ID ZCPW1_HUMAN Reviewed; 648 AA. AC Q9H0M4; A8MVF5; B4DUQ2; Q8NA98; Q9BUD0; Q9NWF7; DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 14-OCT-2008, sequence version 2. DT 24-JAN-2024, entry version 167. DE RecName: Full=Zinc finger CW-type PWWP domain protein 1; GN Name=ZCWPW1; 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] (ISOFORM 1). RC TISSUE=Testis; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 5), AND VARIANT RP ALA-153. RC TISSUE=Embryo, and Testis; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT ALA-153. RC TISSUE=Uterus; 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 [6] RP TISSUE SPECIFICITY. RX PubMed=32352380; DOI=10.7554/elife.53360; RA Mahgoub M., Paiano J., Bruno M., Wu W., Pathuri S., Zhang X., Ralls S., RA Cheng X., Nussenzweig A., Macfarlan T.S.; RT "Dual histone methyl reader ZCWPW1 facilitates repair of meiotic double RT strand breaks in male mice."; RL Elife 9:0-0(2020). RN [7] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=32744506; DOI=10.7554/elife.53392; RA Wells D., Bitoun E., Moralli D., Zhang G., Hinch A., Jankowska J., RA Donnelly P., Green C., Myers S.R.; RT "ZCWPW1 is recruited to recombination hotspots by PRDM9, and is essential RT for meiotic double strand break repair."; RL Elife 9:0-0(2020). RN [8] RP STRUCTURE BY NMR OF 245-307. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the ZF-CW domain in zinc finger CW-type PWWP domain RT protein 1."; RL Submitted (JUN-2007) to the PDB data bank. RN [9] RP STRUCTURE BY NMR OF 246-307, DOMAIN CW-TYPE ZINC FINGER, FUNCTION, AND RP MUTAGENESIS OF TRP-256; GLU-300; GLU-301; THR-302 AND TRP-303. RX PubMed=20826339; DOI=10.1016/j.str.2010.06.012; RA He F., Umehara T., Saito K., Harada T., Watanabe S., Yabuki T., Kigawa T., RA Takahashi M., Kuwasako K., Tsuda K., Matsuda T., Aoki M., Seki E., RA Kobayashi N., Guentert P., Yokoyama S., Muto Y.; RT "Structural insight into the zinc finger CW domain as a histone RT modification reader."; RL Structure 18:1127-1139(2010). CC -!- FUNCTION: Dual histone methylation reader specific for PRDM9-catalyzed CC histone marks (H3K4me3 and H3K36me3) (PubMed:32744506, CC PubMed:20826339). Facilitates the repair of PRDM9-induced meiotic CC double-strand breaks (DSBs) (By similarity). Essential for male CC fertility and spermatogenesis (By similarity). Required for meiosis CC prophase I progression in male but not in female germ cells (By CC similarity). {ECO:0000250|UniProtKB:Q6IR42, CC ECO:0000269|PubMed:20826339, ECO:0000269|PubMed:32744506}. CC -!- INTERACTION: CC Q9H0M4-4; Q96JM7-2: L3MBTL3; NbExp=3; IntAct=EBI-16429732, EBI-11985629; CC Q9H0M4-4; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-16429732, EBI-16439278; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6IR42}. CC Chromosome {ECO:0000250|UniProtKB:Q6IR42}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=Q9H0M4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9H0M4-2; Sequence=VSP_011432, VSP_011433, VSP_011434, CC VSP_035590; CC Name=3; CC IsoId=Q9H0M4-3; Sequence=VSP_011431, VSP_011432, VSP_011436, CC VSP_035592; CC Name=4; CC IsoId=Q9H0M4-4; Sequence=VSP_011431, VSP_011432, VSP_035591; CC Name=5; CC IsoId=Q9H0M4-5; Sequence=VSP_011432, VSP_011436, VSP_035592; CC -!- TISSUE SPECIFICITY: Testis. {ECO:0000269|PubMed:32352380, CC ECO:0000269|PubMed:32744506}. CC -!- DOMAIN: The CW-TYPE zinc finger mediates its binding to trimethylated CC histone H3K4me3. {ECO:0000269|PubMed:20826339}. CC -!- SEQUENCE CAUTION: CC Sequence=CAB66669.1; Type=Frameshift; Evidence={ECO:0000305}; 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; AL136735; CAB66669.1; ALT_FRAME; mRNA. DR EMBL; AK000919; BAA91424.1; -; mRNA. DR EMBL; AK093038; BAC04028.1; -; mRNA. DR EMBL; AK300745; BAG62414.1; -; mRNA. DR EMBL; AC005071; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC092849; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471091; EAW76540.1; -; Genomic_DNA. DR EMBL; CH471091; EAW76541.1; -; Genomic_DNA. DR EMBL; BC002725; AAH02725.1; -; mRNA. DR CCDS; CCDS43623.1; -. [Q9H0M4-1] DR CCDS; CCDS59067.1; -. [Q9H0M4-5] DR RefSeq; NP_001244937.1; NM_001258008.1. [Q9H0M4-5] DR RefSeq; NP_060454.3; NM_017984.4. [Q9H0M4-1] DR PDB; 2E61; NMR; -; A=246-307. DR PDB; 2RR4; NMR; -; A=246-307. DR PDBsum; 2E61; -. DR PDBsum; 2RR4; -. DR AlphaFoldDB; Q9H0M4; -. DR BMRB; Q9H0M4; -. DR SMR; Q9H0M4; -. DR BioGRID; 120381; 9. DR DIP; DIP-59044N; -. DR IntAct; Q9H0M4; 6. DR MINT; Q9H0M4; -. DR STRING; 9606.ENSP00000381109; -. DR ChEMBL; CHEMBL4739863; -. DR GlyCosmos; Q9H0M4; 1 site, 1 glycan. DR GlyGen; Q9H0M4; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q9H0M4; -. DR PhosphoSitePlus; Q9H0M4; -. DR BioMuta; ZCWPW1; -. DR DMDM; 209572701; -. DR MassIVE; Q9H0M4; -. DR PaxDb; 9606-ENSP00000381109; -. DR PeptideAtlas; Q9H0M4; -. DR ProteomicsDB; 5202; -. DR ProteomicsDB; 80298; -. [Q9H0M4-1] DR ProteomicsDB; 80299; -. [Q9H0M4-2] DR ProteomicsDB; 80300; -. [Q9H0M4-3] DR ProteomicsDB; 80301; -. [Q9H0M4-4] DR Antibodypedia; 8914; 84 antibodies from 16 providers. DR DNASU; 55063; -. DR Ensembl; ENST00000360951.8; ENSP00000354210.4; ENSG00000078487.18. [Q9H0M4-5] DR Ensembl; ENST00000398027.6; ENSP00000381109.2; ENSG00000078487.18. [Q9H0M4-1] DR Ensembl; ENST00000490721.5; ENSP00000419187.1; ENSG00000078487.18. [Q9H0M4-4] DR GeneID; 55063; -. DR KEGG; hsa:55063; -. DR UCSC; uc003uus.4; human. [Q9H0M4-1] DR AGR; HGNC:23486; -. DR CTD; 55063; -. DR DisGeNET; 55063; -. DR GeneCards; ZCWPW1; -. DR HGNC; HGNC:23486; ZCWPW1. DR HPA; ENSG00000078487; Tissue enriched (testis). DR MIM; 618900; gene. DR neXtProt; NX_Q9H0M4; -. DR OpenTargets; ENSG00000078487; -. DR PharmGKB; PA134913967; -. DR VEuPathDB; HostDB:ENSG00000078487; -. DR eggNOG; ENOG502QSQZ; Eukaryota. DR GeneTree; ENSGT00560000077278; -. DR HOGENOM; CLU_029321_1_0_1; -. DR InParanoid; Q9H0M4; -. DR OMA; CAQPIRC; -. DR OrthoDB; 5322065at2759; -. DR PhylomeDB; Q9H0M4; -. DR TreeFam; TF336904; -. DR PathwayCommons; Q9H0M4; -. DR SignaLink; Q9H0M4; -. DR BioGRID-ORCS; 55063; 19 hits in 1153 CRISPR screens. DR ChiTaRS; ZCWPW1; human. DR EvolutionaryTrace; Q9H0M4; -. DR GenomeRNAi; 55063; -. DR Pharos; Q9H0M4; Tbio. DR PRO; PR:Q9H0M4; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; Q9H0M4; Protein. DR Bgee; ENSG00000078487; Expressed in right testis and 131 other cell types or tissues. DR ExpressionAtlas; Q9H0M4; baseline and differential. DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; ISS:ARUK-UCL. DR GO; GO:0008327; F:methyl-CpG binding; IDA:UniProtKB. DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; ISS:UniProtKB. DR GO; GO:0007127; P:meiosis I; ISS:ARUK-UCL. DR GO; GO:0045911; P:positive regulation of DNA recombination; ISS:ARUK-UCL. DR GO; GO:2000781; P:positive regulation of double-strand break repair; ISS:UniProtKB. DR GO; GO:0007283; P:spermatogenesis; ISS:ARUK-UCL. DR CDD; cd20145; PWWP_ZCWPW1; 1. DR Gene3D; 2.30.30.140; -; 1. DR Gene3D; 3.30.40.100; -; 1. DR InterPro; IPR000313; PWWP_dom. DR InterPro; IPR042778; ZCWPW1/ZCWPW2. DR InterPro; IPR011124; Znf_CW. DR PANTHER; PTHR15999; UNCHARACTERIZED; 1. DR PANTHER; PTHR15999:SF2; ZINC FINGER CW-TYPE PWWP DOMAIN PROTEIN 1; 1. DR Pfam; PF00855; PWWP; 1. DR Pfam; PF07496; zf-CW; 1. DR SMART; SM00293; PWWP; 1. DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1. DR PROSITE; PS50812; PWWP; 1. DR PROSITE; PS51050; ZF_CW; 1. DR Genevisible; Q9H0M4; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Chromosome; Coiled coil; KW Differentiation; Metal-binding; Nucleus; Phosphoprotein; KW Reference proteome; Spermatogenesis; Zinc; Zinc-finger. FT CHAIN 1..648 FT /note="Zinc finger CW-type PWWP domain protein 1" FT /id="PRO_0000066567" FT DOMAIN 317..383 FT /note="PWWP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162" FT ZN_FING 250..304 FT /note="CW-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454, FT ECO:0000269|PubMed:20826339" FT REGION 1..103 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 137..237 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 436..648 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 74..109 FT /evidence="ECO:0000255" FT COMPBIAS 28..43 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 55..101 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 137..166 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 205..237 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 452..476 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 259 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454" FT BINDING 264 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454" FT BINDING 285 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454" FT BINDING 296 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454" FT MOD_RES 636 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6IR42" FT VAR_SEQ 1..121 FT /note="Missing (in isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_011431" FT VAR_SEQ 211 FT /note="H -> QD (in isoform 2, isoform 3, isoform 4 and FT isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_011432" FT VAR_SEQ 289 FT /note="T -> TA (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_011433" FT VAR_SEQ 453..466 FT /note="LEKKEKEEELEKEE -> TQNGKERRPREFRF (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_011434" FT VAR_SEQ 467..648 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_035590" FT VAR_SEQ 471..523 FT /note="DPILPIRKRVKIQTQKTKPRGLGGDAGTADGRGRTLQRKIMKRSLGRKSTAP FT P -> ALRKNLKLPRARPWQPAFQREKKLEQCQRTWAYQRVRGPAPHLRKKSPDTGNP FT (in isoform 3 and isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_011436" FT VAR_SEQ 491..541 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_035591" FT VAR_SEQ 524..648 FT /note="Missing (in isoform 3 and isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_035592" FT VARIANT 153 FT /note="T -> A (in dbSNP:rs6465770)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334" FT /id="VAR_019659" FT VARIANT 365 FT /note="E -> K (in dbSNP:rs6970350)" FT /id="VAR_047050" FT MUTAGEN 256 FT /note="W->I: Loss of histone H3K4me3 binding; when FT associated with R-301; L-302 and P-303." FT /evidence="ECO:0000269|PubMed:20826339" FT MUTAGEN 300 FT /note="E->A: Reduced histone H3K4me3 binding but complete FT loss of non-methylated histone H3K4 binding." FT /evidence="ECO:0000269|PubMed:20826339" FT MUTAGEN 301 FT /note="E->R: Loss of histone H3K4me3 binding; when FT associated with I-256; L-302 and P-303." FT /evidence="ECO:0000269|PubMed:20826339" FT MUTAGEN 302 FT /note="T->L: Loss of histone H3K4me3 binding; when FT associated with I-256; R-301 and P-303." FT /evidence="ECO:0000269|PubMed:20826339" FT MUTAGEN 303 FT /note="W->A: Reduced histone H3K4me3 binding but no effect FT on non-methylated histone H3K4 binding." FT /evidence="ECO:0000269|PubMed:20826339" FT MUTAGEN 303 FT /note="W->E: Silghtly reduced histone H3K4me3 and FT non-methylated histone H3K4 binding." FT /evidence="ECO:0000269|PubMed:20826339" FT MUTAGEN 303 FT /note="W->P: Loss of histone H3K4me3 binding; when FT associated with I-256; R-301 and L-302." FT /evidence="ECO:0000269|PubMed:20826339" FT STRAND 247..249 FT /evidence="ECO:0007829|PDB:2E61" FT STRAND 256..258 FT /evidence="ECO:0007829|PDB:2E61" FT TURN 262..264 FT /evidence="ECO:0007829|PDB:2E61" FT STRAND 267..269 FT /evidence="ECO:0007829|PDB:2E61" FT TURN 276..278 FT /evidence="ECO:0007829|PDB:2E61" FT HELIX 285..287 FT /evidence="ECO:0007829|PDB:2E61" FT HELIX 291..293 FT /evidence="ECO:0007829|PDB:2E61" FT STRAND 295..298 FT /evidence="ECO:0007829|PDB:2E61" SQ SEQUENCE 648 AA; 72007 MW; 4F267947AC00B1B4 CRC64; MMTTLQNKEE CGKGPKRIFA PPAQKSYSLL PCSPNSPKEE TPGISSPETE ARISLPKASL KKKEEKATMK NVPSREQEKK RKAQINKQAE KKEKEKSSLT NAEFEEIVQI VLQKSLQECL GMGSGLDFAE TSCAQPVVST QSDKEPGITA SATDTDNANG EEVPHTQEIS VSWEGEAAPE IRTSKLGQPD PAPSKKKSNR LTLSKRKKEA HEKVEKTQGG HEHRQEDRLK KTVQDHSQIR DQQKGEISGF GQCLVWVQCS FPNCGKWRRL CGNIDPSVLP DNWSCDQNTD VQYNRCDIPE ETWTGLESDV AYASYIPGSI IWAKQYGYPW WPGMIESDPD LGEYFLFTSH LDSLPSKYHV TFFGETVSRA WIPVNMLKNF QELSLELSVM KKRRNDCSQK LGVALMMAQE AEQISIQERV NLFGFWSRFN GSNSNGERKD LQLSGLNSPG SCLEKKEKEE ELEKEEGEKT DPILPIRKRV KIQTQKTKPR GLGGDAGTAD GRGRTLQRKI MKRSLGRKST APPAPRMGRK EGQGNSDSDQ PGPKKKFKAP QSKALAASFS EGKEVRTVPK NLGLSACKGA CPSSAKEEPR HREPLTQEAG SVPLEDEASS DLDLEQLMED VGRELGQSGE LQHSNSDGED FPVALFGK //