ID NSD3_HUMAN Reviewed; 1437 AA. AC Q9BZ95; B7ZL11; D3DSX1; Q1RMD3; Q3B796; Q6ZSA5; Q9BYU8; Q9BYU9; Q9H2M8; AC Q9H9W9; Q9NXA6; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 27-MAR-2024, entry version 199. DE RecName: Full=Histone-lysine N-methyltransferase NSD3; DE EC=2.1.1.370 {ECO:0000269|PubMed:16682010}; DE EC=2.1.1.371 {ECO:0000269|PubMed:16682010}; DE AltName: Full=Nuclear SET domain-containing protein 3; DE AltName: Full=Protein whistle; DE AltName: Full=WHSC1-like 1 isoform 9 with methyltransferase activity to lysine; DE AltName: Full=Wolf-Hirschhorn syndrome candidate 1-like protein 1; DE Short=WHSC1-like protein 1; GN Name=NSD3 {ECO:0000312|HGNC:HGNC:12767}; Synonyms=WHSC1L1; GN ORFNames=DC28; 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 [MRNA] (ISOFORMS 1 AND 3). RX PubMed=11549311; DOI=10.1006/geno.2001.6581; RA Stec I., van Ommen G.-J.B., den Dunnen J.T.; RT "WHSC1L1, on human chromosome 8p11.2, closely resembles WHSC1 and maps to a RT duplicated region shared with 4p16.3."; RL Genomics 76:5-8(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND TISSUE SPECIFICITY. RX PubMed=11374904; DOI=10.1006/geno.2001.6524; RA Angrand P.-O., Apiou F., Stewart F., Dutrillaux B., Losson R., Chambon P.; RT "NSD3, a new SET domain-containing gene, maps to 8p12 and is amplified in RT human breast cancer cell lines."; RL Genomics 74:79-88(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Dendritic cell; RA Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.; RT "A novel gene from human dendritic cells."; RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 1-383 (ISOFORM 4). RC TISSUE=Brain, and Teratocarcinoma; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16421571; DOI=10.1038/nature04406; RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., RA Platzer M., Shimizu N., Lander E.S.; RT "DNA sequence and analysis of human chromosome 8."; RL Nature 439:331-335(2006). RN [6] 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 5). RC TISSUE=Brain, and Placenta; 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 [8] RP CHROMOSOMAL TRANSLOCATION WITH NUP98. RX PubMed=11986249; DOI=10.1182/blood.v99.10.3857; RA Rosati R., La Starza R., Veronese A., Aventin A., Schwienbacher C., RA Vallespi T., Negrini M., Martelli M.F., Mecucci C.; RT "NUP98 is fused to the NSD3 gene in acute myeloid leukemia associated with RT t(8;11)(p11.2;p15)."; RL Blood 99:3857-3860(2002). RN [9] RP INVOLVEMENT IN NSCLC. RX PubMed=15983384; DOI=10.1073/pnas.0504126102; RA Tonon G., Wong K.-K., Maulik G., Brennan C., Feng B., Zhang Y., RA Khatry D.B., Protopopov A., You M.J., Aguirre A.J., Martin E.S., Yang Z., RA Ji H., Chin L., Depinho R.A.; RT "High-resolution genomic profiles of human lung cancer."; RL Proc. Natl. Acad. Sci. U.S.A. 102:9625-9630(2005). RN [10] RP CATALYTIC ACTIVITY, AND FUNCTION. RX PubMed=16682010; DOI=10.1016/j.bbrc.2006.04.095; RA Kim S.M., Kee H.J., Eom G.H., Choe N.W., Kim J.Y., Kim Y.S., Kim S.K., RA Kook H., Kook H., Seo S.B.; RT "Characterization of a novel WHSC1-associated SET domain protein with H3K4 RT and H3K27 methyltransferase activity."; RL Biochem. Biophys. Res. Commun. 345:318-323(2006). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-790, 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 [12] RP INTERACTION WITH BRD4. RX PubMed=21555454; DOI=10.1128/mcb.01341-10; RA Rahman S., Sowa M.E., Ottinger M., Smith J.A., Shi Y., Harper J.W., RA Howley P.M.; RT "The Brd4 extraterminal domain confers transcription activation independent RT of pTEFb by recruiting multiple proteins, including NSD3."; RL Mol. Cell. Biol. 31:2641-2652(2011). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-457; SER-585; SER-587; RP SER-590 AND SER-655, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [15] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-245; LYS-532 AND LYS-1151, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [16] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-245, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033; RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., RA Vertegaal A.C.; RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."; RL Cell Rep. 10:1778-1791(2015). RN [17] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-218, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25755297; DOI=10.1074/mcp.o114.044792; RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., RA Vertegaal A.C.; RT "System-wide analysis of SUMOylation dynamics in response to replication RT stress reveals novel small ubiquitin-like modified target proteins and RT acceptor lysines relevant for genome stability."; RL Mol. Cell. Proteomics 14:1419-1434(2015). RN [18] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-218; LYS-245; LYS-413; LYS-502; RP LYS-532 AND LYS-628, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [19] RP INTERACTION WITH BRD4. RX PubMed=29176719; DOI=10.1038/s41598-017-16588-8; RA Konuma T., Yu D., Zhao C., Ju Y., Sharma R., Ren C., Zhang Q., Zhou M.M., RA Zeng L.; RT "Structural Mechanism of the Oxygenase JMJD6 Recognition by the RT Extraterminal (ET) Domain of BRD4."; RL Sci. Rep. 7:16272-16272(2017). RN [20] RP INTERACTION WITH BRD3, AND DOMAIN. RX PubMed=29567837; DOI=10.1074/jbc.ra117.000678; RA Wai D.C.C., Szyszka T.N., Campbell A.E., Kwong C., Wilkinson-White L.E., RA Silva A.P.G., Low J.K.K., Kwan A.H., Gamsjaeger R., Chalmers J.D., RA Patrick W.M., Lu B., Vakoc C.R., Blobel G.A., Mackay J.P.; RT "The BRD3 ET domain recognizes a short peptide motif through a mechanism RT that is conserved across chromatin remodelers and transcriptional RT regulators."; RL J. Biol. Chem. 293:7160-7175(2018). RN [21] RP STRUCTURE BY NMR OF 957-1053. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of second PWWP domain of WHSC1L1 protein."; RL Submitted (DEC-2005) to the PDB data bank. RN [22] {ECO:0007744|PDB:7JYN} RP STRUCTURE BY NMR OF 148-184 IN COMPLEX WITH BRD3, AND INTERACTION WITH RP BRD3. RX PubMed=33592170; DOI=10.1016/j.str.2021.01.010; RA Aiyer S., Swapna G.V.T., Ma L.C., Liu G., Hao J., Chalmers G., Jacobs B.C., RA Montelione G.T., Roth M.J.; RT "A common binding motif in the ET domain of BRD3 forms polymorphic RT structural interfaces with host and viral proteins."; RL Structure 29:886-898(2021). CC -!- FUNCTION: Histone methyltransferase. Preferentially dimethylates 'Lys- CC 4' and 'Lys-27' of histone H3 forming H3K2me2 and H3K27me2. H3 'Lys-4' CC methylation represents a specific tag for epigenetic transcriptional CC activation, while 'Lys-27' is a mark for transcriptional repression. CC {ECO:0000269|PubMed:16682010}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl(4)-[histone H3] + 2 S-adenosyl-L-methionine = 2 H(+) + CC N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + 2 S-adenosyl-L- CC homocysteine; Xref=Rhea:RHEA:64448, Rhea:RHEA-COMP:15540, Rhea:RHEA- CC COMP:15547, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61976; EC=2.1.1.370; CC Evidence={ECO:0000269|PubMed:16682010}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl(27)-[histone H3] + 2 S-adenosyl-L-methionine = 2 H(+) CC + N(6),N(6)-dimethyl-L-lysyl(27)-[histone H3] + 2 S-adenosyl-L- CC homocysteine; Xref=Rhea:RHEA:64452, Rhea:RHEA-COMP:15539, Rhea:RHEA- CC COMP:15548, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61976; EC=2.1.1.371; CC Evidence={ECO:0000269|PubMed:16682010}; CC -!- SUBUNIT: Interacts with BRD4 (PubMed:21555454, PubMed:29176719). CC Interacts (via KIKL motif) with BRD3 (via NET domain) (PubMed:29567837, CC PubMed:33592170). {ECO:0000269|PubMed:21555454, CC ECO:0000269|PubMed:29176719, ECO:0000269|PubMed:29567837, CC ECO:0000269|PubMed:33592170}. CC -!- INTERACTION: CC Q9BZ95; Q13315: ATM; NbExp=3; IntAct=EBI-3390132, EBI-495465; CC Q9BZ95; P45973: CBX5; NbExp=2; IntAct=EBI-3390132, EBI-78219; CC Q9BZ95; Q9UER7: DAXX; NbExp=2; IntAct=EBI-3390132, EBI-77321; CC Q9BZ95; P03372: ESR1; NbExp=3; IntAct=EBI-3390132, EBI-78473; CC Q9BZ95; V9HWG0: HEL25; NbExp=3; IntAct=EBI-3390132, EBI-10183977; CC Q9BZ95; P09017: HOXC4; NbExp=2; IntAct=EBI-3390132, EBI-3923226; CC Q9BZ95; Q6P2C6: MLLT6; NbExp=3; IntAct=EBI-3390132, EBI-5773143; CC Q9BZ95; P41218: MNDA; NbExp=2; IntAct=EBI-3390132, EBI-2829677; CC Q9BZ95; Q06609: RAD51; NbExp=4; IntAct=EBI-3390132, EBI-297202; CC Q9BZ95; O95391: SLU7; NbExp=2; IntAct=EBI-3390132, EBI-750559; CC Q9BZ95-3; P45973: CBX5; NbExp=3; IntAct=EBI-22002759, EBI-78219; CC Q9BZ95-3; P22607: FGFR3; NbExp=3; IntAct=EBI-22002759, EBI-348399; CC Q9BZ95-3; P01112: HRAS; NbExp=3; IntAct=EBI-22002759, EBI-350145; CC Q9BZ95-3; P02545: LMNA; NbExp=3; IntAct=EBI-22002759, EBI-351935; CC Q9BZ95-3; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-22002759, EBI-5235340; CC Q9BZ95-3; P37173: TGFBR2; NbExp=3; IntAct=EBI-22002759, EBI-296151; CC Q9BZ95-3; Q9Y649; NbExp=3; IntAct=EBI-22002759, EBI-25900580; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=Q9BZ95-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9BZ95-2; Sequence=VSP_021430; CC Name=3; CC IsoId=Q9BZ95-3; Sequence=VSP_021428, VSP_021429; CC Name=4; CC IsoId=Q9BZ95-4; Sequence=VSP_021427; CC Name=5; CC IsoId=Q9BZ95-5; Sequence=VSP_054489; CC -!- TISSUE SPECIFICITY: Highly expressed in brain, heart and skeletal CC muscle. Expressed at lower level in liver and lung. CC {ECO:0000269|PubMed:11374904}. CC -!- DOMAIN: The KIKL motif recognizes and binds the NET domain of BRD3. CC {ECO:0000269|PubMed:29567837}. CC -!- DISEASE: Note=Defects in NSD3 may be involved in non small cell lung CC carcinomas (NSCLC). Amplified or overexpressed in NSCLC. CC {ECO:0000269|PubMed:15983384}. CC -!- DISEASE: Note=A chromosomal aberration involving NSD3 is found in CC childhood acute myeloid leukemia. Translocation t(8;11)(p11.2;p15) with CC NUP98. {ECO:0000269|PubMed:11986249}. CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase CC superfamily. Histone-lysine methyltransferase family. SET2 subfamily. CC {ECO:0000255|PROSITE-ProRule:PRU00190}. CC -!- SEQUENCE CAUTION: CC Sequence=AAG44637.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAI07735.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC Sequence=BAA91110.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/42810/WHSC1L1NSD3"; 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; AF332468; AAK00354.1; -; mRNA. DR EMBL; AF332469; AAK00355.1; -; mRNA. DR EMBL; AJ295990; CAC28350.1; -; mRNA. DR EMBL; AJ295991; CAC28351.1; -; mRNA. DR EMBL; AJ295992; CAC28352.1; -; mRNA. DR EMBL; AF255649; AAG44637.1; ALT_FRAME; mRNA. DR EMBL; AK000360; BAA91110.1; ALT_INIT; mRNA. DR EMBL; AK022560; BAB14099.1; -; mRNA. DR EMBL; AK127594; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; CH471080; EAW63320.1; -; Genomic_DNA. DR EMBL; CH471080; EAW63321.1; -; Genomic_DNA. DR EMBL; BC012059; AAH12059.1; -; mRNA. DR EMBL; BC062631; AAH62631.1; -; mRNA. DR EMBL; BC101717; AAI01718.1; -; mRNA. DR EMBL; BC107734; AAI07735.1; ALT_SEQ; mRNA. DR EMBL; BC113469; AAI13470.1; -; mRNA. DR EMBL; BC115006; AAI15007.1; -; mRNA. DR EMBL; BC143510; AAI43511.1; -; mRNA. DR EMBL; AC087362; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC087623; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS43729.1; -. [Q9BZ95-1] DR CCDS; CCDS6105.1; -. [Q9BZ95-3] DR RefSeq; NP_060248.2; NM_017778.2. [Q9BZ95-3] DR RefSeq; NP_075447.1; NM_023034.1. [Q9BZ95-1] DR PDB; 2DAQ; NMR; -; A=957-1053. DR PDB; 2NCZ; NMR; -; B=152-163. DR PDB; 2ND1; NMR; -; B=593-605. DR PDB; 4GND; X-ray; 2.27 A; A/C=1310-1413. DR PDB; 4GNE; X-ray; 1.47 A; A=1310-1413. DR PDB; 4GNF; X-ray; 1.55 A; A=1310-1413. DR PDB; 4GNG; X-ray; 1.73 A; A/D=1310-1413. DR PDB; 4RXJ; X-ray; 2.10 A; A=953-1064. DR PDB; 5UPD; X-ray; 1.80 A; A=1054-1285. DR PDB; 6CEN; X-ray; 1.61 A; A=1058-1285. DR PDB; 6G24; X-ray; 2.10 A; A=263-398. DR PDB; 6G25; X-ray; 1.43 A; A=263-398. DR PDB; 6G27; X-ray; 1.65 A; A=263-398. DR PDB; 6G29; X-ray; 1.70 A; A=263-398. DR PDB; 6G2B; X-ray; 1.61 A; A=263-398. DR PDB; 6G2C; X-ray; 1.76 A; A=263-398. DR PDB; 6G2E; X-ray; 1.85 A; A=263-398. DR PDB; 6G2F; X-ray; 1.74 A; A=263-398. DR PDB; 6G2O; X-ray; 1.81 A; A=263-398. DR PDB; 6G3P; X-ray; 2.80 A; A/B/C/D=247-398. DR PDB; 6G3T; X-ray; 2.53 A; A/B/C/D=247-398. DR PDB; 7CRP; EM; 3.20 A; I=680-1437. DR PDB; 7CRQ; EM; 3.15 A; I/L=680-1437. DR PDB; 7CRR; EM; 3.48 A; I=680-1437. DR PDB; 7JYN; NMR; -; B=148-184. DR PDBsum; 2DAQ; -. DR PDBsum; 2NCZ; -. DR PDBsum; 2ND1; -. DR PDBsum; 4GND; -. DR PDBsum; 4GNE; -. DR PDBsum; 4GNF; -. DR PDBsum; 4GNG; -. DR PDBsum; 4RXJ; -. DR PDBsum; 5UPD; -. DR PDBsum; 6CEN; -. DR PDBsum; 6G24; -. DR PDBsum; 6G25; -. DR PDBsum; 6G27; -. DR PDBsum; 6G29; -. DR PDBsum; 6G2B; -. DR PDBsum; 6G2C; -. DR PDBsum; 6G2E; -. DR PDBsum; 6G2F; -. DR PDBsum; 6G2O; -. DR PDBsum; 6G3P; -. DR PDBsum; 6G3T; -. DR PDBsum; 7CRP; -. DR PDBsum; 7CRQ; -. DR PDBsum; 7CRR; -. DR PDBsum; 7JYN; -. DR AlphaFoldDB; Q9BZ95; -. DR EMDB; EMD-30455; -. DR EMDB; EMD-30456; -. DR EMDB; EMD-30457; -. DR SASBDB; Q9BZ95; -. DR SMR; Q9BZ95; -. DR BioGRID; 120250; 109. DR DIP; DIP-62074N; -. DR IntAct; Q9BZ95; 50. DR MINT; Q9BZ95; -. DR STRING; 9606.ENSP00000313983; -. DR BindingDB; Q9BZ95; -. DR ChEMBL; CHEMBL3108646; -. DR GlyGen; Q9BZ95; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9BZ95; -. DR PhosphoSitePlus; Q9BZ95; -. DR SwissPalm; Q9BZ95; -. DR BioMuta; NSD3; -. DR DMDM; 74761342; -. DR EPD; Q9BZ95; -. DR jPOST; Q9BZ95; -. DR MassIVE; Q9BZ95; -. DR MaxQB; Q9BZ95; -. DR PaxDb; 9606-ENSP00000313983; -. DR PeptideAtlas; Q9BZ95; -. DR ProteomicsDB; 7208; -. DR ProteomicsDB; 79779; -. [Q9BZ95-1] DR ProteomicsDB; 79780; -. [Q9BZ95-2] DR ProteomicsDB; 79781; -. [Q9BZ95-3] DR ProteomicsDB; 79782; -. [Q9BZ95-4] DR Pumba; Q9BZ95; -. DR ABCD; Q9BZ95; 2 sequenced antibodies. DR Antibodypedia; 984; 419 antibodies from 35 providers. DR DNASU; 54904; -. DR Ensembl; ENST00000316985.7; ENSP00000313410.3; ENSG00000147548.17. [Q9BZ95-3] DR Ensembl; ENST00000317025.13; ENSP00000313983.7; ENSG00000147548.17. [Q9BZ95-1] DR Ensembl; ENST00000433384.6; ENSP00000393284.2; ENSG00000147548.17. [Q9BZ95-2] DR Ensembl; ENST00000527502.5; ENSP00000434730.1; ENSG00000147548.17. [Q9BZ95-5] DR GeneID; 54904; -. DR KEGG; hsa:54904; -. DR MANE-Select; ENST00000317025.13; ENSP00000313983.7; NM_023034.2; NP_075447.1. DR UCSC; uc003xli.4; human. [Q9BZ95-1] DR AGR; HGNC:12767; -. DR CTD; 54904; -. DR DisGeNET; 54904; -. DR GeneCards; NSD3; -. DR HGNC; HGNC:12767; NSD3. DR HPA; ENSG00000147548; Low tissue specificity. DR MIM; 607083; gene. DR neXtProt; NX_Q9BZ95; -. DR OpenTargets; ENSG00000147548; -. DR PharmGKB; PA37370; -. DR VEuPathDB; HostDB:ENSG00000147548; -. DR eggNOG; KOG1081; Eukaryota. DR GeneTree; ENSGT00940000155355; -. DR HOGENOM; CLU_004494_2_1_1; -. DR InParanoid; Q9BZ95; -. DR OMA; DAGWPTY; -. DR OrthoDB; 950362at2759; -. DR PhylomeDB; Q9BZ95; -. DR TreeFam; TF329088; -. DR BioCyc; MetaCyc:HS07446-MONOMER; -. DR BRENDA; 2.1.1.356; 2681. DR BRENDA; 2.1.1.370; 2681. DR BRENDA; 2.1.1.371; 2681. DR BRENDA; 2.1.1.372; 2681. DR PathwayCommons; Q9BZ95; -. DR Reactome; R-HSA-3214841; PKMTs methylate histone lysines. DR SignaLink; Q9BZ95; -. DR SIGNOR; Q9BZ95; -. DR BioGRID-ORCS; 54904; 19 hits in 1176 CRISPR screens. DR ChiTaRS; WHSC1L1; human. DR EvolutionaryTrace; Q9BZ95; -. DR GeneWiki; WHSC1L1; -. DR GenomeRNAi; 54904; -. DR Pharos; Q9BZ95; Tchem. DR PRO; PR:Q9BZ95; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; Q9BZ95; Protein. DR Bgee; ENSG00000147548; Expressed in pylorus and 188 other cell types or tissues. DR ExpressionAtlas; Q9BZ95; baseline and differential. DR GO; GO:0000785; C:chromatin; IBA:GO_Central. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IMP:UniProtKB. DR GO; GO:0140938; F:histone H3 methyltransferase activity; TAS:Reactome. DR GO; GO:0140952; F:histone H3K27 dimethyltransferase activity; IDA:UniProtKB. DR GO; GO:0140951; F:histone H3K27 trimethyltransferase activity; IDA:UniProtKB. DR GO; GO:0046975; F:histone H3K36 methyltransferase activity; IMP:UniProtKB. DR GO; GO:0140946; F:histone H3K4 dimethyltransferase activity; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0140537; F:transcription regulator activator activity; IMP:UniProtKB. DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IMP:UniProtKB. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central. DR CDD; cd15649; PHD1_NSD3; 1. DR CDD; cd15652; PHD2_NSD3; 1. DR CDD; cd15655; PHD3_NSD3; 1. DR CDD; cd15658; PHD4_NSD3; 1. DR CDD; cd15661; PHD5_NSD3; 1. DR CDD; cd20163; PWWP_NSD3_rpt1; 1. DR CDD; cd20166; PWWP_NSD3_rpt2; 1. DR CDD; cd19212; SET_NSD3; 1. DR Gene3D; 2.30.30.140; -; 2. DR Gene3D; 2.170.270.10; SET domain; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 4. DR IDEAL; IID00496; -. DR InterPro; IPR006560; AWS_dom. DR InterPro; IPR041306; C5HCH. DR InterPro; IPR047456; PHD2_NSD3. DR InterPro; IPR047458; PHD4_NSD3. DR InterPro; IPR047527; PHD5_NSD3. DR InterPro; IPR003616; Post-SET_dom. DR InterPro; IPR000313; PWWP_dom. DR InterPro; IPR047451; PWWP_NSD3_rpt1. DR InterPro; IPR047453; PWWP_NSD3_rpt2. DR InterPro; IPR001214; SET_dom. DR InterPro; IPR046341; SET_dom_sf. DR InterPro; IPR047461; SET_NSD3. DR InterPro; IPR019786; Zinc_finger_PHD-type_CS. DR InterPro; IPR011011; Znf_FYVE_PHD. DR InterPro; IPR001965; Znf_PHD. DR InterPro; IPR019787; Znf_PHD-finger. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR PANTHER; PTHR22884:SF473; HISTONE-LYSINE N-METHYLTRANSFERASE NSD3; 1. DR PANTHER; PTHR22884; SET DOMAIN PROTEINS; 1. DR Pfam; PF17907; AWS; 1. DR Pfam; PF17982; C5HCH; 1. DR Pfam; PF00855; PWWP; 2. DR Pfam; PF00856; SET; 1. DR SMART; SM00570; AWS; 1. DR SMART; SM00249; PHD; 5. DR SMART; SM00508; PostSET; 1. DR SMART; SM00293; PWWP; 2. DR SMART; SM00317; SET; 1. DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 3. DR SUPFAM; SSF82199; SET domain; 1. DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 2. DR PROSITE; PS51215; AWS; 1. DR PROSITE; PS50868; POST_SET; 1. DR PROSITE; PS50812; PWWP; 2. DR PROSITE; PS50280; SET; 1. DR PROSITE; PS01359; ZF_PHD_1; 1. DR PROSITE; PS50016; ZF_PHD_2; 2. DR Genevisible; Q9BZ95; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Chromatin regulator; KW Chromosomal rearrangement; Chromosome; Coiled coil; Isopeptide bond; KW Metal-binding; Methyltransferase; Nucleus; Phosphoprotein; Proto-oncogene; KW Reference proteome; Repeat; S-adenosyl-L-methionine; Transcription; KW Transcription regulation; Transferase; Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..1437 FT /note="Histone-lysine N-methyltransferase NSD3" FT /id="PRO_0000259521" FT DOMAIN 270..333 FT /note="PWWP 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162" FT DOMAIN 960..1022 FT /note="PWWP 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162" FT DOMAIN 1093..1143 FT /note="AWS" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00562" FT DOMAIN 1145..1262 FT /note="SET" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190" FT DOMAIN 1269..1285 FT /note="Post-SET" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155" FT ZN_FING 701..748 FT /note="PHD-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146" FT ZN_FING 749..805 FT /note="PHD-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146" FT ZN_FING 862..955 FT /note="PHD-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146" FT ZN_FING 1321..1368 FT /note="PHD-type 4; atypical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146" FT REGION 121..157 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 181..252 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 344..365 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 406..465 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 540..696 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 1033..1069 FT /evidence="ECO:0000255" FT MOTIF 154..157 FT /note="KIKL" FT /evidence="ECO:0000269|PubMed:29567837" FT COMPBIAS 124..142 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 202..246 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 348..365 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 425..446 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 447..465 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 540..574 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 575..604 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 607..621 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 639..658 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 666..696 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 150 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 457 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 585 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 587 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 590 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 655 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 790 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT CROSSLNK 218 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 245 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT CROSSLNK 413 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 502 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 532 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 628 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1151 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447" FT VAR_SEQ 67..129 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_021427" FT VAR_SEQ 620..645 FT /note="ASEISDSCKPLKKRSRASTDVEMTSS -> SADRGVQGSVRFSDSSVSAAIE FT ETVD (in isoform 3)" FT /evidence="ECO:0000303|PubMed:11374904, FT ECO:0000303|PubMed:11549311, ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3" FT /id="VSP_021428" FT VAR_SEQ 646..1437 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:11374904, FT ECO:0000303|PubMed:11549311, ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3" FT /id="VSP_021429" FT VAR_SEQ 871..919 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11374904" FT /id="VSP_021430" FT VAR_SEQ 1196..1206 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_054489" FT VARIANT 186 FT /note="T -> M (in dbSNP:rs13034)" FT /id="VAR_061215" FT VARIANT 383 FT /note="R -> P (in dbSNP:rs2234552)" FT /id="VAR_028950" FT CONFLICT 436 FT /note="G -> R (in Ref. 7; AAI15007)" FT /evidence="ECO:0000305" FT CONFLICT 578 FT /note="R -> G (in Ref. 7; AAI15007)" FT /evidence="ECO:0000305" FT CONFLICT 829 FT /note="G -> E (in Ref. 2; CAC28350/CAC28351)" FT /evidence="ECO:0000305" FT CONFLICT 926 FT /note="C -> R (in Ref. 7; AAI15007)" FT /evidence="ECO:0000305" FT CONFLICT 1308 FT /note="K -> R (in Ref. 7; AAI15007)" FT /evidence="ECO:0000305" FT CONFLICT 1430 FT /note="D -> G (in Ref. 7; AAI15007)" FT /evidence="ECO:0000305" FT STRAND 154..158 FT /evidence="ECO:0007829|PDB:2NCZ" FT STRAND 163..165 FT /evidence="ECO:0007829|PDB:7JYN" FT STRAND 169..171 FT /evidence="ECO:0007829|PDB:7JYN" FT HELIX 252..255 FT /evidence="ECO:0007829|PDB:6G3P" FT STRAND 273..276 FT /evidence="ECO:0007829|PDB:6G25" FT STRAND 284..288 FT /evidence="ECO:0007829|PDB:6G25" FT TURN 292..294 FT /evidence="ECO:0007829|PDB:6G25" FT STRAND 297..300 FT /evidence="ECO:0007829|PDB:6G25" FT STRAND 302..304 FT /evidence="ECO:0007829|PDB:6G3T" FT STRAND 306..312 FT /evidence="ECO:0007829|PDB:6G25" FT STRAND 314..316 FT /evidence="ECO:0007829|PDB:6G25" FT STRAND 318..323 FT /evidence="ECO:0007829|PDB:6G25" FT HELIX 324..326 FT /evidence="ECO:0007829|PDB:6G25" FT STRAND 327..329 FT /evidence="ECO:0007829|PDB:6G25" FT HELIX 333..335 FT /evidence="ECO:0007829|PDB:6G25" FT HELIX 336..341 FT /evidence="ECO:0007829|PDB:6G25" FT HELIX 350..357 FT /evidence="ECO:0007829|PDB:6G3P" FT HELIX 362..379 FT /evidence="ECO:0007829|PDB:6G25" FT HELIX 383..390 FT /evidence="ECO:0007829|PDB:6G25" FT STRAND 963..969 FT /evidence="ECO:0007829|PDB:4RXJ" FT STRAND 972..978 FT /evidence="ECO:0007829|PDB:4RXJ" FT TURN 981..983 FT /evidence="ECO:0007829|PDB:4RXJ" FT HELIX 986..989 FT /evidence="ECO:0007829|PDB:4RXJ" FT STRAND 997..1002 FT /evidence="ECO:0007829|PDB:4RXJ" FT TURN 1003..1006 FT /evidence="ECO:0007829|PDB:4RXJ" FT STRAND 1007..1012 FT /evidence="ECO:0007829|PDB:4RXJ" FT HELIX 1013..1015 FT /evidence="ECO:0007829|PDB:4RXJ" FT STRAND 1016..1018 FT /evidence="ECO:0007829|PDB:4RXJ" FT STRAND 1025..1027 FT /evidence="ECO:0007829|PDB:2DAQ" FT HELIX 1036..1052 FT /evidence="ECO:0007829|PDB:2DAQ" FT TURN 1060..1062 FT /evidence="ECO:0007829|PDB:6CEN" FT HELIX 1092..1094 FT /evidence="ECO:0007829|PDB:6CEN" FT STRAND 1104..1106 FT /evidence="ECO:0007829|PDB:6CEN" FT STRAND 1110..1112 FT /evidence="ECO:0007829|PDB:5UPD" FT HELIX 1115..1118 FT /evidence="ECO:0007829|PDB:6CEN" FT TURN 1125..1127 FT /evidence="ECO:0007829|PDB:6CEN" FT HELIX 1131..1133 FT /evidence="ECO:0007829|PDB:6CEN" FT HELIX 1138..1141 FT /evidence="ECO:0007829|PDB:6CEN" FT STRAND 1147..1151 FT /evidence="ECO:0007829|PDB:6CEN" FT STRAND 1153..1155 FT /evidence="ECO:0007829|PDB:6CEN" FT STRAND 1157..1163 FT /evidence="ECO:0007829|PDB:6CEN" FT STRAND 1170..1174 FT /evidence="ECO:0007829|PDB:6CEN" FT STRAND 1177..1179 FT /evidence="ECO:0007829|PDB:6CEN" FT HELIX 1181..1193 FT /evidence="ECO:0007829|PDB:6CEN" FT STRAND 1201..1205 FT /evidence="ECO:0007829|PDB:6CEN" FT STRAND 1208..1211 FT /evidence="ECO:0007829|PDB:6CEN" FT TURN 1212..1214 FT /evidence="ECO:0007829|PDB:6CEN" FT HELIX 1218..1221 FT /evidence="ECO:0007829|PDB:6CEN" FT STRAND 1229..1237 FT /evidence="ECO:0007829|PDB:6CEN" FT STRAND 1240..1249 FT /evidence="ECO:0007829|PDB:6CEN" FT STRAND 1253..1255 FT /evidence="ECO:0007829|PDB:7CRQ" FT STRAND 1262..1264 FT /evidence="ECO:0007829|PDB:7CRQ" FT STRAND 1277..1279 FT /evidence="ECO:0007829|PDB:7CRQ" FT TURN 1325..1327 FT /evidence="ECO:0007829|PDB:4GNE" FT STRAND 1331..1335 FT /evidence="ECO:0007829|PDB:4GNE" FT HELIX 1348..1350 FT /evidence="ECO:0007829|PDB:4GNE" FT STRAND 1357..1359 FT /evidence="ECO:0007829|PDB:4GNG" FT HELIX 1363..1365 FT /evidence="ECO:0007829|PDB:4GNE" FT TURN 1368..1370 FT /evidence="ECO:0007829|PDB:4GNE" FT STRAND 1375..1377 FT /evidence="ECO:0007829|PDB:4GNG" FT STRAND 1379..1382 FT /evidence="ECO:0007829|PDB:4GNE" FT TURN 1387..1389 FT /evidence="ECO:0007829|PDB:4GNE" FT TURN 1391..1393 FT /evidence="ECO:0007829|PDB:4GNF" FT TURN 1398..1401 FT /evidence="ECO:0007829|PDB:4GNE" SQ SEQUENCE 1437 AA; 161613 MW; 87E54997A996F7CC CRC64; MDFSFSFMQG IMGNTIQQPP QLIDSANIRQ EDAFDNNSDI AEDGGQTPYE ATLQQGFQYP ATTEDLPPLT NGYPSSISVY ETQTKYQSYN QYPNGSANGF GAVRNFSPTD YYHSEIPNTR PHEILEKPSP PQPPPPPSVP QTVIPKKTGS PEIKLKITKT IQNGRELFES SLCGDLLNEV QASEHTKSKH ESRKEKRKKS NKHDSSRSEE RKSHKIPKLE PEEQNRPNER VDTVSEKPRE EPVLKEEAPV QPILSSVPTT EVSTGVKFQV GDLVWSKVGT YPWWPCMVSS DPQLEVHTKI NTRGAREYHV QFFSNQPERA WVHEKRVREY KGHKQYEELL AEATKQASNH SEKQKIRKPR PQRERAQWDI GIAHAEKALK MTREERIEQY TFIYIDKQPE EALSQAKKSV ASKTEVKKTR RPRSVLNTQP EQTNAGEVAS SLSSTEIRRH SQRRHTSAEE EEPPPVKIAW KTAAARKSLP ASITMHKGSL DLQKCNMSPV VKIEQVFALQ NATGDGKFID QFVYSTKGIG NKTEISVRGQ DRLIISTPNQ RNEKPTQSVS SPEATSGSTG SVEKKQQRRS IRTRSESEKS TEVVPKKKIK KEQVETVPQA TVKTGLQKGA SEISDSCKPL KKRSRASTDV EMTSSAYRDT SDSDSRGLSD LQVGFGKQVD SPSATADADV SDVQSMDSSL SRRGTGMSKK DTVCQICESS GDSLIPCEGE CCKHFHLECL GLASLPDSKF ICMECKTGQH PCFSCKVSGK DVKRCSVGAC GKFYHEACVR KFPTAIFESK GFRCPQHCCS ACSMEKDIHK ASKGRMMRCL RCPVAYHSGD ACIAAGSMLV SSYILICSNH SKRSSNSSAV NVGFCFVCAR GLIVQDHSDP MFSSYAYKSH YLLNESNRAE LMKLPMIPSS SASKKKCEKG GRLLCCESCP ASFHPECLSI EMPEGCWNCN DCKAGKKLHY KQIVWVKLGN YRWWPAEICN PRSVPLNIQG LKHDLGDFPV FFFGSHDYYW VHQGRVFPYV EGDKSFAEGQ TSINKTFKKA LEEAAKRFQE LKAQRESKEA LEIEKNSRKP PPYKHIKANK VIGKVQIQVA DLSEIPRCNC KPADENPCGL ESECLNRMLQ YECHPQVCPA GDRCQNQCFT KRLYPDAEII KTERRGWGLR TKRSIKKGEF VNEYVGELID EEECRLRIKR AHENSVTNFY MLTVTKDRII DAGPKGNYSR FMNHSCNPNC ETQKWTVNGD VRVGLFALCD IPAGMELTFN YNLDCLGNGR TECHCGADNC SGFLGVRPKS ACASTNEEKA KNAKLKQKRR KIKTEPKQMH EDYCFQCGDG GELVMCDKKD CPKAYHLLCL NLTQPPYGKW ECPWHQCDEC SSAAVSFCEF CPHSFCKDHE KGALVPSALE GRLCCSEHDP MAPVSPEYWS KIKCKWESQD HGEEVKE //