ZCPW1_HUMAN
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 03-AUG-2022, entry version 159.
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};
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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 GlyGen; Q9H0M4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H0M4; -.
DR PhosphoSitePlus; Q9H0M4; -.
DR BioMuta; ZCWPW1; -.
DR DMDM; 209572701; -.
DR MassIVE; Q9H0M4; -.
DR PaxDb; Q9H0M4; -.
DR PeptideAtlas; Q9H0M4; -.
DR PRIDE; 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; 70 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 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; TQKLHSM; -.
DR OrthoDB; 1159953at2759; -.
DR PhylomeDB; Q9H0M4; -.
DR TreeFam; TF336904; -.
DR PathwayCommons; Q9H0M4; -.
DR SignaLink; Q9H0M4; -.
DR BioGRID-ORCS; 55063; 18 hits in 1074 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 129 other tissues.
DR ExpressionAtlas; Q9H0M4; baseline and differential.
DR Genevisible; Q9H0M4; HS.
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 InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR042778; ZCWPW1/ZCWPW2.
DR InterPro; IPR011124; Znf_CW.
DR PANTHER; PTHR15999; PTHR15999; 1.
DR Pfam; PF00855; PWWP; 1.
DR Pfam; PF07496; zf-CW; 1.
DR SMART; SM00293; PWWP; 1.
DR PROSITE; PS50812; PWWP; 1.
DR PROSITE; PS51050; ZF_CW; 1.
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 non-
FT 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
