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Database: UniProt
Entry: O96028
LinkDB: O96028
Original site: O96028 
ID   NSD2_HUMAN              Reviewed;        1365 AA.
AC   O96028; A2A2T2; A2A2T3; A2A2T4; A7MCZ1; D3DVQ2; O96031; Q4VBY8;
AC   Q672J1; Q6IS00; Q86V01; Q9BZB4; Q9UI92; Q9UPR2;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   10-APR-2019, entry version 176.
DE   RecName: Full=Histone-lysine N-methyltransferase NSD2;
DE            EC=2.1.1.43;
DE   AltName: Full=Multiple myeloma SET domain-containing protein;
DE            Short=MMSET;
DE   AltName: Full=Nuclear SET domain-containing protein 2;
DE   AltName: Full=Protein trithorax-5;
DE   AltName: Full=Wolf-Hirschhorn syndrome candidate 1 protein;
GN   Name=NSD2 {ECO:0000312|HGNC:HGNC:12766};
GN   Synonyms=KIAA1090, MMSET, TRX5, WHSC1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), AND CHROMOSOMAL
RP   TRANSLOCATION WITH IGH.
RC   TISSUE=Myeloma;
RX   PubMed=9787135;
RA   Chesi M., Nardini E., Lim R.S.C., Smith K.D., Kuehl W.M.,
RA   Bergsagel P.L.;
RT   "The t(4;14) translocation in myeloma dysregulates both FGFR3 and a
RT   novel gene, MMSET, resulting in IgH/MMSET hybrid transcripts.";
RL   Blood 92:3025-3034(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 3 AND 5), TISSUE
RP   SPECIFICITY, AND CHROMOSOMAL TRANSLOCATION WITH IGH.
RX   PubMed=9618163; DOI=10.1093/hmg/7.7.1071;
RA   Stec I., Wright T.J., van Ommen G.-J.B., de Boer P.A.,
RA   van Haeringen A., Moorman A.F.M., Altherr M.R., den Dunnen J.T.;
RT   "WHSC1, a 90 kb SET domain-containing gene, expressed in early
RT   development and homologous to a Drosophila dysmorphy gene maps in the
RT   Wolf-Hirschhorn syndrome critical region and is fused to IgH in
RT   t(4;14) multiple myeloma.";
RL   Hum. Mol. Genet. 7:1071-1082(1998).
RN   [3]
RP   ERRATUM.
RA   Stec I., Wright T.J., van Ommen G.-J.B., de Boer P.A.,
RA   van Haeringen A., Moorman A.F.M., Altherr M.R., den Dunnen J.T.;
RL   Hum. Mol. Genet. 7:1527-1527(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, AND DNA-BINDING.
RX   PubMed=11152655; DOI=10.1165/ajrcmb.24.1.4224;
RA   Garlisi C.G., Uss A.S., Xiao H., Tian F., Sheridan K.E., Wang L.,
RA   Motasim Billah M., Egan R.W., Stranick K.S., Umland S.P.;
RT   "A unique mRNA initiated within a middle intron of WHSC1/MMSET encodes
RT   a DNA binding protein that suppresses human IL-5 transcription.";
RL   Am. J. Respir. Cell Mol. Biol. 24:90-98(2001).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), AND SUBCELLULAR LOCATION.
RX   PubMed=15677557; DOI=10.1182/blood-2004-09-3704;
RA   Keats J.J., Maxwell C.A., Taylor B.J., Hendzel M.J., Chesi M.,
RA   Bergsagel P.L., Larratt L.M., Mant M.J., Reiman T., Belch A.R.,
RA   Pilarski L.M.;
RT   "Overexpression of transcripts originating from the MMSET locus
RT   characterizes all t(4;14)(p16;q32)-positive multiple myeloma
RT   patients.";
RL   Blood 105:4060-4069(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Angrand P.-O., Valvatne H., Jeanmougin F., Adamson A.,
RA   van der Hoeven F., Olsen L., Tekotte H., Huang N., Poch O.,
RA   Lamerdin J., Chambon P., Losson R., Stewart A., Aasland R.;
RT   "Mammalian trithorax- and ASH1-like proteins: putative chromatin
RT   regulators which contain PHD fingers and SET domains.";
RL   Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA   Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N.,
RA   Tanaka A., Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XIV.
RT   The complete sequences of 100 new cDNA clones from brain which code
RT   for large proteins in vitro.";
RL   DNA Res. 6:197-205(1999).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Amygdala;
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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 4.";
RL   Nature 434:724-731(2005).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [11]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4 AND 6).
RC   TISSUE=Ovary, and Spleen;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [12]
RP   CHROMOSOMAL TRANSLOCATION WITH IGH.
RX   PubMed=10945609;
RA   Malgeri U., Baldini L., Perfetti V., Fabris S., Vignarelli M.C.,
RA   Colombo G., Lotti V., Compasso S., Bogni S., Lombardi L., Maiolo A.T.,
RA   Neri A.;
RT   "Detection of t(4;14)(p16.3;q32) chromosomal translocation in multiple
RT   myeloma by reverse transcription-polymerase chain reaction analysis of
RT   IGH-MMSET fusion transcripts.";
RL   Cancer Res. 60:4058-4061(2000).
RN   [13]
RP   CHROMOSOMAL TRANSLOCATION WITH IGH.
RX   PubMed=11337357; DOI=10.1016/S0002-9440(10)64115-6;
RA   Perfetti V., Coluccia A.M., Intini D., Malgeri U., Vignarelli M.C.,
RA   Casarini S., Merlini G., Neri A.;
RT   "Translocation T(4;14)(p16.3;q32) is a recurrent genetic lesion in
RT   primary amyloidosis.";
RL   Am. J. Pathol. 158:1599-1603(2001).
RN   [14]
RP   CHROMOSOMAL TRANSLOCATION WITH IGH.
RX   PubMed=12433679; DOI=10.1182/blood-2002-09-2801;
RA   Santra M., Zhan F., Tian E., Barlogie B., Shaughnessy J. Jr.;
RT   "A subset of multiple myeloma harboring the t(4;14)(p16;q32)
RT   translocation lacks FGFR3 expression but maintains an IGH/MMSET fusion
RT   transcript.";
RL   Blood 101:2374-2376(2003).
RN   [15]
RP   CHROMOSOMAL TRANSLOCATION WITH IGH.
RX   PubMed=15257719; DOI=10.1111/j.1365-2141.2004.05048.x;
RA   Intini D., Fabris S., Storlazzi T., Otsuki T., Ciceri G., Verdelli D.,
RA   Lombardi L., Rocchi M., Neri A.;
RT   "Identification of a novel IGH-MMSET fusion transcript in a human
RT   myeloma cell line with the t(4;14)(p16.3;q32) chromosomal
RT   translocation.";
RL   Br. J. Haematol. 126:437-439(2004).
RN   [16]
RP   FUNCTION.
RX   PubMed=16115125; DOI=10.1111/j.1365-2141.2005.05664.x;
RA   Hudlebusch H.R., Theilgaard-Moench K., Lodahl M., Johnsen H.E.,
RA   Rasmussen T.;
RT   "Identification of ID-1 as a potential target gene of MMSET in
RT   multiple myeloma.";
RL   Br. J. Haematol. 130:700-708(2005).
RN   [17]
RP   SUBCELLULAR LOCATION.
RX   PubMed=16197452; DOI=10.1111/j.1365-2141.2005.05741.x;
RA   Todoerti K., Ronchetti D., Agnelli L., Castellani S., Marelli S.,
RA   Deliliers G.L., Zanella A., Lombardi L., Neri A.;
RT   "Transcription repression activity is associated with the type I
RT   isoform of the MMSET gene involved in t(4;14) in multiple myeloma.";
RL   Br. J. Haematol. 131:214-218(2005).
RN   [18]
RP   INVOLVEMENT IN WHS.
RX   PubMed=15734578; DOI=10.1016/j.tig.2005.01.008;
RA   Bergemann A.D., Cole F., Hirschhorn K.;
RT   "The etiology of Wolf-Hirschhorn syndrome.";
RL   Trends Genet. 21:188-195(2005).
RN   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-544, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [20]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=18172012; DOI=10.1128/MCB.02130-07;
RA   Kim J.Y., Kee H.J., Choe N.W., Kim S.M., Eom G.H., Baek H.J., Kook H.,
RA   Kook H., Seo S.B.;
RT   "Multiple-myeloma-related WHSC1/MMSET isoform RE-IIBP is a histone
RT   methyltransferase with transcriptional repression activity.";
RL   Mol. Cell. Biol. 28:2023-2034(2008).
RN   [21]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121 AND THR-544, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [22]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [23]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-110; THR-114; SER-121;
RP   SER-376 AND THR-544, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP   SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [24]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-544, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [25]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-110; SER-121; SER-172;
RP   THR-422; THR-544 AND SER-614, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE 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   [26]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Colon carcinoma;
RX   PubMed=24129315; DOI=10.1074/mcp.O113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
RA   Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
RA   Vemulapalli V., Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
CC   -!- FUNCTION: Histone methyltransferase with histone H3 'Lys-27'
CC       (H3K27me) methyltransferase activity. Isoform 2 may act as a
CC       transcription regulator that binds DNA and suppresses IL5
CC       transcription through HDAC recruitment.
CC       {ECO:0000269|PubMed:11152655, ECO:0000269|PubMed:16115125,
CC       ECO:0000269|PubMed:18172012}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.43;
CC         Evidence={ECO:0000269|PubMed:18172012};
CC   -!- INTERACTION:
CC       P10275:AR; NbExp=5; IntAct=EBI-2693298, EBI-608057;
CC       Q14676:MDC1; NbExp=3; IntAct=EBI-15910280, EBI-495644;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
CC       ProRule:PRU00267, ECO:0000269|PubMed:15677557,
CC       ECO:0000269|PubMed:16197452}. Chromosome {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Isoform 4: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=7;
CC       Name=1;
CC         IsoId=O96028-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O96028-2; Sequence=VSP_021414, VSP_021423;
CC         Note=Ref.7 (BAA83042) and Ref.11 (AAI52413) sequences are in
CC         conflict in position: 26:M->V. {ECO:0000305};
CC       Name=3;
CC         IsoId=O96028-3; Sequence=VSP_021419, VSP_021422;
CC       Name=4; Synonyms=RE-IIBP, IL-5 promoter REII-region-binding
CC       protein;
CC         IsoId=O96028-4; Sequence=VSP_021413;
CC       Name=5;
CC         IsoId=O96028-5; Sequence=VSP_021420, VSP_021421;
CC       Name=6;
CC         IsoId=O96028-6; Sequence=VSP_021417, VSP_021418;
CC         Note=No experimental confirmation available.;
CC       Name=7;
CC         IsoId=O96028-7; Sequence=VSP_021415, VSP_021416;
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC       {ECO:0000269|PubMed:9618163}.
CC   -!- DISEASE: Note=A chromosomal aberration involving NSD2 is a cause
CC       of multiple myeloma tumors. Translocation t(4;14)(p16.3;q32.3)
CC       with IgH.
CC   -!- DISEASE: Note=NSD2 is located in the Wolf-Hirschhorn syndrome
CC       (WHS) critical region. WHS results from by sub-telomeric deletions
CC       in the short arm of chromosome 4. NSD2 is deleted in every case,
CC       however deletion of linked genes contributes to both the severity
CC       of the core characteristics and the presence of the additional
CC       syndromic problems.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. SET2 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA83042.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/WHSC1ID42809ch4p16.html";
DR   EMBL; AF071593; AAC24150.1; -; mRNA.
DR   EMBL; AF071594; AAC24151.1; -; mRNA.
DR   EMBL; AF083386; AAD19343.1; -; mRNA.
DR   EMBL; AF083387; AAD21770.1; -; mRNA.
DR   EMBL; AF083388; AAD21771.1; -; mRNA.
DR   EMBL; AF083389; AAD19344.1; -; mRNA.
DR   EMBL; AF083390; AAD19345.1; -; mRNA.
DR   EMBL; AF083391; AAD19346.1; -; mRNA.
DR   EMBL; AF178206; AAF23369.1; -; Genomic_DNA.
DR   EMBL; AF178199; AAF23369.1; JOINED; Genomic_DNA.
DR   EMBL; AF178198; AAF23369.1; JOINED; Genomic_DNA.
DR   EMBL; AF178202; AAF23369.1; JOINED; Genomic_DNA.
DR   EMBL; AF178204; AAF23369.1; JOINED; Genomic_DNA.
DR   EMBL; AF178205; AAF23369.1; JOINED; Genomic_DNA.
DR   EMBL; AF178203; AAF23369.1; JOINED; Genomic_DNA.
DR   EMBL; AF178201; AAF23369.1; JOINED; Genomic_DNA.
DR   EMBL; AF178200; AAF23369.1; JOINED; Genomic_DNA.
DR   EMBL; AF178219; AAF23370.1; -; Genomic_DNA.
DR   EMBL; AF178198; AAF23370.1; JOINED; Genomic_DNA.
DR   EMBL; AF178199; AAF23370.1; JOINED; Genomic_DNA.
DR   EMBL; AF178200; AAF23370.1; JOINED; Genomic_DNA.
DR   EMBL; AF178202; AAF23370.1; JOINED; Genomic_DNA.
DR   EMBL; AF178204; AAF23370.1; JOINED; Genomic_DNA.
DR   EMBL; AF178207; AAF23370.1; JOINED; Genomic_DNA.
DR   EMBL; AF178216; AAF23370.1; JOINED; Genomic_DNA.
DR   EMBL; AF178215; AAF23370.1; JOINED; Genomic_DNA.
DR   EMBL; AF178214; AAF23370.1; JOINED; Genomic_DNA.
DR   EMBL; AF178213; AAF23370.1; JOINED; Genomic_DNA.
DR   EMBL; AF178212; AAF23370.1; JOINED; Genomic_DNA.
DR   EMBL; AF178211; AAF23370.1; JOINED; Genomic_DNA.
DR   EMBL; AF178210; AAF23370.1; JOINED; Genomic_DNA.
DR   EMBL; AF178209; AAF23370.1; JOINED; Genomic_DNA.
DR   EMBL; AF178208; AAF23370.1; JOINED; Genomic_DNA.
DR   EMBL; AF178218; AAF23370.1; JOINED; Genomic_DNA.
DR   EMBL; AF178217; AAF23370.1; JOINED; Genomic_DNA.
DR   EMBL; AF178205; AAF23370.1; JOINED; Genomic_DNA.
DR   EMBL; AF178203; AAF23370.1; JOINED; Genomic_DNA.
DR   EMBL; AF178201; AAF23370.1; JOINED; Genomic_DNA.
DR   EMBL; AF330040; AAK00344.1; -; mRNA.
DR   EMBL; AY694128; AAU09264.1; -; mRNA.
DR   EMBL; AJ007042; CAB45386.1; -; mRNA.
DR   EMBL; AB029013; BAA83042.2; ALT_INIT; mRNA.
DR   EMBL; AK289697; BAF82386.1; -; mRNA.
DR   EMBL; AC105448; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL132868; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471131; EAW82548.1; -; Genomic_DNA.
DR   EMBL; CH471131; EAW82552.1; -; Genomic_DNA.
DR   EMBL; CH471131; EAW82557.1; -; Genomic_DNA.
DR   EMBL; CH471131; EAW82553.1; -; Genomic_DNA.
DR   EMBL; CH471131; EAW82556.1; -; Genomic_DNA.
DR   EMBL; BC052254; AAH52254.1; -; mRNA.
DR   EMBL; BC070176; AAH70176.1; -; mRNA.
DR   EMBL; BC094825; AAH94825.2; -; mRNA.
DR   EMBL; BC141815; AAI41816.1; -; mRNA.
DR   EMBL; BC152412; AAI52413.1; -; mRNA.
DR   CCDS; CCDS3356.1; -. [O96028-3]
DR   CCDS; CCDS33940.1; -. [O96028-1]
DR   CCDS; CCDS46999.1; -. [O96028-5]
DR   RefSeq; NP_001035889.1; NM_001042424.2. [O96028-1]
DR   RefSeq; NP_015627.1; NM_007331.1. [O96028-5]
DR   RefSeq; NP_579877.1; NM_133330.2. [O96028-1]
DR   RefSeq; NP_579878.1; NM_133331.2. [O96028-1]
DR   RefSeq; NP_579889.1; NM_133334.2. [O96028-3]
DR   RefSeq; NP_579890.1; NM_133335.3. [O96028-1]
DR   RefSeq; XP_005248058.1; XM_005248001.3. [O96028-1]
DR   RefSeq; XP_005248062.1; XM_005248005.2. [O96028-3]
DR   RefSeq; XP_006713977.1; XM_006713914.3. [O96028-3]
DR   RefSeq; XP_011511859.1; XM_011513557.2. [O96028-1]
DR   RefSeq; XP_011511862.1; XM_011513560.2. [O96028-4]
DR   RefSeq; XP_016864076.1; XM_017008587.1. [O96028-4]
DR   RefSeq; XP_016864077.1; XM_017008588.1. [O96028-4]
DR   UniGene; Hs.113876; -.
DR   PDB; 5LSU; X-ray; 2.14 A; A/B=973-1203.
DR   PDB; 5VC8; X-ray; 1.80 A; A/B=211-350.
DR   PDBsum; 5LSU; -.
DR   PDBsum; 5VC8; -.
DR   ProteinModelPortal; O96028; -.
DR   SMR; O96028; -.
DR   BioGrid; 113306; 72.
DR   DIP; DIP-57224N; -.
DR   IntAct; O96028; 6.
DR   MINT; O96028; -.
DR   STRING; 9606.ENSP00000372351; -.
DR   BindingDB; O96028; -.
DR   ChEMBL; CHEMBL3108645; -.
DR   iPTMnet; O96028; -.
DR   PhosphoSitePlus; O96028; -.
DR   BioMuta; NSD2; -.
DR   EPD; O96028; -.
DR   jPOST; O96028; -.
DR   MaxQB; O96028; -.
DR   PaxDb; O96028; -.
DR   PeptideAtlas; O96028; -.
DR   PRIDE; O96028; -.
DR   ProteomicsDB; 51216; -.
DR   ProteomicsDB; 51217; -. [O96028-2]
DR   ProteomicsDB; 51218; -. [O96028-3]
DR   ProteomicsDB; 51219; -. [O96028-4]
DR   ProteomicsDB; 51220; -. [O96028-5]
DR   ProteomicsDB; 51221; -. [O96028-6]
DR   ProteomicsDB; 51222; -. [O96028-7]
DR   DNASU; 7468; -.
DR   Ensembl; ENST00000312087; ENSP00000308780; ENSG00000109685. [O96028-3]
DR   Ensembl; ENST00000353275; ENSP00000329167; ENSG00000109685. [O96028-3]
DR   Ensembl; ENST00000382888; ENSP00000372344; ENSG00000109685. [O96028-2]
DR   Ensembl; ENST00000382891; ENSP00000372347; ENSG00000109685. [O96028-1]
DR   Ensembl; ENST00000382892; ENSP00000372348; ENSG00000109685. [O96028-1]
DR   Ensembl; ENST00000382895; ENSP00000372351; ENSG00000109685. [O96028-1]
DR   Ensembl; ENST00000398261; ENSP00000381311; ENSG00000109685. [O96028-3]
DR   Ensembl; ENST00000420906; ENSP00000399251; ENSG00000109685. [O96028-5]
DR   Ensembl; ENST00000436793; ENSP00000416725; ENSG00000109685. [O96028-7]
DR   Ensembl; ENST00000503128; ENSP00000425761; ENSG00000109685. [O96028-3]
DR   Ensembl; ENST00000508803; ENSP00000423972; ENSG00000109685. [O96028-1]
DR   Ensembl; ENST00000512700; ENSP00000427516; ENSG00000109685. [O96028-7]
DR   Ensembl; ENST00000514045; ENSP00000421681; ENSG00000109685. [O96028-5]
DR   GeneID; 7468; -.
DR   KEGG; hsa:7468; -.
DR   UCSC; uc003gdy.2; human. [O96028-1]
DR   CTD; 7468; -.
DR   DisGeNET; 7468; -.
DR   EuPathDB; HostDB:ENSG00000109685.17; -.
DR   GeneCards; NSD2; -.
DR   GeneReviews; NSD2; -.
DR   HGNC; HGNC:12766; NSD2.
DR   HPA; CAB068246; -.
DR   HPA; CAB068247; -.
DR   HPA; HPA015801; -.
DR   MalaCards; NSD2; -.
DR   MIM; 602952; gene.
DR   neXtProt; NX_O96028; -.
DR   OpenTargets; ENSG00000109685; -.
DR   Orphanet; 280; Wolf-Hirschhorn syndrome.
DR   PharmGKB; PA37369; -.
DR   eggNOG; KOG1081; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00940000157429; -.
DR   HOGENOM; HOG000230892; -.
DR   HOVERGEN; HBG079978; -.
DR   InParanoid; O96028; -.
DR   KO; K11424; -.
DR   OMA; EYVMVHR; -.
DR   OrthoDB; 507784at2759; -.
DR   PhylomeDB; O96028; -.
DR   TreeFam; TF329088; -.
DR   BRENDA; 2.1.1.43; 2681.
DR   Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
DR   Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR   Reactome; R-HSA-5693571; Nonhomologous End-Joining (NHEJ).
DR   Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
DR   Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
DR   SIGNOR; O96028; -.
DR   ChiTaRS; WHSC1; human.
DR   GeneWiki; WHSC1; -.
DR   GenomeRNAi; 7468; -.
DR   PRO; PR:O96028; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   Bgee; ENSG00000109685; Expressed in 223 organ(s), highest expression level in testis.
DR   ExpressionAtlas; O96028; baseline and differential.
DR   Genevisible; O96028; HS.
DR   GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:HPA.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); IBA:GO_Central.
DR   GO; GO:0042799; F:histone methyltransferase activity (H4-K20 specific); TAS:Reactome.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; TAS:Reactome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:Ensembl.
DR   GO; GO:0003289; P:atrial septum primum morphogenesis; IEA:Ensembl.
DR   GO; GO:0003290; P:atrial septum secundum morphogenesis; IEA:Ensembl.
DR   GO; GO:0060348; P:bone development; IEA:Ensembl.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; TAS:Reactome.
DR   GO; GO:0003149; P:membranous septum morphogenesis; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0048298; P:positive regulation of isotype switching to IgA isotypes; IEA:Ensembl.
DR   GO; GO:2001032; P:regulation of double-strand break repair via nonhomologous end joining; IEA:Ensembl.
DR   GO; GO:0070201; P:regulation of establishment of protein localization; IEA:Ensembl.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   Gene3D; 1.10.30.10; -; 1.
DR   Gene3D; 3.30.40.10; -; 4.
DR   InterPro; IPR006560; AWS_dom.
DR   InterPro; IPR009071; HMG_box_dom.
DR   InterPro; IPR036910; HMG_box_dom_sf.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR000313; PWWP_dom.
DR   InterPro; IPR001214; SET_dom.
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; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF17907; AWS; 1.
DR   Pfam; PF00505; HMG_box; 1.
DR   Pfam; PF00855; PWWP; 2.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00570; AWS; 1.
DR   SMART; SM00398; HMG; 1.
DR   SMART; SM00249; PHD; 4.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00293; PWWP; 2.
DR   SMART; SM00184; RING; 2.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF47095; SSF47095; 1.
DR   SUPFAM; SSF57903; SSF57903; 3.
DR   PROSITE; PS51215; AWS; 1.
DR   PROSITE; PS50118; HMG_BOX_2; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50812; PWWP; 2.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 2.
DR   PROSITE; PS50016; ZF_PHD_2; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Chromatin regulator;
KW   Chromosomal rearrangement; Chromosome; Complete proteome; Cytoplasm;
KW   DNA-binding; Metal-binding; Methyltransferase; Nucleus;
KW   Phosphoprotein; Proto-oncogene; Reference proteome; Repeat;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase; Zinc; Zinc-finger.
FT   CHAIN         1   1365       Histone-lysine N-methyltransferase NSD2.
FT                                /FTId=PRO_0000259519.
FT   DOMAIN      222    286       PWWP 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00162}.
FT   DOMAIN      880    942       PWWP 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00162}.
FT   DOMAIN     1011   1061       AWS. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00562}.
FT   DOMAIN     1063   1180       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN     1187   1203       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   DNA_BIND    453    521       HMG box. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00267}.
FT   ZN_FING     667    713       PHD-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   ZN_FING     714    770       PHD-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   ZN_FING     831    875       PHD-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   ZN_FING    1239   1286       PHD-type 4; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00146}.
FT   MOD_RES     110    110       Phosphothreonine.
FT                                {ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES     114    114       Phosphothreonine.
FT                                {ECO:0000244|PubMed:19690332}.
FT   MOD_RES     121    121       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES     172    172       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     376    376       Phosphoserine.
FT                                {ECO:0000244|PubMed:19690332}.
FT   MOD_RES     422    422       Phosphothreonine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     544    544       Phosphothreonine.
FT                                {ECO:0000244|PubMed:17081983,
FT                                ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES     614    614       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   VAR_SEQ       1    781       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:11152655,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_021413.
FT   VAR_SEQ       1    652       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:10470851,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_021414.
FT   VAR_SEQ     255    273       QKKSARQYHVQFFGDAPER -> IFKSKKFEHLKTSQIVLK
FT                                D (in isoform 7).
FT                                {ECO:0000303|PubMed:15677557}.
FT                                /FTId=VSP_021415.
FT   VAR_SEQ     274   1365       Missing (in isoform 7).
FT                                {ECO:0000303|PubMed:15677557}.
FT                                /FTId=VSP_021416.
FT   VAR_SEQ     472    484       VAEHPDASGEEIE -> STKLCFMLASFRI (in
FT                                isoform 6).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_021417.
FT   VAR_SEQ     485   1365       Missing (in isoform 6).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_021418.
FT   VAR_SEQ     628    647       VSDSPGDEPSESPYESADET -> LLWEPTPVKLDLNPAAL
FT                                YCT (in isoform 3).
FT                                {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:9618163,
FT                                ECO:0000303|PubMed:9787135}.
FT                                /FTId=VSP_021419.
FT   VAR_SEQ     629    629       S -> K (in isoform 5).
FT                                {ECO:0000303|PubMed:9618163}.
FT                                /FTId=VSP_021420.
FT   VAR_SEQ     630   1365       Missing (in isoform 5).
FT                                {ECO:0000303|PubMed:9618163}.
FT                                /FTId=VSP_021421.
FT   VAR_SEQ     648   1365       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:9618163,
FT                                ECO:0000303|PubMed:9787135}.
FT                                /FTId=VSP_021422.
FT   VAR_SEQ     653    712       VSSKKSERGVTAKKEYVCQLCEKPGSLLLCEGPCCGAFHLA
FT                                CLGLSRRPEGRFTCSECAS -> MAGSFCWRMLGLVSKVGN
FT                                RARCFSSMAASEEELLDFSGSELQFNSCSLHLSLHPFFNFL
FT                                L (in isoform 2).
FT                                {ECO:0000303|PubMed:10470851,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_021423.
FT   CONFLICT    210    210       T -> A (in Ref. 5; AAU09264).
FT                                {ECO:0000305}.
FT   STRAND      225    228       {ECO:0000244|PDB:5VC8}.
FT   STRAND      236    240       {ECO:0000244|PDB:5VC8}.
FT   TURN        244    246       {ECO:0000244|PDB:5VC8}.
FT   STRAND      249    252       {ECO:0000244|PDB:5VC8}.
FT   STRAND      260    266       {ECO:0000244|PDB:5VC8}.
FT   STRAND      273    277       {ECO:0000244|PDB:5VC8}.
FT   HELIX       278    280       {ECO:0000244|PDB:5VC8}.
FT   STRAND      281    283       {ECO:0000244|PDB:5VC8}.
FT   HELIX       287    289       {ECO:0000244|PDB:5VC8}.
FT   HELIX       290    300       {ECO:0000244|PDB:5VC8}.
FT   HELIX       304    311       {ECO:0000244|PDB:5VC8}.
FT   HELIX       316    333       {ECO:0000244|PDB:5VC8}.
FT   HELIX       337    344       {ECO:0000244|PDB:5VC8}.
FT   HELIX       346    348       {ECO:0000244|PDB:5VC8}.
FT   HELIX       974    981       {ECO:0000244|PDB:5LSU}.
FT   HELIX      1010   1012       {ECO:0000244|PDB:5LSU}.
FT   STRAND     1022   1024       {ECO:0000244|PDB:5LSU}.
FT   HELIX      1033   1036       {ECO:0000244|PDB:5LSU}.
FT   TURN       1043   1045       {ECO:0000244|PDB:5LSU}.
FT   TURN       1047   1050       {ECO:0000244|PDB:5LSU}.
FT   HELIX      1056   1059       {ECO:0000244|PDB:5LSU}.
FT   STRAND     1065   1069       {ECO:0000244|PDB:5LSU}.
FT   STRAND     1071   1081       {ECO:0000244|PDB:5LSU}.
FT   STRAND     1088   1092       {ECO:0000244|PDB:5LSU}.
FT   STRAND     1095   1097       {ECO:0000244|PDB:5LSU}.
FT   HELIX      1099   1111       {ECO:0000244|PDB:5LSU}.
FT   STRAND     1119   1123       {ECO:0000244|PDB:5LSU}.
FT   STRAND     1126   1129       {ECO:0000244|PDB:5LSU}.
FT   TURN       1130   1132       {ECO:0000244|PDB:5LSU}.
FT   HELIX      1136   1139       {ECO:0000244|PDB:5LSU}.
FT   STRAND     1147   1155       {ECO:0000244|PDB:5LSU}.
FT   STRAND     1158   1167       {ECO:0000244|PDB:5LSU}.
FT   HELIX      1179   1181       {ECO:0000244|PDB:5LSU}.
FT   STRAND     1183   1185       {ECO:0000244|PDB:5LSU}.
SQ   SEQUENCE   1365 AA;  152258 MW;  7B3128E1FA893AAA CRC64;
     MEFSIKQSPL SVQSVVKCIK MKQAPEILGS ANGKTPSCEV NRECSVFLSK AQLSSSLQEG
     VMQKFNGHDA LPFIPADKLK DLTSRVFNGE PGAHDAKLRF ESQEMKGIGT PPNTTPIKNG
     SPEIKLKITK TYMNGKPLFE SSICGDSAAD VSQSEENGQK PENKARRNRK RSIKYDSLLE
     QGLVEAALVS KISSPSDKKI PAKKESCPNT GRDKDHLLKY NVGDLVWSKV SGYPWWPCMV
     SADPLLHSYT KLKGQKKSAR QYHVQFFGDA PERAWIFEKS LVAFEGEGQF EKLCQESAKQ
     APTKAEKIKL LKPISGKLRA QWEMGIVQAE EAASMSVEER KAKFTFLYVG DQLHLNPQVA
     KEAGIAAESL GEMAESSGVS EEAAENPKSV REECIPMKRR RRAKLCSSAE TLESHPDIGK
     STPQKTAEAD PRRGVGSPPG RKKTTVSMPR SRKGDAASQF LVFCQKHRDE VVAEHPDASG
     EEIEELLRSQ WSLLSEKQRA RYNTKFALVA PVQAEEDSGN VNGKKRNHTK RIQDPTEDAE
     AEDTPRKRLR TDKHSLRKRD TITDKTARTS SYKAMEAASS LKSQAATKNL SDACKPLKKR
     NRASTAASSA LGFSKSSSPS ASLTENEVSD SPGDEPSESP YESADETQTE VSVSSKKSER
     GVTAKKEYVC QLCEKPGSLL LCEGPCCGAF HLACLGLSRR PEGRFTCSEC ASGIHSCFVC
     KESKTDVKRC VVTQCGKFYH EACVKKYPLT VFESRGFRCP LHSCVSCHAS NPSNPRPSKG
     KMMRCVRCPV AYHSGDACLA AGCSVIASNS IICTAHFTAR KGKRHHAHVN VSWCFVCSKG
     GSLLCCESCP AAFHPDCLNI EMPDGSWFCN DCRAGKKLHF QDIIWVKLGN YRWWPAEVCH
     PKNVPPNIQK MKHEIGEFPV FFFGSKDYYW THQARVFPYM EGDRGSRYQG VRGIGRVFKN
     ALQEAEARFR EIKLQREARE TQESERKPPP YKHIKVNKPY GKVQIYTADI SEIPKCNCKP
     TDENPCGFDS ECLNRMLMFE CHPQVCPAGE FCQNQCFTKR QYPETKIIKT DGKGWGLVAK
     RDIRKGEFVN EYVGELIDEE ECMARIKHAH ENDITHFYML TIDKDRIIDA GPKGNYSRFM
     NHSCQPNCET LKWTVNGDTR VGLFAVCDIP AGTELTFNYN LDCLGNEKTV CRCGASNCSG
     FLGDRPKTST TLSSEEKGKK TKKKTRRRRA KGEGKRQSED ECFRCGDGGQ LVLCDRKFCT
     KAYHLSCLGL GKRPFGKWEC PWHHCDVCGK PSTSFCHLCP NSFCKEHQDG TAFSCTPDGR
     SYCCEHDLGA ASVRSTKTEK PPPEPGKPKG KRRRRRGWRR VTEGK
//
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