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   02-JUN-2021, entry version 145.
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}.
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   SMR; Q96ES7; -.
DR   BioGRID; 125213; 118.
DR   ComplexPortal; CPX-1004; PCAF-containing ATAC complex.
DR   ComplexPortal; CPX-900; SAGA complex.
DR   ComplexPortal; CPX-997; GCN5-containing ATAC complex.
DR   CORUM; Q96ES7; -.
DR   IntAct; Q96ES7; 103.
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; 115 antibodies.
DR   DNASU; 112869; -.
DR   Ensembl; ENST00000317058; ENSP00000316114; ENSG00000176476.
DR   GeneID; 112869; -.
DR   KEGG; hsa:112869; -.
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:ENSG00000176476.8; -.
DR   eggNOG; KOG3038; Eukaryota.
DR   GeneTree; ENSGT00390000015229; -.
DR   HOGENOM; CLU_056816_0_0_1; -.
DR   InParanoid; Q96ES7; -.
DR   OMA; DPHALFP; -.
DR   OrthoDB; 1040796at2759; -.
DR   PhylomeDB; Q96ES7; -.
DR   TreeFam; TF314958; -.
DR   PathwayCommons; Q96ES7; -.
DR   Reactome; R-HSA-3214847; HATs acetylate histones.
DR   BioGRID-ORCS; 112869; 390 hits in 1007 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 testis and 223 other tissues.
DR   ExpressionAtlas; Q96ES7; baseline and differential.
DR   Genevisible; Q96ES7; HS.
DR   GO; GO:0005671; C:Ada2/Gcn5/Ada3 transcription activator complex; IDA:BHF-UCL.
DR   GO; GO:0000124; C:SAGA complex; IBA:GO_Central.
DR   GO; GO:0070461; C:SAGA-type complex; IDA:UniProtKB.
DR   GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR   GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
DR   GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
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   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
//