YETS4_HUMAN
ID YETS4_HUMAN Reviewed; 227 AA.
AC O95619; Q9NQD0;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=YEATS domain-containing protein 4 {ECO:0000305};
DE AltName: Full=Glioma-amplified sequence 41 {ECO:0000303|PubMed:9302258};
DE Short=Gas41 {ECO:0000303|PubMed:9302258};
DE AltName: Full=NuMA-binding protein 1;
DE Short=NuBI-1;
DE Short=NuBI1;
GN Name=YEATS4 {ECO:0000312|HGNC:HGNC:24859};
GN Synonyms=GAS41 {ECO:0000303|PubMed:9302258};
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].
RX PubMed=9302258; DOI=10.1093/hmg/6.11.1817;
RA Fischer U., Heckel D., Michel A., Janka M., Hulsebos T., Meese E.;
RT "Cloning of a novel transcription factor-like gene amplified in human
RT glioma including astrocytoma grade I.";
RL Hum. Mol. Genet. 6:1817-1822(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INTERACTION WITH NUMA1,
RP AND TISSUE SPECIFICITY.
RX PubMed=10913114; DOI=10.1074/jbc.m000994200;
RA Harborth J., Weber K., Osborn M.;
RT "GAS41, a highly conserved protein in eukaryotic nuclei, binds to NuMA.";
RL J. Biol. Chem. 275:31979-31985(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 MRNA].
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 PROTEIN SEQUENCE OF 5-15; 18-32; 56-64; 120-131; 168-178 AND 217-227,
RP FUNCTION, IDENTIFICATION IN NUA4 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=12963728; DOI=10.1074/jbc.c300389200;
RA Cai Y., Jin J., Tomomori-Sato C., Sato S., Sorokina I., Parmely T.J.,
RA Conaway R.C., Conaway J.W.;
RT "Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-
RT containing histone acetyltransferase complex.";
RL J. Biol. Chem. 278:42733-42736(2003).
RN [6]
RP INTERACTION WITH TACC1.
RX PubMed=11903063; DOI=10.1042/0264-6021:3630195;
RA Lauffart B., Howell S.J., Tasch J.E., Cowell J.K., Still I.H.;
RT "Interaction of the transforming acidic coiled-coil 1 (TACC1) protein with
RT ch-TOG and GAS41/NuBI1 suggests multiple TACC1-containing protein complexes
RT in human cells.";
RL Biochem. J. 363:195-200(2002).
RN [7]
RP INTERACTION WITH MLLT10 AND SMARCB1.
RX PubMed=11756182; DOI=10.1182/blood.v99.1.275;
RA Debernardi S., Bassini A., Jones L.K., Chaplin T., Linder B.,
RA de Bruijn D.R.H., Meese E., Young B.D.;
RT "The MLL fusion partner AF10 binds GAS41, a protein that interacts with the
RT human SWI/SNF complex.";
RL Blood 99:275-281(2002).
RN [8]
RP INTERACTION WITH TACC2.
RX PubMed=12620397; DOI=10.1016/s0888-7543(02)00039-3;
RA Lauffart B., Gangisetty O., Still I.H.;
RT "Molecular cloning, genomic structure and interactions of the putative
RT breast tumor suppressor TACC2.";
RL Genomics 81:192-201(2003).
RN [9]
RP REVIEW ON NUA4 COMPLEX.
RX PubMed=15196461; DOI=10.1016/j.gde.2004.02.009;
RA Doyon Y., Cote J.;
RT "The highly conserved and multifunctional NuA4 HAT complex.";
RL Curr. Opin. Genet. Dev. 14:147-154(2004).
RN [10]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN NUA4
RP COMPLEX, AND IDENTIFICATION IN NUA4-RELATED SRCAP-CONTAINING COMPLEX.
RX PubMed=14966270; DOI=10.1128/mcb.24.5.1884-1896.2004;
RA Doyon Y., Selleck W., Lane W.S., Tan S., Cote J.;
RT "Structural and functional conservation of the NuA4 histone
RT acetyltransferase complex from yeast to humans.";
RL Mol. Cell. Biol. 24:1884-1896(2004).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=18445686; DOI=10.1242/jcs.019174;
RA Tegha-Dunghu J., Neumann B., Reber S., Krause R., Erfle H., Walter T.,
RA Held M., Rogers P., Hupfeld K., Ruppert T., Ellenberg J., Gruss O.J.;
RT "EML3 is a nuclear microtubule-binding protein required for the correct
RT alignment of chromosomes in metaphase.";
RL J. Cell Sci. 121:1718-1726(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-37, AND IDENTIFICATION BY MASS
RP 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 [14]
RP FUNCTION, IDENTIFICATION IN NUA4-RELATED SRCAP-CONTAINING COMPLEX, DOMAIN,
RP AND MUTAGENESIS OF TYR-74 AND TRP-93.
RX PubMed=29437725; DOI=10.1101/gad.303784.117;
RA Hsu C.C., Shi J., Yuan C., Zhao D., Jiang S., Lyu J., Wang X., Li H.,
RA Wen H., Li W., Shi X.;
RT "Recognition of histone acetylation by the GAS41 YEATS domain promotes
RT H2A.Z deposition in non-small cell lung cancer.";
RL Genes Dev. 32:58-69(2018).
RN [15] {ECO:0007744|PDB:5VNA, ECO:0007744|PDB:5VNB}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-148 IN COMPLEX WITH ACETYLATED
RP HISTONE H3, AND FUNCTION.
RX PubMed=30071723; DOI=10.1021/acschembio.8b00674;
RA Cho H.J., Li H., Linhares B.M., Kim E., Ndoj J., Miao H., Grembecka J.,
RA Cierpicki T.;
RT "GAS41 recognizes diacetylated histone H3 through a bivalent binding
RT mode.";
RL ACS Chem. Biol. 13:2739-2746(2018).
RN [16] {ECO:0007744|PDB:5XTZ}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 15-159 IN COMPLEX WITH ACETYLATED
RP HISTONE H3, AND FUNCTION.
RX PubMed=29900004; DOI=10.1038/s41421-018-0027-0;
RA Hsu C.C., Zhao D., Shi J., Peng D., Guan H., Li Y., Huang Y., Wen H.,
RA Li W., Li H., Shi X.;
RT "Gas41 links histone acetylation to H2A.Z deposition and maintenance of
RT embryonic stem cell identity.";
RL Cell Discov. 4:28-28(2018).
RN [17] {ECO:0007744|PDB:5Y8V}
RP X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 21-160, FUNCTION, AND MUTAGENESIS
RP OF HIS-43.
RX PubMed=29463709; DOI=10.1073/pnas.1717664115;
RA Wang Y., Jin J., Chung M.W.H., Feng L., Sun H., Hao Q.;
RT "Identification of the YEATS domain of GAS41 as a pH-dependent reader of
RT histone succinylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:2365-2370(2018).
CC -!- FUNCTION: Chromatin reader component of the NuA4 histone
CC acetyltransferase (HAT) complex, a complex involved in transcriptional
CC activation of select genes principally by acetylation of nucleosomal
CC histones H4 and H2A (PubMed:12963728, PubMed:14966270). Specifically
CC recognizes and binds acylated histone H3, with a preference for histone
CC H3 diacetylated at 'Lys-18' and 'Lys-27' (H3K18ac and H3K27ac) or
CC histone H3 diacetylated at 'Lys-14' and 'Lys-27' (H3K14ac and H3K27ac)
CC (PubMed:29437725, PubMed:30071723, PubMed:29900004). Also able to
CC recognize and bind crotonylated histone H3 (PubMed:30071723). May also
CC recognize and bind histone H3 succinylated at 'Lys-122' (H3K122succ);
CC additional evidences are however required to confirm this result in
CC vivo (PubMed:29463709). Plays a key role in histone variant H2AZ1/H2A.Z
CC deposition into specific chromatin regions: recognizes and binds
CC H3K14ac and H3K27ac on the promoters of actively transcribed genes and
CC recruits NuA4-related complex to deposit H2AZ1/H2A.Z (PubMed:29437725).
CC H2AZ1/H2A.Z deposition is required for maintenance of embryonic stem
CC cell (By similarity). {ECO:0000250|UniProtKB:Q9CR11,
CC ECO:0000269|PubMed:12963728, ECO:0000269|PubMed:14966270,
CC ECO:0000269|PubMed:29437725, ECO:0000269|PubMed:29463709,
CC ECO:0000269|PubMed:29900004, ECO:0000269|PubMed:30071723}.
CC -!- SUBUNIT: Component of numerous complexes with chromatin remodeling and
CC histone acetyltransferase activity (PubMed:12963728, PubMed:14966270).
CC Component of the NuA4 histone acetyltransferase complex which contains
CC the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400,
CC BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin,
CC ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41,
CC VPS72/YL1 and MEAF6 (PubMed:12963728, PubMed:14966270). The NuA4
CC complex interacts with MYC and the adenovirus E1A protein
CC (PubMed:12963728, PubMed:14966270). Component of a NuA4-related complex
CC which contains EP400, TRRAP/PAF400, SRCAP, BRD8/SMAP, EPC1,
CC DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, actin, ACTL6A/BAF53A, VPS72 and
CC YEATS4/GAS41 (PubMed:14966270, PubMed:29437725). Interacts with
CC MLLT10/AF10 (PubMed:11756182). Also interacts with the SWI/SNF
CC component SMARCB1/BAF47, TACC1 and TACC2, and the nuclear matrix
CC protein NUMA1 (PubMed:10913114, PubMed:11903063, PubMed:12620397,
CC PubMed:11756182). {ECO:0000269|PubMed:10913114,
CC ECO:0000269|PubMed:11756182, ECO:0000269|PubMed:11903063,
CC ECO:0000269|PubMed:12620397, ECO:0000269|PubMed:12963728,
CC ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:29437725}.
CC -!- INTERACTION:
CC O95619; Q8NFD2: ANKK1; NbExp=4; IntAct=EBI-399269, EBI-13280688;
CC O95619; O75410: TACC1; NbExp=6; IntAct=EBI-399269, EBI-624237;
CC O95619; P09493-10: TPM1; NbExp=3; IntAct=EBI-399269, EBI-12123928;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00376,
CC ECO:0000269|PubMed:10913114, ECO:0000269|PubMed:18445686}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, lung,
CC pancreas, placenta and skeletal muscle. {ECO:0000269|PubMed:10913114}.
CC -!- DOMAIN: The YEATS domain specifically recognizes and binds acylated
CC histones, with a preference for histone H3 diacetylated at 'Lys-14' and
CC 'Lys-27' (H3K14ac and H3K27ac). {ECO:0000269|PubMed:29437725}.
CC -!- CAUTION: According to a report, recognizes and binds histone H3
CC succinylated at 'Lys-122' (H3K122succ) (PubMed:29463709). However,
CC another report only observed poor binding with succinylated histone H3
CC (PubMed:30071723). {ECO:0000269|PubMed:29463709,
CC ECO:0000269|PubMed:30071723}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC01935.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U61384; AAD12188.1; -; mRNA.
DR EMBL; AJ245746; CAC01935.1; ALT_INIT; mRNA.
DR EMBL; AK001413; BAA91678.1; -; mRNA.
DR EMBL; BC000994; AAH00994.1; -; mRNA.
DR CCDS; CCDS8990.1; -.
DR RefSeq; NP_001287879.1; NM_001300950.1.
DR RefSeq; NP_006521.1; NM_006530.3.
DR PDB; 5R68; X-ray; 1.64 A; A/B=18-190.
DR PDB; 5R69; X-ray; 1.83 A; A/B=18-190.
DR PDB; 5VNA; X-ray; 2.10 A; A/B/C/D=1-148.
DR PDB; 5VNB; X-ray; 2.40 A; A/B/C/D=1-148.
DR PDB; 5XTZ; X-ray; 2.10 A; A/B/C/D=15-159.
DR PDB; 5Y8V; X-ray; 2.61 A; A/B/C/D=21-160.
DR PDB; 7EIF; X-ray; 1.58 A; A=19-159.
DR PDB; 7JFY; X-ray; 2.10 A; A/B/C/D=1-148.
DR PDBsum; 5R68; -.
DR PDBsum; 5R69; -.
DR PDBsum; 5VNA; -.
DR PDBsum; 5VNB; -.
DR PDBsum; 5XTZ; -.
DR PDBsum; 5Y8V; -.
DR PDBsum; 7EIF; -.
DR PDBsum; 7JFY; -.
DR AlphaFoldDB; O95619; -.
DR SMR; O95619; -.
DR BioGRID; 113761; 200.
DR ComplexPortal; CPX-974; SRCAP chromatin remodeling complex.
DR ComplexPortal; CPX-978; NuA4 histone acetyltransferase complex.
DR CORUM; O95619; -.
DR IntAct; O95619; 103.
DR MINT; O95619; -.
DR STRING; 9606.ENSP00000247843; -.
DR GlyGen; O95619; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O95619; -.
DR MetOSite; O95619; -.
DR PhosphoSitePlus; O95619; -.
DR BioMuta; YEATS4; -.
DR EPD; O95619; -.
DR jPOST; O95619; -.
DR MassIVE; O95619; -.
DR MaxQB; O95619; -.
DR PaxDb; O95619; -.
DR PeptideAtlas; O95619; -.
DR PRIDE; O95619; -.
DR ProteomicsDB; 50951; -.
DR Antibodypedia; 16961; 401 antibodies from 32 providers.
DR DNASU; 8089; -.
DR Ensembl; ENST00000247843.7; ENSP00000247843.2; ENSG00000127337.7.
DR GeneID; 8089; -.
DR KEGG; hsa:8089; -.
DR MANE-Select; ENST00000247843.7; ENSP00000247843.2; NM_006530.4; NP_006521.1.
DR UCSC; uc001sux.4; human.
DR CTD; 8089; -.
DR DisGeNET; 8089; -.
DR GeneCards; YEATS4; -.
DR HGNC; HGNC:24859; YEATS4.
DR HPA; ENSG00000127337; Low tissue specificity.
DR MIM; 602116; gene.
DR neXtProt; NX_O95619; -.
DR OpenTargets; ENSG00000127337; -.
DR PharmGKB; PA134992686; -.
DR VEuPathDB; HostDB:ENSG00000127337; -.
DR eggNOG; KOG3149; Eukaryota.
DR GeneTree; ENSGT00940000155811; -.
DR HOGENOM; CLU_051385_3_0_1; -.
DR InParanoid; O95619; -.
DR OMA; PYHNEDM; -.
DR OrthoDB; 1482359at2759; -.
DR PhylomeDB; O95619; -.
DR PathwayCommons; O95619; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR Reactome; R-HSA-8866907; Activation of the TFAP2 (AP-2) family of transcription factors.
DR SignaLink; O95619; -.
DR BioGRID-ORCS; 8089; 554 hits in 1089 CRISPR screens.
DR ChiTaRS; YEATS4; human.
DR GenomeRNAi; 8089; -.
DR Pharos; O95619; Tbio.
DR PRO; PR:O95619; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; O95619; protein.
DR Bgee; ENSG00000127337; Expressed in oocyte and 191 other tissues.
DR ExpressionAtlas; O95619; baseline and differential.
DR Genevisible; O95619; HS.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; NAS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0000786; C:nucleosome; IDA:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0070577; F:lysine-acetylated histone binding; IDA:UniProtKB.
DR GO; GO:0140030; F:modification-dependent protein binding; IDA:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; NAS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR GO; GO:0043486; P:histone exchange; IC:ComplexPortal.
DR GO; GO:0043968; P:histone H2A acetylation; IDA:UniProtKB.
DR GO; GO:0043967; P:histone H4 acetylation; IDA:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; NAS:UniProtKB.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IDA:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; IC:ComplexPortal.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:ComplexPortal.
DR GO; GO:2000779; P:regulation of double-strand break repair; IC:ComplexPortal.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR Gene3D; 2.60.40.1970; -; 1.
DR InterPro; IPR038704; YEAST_sf.
DR InterPro; IPR005033; YEATS.
DR Pfam; PF03366; YEATS; 1.
DR PROSITE; PS51037; YEATS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; Coiled coil; Direct protein sequencing;
KW Growth regulation; Isopeptide bond; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..227
FT /note="YEATS domain-containing protein 4"
FT /id="PRO_0000066204"
FT DOMAIN 15..158
FT /note="YEATS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00376"
FT REGION 93..97
FT /note="Diacetylated histone H3 binding"
FT /evidence="ECO:0000269|PubMed:29900004,
FT ECO:0000269|PubMed:30071723, ECO:0007744|PDB:5VNB,
FT ECO:0007744|PDB:5XTZ"
FT REGION 163..227
FT /note="Interaction with MLLT10"
FT /evidence="ECO:0000269|PubMed:11756182"
FT REGION 168..227
FT /note="Interaction with TACC1"
FT /evidence="ECO:0000269|PubMed:11903063"
FT COILED 178..226
FT /evidence="ECO:0000255"
FT SITE 73
FT /note="Interacts with diacetylated histone H3"
FT /evidence="ECO:0000269|PubMed:29900004,
FT ECO:0000269|PubMed:30071723, ECO:0007744|PDB:5VNB,
FT ECO:0007744|PDB:5XTZ"
FT CROSSLNK 37
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT MUTAGEN 43
FT /note="H->A: Impaired binding to histone H3 succinylated at
FT 'Lys-122' (H3K122succ)."
FT /evidence="ECO:0000269|PubMed:29463709"
FT MUTAGEN 74
FT /note="Y->A: Impaired binding to histone H3 diacetylated at
FT 'Lys-14' and 'Lys-27' (H3K14ac and H3K27ac), and subsequent
FT deposition of histone H2AZ1/H2A.Z into specific chromatin
FT regions; when associated with A-93."
FT /evidence="ECO:0000269|PubMed:29437725"
FT MUTAGEN 93
FT /note="W->A: Impaired binding to histone H3 diacetylated at
FT 'Lys-14' and 'Lys-27' (H3K14ac and H3K27ac), and subsequent
FT deposition of histone H2AZ1/H2A.Z into specific chromatin
FT regions; when associated with A-74."
FT /evidence="ECO:0000269|PubMed:29437725"
FT CONFLICT 159
FT /note="R -> C (in Ref. 2; CAC01935)"
FT /evidence="ECO:0000305"
FT STRAND 20..33
FT /evidence="ECO:0007829|PDB:5R68"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:5R68"
FT STRAND 45..56
FT /evidence="ECO:0007829|PDB:5R68"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:5R68"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:5R68"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:5R68"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:5R68"
FT STRAND 83..93
FT /evidence="ECO:0007829|PDB:5R68"
FT STRAND 97..106
FT /evidence="ECO:0007829|PDB:5R68"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:5R68"
FT HELIX 124..128
FT /evidence="ECO:0007829|PDB:5VNA"
FT STRAND 134..146
FT /evidence="ECO:0007829|PDB:5R68"
FT HELIX 149..155
FT /evidence="ECO:0007829|PDB:5R68"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:5R69"
SQ SEQUENCE 227 AA; 26499 MW; 34C4692B227A7B85 CRC64;
MFKRMAEFGP DSGGRVKGVT IVKPIVYGNV ARYFGKKREE DGHTHQWTVY VKPYRNEDMS
AYVKKIQFKL HESYGNPLRV VTKPPYEITE TGWGEFEIII KIFFIDPNER PVTLYHLLKL
FQSDTNAMLG KKTVVSEFYD EMIFQDPTAM MQQLLTTSRQ LTLGAYKHET EFAELEVKTR
EKLEAAKKKT SFEIAELKER LKASRETINC LKNEIRKLEE DDQAKDI
