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Database: UniProt
Entry: Q9H7B4
LinkDB: Q9H7B4
Original site: Q9H7B4 
ID   SMYD3_HUMAN             Reviewed;         428 AA.
AC   Q9H7B4; A8K0P0; B1AN38; Q86TL8; Q8N5Z6; Q96AI5;
DT   16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 4.
DT   10-APR-2019, entry version 160.
DE   RecName: Full=Histone-lysine N-methyltransferase SMYD3;
DE            EC=2.1.1.43;
DE   AltName: Full=SET and MYND domain-containing protein 3;
DE   AltName: Full=Zinc finger MYND domain-containing protein 1;
GN   Name=SMYD3; Synonyms=ZMYND1, ZNFN3A1;
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] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH HSPCA; HELZ
RP   AND POLR2A, AND DNA-BINDING.
RX   PubMed=15235609; DOI=10.1038/ncb1151;
RA   Hamamoto R., Furukawa Y., Morita M., Iimura Y., Silva F.P., Li M.,
RA   Yagyu R., Nakamura Y.;
RT   "SMYD3 encodes a histone methyltransferase involved in the
RT   proliferation of cancer cells.";
RL   Nat. Cell Biol. 6:731-740(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
RA   Sha J.H., Zhou Z.M., Xu M.;
RL   Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Colon, and Melanoma;
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   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [8]
RP   CATALYTIC ACTIVITY, AND FUNCTION.
RX   PubMed=22419068; DOI=10.4161/epi.19506;
RA   Van Aller G.S., Reynoird N., Barbash O., Huddleston M., Liu S.,
RA   Zmoos A.F., McDevitt P., Sinnamon R., Le B., Mas G., Annan R.,
RA   Sage J., Garcia B.A., Tummino P.J., Gozani O., Kruger R.G.;
RT   "Smyd3 regulates cancer cell phenotypes and catalyzes histone H4
RT   lysine 5 methylation.";
RL   Epigenetics 7:340-343(2012).
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA   Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA   Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-
RT   terminal acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-22, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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   [11]
RP   INTERACTION WITH HSP90AA1, DOMAIN C-TERMINAL, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=25738358; DOI=10.18632/oncotarget.2970;
RA   Brown M.A., Foreman K., Harriss J., Das C., Zhu L., Edwards M.,
RA   Shaaban S., Tucker H.;
RT   "C-terminal domain of SMYD3 serves as a unique HSP90-regulated motif
RT   in oncogenesis.";
RL   Oncotarget 6:4005-4019(2015).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH
RP   S-ADENOSYL-L-METHIONINE AND ZINC IONS.
RG   Structural genomics consortium (SGC);
RT   "Crystal structure of human histone-lysine n-methyltransferase SMYD3
RT   in complex with S-adenosyl-L-methionine.";
RL   Submitted (APR-2010) to the PDB data bank.
CC   -!- FUNCTION: Histone methyltransferase. Specifically methylates 'Lys-
CC       4' of histone H3, inducing di- and tri-methylation, but not
CC       monomethylation (PubMed:15235609, PubMed:22419068). Also
CC       methylates 'Lys-5' of histone H4 (PubMed:22419068). Plays an
CC       important role in transcriptional activation as a member of an RNA
CC       polymerase complex (PubMed:15235609). Binds DNA containing 5'-
CC       CCCTCC-3' or 5'-GAGGGG-3' sequences (PubMed:15235609).
CC       {ECO:0000269|PubMed:15235609, ECO:0000269|PubMed:22419068}.
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:0000255|PROSITE-ProRule:PRU00907,
CC         ECO:0000269|PubMed:15235609, ECO:0000269|PubMed:22419068};
CC   -!- ACTIVITY REGULATION: Histone methyltransferase activity strongly
CC       stimulated by HSPCA. {ECO:0000269|PubMed:15235609}.
CC   -!- SUBUNIT: Interacts with HSPCA (PubMed:15235609). Interacts with
CC       HELZ (PubMed:15235609). Interacts with POLR2A; the interaction may
CC       be indirect and may be mediated by HELZ (PubMed:15235609).
CC       Interacts with HSP90AA1; this interaction enhances SMYD3 histone-
CC       lysine N-methyltransferase (PubMed:25738358).
CC       {ECO:0000269|PubMed:15235609, ECO:0000269|PubMed:25738358}.
CC   -!- INTERACTION:
CC       Q9Y2U5:MAP3K2; NbExp=3; IntAct=EBI-16204880, EBI-357393;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15235609}.
CC       Nucleus {ECO:0000269|PubMed:15235609,
CC       ECO:0000269|PubMed:25738358}. Note=Mainly cytoplasmic when cells
CC       are arrested at G0/G1. Accumulates in the nucleus at S phase and
CC       G2/M. {ECO:0000269|PubMed:15235609}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9H7B4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9H7B4-2; Sequence=VSP_012416, VSP_012417;
CC         Note=No experimental confirmation available.;
CC       Name=3;
CC         IsoId=Q9H7B4-3; Sequence=VSP_035601;
CC   -!- TISSUE SPECIFICITY: Expressed in skeletal muscles and testis.
CC       Overexpressed in a majority of colorectal and hepatocellular
CC       carcinomas. {ECO:0000269|PubMed:15235609}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. {ECO:0000255|PROSITE-ProRule:PRU00907}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/SMYD3ID46100ch1q44.html";
DR   EMBL; AB057595; BAB86333.1; -; mRNA.
DR   EMBL; AY186742; AAO31695.1; -; mRNA.
DR   EMBL; AK024733; BAB14981.1; -; mRNA.
DR   EMBL; AK289605; BAF82294.1; -; mRNA.
DR   EMBL; AL356583; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL358859; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL445468; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL512412; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471148; EAW77142.1; -; Genomic_DNA.
DR   EMBL; BC017079; AAH17079.2; -; mRNA.
DR   EMBL; BC031010; AAH31010.1; -; mRNA.
DR   CCDS; CCDS31083.1; -. [Q9H7B4-3]
DR   CCDS; CCDS53486.1; -. [Q9H7B4-1]
DR   RefSeq; NP_001161212.1; NM_001167740.1. [Q9H7B4-1]
DR   RefSeq; NP_073580.1; NM_022743.2. [Q9H7B4-3]
DR   RefSeq; XP_011542559.1; XM_011544257.1. [Q9H7B4-2]
DR   UniGene; Hs.567571; -.
DR   PDB; 3MEK; X-ray; 2.10 A; A=1-428.
DR   PDB; 3OXF; X-ray; 2.82 A; A/B=1-428.
DR   PDB; 3OXG; X-ray; 3.41 A; A=1-428.
DR   PDB; 3OXL; X-ray; 3.60 A; A=1-428.
DR   PDB; 3PDN; X-ray; 1.70 A; A=1-428.
DR   PDB; 3QWP; X-ray; 1.53 A; A=1-428.
DR   PDB; 3RU0; X-ray; 1.85 A; A/B=2-428.
DR   PDB; 5CCL; X-ray; 1.50 A; A=1-428.
DR   PDB; 5CCM; X-ray; 2.30 A; A=1-428.
DR   PDB; 5EX0; X-ray; 2.70 A; A=1-428.
DR   PDB; 5EX3; X-ray; 2.41 A; A=1-428.
DR   PDB; 5HI7; X-ray; 2.15 A; A=1-428.
DR   PDB; 5HQ8; X-ray; 1.72 A; A/B=1-428.
DR   PDB; 5V37; X-ray; 1.42 A; A=1-428.
DR   PDB; 5XXD; X-ray; 2.31 A; A=3-425.
DR   PDB; 5XXG; X-ray; 2.14 A; A=3-425.
DR   PDB; 5XXJ; X-ray; 1.69 A; A=3-425.
DR   PDB; 5YJO; X-ray; 2.13 A; A=3-425.
DR   PDBsum; 3MEK; -.
DR   PDBsum; 3OXF; -.
DR   PDBsum; 3OXG; -.
DR   PDBsum; 3OXL; -.
DR   PDBsum; 3PDN; -.
DR   PDBsum; 3QWP; -.
DR   PDBsum; 3RU0; -.
DR   PDBsum; 5CCL; -.
DR   PDBsum; 5CCM; -.
DR   PDBsum; 5EX0; -.
DR   PDBsum; 5EX3; -.
DR   PDBsum; 5HI7; -.
DR   PDBsum; 5HQ8; -.
DR   PDBsum; 5V37; -.
DR   PDBsum; 5XXD; -.
DR   PDBsum; 5XXG; -.
DR   PDBsum; 5XXJ; -.
DR   PDBsum; 5YJO; -.
DR   ProteinModelPortal; Q9H7B4; -.
DR   SMR; Q9H7B4; -.
DR   BioGrid; 122268; 30.
DR   DIP; DIP-32653N; -.
DR   IntAct; Q9H7B4; 19.
DR   MINT; Q9H7B4; -.
DR   STRING; 9606.ENSP00000419184; -.
DR   BindingDB; Q9H7B4; -.
DR   ChEMBL; CHEMBL2321643; -.
DR   iPTMnet; Q9H7B4; -.
DR   PhosphoSitePlus; Q9H7B4; -.
DR   BioMuta; SMYD3; -.
DR   DMDM; 212276523; -.
DR   EPD; Q9H7B4; -.
DR   jPOST; Q9H7B4; -.
DR   MaxQB; Q9H7B4; -.
DR   PaxDb; Q9H7B4; -.
DR   PeptideAtlas; Q9H7B4; -.
DR   PRIDE; Q9H7B4; -.
DR   ProteomicsDB; 81096; -.
DR   ProteomicsDB; 81097; -. [Q9H7B4-2]
DR   ProteomicsDB; 81098; -. [Q9H7B4-3]
DR   DNASU; 64754; -.
DR   Ensembl; ENST00000490107; ENSP00000419184; ENSG00000185420. [Q9H7B4-1]
DR   Ensembl; ENST00000630181; ENSP00000487434; ENSG00000185420. [Q9H7B4-3]
DR   GeneID; 64754; -.
DR   KEGG; hsa:64754; -.
DR   UCSC; uc001ibl.4; human. [Q9H7B4-1]
DR   CTD; 64754; -.
DR   DisGeNET; 64754; -.
DR   EuPathDB; HostDB:ENSG00000185420.18; -.
DR   GeneCards; SMYD3; -.
DR   HGNC; HGNC:15513; SMYD3.
DR   HPA; CAB012229; -.
DR   HPA; HPA045821; -.
DR   HPA; HPA054352; -.
DR   MIM; 608783; gene.
DR   neXtProt; NX_Q9H7B4; -.
DR   OpenTargets; ENSG00000185420; -.
DR   PharmGKB; PA37972; -.
DR   eggNOG; KOG2084; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00940000156766; -.
DR   HOGENOM; HOG000007850; -.
DR   HOVERGEN; HBG105004; -.
DR   InParanoid; Q9H7B4; -.
DR   KO; K11426; -.
DR   OMA; DVCKVCL; -.
DR   OrthoDB; 981799at2759; -.
DR   PhylomeDB; Q9H7B4; -.
DR   TreeFam; TF106487; -.
DR   Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
DR   ChiTaRS; SMYD3; human.
DR   EvolutionaryTrace; Q9H7B4; -.
DR   GeneWiki; SMYD3; -.
DR   GenomeRNAi; 64754; -.
DR   PRO; PR:Q9H7B4; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   Bgee; ENSG00000185420; Expressed in 198 organ(s), highest expression level in caput epididymis.
DR   ExpressionAtlas; Q9H7B4; baseline and differential.
DR   Genevisible; Q9H7B4; HS.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IMP:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000993; F:RNA polymerase II complex binding; IEA:Ensembl.
DR   GO; GO:0001162; F:RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR   GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IEA:Ensembl.
DR   GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
DR   GO; GO:0045184; P:establishment of protein localization; IEA:Ensembl.
DR   GO; GO:0014904; P:myotube cell development; IEA:Ensembl.
DR   GO; GO:0006469; P:negative regulation of protein kinase activity; IEA:Ensembl.
DR   GO; GO:0006334; P:nucleosome assembly; IEA:Ensembl.
DR   GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   Gene3D; 1.25.40.10; -; 1.
DR   InterPro; IPR025805; Hist-Lys_N-MeTrfase_Smyd3.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR002893; Znf_MYND.
DR   Pfam; PF00856; SET; 1.
DR   Pfam; PF01753; zf-MYND; 1.
DR   SMART; SM00317; SET; 1.
DR   PROSITE; PS51574; SAM_MT43_2; 1.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS01360; ZF_MYND_1; 1.
DR   PROSITE; PS50865; ZF_MYND_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Chromatin regulator;
KW   Complete proteome; Cytoplasm; Metal-binding; Methyltransferase;
KW   Nucleus; Phosphoprotein; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase; Zinc; Zinc-finger.
FT   CHAIN         1    428       Histone-lysine N-methyltransferase SMYD3.
FT                                /FTId=PRO_0000218312.
FT   DOMAIN        4    240       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   ZN_FING      49     87       MYND-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00134}.
FT   REGION       14     16       S-adenosyl-L-methionine binding.
FT                                {ECO:0000269|Ref.12}.
FT   REGION      205    206       S-adenosyl-L-methionine binding.
FT                                {ECO:0000269|Ref.12}.
FT   REGION      272    428       C-terminal domain; essential for histone
FT                                methyltransferase activity, nuclear
FT                                localization and mediates interaction
FT                                with HSP90AA1.
FT                                {ECO:0000269|PubMed:25738358}.
FT   BINDING     124    124       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190,
FT                                ECO:0000269|Ref.12}.
FT   BINDING     132    132       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190,
FT                                ECO:0000269|Ref.12}.
FT   BINDING     181    181       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190,
FT                                ECO:0000269|Ref.12}.
FT   BINDING     239    239       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190,
FT                                ECO:0000269|Ref.12}.
FT   BINDING     259    259       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190,
FT                                ECO:0000269|Ref.12}.
FT   MOD_RES       1      1       N-acetylmethionine.
FT                                {ECO:0000244|PubMed:22814378}.
FT   MOD_RES      22     22       Phosphothreonine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   VAR_SEQ       1    170       Missing (in isoform 2).
FT                                {ECO:0000303|Ref.2}.
FT                                /FTId=VSP_012416.
FT   VAR_SEQ       1     59       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_035601.
FT   VAR_SEQ     171    176       LFEAFA -> MEEEEE (in isoform 2).
FT                                {ECO:0000303|Ref.2}.
FT                                /FTId=VSP_012417.
FT   CONFLICT     13     13       K -> N (in Ref. 1; BAB86333 and 6;
FT                                AAH31010). {ECO:0000305}.
FT   CONFLICT    140    140       K -> R (in Ref. 6; AAH31010).
FT                                {ECO:0000305}.
FT   STRAND        5     10       {ECO:0000244|PDB:5V37}.
FT   STRAND       12     22       {ECO:0000244|PDB:5V37}.
FT   STRAND       29     33       {ECO:0000244|PDB:5V37}.
FT   STRAND       36     40       {ECO:0000244|PDB:5V37}.
FT   HELIX        42     44       {ECO:0000244|PDB:5V37}.
FT   TURN         45     47       {ECO:0000244|PDB:5CCL}.
FT   TURN         50     52       {ECO:0000244|PDB:5V37}.
FT   TURN         63     65       {ECO:0000244|PDB:5V37}.
FT   STRAND       69     72       {ECO:0000244|PDB:5V37}.
FT   HELIX        73     78       {ECO:0000244|PDB:5V37}.
FT   HELIX        80     93       {ECO:0000244|PDB:5V37}.
FT   HELIX       100    114       {ECO:0000244|PDB:5V37}.
FT   HELIX       119    121       {ECO:0000244|PDB:5V37}.
FT   STRAND      122    124       {ECO:0000244|PDB:5V37}.
FT   HELIX       126    128       {ECO:0000244|PDB:5V37}.
FT   HELIX       133    135       {ECO:0000244|PDB:5V37}.
FT   HELIX       138    154       {ECO:0000244|PDB:5V37}.
FT   TURN        155    158       {ECO:0000244|PDB:5V37}.
FT   HELIX       162    164       {ECO:0000244|PDB:5V37}.
FT   HELIX       171    181       {ECO:0000244|PDB:5V37}.
FT   STRAND      183    186       {ECO:0000244|PDB:5V37}.
FT   STRAND      192    197       {ECO:0000244|PDB:5V37}.
FT   HELIX       201    203       {ECO:0000244|PDB:5V37}.
FT   STRAND      211    217       {ECO:0000244|PDB:5V37}.
FT   STRAND      220    225       {ECO:0000244|PDB:5V37}.
FT   STRAND      234    237       {ECO:0000244|PDB:5V37}.
FT   HELIX       246    255       {ECO:0000244|PDB:5V37}.
FT   HELIX       264    268       {ECO:0000244|PDB:5V37}.
FT   TURN        269    271       {ECO:0000244|PDB:5V37}.
FT   HELIX       272    275       {ECO:0000244|PDB:5V37}.
FT   HELIX       280    298       {ECO:0000244|PDB:5V37}.
FT   HELIX       302    313       {ECO:0000244|PDB:5V37}.
FT   TURN        316    319       {ECO:0000244|PDB:5HQ8}.
FT   HELIX       325    340       {ECO:0000244|PDB:5V37}.
FT   HELIX       344    361       {ECO:0000244|PDB:5V37}.
FT   HELIX       367    382       {ECO:0000244|PDB:5V37}.
FT   HELIX       386    403       {ECO:0000244|PDB:5V37}.
FT   TURN        404    407       {ECO:0000244|PDB:3OXF}.
FT   HELIX       409    424       {ECO:0000244|PDB:5V37}.
SQ   SEQUENCE   428 AA;  49097 MW;  2079357016F200AC CRC64;
     MEPLKVEKFA TAKRGNGLRA VTPLRPGELL FRSDPLAYTV CKGSRGVVCD RCLLGKEKLM
     RCSQCRVAKY CSAKCQKKAW PDHKRECKCL KSCKPRYPPD SVRLLGRVVF KLMDGAPSES
     EKLYSFYDLE SNINKLTEDK KEGLRQLVMT FQHFMREEIQ DASQLPPAFD LFEAFAKVIC
     NSFTICNAEM QEVGVGLYPS ISLLNHSCDP NCSIVFNGPH LLLRAVRDIE VGEELTICYL
     DMLMTSEERR KQLRDQYCFE CDCFRCQTQD KDADMLTGDE QVWKEVQESL KKIEELKAHW
     KWEQVLAMCQ AIISSNSERL PDINIYQLKV LDCAMDACIN LGLLEEALFY GTRTMEPYRI
     FFPGSHPVRG VQVMKVGKLQ LHQGMFPQAM KNLRLAFDIM RVTHGREHSL IEDLILLLEE
     CDANIRAS
//
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