ID SGF29_HUMAN Reviewed; 293 AA. AC Q96ES7; Q96MF5; DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-NOV-2024, entry version 162. DE RecName: Full=SAGA-associated factor 29 {ECO:0000305}; DE AltName: Full=Coiled-coil domain-containing protein 101; DE AltName: Full=SAGA complex-associated factor 29 {ECO:0000312|HGNC:HGNC:25156}; GN Name=SGF29 {ECO:0000312|HGNC:HGNC:25156}; GN Synonyms=CCDC101 {ECO:0000312|HGNC:HGNC:25156}; 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=Skeletal muscle; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Ovary; 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 [3] 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 [4] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-288, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [5] RP FUNCTION, METHYLATED HISTONE-BINDING, IDENTIFICATION IN A SAGA-TYPE RP COMPLEX, AND MUTAGENESIS OF TRP-175; GLU-179; PRO-214; GLN-232; TYR-238; RP TYR-245; PRO-256; PHE-264 AND ARG-282. RX PubMed=20850016; DOI=10.1016/j.cell.2010.08.020; RA Vermeulen M., Eberl H.C., Matarese F., Marks H., Denissov S., Butter F., RA Lee K.K., Olsen J.V., Hyman A.A., Stunnenberg H.G., Mann M.; RT "Quantitative interaction proteomics and genome-wide profiling of RT epigenetic histone marks and their readers."; RL Cell 142:967-980(2010). RN [6] 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 [7] RP FUNCTION. RX PubMed=23894581; DOI=10.1371/journal.pone.0070035; RA Schram A.W., Baas R., Jansen P.W., Riss A., Tora L., Vermeulen M., RA Timmers H.T.; RT "A dual role for SAGA-associated factor 29 (SGF29) in ER stress survival by RT coordination of both histone H3 acetylation and histone H3 lysine-4 RT trimethylation."; RL PLoS ONE 8:E70035-E70035(2013). RN [8] RP DOMAIN, FUNCTION, AND MUTAGENESIS OF TYR-238; TYR-245 AND ASP-266. RX PubMed=26421618; DOI=10.1371/journal.pone.0139205; RA Pieters B.J., Meulenbroeks E., Belle R., Mecinovic J.; RT "The role of electrostatic interactions in binding of histone H3K4me2/3 to RT the Sgf29 tandem Tudor domain."; RL PLoS ONE 10:E0139205-E0139205(2015). RN [9] RP X-RAY CRYSTALLOGRAPHY (1.26 ANGSTROMS) OF 115-293 IN COMPLEX WITH H3K4ME2 RP PEPTIDE, FUNCTION, INTERACTION WITH H3K4ME2 AND H3K4ME3, MUTAGENESIS OF RP ASP-194; ASP-196; TYR-238; GLN-240; THR-242; TYR-245; PHE-264 AND ASP-266, RP AND DOMAIN. RX PubMed=21685874; DOI=10.1038/emboj.2011.193; RA Bian C., Xu C., Ruan J., Lee K.K., Burke T.L., Tempel W., Barsyte D., RA Li J., Wu M., Zhou B.O., Fleharty B.E., Paulson A., Allali-Hassani A., RA Zhou J.Q., Mer G., Grant P.A., Workman J.L., Zang J., Min J.; RT "Sgf29 binds histone H3K4me2/3 and is required for SAGA complex recruitment RT and histone H3 acetylation."; RL EMBO J. 30:2829-2842(2011). RN [10] {ECO:0007744|PDB:5C0M} RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 115-293 IN COMPLEX WITH H3K4ME3 RP PEPTIDE, DOMAIN, AND FUNCTION. RX PubMed=26578293; DOI=10.1038/ncomms9911; RA Kamps J.J., Huang J., Poater J., Xu C., Pieters B.J., Dong A., Min J., RA Sherman W., Beuming T., Matthias Bickelhaupt F., Li H., Mecinovic J.; RT "Chemical basis for the recognition of trimethyllysine by epigenetic reader RT proteins."; RL Nat. Commun. 6:8911-8911(2015). CC -!- FUNCTION: Chromatin reader component of some histone acetyltransferase CC (HAT) SAGA-type complexes like the TFTC-HAT, ATAC or STAGA complexes CC (PubMed:19103755, PubMed:20850016, PubMed:21685874, PubMed:26421618, CC PubMed:26578293). SGF29 specifically recognizes and binds methylated CC 'Lys-4' of histone H3 (H3K4me), with a preference for trimethylated CC form (H3K4me3) (PubMed:20850016, PubMed:21685874, PubMed:26421618, CC PubMed:26578293). In the SAGA-type complexes, SGF29 is required to CC recruit complexes to H3K4me (PubMed:20850016). Involved in the response CC to endoplasmic reticulum (ER) stress by recruiting the SAGA complex to CC H3K4me, thereby promoting histone H3 acetylation and cell survival CC (PubMed:23894581). Also binds non-histone proteins that are methylated CC on Lys residues: specifically recognizes and binds CGAS monomethylated CC on 'Lys-506' (By similarity). {ECO:0000250|UniProtKB:Q9DA08, CC ECO:0000269|PubMed:19103755, ECO:0000269|PubMed:20850016, CC ECO:0000269|PubMed:21685874, ECO:0000269|PubMed:23894581, CC ECO:0000269|PubMed:26421618, ECO:0000269|PubMed:26578293}. CC -!- SUBUNIT: Interacts with dimethylated and trimethylated 'Lys-4' of CC histone H3 (H3K4me2 and H3K4me3), with a preference for the CC trimethylated form (H3K4me3) (PubMed:21685874, PubMed:26578293). CC Component of some SAGA-type complexes (PubMed:20850016). Component of CC the ADA2A-containing complex (ATAC), composed of KAT14, KAT2A, TADA2L, CC TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1 (PubMed:19103755). CC Interacts with (methylated) CGAS (By similarity). Interacts with CC TADA3L, GCN5L2, SUPT3H and MYC (By similarity). CC {ECO:0000250|UniProtKB:P0C606, ECO:0000250|UniProtKB:Q9DA08, CC ECO:0000269|PubMed:19103755, ECO:0000269|PubMed:20850016, CC ECO:0000269|PubMed:21685874, ECO:0000269|PubMed:26578293}. CC -!- INTERACTION: CC Q96ES7; Q14457: BECN1; NbExp=4; IntAct=EBI-743117, EBI-949378; CC Q96ES7; A1L168: C20orf202; NbExp=3; IntAct=EBI-743117, EBI-18396958; CC Q96ES7; Q68D86: CCDC102B; NbExp=3; IntAct=EBI-743117, EBI-10171570; CC Q96ES7; Q8NHS4: CLHC1; NbExp=3; IntAct=EBI-743117, EBI-10203156; CC Q96ES7; Q8NFT6-2: DBF4B; NbExp=3; IntAct=EBI-743117, EBI-12205861; CC Q96ES7; P68431: H3C12; NbExp=25; IntAct=EBI-743117, EBI-79722; CC Q96ES7; P28290: ITPRID2; NbExp=5; IntAct=EBI-743117, EBI-722905; CC Q96ES7; Q99661: KIF2C; NbExp=4; IntAct=EBI-743117, EBI-1642317; CC Q96ES7; Q9Y448: KNSTRN; NbExp=8; IntAct=EBI-743117, EBI-373334; CC Q96ES7; A1A4E9: KRT13; NbExp=3; IntAct=EBI-743117, EBI-10171552; CC Q96ES7; P19012: KRT15; NbExp=7; IntAct=EBI-743117, EBI-739566; CC Q96ES7; P08779: KRT16; NbExp=4; IntAct=EBI-743117, EBI-356410; CC Q96ES7; P08727: KRT19; NbExp=5; IntAct=EBI-743117, EBI-742756; CC Q96ES7; Q2M2I5: KRT24; NbExp=3; IntAct=EBI-743117, EBI-2952736; CC Q96ES7; Q7Z3Y8: KRT27; NbExp=4; IntAct=EBI-743117, EBI-3044087; CC Q96ES7; Q14525: KRT33B; NbExp=3; IntAct=EBI-743117, EBI-1049638; CC Q96ES7; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-743117, EBI-739832; CC Q96ES7; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-743117, EBI-1216080; CC Q96ES7; Q9P086: MED11; NbExp=3; IntAct=EBI-743117, EBI-394704; CC Q96ES7; Q9NPJ6: MED4; NbExp=3; IntAct=EBI-743117, EBI-394607; CC Q96ES7; P13349: MYF5; NbExp=5; IntAct=EBI-743117, EBI-17491620; CC Q96ES7; O14777: NDC80; NbExp=8; IntAct=EBI-743117, EBI-715849; CC Q96ES7; Q2NL68: PROSER3; NbExp=3; IntAct=EBI-743117, EBI-11336487; CC Q96ES7; Q6NUQ1: RINT1; NbExp=7; IntAct=EBI-743117, EBI-726876; CC Q96ES7; A1L190: SYCE3; NbExp=3; IntAct=EBI-743117, EBI-10283466; CC Q96ES7; Q8N3V7: SYNPO; NbExp=5; IntAct=EBI-743117, EBI-352936; CC Q96ES7; O75528: TADA3; NbExp=15; IntAct=EBI-743117, EBI-473249; CC Q96ES7; P15884: TCF4; NbExp=7; IntAct=EBI-743117, EBI-533224; CC Q96ES7; P15884-3: TCF4; NbExp=3; IntAct=EBI-743117, EBI-13636688; CC Q96ES7; Q9BXU0: TEX12; NbExp=3; IntAct=EBI-743117, EBI-12090309; CC Q96ES7; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-743117, EBI-1105213; CC Q96ES7; Q8TDR0-2: TRAF3IP1; NbExp=3; IntAct=EBI-743117, EBI-11946508; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P0C606}. CC -!- DOMAIN: The SGF29 C-terminal (also named tudor-like) domain mediates CC binding to methylated 'Lys-4' of histone H3 (H3K4me), with a preference CC for trimethylated form (H3K4me3). {ECO:0000255|PROSITE- CC ProRule:PRU00851, ECO:0000269|PubMed:21685874, CC ECO:0000269|PubMed:26421618, ECO:0000269|PubMed:26578293}. CC -!- SIMILARITY: Belongs to the SGF29 family. {ECO:0000255|PROSITE- CC ProRule:PRU00851}. 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; AK057008; BAB71340.1; -; mRNA. DR EMBL; BC011981; AAH11981.1; -; mRNA. DR CCDS; CCDS10635.1; -. DR RefSeq; NP_612423.1; NM_138414.2. DR PDB; 3LX7; X-ray; 1.78 A; A=138-293. DR PDB; 3ME9; X-ray; 1.37 A; A/B=115-293. DR PDB; 3MEA; X-ray; 1.26 A; A=129-291. DR PDB; 3MET; X-ray; 2.00 A; A/B=115-293. DR PDB; 3MEU; X-ray; 1.28 A; A/B=115-293. DR PDB; 3MEV; X-ray; 1.83 A; A/B=115-293. DR PDB; 3MEW; X-ray; 1.92 A; A=129-287. DR PDB; 5C0M; X-ray; 1.60 A; A/B=115-293. DR PDBsum; 3LX7; -. DR PDBsum; 3ME9; -. DR PDBsum; 3MEA; -. DR PDBsum; 3MET; -. DR PDBsum; 3MEU; -. DR PDBsum; 3MEV; -. DR PDBsum; 3MEW; -. DR PDBsum; 5C0M; -. DR AlphaFoldDB; Q96ES7; -. DR SMR; Q96ES7; -. DR BioGRID; 125213; 175. DR ComplexPortal; CPX-1004; PCAF-containing ATAC complex. DR ComplexPortal; CPX-6802; SAGA complex, KAT2B variant. DR ComplexPortal; CPX-900; SAGA complex, KAT2A variant. DR ComplexPortal; CPX-997; GCN5-containing ATAC complex. DR CORUM; Q96ES7; -. DR IntAct; Q96ES7; 147. DR MINT; Q96ES7; -. DR STRING; 9606.ENSP00000316114; -. DR ChEMBL; CHEMBL4523425; -. DR GlyGen; Q96ES7; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q96ES7; -. DR PhosphoSitePlus; Q96ES7; -. DR BioMuta; SGF29; -. DR DMDM; 74731608; -. DR jPOST; Q96ES7; -. DR MassIVE; Q96ES7; -. DR PaxDb; 9606-ENSP00000316114; -. DR PeptideAtlas; Q96ES7; -. DR ProteomicsDB; 76446; -. DR Pumba; Q96ES7; -. DR Antibodypedia; 56026; 112 antibodies from 20 providers. DR DNASU; 112869; -. DR Ensembl; ENST00000317058.8; ENSP00000316114.3; ENSG00000176476.9. DR GeneID; 112869; -. DR KEGG; hsa:112869; -. DR MANE-Select; ENST00000317058.8; ENSP00000316114.3; NM_138414.3; NP_612423.1. DR UCSC; uc002dqf.4; human. DR AGR; HGNC:25156; -. DR CTD; 112869; -. DR DisGeNET; 112869; -. DR GeneCards; SGF29; -. DR HGNC; HGNC:25156; SGF29. DR HPA; ENSG00000176476; Low tissue specificity. DR MIM; 613374; gene. DR neXtProt; NX_Q96ES7; -. DR OpenTargets; ENSG00000176476; -. DR PharmGKB; PA144596468; -. DR VEuPathDB; HostDB:ENSG00000176476; -. DR eggNOG; KOG3038; Eukaryota. DR GeneTree; ENSGT00390000015229; -. DR HOGENOM; CLU_056816_0_0_1; -. DR InParanoid; Q96ES7; -. DR OMA; EQKDRHT; -. DR OrthoDB; 2876824at2759; -. DR PhylomeDB; Q96ES7; -. DR TreeFam; TF314958; -. DR PathwayCommons; Q96ES7; -. DR Reactome; R-HSA-3214847; HATs acetylate histones. DR Reactome; R-HSA-9772755; Formation of WDR5-containing histone-modifying complexes. DR SignaLink; Q96ES7; -. DR SIGNOR; Q96ES7; -. DR BioGRID-ORCS; 112869; 425 hits in 1166 CRISPR screens. DR ChiTaRS; SGF29; human. DR EvolutionaryTrace; Q96ES7; -. DR GenomeRNAi; 112869; -. DR Pharos; Q96ES7; Tbio. DR PRO; PR:Q96ES7; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q96ES7; protein. DR Bgee; ENSG00000176476; Expressed in hindlimb stylopod muscle and 187 other cell types or tissues. DR ExpressionAtlas; Q96ES7; 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:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0000124; C:SAGA complex; IBA:GO_Central. DR GO; GO:0070461; C:SAGA-type complex; IDA:UniProtKB. DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB. DR GO; GO:0071169; P:establishment of protein localization to chromatin; TAS:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; NAS:ComplexPortal. 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:0006282; P:regulation of DNA repair; NAS: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:0043484; P:regulation of RNA splicing; NAS: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 GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:UniProtKB. DR GO; GO:0045815; P:transcription initiation-coupled chromatin remodeling; IMP:UniProtKB. DR CDD; cd20393; Tudor_SGF29_rpt1; 1. DR CDD; cd20394; Tudor_SGF29_rpt2; 1. DR FunFam; 2.30.30.140:FF:000026; SAGA-associated factor 29 homolog; 1. DR FunFam; 2.30.30.140:FF:000029; SAGA-associated factor 29 homolog; 1. DR Gene3D; 2.30.30.140; -; 2. DR InterPro; IPR037802; SGF29. DR InterPro; IPR010750; SGF29_tudor-like_dom. DR InterPro; IPR047288; Tudor_SGF29_rpt1. DR InterPro; IPR047287; Tudor_SGF29_rpt2. DR PANTHER; PTHR21539:SF0; SAGA-ASSOCIATED FACTOR 29; 1. DR PANTHER; PTHR21539; UNCHARACTERIZED; 1. DR Pfam; PF07039; SGF29_Tudor; 1. DR PROSITE; PS51518; SGF29_C; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Chromatin regulator; Coiled coil; Nucleus; KW Proteomics identification; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1..293 FT /note="SAGA-associated factor 29" FT /id="PRO_0000274268" FT DOMAIN 152..293 FT /note="SGF29 C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00851" FT REGION 194..196 FT /note="Histone H3K4me3 N-terminus binding" FT /evidence="ECO:0000269|PubMed:21685874, FT ECO:0000269|PubMed:26578293" FT REGION 240..243 FT /note="Histone H3K4me3 N-terminus binding" FT /evidence="ECO:0000269|PubMed:21685874, FT ECO:0000269|PubMed:26578293" FT REGION 264..266 FT /note="Histone H3K4me3 binding" FT /evidence="ECO:0000269|PubMed:21685874" FT COILED 3..88 FT /evidence="ECO:0000255" FT SITE 238 FT /note="Histone H3K4me3 binding" FT /evidence="ECO:0000269|PubMed:21685874" FT SITE 245 FT /note="Histone H3K4me3 binding" FT /evidence="ECO:0000269|PubMed:21685874, FT ECO:0000269|PubMed:26578293" FT MOD_RES 288 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MUTAGEN 175 FT /note="W->A: Does not strongly affect binding to H3K4me." FT /evidence="ECO:0000269|PubMed:20850016" FT MUTAGEN 179 FT /note="E->A: Does not strongly affect binding to H3K4me." FT /evidence="ECO:0000269|PubMed:20850016" FT MUTAGEN 194 FT /note="D->A,R: Abolishes H3K4me3 binding." FT /evidence="ECO:0000269|PubMed:21685874" FT MUTAGEN 196 FT /note="D->R: Abolishes H3K4me3 binding." FT /evidence="ECO:0000269|PubMed:21685874" FT MUTAGEN 214 FT /note="P->A: Does not strongly affect binding to H3K4me." FT /evidence="ECO:0000269|PubMed:20850016" FT MUTAGEN 232 FT /note="Q->A: Does not strongly affect binding to H3K4me." FT /evidence="ECO:0000269|PubMed:20850016" FT MUTAGEN 238 FT /note="Y->A: Strongly reduced H3K4me3 binding." FT /evidence="ECO:0000269|PubMed:20850016, FT ECO:0000269|PubMed:21685874" FT MUTAGEN 238 FT /note="Y->F: Does not affect binding to H3K4me3." FT /evidence="ECO:0000269|PubMed:26421618" FT MUTAGEN 240 FT /note="Q->A: Slightly reduced H3K4me3 binding." FT /evidence="ECO:0000269|PubMed:21685874" FT MUTAGEN 242 FT /note="T->A: Almost abolished H3K4me3 binding." FT /evidence="ECO:0000269|PubMed:21685874" FT MUTAGEN 245 FT /note="Y->A: Abolishes H3K4me3 binding." FT /evidence="ECO:0000269|PubMed:20850016, FT ECO:0000269|PubMed:21685874" FT MUTAGEN 245 FT /note="Y->F: Reduced H3K4me3 binding." FT /evidence="ECO:0000269|PubMed:26421618" FT MUTAGEN 256 FT /note="P->A: Does not strongly affect binding to H3K4me." FT /evidence="ECO:0000269|PubMed:20850016" FT MUTAGEN 264 FT /note="F->A: Strongly reduced binding to H3K4me3." FT /evidence="ECO:0000269|PubMed:20850016, FT ECO:0000269|PubMed:21685874" FT MUTAGEN 266 FT /note="D->A,F,Y,W: Strongly reduced binding to H3K4me3." FT /evidence="ECO:0000269|PubMed:21685874, FT ECO:0000269|PubMed:26421618" FT MUTAGEN 266 FT /note="D->E: Does not affect binding to H3K4me3." FT /evidence="ECO:0000269|PubMed:26421618" FT MUTAGEN 266 FT /note="D->N: Slightly reduced binding to H3K4me3." FT /evidence="ECO:0000269|PubMed:26421618" FT MUTAGEN 282 FT /note="R->A: Does not strongly affect binding to H3K4me." FT /evidence="ECO:0000269|PubMed:20850016" FT CONFLICT 249 FT /note="I -> N (in Ref. 1; BAB71340)" FT /evidence="ECO:0000305" FT HELIX 115..129 FT /evidence="ECO:0007829|PDB:3MEU" FT STRAND 161..167 FT /evidence="ECO:0007829|PDB:3MEA" FT STRAND 173..184 FT /evidence="ECO:0007829|PDB:3MEA" FT TURN 185..188 FT /evidence="ECO:0007829|PDB:3MEA" FT STRAND 189..194 FT /evidence="ECO:0007829|PDB:3MEA" FT STRAND 201..206 FT /evidence="ECO:0007829|PDB:3MEA" FT HELIX 207..209 FT /evidence="ECO:0007829|PDB:3MEA" FT STRAND 210..212 FT /evidence="ECO:0007829|PDB:3MEA" FT STRAND 215..217 FT /evidence="ECO:0007829|PDB:3MEA" FT TURN 220..222 FT /evidence="ECO:0007829|PDB:3MEA" FT HELIX 224..226 FT /evidence="ECO:0007829|PDB:3MEA" FT STRAND 233..237 FT /evidence="ECO:0007829|PDB:3MEA" FT STRAND 241..251 FT /evidence="ECO:0007829|PDB:3MEA" FT STRAND 260..265 FT /evidence="ECO:0007829|PDB:3MEA" FT STRAND 277..279 FT /evidence="ECO:0007829|PDB:3MEA" FT HELIX 281..283 FT /evidence="ECO:0007829|PDB:3MEA" FT STRAND 284..286 FT /evidence="ECO:0007829|PDB:3MEA" SQ SEQUENCE 293 AA; 33238 MW; A1B4A8D9B0044CC7 CRC64; MALVSADSRI AELLTELHQL IKQTQEERSR SEHNLVNIQK THERMQTENK ISPYYRTKLR GLYTTAKADA EAECNILRKA LDKIAEIKSL LEERRIAAKI AGLYNDSEPP RKTMRRGVLM TLLQQSAMTL PLWIGKPGDK PPPLCGAIPA SGDYVARPGD KVAARVKAVD GDEQWILAEV VSYSHATNKY EVDDIDEEGK ERHTLSRRRV IPLPQWKANP ETDPEALFQK EQLVLALYPQ TTCFYRALIH APPQRPQDDY SVLFEDTSYA DGYSPPLNVA QRYVVACKEP KKK //