GenomeNet

Database: UniProt
Entry: Q9BZ95
LinkDB: Q9BZ95
Original site: Q9BZ95 
ID   NSD3_HUMAN              Reviewed;        1437 AA.
AC   Q9BZ95; B7ZL11; D3DSX1; Q1RMD3; Q3B796; Q6ZSA5; Q9BYU8; Q9BYU9;
AC   Q9H2M8; Q9H9W9; Q9NXA6;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   13-FEB-2019, entry version 169.
DE   RecName: Full=Histone-lysine N-methyltransferase NSD3;
DE            EC=2.1.1.43;
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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
RT   to a 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
RP   SPECIFICITY.
RX   PubMed=11374904; DOI=10.1006/geno.2001.6524;
RA   Angrand P.-O., Apiou F., Stewart F., Dutrillaux B., Losson R.,
RA   Chambon P.;
RT   "NSD3, a new SET domain-containing gene, maps to 8p12 and is amplified
RT   in 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
RP   SEQUENCE [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.,
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   [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.,
RA   Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
RA   Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA   Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
RA   Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
RA   DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
RA   Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
RA   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.,
RA   O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
RA   Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
RA   Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
RA   Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
RA   Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
RA   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.,
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   [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
RT   project: 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
RT   with 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.,
RA   Yang Z., 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   ENZYME 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
RT   H3K4 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
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA   Walther T.C., 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
RT   independent of pTEFb by recruiting multiple proteins, including
RT   NSD3.";
RL   Mol. Cell. Biol. 31:2641-2652(2011).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome 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
RP   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   [15]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-245; LYS-532 AND LYS-1151,
RP   AND 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
RP   MASS 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
RP   MASS 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
RT   replication stress reveals novel small ubiquitin-like modified target
RT   proteins and 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;
RP   LYS-502; LYS-532 AND LYS-628, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE 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-
RT   modification 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.,
RA   Zhou M.M., 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 methylates
CC       'Lys-4' and 'Lys-27' of histone H3. H3 'Lys-4' methylation
CC       represents a specific tag for epigenetic transcriptional
CC       activation, while 'Lys-27' is a mark for transcriptional
CC       repression. {ECO:0000269|PubMed:16682010}.
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:16682010};
CC   -!- SUBUNIT: Interacts with BRD4. {ECO:0000269|PubMed:21555454,
CC       ECO:0000269|PubMed:29176719}.
CC   -!- INTERACTION:
CC       Q13315:ATM; NbExp=3; IntAct=EBI-3390132, EBI-495465;
CC       Q9UER7:DAXX; NbExp=2; IntAct=EBI-3390132, EBI-77321;
CC       V9HWG0:HEL25; NbExp=3; IntAct=EBI-3390132, EBI-10183977;
CC       P09017:HOXC4; NbExp=2; IntAct=EBI-3390132, EBI-3923226;
CC       Q6P2C6:MLLT6; NbExp=3; IntAct=EBI-3390132, EBI-5773143;
CC       P41218:MNDA; NbExp=2; IntAct=EBI-3390132, EBI-2829677;
CC       Q06609:RAD51; NbExp=4; IntAct=EBI-3390132, EBI-297202;
CC       O95391:SLU7; NbExp=2; IntAct=EBI-3390132, EBI-750559;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome
CC       {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         Note=No experimental confirmation available.;
CC       Name=5;
CC         IsoId=Q9BZ95-5; Sequence=VSP_054489;
CC         Note=No experimental confirmation available.;
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
CC       lung 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)
CC       with NUP98. {ECO:0000269|PubMed:11986249}.
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=AAG44637.1; Type=Frameshift; Positions=Several; 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=Translation N-terminally extended.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/WHSC1L1NSD3ID42810ch8p11.html";
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   UniGene; Hs.434966; -.
DR   UniGene; Hs.608111; -.
DR   UniGene; Hs.655314; -.
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   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   ProteinModelPortal; Q9BZ95; -.
DR   SMR; Q9BZ95; -.
DR   BioGrid; 120250; 64.
DR   DIP; DIP-62074N; -.
DR   IntAct; Q9BZ95; 38.
DR   MINT; Q9BZ95; -.
DR   STRING; 9606.ENSP00000313983; -.
DR   BindingDB; Q9BZ95; -.
DR   ChEMBL; CHEMBL3108646; -.
DR   iPTMnet; Q9BZ95; -.
DR   PhosphoSitePlus; Q9BZ95; -.
DR   BioMuta; WHSC1L1; -.
DR   DMDM; 74761342; -.
DR   EPD; Q9BZ95; -.
DR   MaxQB; Q9BZ95; -.
DR   PaxDb; Q9BZ95; -.
DR   PeptideAtlas; Q9BZ95; -.
DR   PRIDE; Q9BZ95; -.
DR   ProteomicsDB; 79779; -.
DR   ProteomicsDB; 79780; -. [Q9BZ95-2]
DR   ProteomicsDB; 79781; -. [Q9BZ95-3]
DR   ProteomicsDB; 79782; -. [Q9BZ95-4]
DR   DNASU; 54904; -.
DR   Ensembl; ENST00000316985; ENSP00000313410; ENSG00000147548. [Q9BZ95-3]
DR   Ensembl; ENST00000317025; ENSP00000313983; ENSG00000147548. [Q9BZ95-1]
DR   Ensembl; ENST00000433384; ENSP00000393284; ENSG00000147548. [Q9BZ95-2]
DR   Ensembl; ENST00000527502; ENSP00000434730; ENSG00000147548. [Q9BZ95-5]
DR   GeneID; 54904; -.
DR   KEGG; hsa:54904; -.
DR   UCSC; uc003xli.4; human. [Q9BZ95-1]
DR   CTD; 54904; -.
DR   DisGeNET; 54904; -.
DR   EuPathDB; HostDB:ENSG00000147548.16; -.
DR   GeneCards; NSD3; -.
DR   HGNC; HGNC:12767; NSD3.
DR   HPA; CAB013721; -.
DR   HPA; HPA005659; -.
DR   HPA; HPA018893; -.
DR   MalaCards; NSD3; -.
DR   MIM; 607083; gene.
DR   neXtProt; NX_Q9BZ95; -.
DR   OpenTargets; ENSG00000147548; -.
DR   PharmGKB; PA37370; -.
DR   eggNOG; KOG1081; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00940000155355; -.
DR   HOVERGEN; HBG079979; -.
DR   InParanoid; Q9BZ95; -.
DR   KO; K11425; -.
DR   OMA; CKLESQD; -.
DR   OrthoDB; EOG091G00XD; -.
DR   PhylomeDB; Q9BZ95; -.
DR   TreeFam; TF329088; -.
DR   Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
DR   ChiTaRS; WHSC1L1; human.
DR   EvolutionaryTrace; Q9BZ95; -.
DR   GeneWiki; WHSC1L1; -.
DR   GenomeRNAi; 54904; -.
DR   PRO; PR:Q9BZ95; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   Bgee; ENSG00000147548; Expressed in 209 organ(s), highest expression level in kidney.
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:0003713; F:transcription coactivator activity; IMP:UniProtKB.
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; 3.30.40.10; -; 2.
DR   InterPro; IPR006560; AWS_dom.
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; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF17907; AWS; 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   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; Complete proteome;
KW   Isopeptide bond; Metal-binding; Methyltransferase; Nucleus;
KW   Phosphoprotein; Polymorphism; Proto-oncogene; Reference proteome;
KW   Repeat; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN         1   1437       Histone-lysine N-methyltransferase NSD3.
FT                                /FTId=PRO_0000259521.
FT   DOMAIN      270    333       PWWP 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00162}.
FT   DOMAIN      960   1022       PWWP 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00162}.
FT   DOMAIN     1093   1143       AWS. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00562}.
FT   DOMAIN     1145   1262       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN     1269   1285       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   ZN_FING     701    748       PHD-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   ZN_FING     749    805       PHD-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   ZN_FING     862    955       PHD-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   ZN_FING    1321   1368       PHD-type 4; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00146}.
FT   COILED     1033   1069       {ECO:0000255}.
FT   MOD_RES     150    150       Phosphoserine.
FT                                {ECO:0000244|PubMed:21406692}.
FT   MOD_RES     457    457       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     585    585       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     587    587       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     590    590       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     655    655       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     790    790       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   CROSSLNK    218    218       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25755297,
FT                                ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    245    245       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447,
FT                                ECO:0000244|PubMed:25772364,
FT                                ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    413    413       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    502    502       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    532    532       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447,
FT                                ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    628    628       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK   1151   1151       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   VAR_SEQ      67    129       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_021427.
FT   VAR_SEQ     620    645       ASEISDSCKPLKKRSRASTDVEMTSS -> SADRGVQGSVR
FT                                FSDSSVSAAIEETVD (in isoform 3).
FT                                {ECO:0000303|PubMed:11374904,
FT                                ECO:0000303|PubMed:11549311,
FT                                ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|Ref.3}.
FT                                /FTId=VSP_021428.
FT   VAR_SEQ     646   1437       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:11374904,
FT                                ECO:0000303|PubMed:11549311,
FT                                ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|Ref.3}.
FT                                /FTId=VSP_021429.
FT   VAR_SEQ     871    919       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:11374904}.
FT                                /FTId=VSP_021430.
FT   VAR_SEQ    1196   1206       Missing (in isoform 5).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_054489.
FT   VARIANT     186    186       T -> M (in dbSNP:rs13034).
FT                                /FTId=VAR_061215.
FT   VARIANT     383    383       R -> P (in dbSNP:rs2234552).
FT                                /FTId=VAR_028950.
FT   CONFLICT    436    436       G -> R (in Ref. 7; AAI15007).
FT                                {ECO:0000305}.
FT   CONFLICT    578    578       R -> G (in Ref. 7; AAI15007).
FT                                {ECO:0000305}.
FT   CONFLICT    829    829       G -> E (in Ref. 2; CAC28350/CAC28351).
FT                                {ECO:0000305}.
FT   CONFLICT    926    926       C -> R (in Ref. 7; AAI15007).
FT                                {ECO:0000305}.
FT   CONFLICT   1308   1308       K -> R (in Ref. 7; AAI15007).
FT                                {ECO:0000305}.
FT   CONFLICT   1430   1430       D -> G (in Ref. 7; AAI15007).
FT                                {ECO:0000305}.
FT   STRAND      154    158       {ECO:0000244|PDB:2NCZ}.
FT   STRAND      963    969       {ECO:0000244|PDB:4RXJ}.
FT   STRAND      972    978       {ECO:0000244|PDB:4RXJ}.
FT   TURN        981    983       {ECO:0000244|PDB:4RXJ}.
FT   HELIX       986    989       {ECO:0000244|PDB:4RXJ}.
FT   STRAND      997   1002       {ECO:0000244|PDB:4RXJ}.
FT   TURN       1003   1006       {ECO:0000244|PDB:4RXJ}.
FT   STRAND     1007   1012       {ECO:0000244|PDB:4RXJ}.
FT   HELIX      1013   1015       {ECO:0000244|PDB:4RXJ}.
FT   STRAND     1016   1018       {ECO:0000244|PDB:4RXJ}.
FT   STRAND     1025   1027       {ECO:0000244|PDB:2DAQ}.
FT   HELIX      1036   1052       {ECO:0000244|PDB:2DAQ}.
FT   TURN       1060   1062       {ECO:0000244|PDB:6CEN}.
FT   HELIX      1092   1094       {ECO:0000244|PDB:6CEN}.
FT   STRAND     1104   1106       {ECO:0000244|PDB:6CEN}.
FT   STRAND     1110   1112       {ECO:0000244|PDB:5UPD}.
FT   HELIX      1115   1118       {ECO:0000244|PDB:6CEN}.
FT   TURN       1125   1127       {ECO:0000244|PDB:6CEN}.
FT   HELIX      1131   1133       {ECO:0000244|PDB:6CEN}.
FT   HELIX      1138   1141       {ECO:0000244|PDB:6CEN}.
FT   STRAND     1147   1151       {ECO:0000244|PDB:6CEN}.
FT   STRAND     1153   1155       {ECO:0000244|PDB:6CEN}.
FT   STRAND     1157   1163       {ECO:0000244|PDB:6CEN}.
FT   STRAND     1170   1174       {ECO:0000244|PDB:6CEN}.
FT   STRAND     1177   1179       {ECO:0000244|PDB:6CEN}.
FT   HELIX      1181   1193       {ECO:0000244|PDB:6CEN}.
FT   STRAND     1201   1205       {ECO:0000244|PDB:6CEN}.
FT   STRAND     1208   1211       {ECO:0000244|PDB:6CEN}.
FT   TURN       1212   1214       {ECO:0000244|PDB:6CEN}.
FT   HELIX      1218   1221       {ECO:0000244|PDB:6CEN}.
FT   STRAND     1229   1237       {ECO:0000244|PDB:6CEN}.
FT   STRAND     1240   1249       {ECO:0000244|PDB:6CEN}.
FT   TURN       1325   1327       {ECO:0000244|PDB:4GNE}.
FT   STRAND     1331   1335       {ECO:0000244|PDB:4GNE}.
FT   HELIX      1348   1350       {ECO:0000244|PDB:4GNE}.
FT   STRAND     1357   1359       {ECO:0000244|PDB:4GNG}.
FT   HELIX      1363   1365       {ECO:0000244|PDB:4GNE}.
FT   TURN       1368   1370       {ECO:0000244|PDB:4GNE}.
FT   STRAND     1375   1377       {ECO:0000244|PDB:4GNG}.
FT   STRAND     1379   1382       {ECO:0000244|PDB:4GNE}.
FT   TURN       1387   1389       {ECO:0000244|PDB:4GNE}.
FT   TURN       1391   1393       {ECO:0000244|PDB:4GNF}.
FT   TURN       1398   1401       {ECO:0000244|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
//
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