(2019). CC -!- FUNCTION: Chromatin reader component of the ATAC complex, a complex CC with histone acetyltransferase activity on histones H3 and H4 CC (PubMed:18838386, PubMed:19103755, PubMed:27103431). YEATS2 CC specifically recognizes and binds histone H3 crotonylated at 'Lys-27' CC (H3K27cr) (PubMed:27103431). Crotonylation marks active promoters and CC enhancers and confers resistance to transcriptional repressors CC (PubMed:27103431). {ECO:0000269|PubMed:18838386, CC ECO:0000269|PubMed:19103755, ECO:0000269|PubMed:27103431}. CC -!- SUBUNIT: Component of the ADA2A-containing complex (ATAC), composed of CC KAT14, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, SGF29 and DR1. CC {ECO:0000269|PubMed:18838386, ECO:0000269|PubMed:19103755}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:18838386, CC ECO:0000305|PubMed:19103755}. CC -!- DOMAIN: The YEATS domain specifically recognizes and binds crotonylated CC histones. {ECO:0000269|PubMed:27103431}. CC -!- DISEASE: Epilepsy, familial adult myoclonic, 4 (FAME4) [MIM:615127]: A CC form of familial myoclonic epilepsy, a neurologic disorder CC characterized by cortical hand tremors, myoclonic jerks and occasional CC generalized or focal seizures with a non-progressive or very slowly CC progressive disease course. Usually, myoclonic tremor is the presenting CC symptom, characterized by tremulous finger movements and myoclonic CC jerks of the limbs increased by action and posture. In a minority of CC patients, seizures are the presenting symptom. Some patients exhibit CC mild cognitive impairment. FAME4 inheritance is autosomal dominant. CC {ECO:0000269|PubMed:22713812, ECO:0000269|PubMed:31539032}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SEQUENCE CAUTION: CC Sequence=BAA86511.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; AB033023; BAA86511.1; ALT_INIT; mRNA. DR EMBL; AC068769; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC131160; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471052; EAW78316.1; -; Genomic_DNA. DR EMBL; CH471052; EAW78317.1; -; Genomic_DNA. DR EMBL; BC082270; AAH82270.1; -; mRNA. DR EMBL; BC150273; AAI50274.1; -; mRNA. DR CCDS; CCDS43175.1; -. DR RefSeq; NP_060493.3; NM_018023.4. DR RefSeq; XP_016862298.1; XM_017006809.1. DR RefSeq; XP_016862299.1; XM_017006810.1. DR PDB; 5IQL; X-ray; 2.10 A; A=201-332. DR PDB; 5XNV; X-ray; 2.70 A; A=201-332. DR PDB; 6LSD; X-ray; 2.05 A; A/B=201-332. DR PDB; 7EIE; X-ray; 1.67 A; A/B=202-329. DR PDBsum; 5IQL; -. DR PDBsum; 5XNV; -. DR PDBsum; 6LSD; -. DR PDBsum; 7EIE; -. DR AlphaFoldDB; Q9ULM3; -. DR SMR; Q9ULM3; -. DR BioGRID; 120815; 164. DR ComplexPortal; CPX-1004; PCAF-containing ATAC complex. DR ComplexPortal; CPX-997; GCN5-containing ATAC complex. DR CORUM; Q9ULM3; -. DR IntAct; Q9ULM3; 42. DR MINT; Q9ULM3; -. DR STRING; 9606.ENSP00000306983; -. DR BindingDB; Q9ULM3; -. DR ChEMBL; CHEMBL4296261; -. DR GlyCosmos; Q9ULM3; 5 sites, 2 glycans. DR GlyGen; Q9ULM3; 34 sites, 2 O-linked glycans (34 sites). DR iPTMnet; Q9ULM3; -. DR PhosphoSitePlus; Q9ULM3; -. DR BioMuta; YEATS2; -. DR DMDM; 85542165; -. DR EPD; Q9ULM3; -. DR jPOST; Q9ULM3; -. DR MassIVE; Q9ULM3; -. DR MaxQB; Q9ULM3; -. DR PaxDb; 9606-ENSP00000306983; -. DR PeptideAtlas; Q9ULM3; -. DR ProteomicsDB; 85078; -. DR Pumba; Q9ULM3; -. DR Antibodypedia; 50874; 109 antibodies from 26 providers. DR DNASU; 55689; -. DR Ensembl; ENST00000305135.10; ENSP00000306983.5; ENSG00000163872.16. DR GeneID; 55689; -. DR KEGG; hsa:55689; -. DR MANE-Select; ENST00000305135.10; ENSP00000306983.5; NM_018023.5; NP_060493.3. DR UCSC; uc003fly.2; human. DR AGR; HGNC:25489; -. DR CTD; 55689; -. DR DisGeNET; 55689; -. DR GeneCards; YEATS2; -. DR HGNC; HGNC:25489; YEATS2. DR HPA; ENSG00000163872; Low tissue specificity. DR MalaCards; YEATS2; -. DR MIM; 613373; gene. DR MIM; 615127; phenotype. DR neXtProt; NX_Q9ULM3; -. DR OpenTargets; ENSG00000163872; -. DR Orphanet; 86814; Benign adult familial myoclonic epilepsy. DR PharmGKB; PA134922615; -. DR VEuPathDB; HostDB:ENSG00000163872; -. DR eggNOG; KOG3149; Eukaryota. DR GeneTree; ENSGT00940000156789; -. DR HOGENOM; CLU_258270_0_0_1; -. DR InParanoid; Q9ULM3; -. DR OMA; XVVDVEL; -. DR OrthoDB; 9679at2759; -. DR PhylomeDB; Q9ULM3; -. DR TreeFam; TF314586; -. DR PathwayCommons; Q9ULM3; -. DR Reactome; R-HSA-3214847; HATs acetylate histones. DR Reactome; R-HSA-9772755; Formation of WDR5-containing histone-modifying complexes. DR SignaLink; Q9ULM3; -. DR BioGRID-ORCS; 55689; 380 hits in 1177 CRISPR screens. DR ChiTaRS; YEATS2; human. DR GenomeRNAi; 55689; -. DR Pharos; Q9ULM3; Tbio. DR PRO; PR:Q9ULM3; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q9ULM3; Protein. DR Bgee; ENSG00000163872; Expressed in buccal mucosa cell and 197 other cell types or tissues. DR ExpressionAtlas; Q9ULM3; baseline and differential. DR GO; GO:0140672; C:ATAC complex; IDA:BHF-UCL. DR GO; GO:0072686; C:mitotic spindle; NAS:ComplexPortal. DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IBA:GO_Central. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0042393; F:histone binding; IDA:UniProtKB. DR GO; GO:0140566; F:histone reader activity; IDA:ARUK-UCL. DR GO; GO:0140030; F:modification-dependent protein binding; IDA:UniProtKB. DR GO; GO:0017025; F:TBP-class protein binding; IPI:BHF-UCL. DR GO; GO:0003714; F:transcription corepressor activity; IDA:BHF-UCL. DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL. DR GO; GO:0051726; P:regulation of cell cycle; IMP:ComplexPortal. DR GO; GO:0051302; P:regulation of cell division; IDA:ComplexPortal. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IMP:ComplexPortal. DR GO; GO:0045995; P:regulation of embryonic development; ISO:ComplexPortal. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal. DR GO; GO:0090043; P:regulation of tubulin deacetylation; IMP:ComplexPortal. DR CDD; cd16907; YEATS_YEATS2_like; 1. DR Gene3D; 2.60.40.1970; YEATS domain; 1. DR InterPro; IPR038704; YEAST_sf. DR InterPro; IPR005033; YEATS. DR PANTHER; PTHR23195; YEATS DOMAIN; 1. DR PANTHER; PTHR23195:SF7; YEATS DOMAIN-CONTAINING PROTEIN 2; 1. DR Pfam; PF03366; YEATS; 1. DR PROSITE; PS51037; YEATS; 1. DR Genevisible; Q9ULM3; HS. PE 1: Evidence at protein level; KW 3D-structure; Coiled coil; Epilepsy; Isopeptide bond; Nucleus; KW Phosphoprotein; Reference proteome; Ubl conjugation. FT CHAIN 1..1422 FT /note="YEATS domain-containing protein 2" FT /id="PRO_0000076366" FT DOMAIN 200..345 FT /note="YEATS" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00376" FT REGION 117..198 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 259..261 FT /note="Histone H3K27cr binding" FT /evidence="ECO:0000269|PubMed:27103431, FT ECO:0007744|PDB:5IQL" FT REGION 282..284 FT /note="Histone H3K27cr binding" FT /evidence="ECO:0000269|PubMed:27103431, FT ECO:0007744|PDB:5IQL" FT REGION 465..486 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 513..540 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 794..842 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 47..80 FT /evidence="ECO:0000255" FT COMPBIAS 117..152 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 153..169 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 182..198 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 828..842 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 118 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 120 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q3TUF7" FT MOD_RES 157 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 407 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 447 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 463 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 465 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 471 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 473 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 478 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 536 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 575 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 627 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1219 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 9 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 113 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 370 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 487 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 552 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 592 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25772364, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 649 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 773 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 923 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1110 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 1110 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25772364, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 1130 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1222 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1285 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VARIANT 184 FT /note="I -> V (in dbSNP:rs16858033)" FT /id="VAR_051494" FT VARIANT 530 FT /note="V -> I (in dbSNP:rs262993)" FT /id="VAR_051495" FT VARIANT 993 FT /note="Q -> H (in dbSNP:rs3211095)" FT /id="VAR_051496" FT MUTAGEN 259 FT /note="H->A: Strongly reduced binding to histone H3 FT crotonylated at 'Lys-27' (H3K27cr)." FT /evidence="ECO:0000269|PubMed:27103431" FT MUTAGEN 261 FT /note="S->A: Strongly reduced binding to histone H3 FT crotonylated at 'Lys-27' (H3K27cr)." FT /evidence="ECO:0000269|PubMed:27103431" FT MUTAGEN 262 FT /note="Y->A: Strongly reduced binding to histone H3 FT crotonylated at 'Lys-27' (H3K27cr)." FT /evidence="ECO:0000269|PubMed:27103431" FT MUTAGEN 282 FT /note="W->A: Strongly reduced binding to histone H3 FT crotonylated at 'Lys-27' (H3K27cr)." FT /evidence="ECO:0000269|PubMed:27103431" FT MUTAGEN 283 FT /note="G->A: Abolished binding to histone H3 crotonylated FT at 'Lys-27' (H3K27cr)." FT /evidence="ECO:0000269|PubMed:27103431" FT MUTAGEN 284 FT /note="E->A: Abolished binding to histone H3 crotonylated FT at 'Lys-27' (H3K27cr)." FT /evidence="ECO:0000269|PubMed:27103431" FT MUTAGEN 285 FT /note="F->A: Strongly reduced binding to histone H3 FT crotonylated at 'Lys-27' (H3K27cr)." FT /evidence="ECO:0000269|PubMed:27103431" FT MUTAGEN 313 FT /note="Y->A: Reduced binding to histone H3 crotonylated at FT 'Lys-27' (H3K27cr)." FT /evidence="ECO:0000269|PubMed:27103431" FT STRAND 208..218 FT /evidence="ECO:0007829|PDB:7EIE" FT HELIX 221..223 FT /evidence="ECO:0007829|PDB:7EIE" FT STRAND 232..239 FT /evidence="ECO:0007829|PDB:7EIE" FT TURN 248..250 FT /evidence="ECO:0007829|PDB:7EIE" FT STRAND 251..257 FT /evidence="ECO:0007829|PDB:7EIE" FT HELIX 260..262 FT /evidence="ECO:0007829|PDB:7EIE" FT STRAND 267..270 FT /evidence="ECO:0007829|PDB:7EIE" FT STRAND 272..283 FT /evidence="ECO:0007829|PDB:7EIE" FT STRAND 286..294 FT /evidence="ECO:0007829|PDB:7EIE" FT STRAND 300..306 FT /evidence="ECO:0007829|PDB:7EIE" FT STRAND 314..316 FT /evidence="ECO:0007829|PDB:7EIE" FT STRAND 318..327 FT /evidence="ECO:0007829|PDB:7EIE" SQ SEQUENCE 1422 AA; 150782 MW; 7800718C08B634B3 CRC64; MSGIKRTIKE TDPDYEDVSV ALPNKRHKAI ENSARDAAVQ KIETIIKEQF ALEMKNKEHE IEVIDQRLIE ARRMMDKLRA CIVANYYASA GLLKVSEGSK TCDTMVFNHP AIKKFLESPS RSSSPANQRA ETPSANHSES DSLSQHNDFL SDKDNNSNMD IEERLSNNME QRPSRNTGRD TSRITGSHKT EQRNADLTDE TSRLFVKKTI VVGNVSKYIP PDKREENDQS THKWMVYVRG SRREPSINHF VKKVWFFLHP SYKPNDLVEV REPPFHLTRR GWGEFPVRVQ VHFKDSQNKR IDIIHNLKLD RTYTGLQTLG AETVVDVELH RHSLGEDCIY PQSSESDISD APPSLPLTIP APVKASSPIK QSHEPVPDTS VEKGFPASTE AERHTPFYAL PSSLERTPTK MTTSQKVTFC SHGNSAFQPI ASSCKIVPQS QVPNPESPGK SFQPITMSCK IVSGSPISTP SPSPLPRTPT STPVHVKQGT AGSVINNPYV IMDKQPGQVI GATTPSTGSP TNKISTASQV SQGTGSPVPK IHGSSFVTST VKQEDSLFAS MPPLCPIGSH PKVQSPKPIT GGLGAFTKVI IKQEPGEAPH VPATGAASQS PLPQYVTVKG GHMIAVSPQK QVITPGEGIA QSAKVQPSKV VGVPVGSALP STVKQAVAIS GGQILVAKAS SSVSKAVGPK QVVTQGVAKA IVSGGGGTIV AQPVQTLTKA QVTAAGPQKS GSQGSVMATL QLPATNLANL ANLPPGTKLY LTTNSKNPSG KGKLLLIPQG AILRATNNAN LQSGSAASGG SGAGGGGGGG GGGGSGSGGG GSTGGGGGTA GGGTQSTAGP GGISQHLTYT SYILKQTPQG TFLVGQPSPQ TSGKQLTTGS VVQGTLGVST SSAQGQQTLK VISGQKTTLF TQAAHGGQAS LMKISDSTLK TVPATSQLSK PGTTMLRVAG GVITTATSPA VALSANGPAQ QSEGMAPVSS STVSSVTKTS GQQQVCVSQA TVGTCKAATP TVVSATSLVP TPNPISGKAT VSGLLKIHSS QSSPQQAVLT IPSQLKPLSV NTSGGVQTIL MPVNKVVQSF STSKPPAILP VAAPTPVVPS SAPAAVAKVK TEPETPGPSC LSQEGQTAVK TEESSELGNY VIKIDHLETI QQLLTAVVKK IPLITAKSED ASCFSAKSVE QYYGWNIGKR RAAEWQRAMT MRKVLQEILE KNPRFHHLTP LKTKHIAHWC RCHGYTPPDP ESLRNDGDSI EDVLTQIDSE PECPSSFSSA DNLCRKLEDL QQFQKREPEN EEEVDILSLS EPVKINIKKE QEEKQEEVKF YLPPTPGSEF IGDVTQKIGI TLQPVALHRN VYASVVEDMI LKATEQLVND ILRQALAVGY QTASHNRIPK EITVSNIHQA ICNIPFLDFL TNKHMGILNE DQ //