SGF29_HUMAN
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 03-AUG-2022, entry version 149.
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:26421618, PubMed:21685874,
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:26421618, PubMed:21685874,
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). {ECO:0000269|PubMed:19103755,
CC ECO:0000269|PubMed:20850016, ECO:0000269|PubMed:21685874,
CC ECO:0000269|PubMed:23894581, ECO:0000269|PubMed:26421618,
CC 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 TADA3L, GCN5L2, SUPT3H and MYC (By similarity).
CC {ECO:0000250|UniProtKB:P0C606, ECO:0000269|PubMed:19103755,
CC ECO:0000269|PubMed:20850016, ECO:0000269|PubMed:21685874,
CC ECO:0000269|PubMed:26578293}.
CC -!- INTERACTION:
CC Q96ES7; Q14457: BECN1; NbExp=3; 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; Q9Y448: KNSTRN; NbExp=5; 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=3; 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=3; 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=7; 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=12; IntAct=EBI-743117, EBI-473249;
CC Q96ES7; P15884: TCF4; NbExp=5; 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}.
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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; 169.
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; 113.
DR MINT; Q96ES7; -.
DR STRING; 9606.ENSP00000316114; -.
DR ChEMBL; CHEMBL4523425; -.
DR iPTMnet; Q96ES7; -.
DR PhosphoSitePlus; Q96ES7; -.
DR BioMuta; SGF29; -.
DR DMDM; 74731608; -.
DR EPD; Q96ES7; -.
DR jPOST; Q96ES7; -.
DR MassIVE; Q96ES7; -.
DR MaxQB; Q96ES7; -.
DR PaxDb; Q96ES7; -.
DR PeptideAtlas; Q96ES7; -.
DR PRIDE; Q96ES7; -.
DR ProteomicsDB; 76446; -.
DR Antibodypedia; 56026; 121 antibodies from 21 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 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; TYIAKMG; -.
DR OrthoDB; 1040796at2759; -.
DR PhylomeDB; Q96ES7; -.
DR TreeFam; TF314958; -.
DR PathwayCommons; Q96ES7; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR SignaLink; Q96ES7; -.
DR BioGRID-ORCS; 112869; 402 hits in 1085 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 185 other tissues.
DR ExpressionAtlas; Q96ES7; baseline and differential.
DR Genevisible; Q96ES7; HS.
DR GO; GO:0140672; C:ATAC complex; IDA:BHF-UCL.
DR GO; GO:0072686; C:mitotic spindle; IC:ComplexPortal.
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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0071169; P:establishment of protein localization to chromatin; TAS:UniProtKB.
DR GO; GO:0016573; P:histone acetylation; IDA:UniProtKB.
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:0035521; P:monoubiquitinated histone deubiquitination; IDA:ComplexPortal.
DR GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; IDA:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC: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; IC: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:0043484; P:regulation of RNA splicing; IC: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 InterPro; IPR037802; SGF29.
DR InterPro; IPR010750; SGF29_tudor-like_dom.
DR PANTHER; PTHR21539; PTHR21539; 1.
DR Pfam; PF07039; DUF1325; 1.
DR PROSITE; PS51518; SGF29_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chromatin regulator; Coiled coil; Nucleus;
KW Reference proteome; Transcription; 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
