YETS2_HUMAN
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 03-AUG-2022, entry version 157.
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};
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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; 141.
DR ComplexPortal; CPX-1004; PCAF-containing ATAC complex.
DR ComplexPortal; CPX-997; GCN5-containing ATAC complex.
DR CORUM; Q9ULM3; -.
DR IntAct; Q9ULM3; 38.
DR MINT; Q9ULM3; -.
DR STRING; 9606.ENSP00000306983; -.
DR GlyGen; Q9ULM3; 5 sites, 2 O-linked glycans (5 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; Q9ULM3; -.
DR PeptideAtlas; Q9ULM3; -.
DR PRIDE; Q9ULM3; -.
DR ProteomicsDB; 85078; -.
DR Antibodypedia; 50874; 90 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 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; 1482359at2759; -.
DR PhylomeDB; Q9ULM3; -.
DR TreeFam; TF314586; -.
DR PathwayCommons; Q9ULM3; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR SignaLink; Q9ULM3; -.
DR BioGRID-ORCS; 55689; 368 hits in 1098 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 195 other tissues.
DR ExpressionAtlas; Q9ULM3; baseline and differential.
DR Genevisible; Q9ULM3; HS.
DR GO; GO:0140672; C:ATAC complex; IDA:BHF-UCL.
DR GO; GO:0072686; C:mitotic spindle; IC:ComplexPortal.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
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:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:BHF-UCL.
DR GO; GO:0044154; P:histone H3-K14 acetylation; IDA:ComplexPortal.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; 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:0045995; P:regulation of embryonic development; IC:ComplexPortal.
DR GO; GO:0031063; P:regulation of histone deacetylation; IMP:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:ComplexPortal.
DR GO; GO:0090043; P:regulation of tubulin deacetylation; IMP:ComplexPortal.
DR Gene3D; 2.60.40.1970; -; 1.
DR InterPro; IPR038704; YEAST_sf.
DR InterPro; IPR005033; YEATS.
DR PANTHER; PTHR23195; PTHR23195; 1.
DR Pfam; PF03366; YEATS; 1.
DR PROSITE; PS51037; YEATS; 1.
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 205..218
FT /evidence="ECO:0007829|PDB:6LSD"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:6LSD"
FT STRAND 232..240
FT /evidence="ECO:0007829|PDB:6LSD"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:6LSD"
FT STRAND 251..257
FT /evidence="ECO:0007829|PDB:6LSD"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:6LSD"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:6LSD"
FT STRAND 272..282
FT /evidence="ECO:0007829|PDB:6LSD"
FT STRAND 286..295
FT /evidence="ECO:0007829|PDB:6LSD"
FT STRAND 301..306
FT /evidence="ECO:0007829|PDB:6LSD"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:6LSD"
FT STRAND 318..330
FT /evidence="ECO:0007829|PDB:6LSD"
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
