NSD3_HUMAN
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 03-AUG-2022, entry version 190.
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; 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 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.
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. {ECO:0000269|PubMed:21555454,
CC ECO:0000269|PubMed:29176719}.
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 -!- 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="http://atlasgeneticsoncology.org/Genes/WHSC1L1NSD3ID42810ch8p11.html";
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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 SMR; Q9BZ95; -.
DR BioGRID; 120250; 91.
DR DIP; DIP-62074N; -.
DR IntAct; Q9BZ95; 50.
DR MINT; Q9BZ95; -.
DR STRING; 9606.ENSP00000313983; -.
DR BindingDB; Q9BZ95; -.
DR ChEMBL; CHEMBL3108646; -.
DR iPTMnet; Q9BZ95; -.
DR PhosphoSitePlus; Q9BZ95; -.
DR BioMuta; NSD3; -.
DR DMDM; 74761342; -.
DR EPD; Q9BZ95; -.
DR jPOST; Q9BZ95; -.
DR MassIVE; Q9BZ95; -.
DR MaxQB; Q9BZ95; -.
DR PaxDb; Q9BZ95; -.
DR PeptideAtlas; Q9BZ95; -.
DR PRIDE; 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 ABCD; Q9BZ95; 2 sequenced antibodies.
DR Antibodypedia; 984; 367 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 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; PRSFCKE; -.
DR OrthoDB; 507784at2759; -.
DR PhylomeDB; Q9BZ95; -.
DR TreeFam; TF329088; -.
DR BioCyc; MetaCyc:HS07446-MON; -.
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; 18 hits in 1099 CRISPR screens.
DR ChiTaRS; WHSC1L1; human.
DR EvolutionaryTrace; Q9BZ95; -.
DR GeneWiki; WHSC1L1; -.
DR GenomeRNAi; 54904; -.
DR Pharos; Q9BZ95; Tbio.
DR PRO; PR:Q9BZ95; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9BZ95; protein.
DR Bgee; ENSG00000147548; Expressed in pylorus and 186 other tissues.
DR ExpressionAtlas; Q9BZ95; baseline and differential.
DR Genevisible; Q9BZ95; HS.
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:0046975; F:histone methyltransferase activity (H3-K36 specific); IBA:GO_Central.
DR GO; GO:0018024; F:histone-lysine N-methyltransferase 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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016571; P:histone methylation; IDA:UniProtKB.
DR GO; GO:2001255; P:positive regulation of histone H3-K36 trimethylation; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 2.170.270.10; -; 1.
DR Gene3D; 3.30.40.10; -; 4.
DR IDEAL; IID00496; -.
DR InterPro; IPR006560; AWS_dom.
DR InterPro; IPR041306; C5HCH.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
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 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; SSF57903; 3.
DR SUPFAM; SSF82199; SSF82199; 1.
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.
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 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
