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Entry: Q9NRG4
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ID   SMYD2_HUMAN             Reviewed;         433 AA.
AC   Q9NRG4; B2R9P9; I6L9H7; Q4V765; Q5VSH9; Q96AI4;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 2.
DT   13-FEB-2019, entry version 153.
DE   RecName: Full=N-lysine methyltransferase SMYD2;
DE            EC=2.1.1.-;
DE   AltName: Full=HSKM-B;
DE   AltName: Full=Histone methyltransferase SMYD2;
DE            EC=2.1.1.43;
DE   AltName: Full=Lysine N-methyltransferase 3C;
DE   AltName: Full=SET and MYND domain-containing protein 2;
GN   Name=SMYD2; Synonyms=KMT3C;
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 [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP   GLU-165.
RC   TISSUE=Liver cancer;
RA   Li Y., Wu T., Xu S., Ren S., Chen Z., Han Z.;
RT   "A novel gene expressed in human liver cancer tissue.";
RL   Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP   GLU-165.
RC   TISSUE=Testis;
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP   GLU-165.
RC   TISSUE=Colon;
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   [5]
RP   FUNCTION, INTERACTION WITH TP53, AND MUTAGENESIS OF HIS-207.
RX   PubMed=17108971; DOI=10.1038/nature05287;
RA   Huang J., Perez-Burgos L., Placek B.J., Sengupta R., Richter M.,
RA   Dorsey J.A., Kubicek S., Opravil S., Jenuwein T., Berger S.L.;
RT   "Repression of p53 activity by Smyd2-mediated methylation.";
RL   Nature 444:629-632(2006).
RN   [6]
RP   INDUCTION.
RX   PubMed=17242690; DOI=10.1038/sj.cr.7310121;
RA   Wang C., Chen X., Wang Y., Gong J., Hu G.;
RT   "C/EBPalphap30 plays transcriptional regulatory roles distinct from
RT   C/EBPalphap42.";
RL   Cell Res. 17:374-383(2007).
RN   [7]
RP   FUNCTION.
RX   PubMed=17805299; DOI=10.1038/nature06092;
RA   Huang J., Sengupta R., Espejo A.B., Lee M.G., Dorsey J.A., Richter M.,
RA   Opravil S., Shiekhattar R., Bedford M.T., Jenuwein T., Berger S.L.;
RT   "p53 is regulated by the lysine demethylase LSD1.";
RL   Nature 449:105-108(2007).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH EPB41L3; HSP90AA1
RP   AND TP53.
RX   PubMed=18065756; DOI=10.1074/mcp.M700271-MCP200;
RA   Abu-Farha M., Lambert J.P., Al-Madhoun A.S., Elisma F., Skerjanc I.S.,
RA   Figeys D.;
RT   "The tale of two domains: proteomics and genomics analysis of SMYD2, a
RT   new histone methyltransferase.";
RL   Mol. Cell. Proteomics 7:560-572(2008).
RN   [9]
RP   FUNCTION, INTERACTION WITH RB, AND MUTAGENESIS OF TYR-240.
RX   PubMed=20870719; DOI=10.1074/jbc.M110.137612;
RA   Saddic L.A., West L.E., Aslanian A., Yates J.R. III, Rubin S.M.,
RA   Gozani O., Sage J.;
RT   "Methylation of the retinoblastoma tumor suppressor by SMYD2.";
RL   J. Biol. Chem. 285:37733-37740(2010).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
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   X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS) IN COMPLEX WITH
RP   S-ADENOSYL-L-METHIONINE AND ZINC IONS.
RX   PubMed=21724641; DOI=10.1093/jmcb/mjr015;
RA   Xu S., Zhong C., Zhang T., Ding J.;
RT   "Structure of human lysine methyltransferase Smyd2 reveals insights
RT   into the substrate divergence in Smyd proteins.";
RL   J. Mol. Cell Biol. 3:293-300(2011).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEXES WITH TP53/P53
RP   PEPTIDE; S-ADENOSYL-L-METHIONINE AND ZINC IONS, FUNCTION IN P53/TP53
RP   METHYLATION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLU-187; GLU-189;
RP   GLU-190; TYR-245; ASP-252; ARG-253; ARG-306; TYR-374; GLU-429 AND
RP   GLU-431.
RX   PubMed=21880715; DOI=10.1074/jbc.M111.262410;
RA   Wang L., Li L., Zhang H., Luo X., Dai J., Zhou S., Gu J., Zhu J.,
RA   Atadja P., Lu C., Li E., Zhao K.;
RT   "Structure of human SMYD2 protein reveals the basis of p53 tumor
RT   suppressor methylation.";
RL   J. Biol. Chem. 286:38725-38737(2011).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEXES WITH P53/TP53
RP   PEPTIDE; S-ADENOSYL-L-METHIONINE; SYNTHETIC INHIBITOR AND ZINC IONS,
RP   FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF TYR-240.
RX   PubMed=21782458; DOI=10.1016/j.str.2011.06.011;
RA   Ferguson A.D., Larsen N.A., Howard T., Pollard H., Green I.,
RA   Grande C., Cheung T., Garcia-Arenas R., Cowen S., Wu J., Godin R.,
RA   Chen H., Keen N.;
RT   "Structural basis of substrate methylation and inhibition of SMYD2.";
RL   Structure 19:1262-1273(2011).
CC   -!- FUNCTION: Protein-lysine N-methyltransferase that methylates both
CC       histones and non-histone proteins, including p53/TP53 and RB1.
CC       Specifically methylates histone H3 'Lys-4' (H3K4me) and
CC       dimethylates histone H3 'Lys-36' (H3K36me2). Shows even higher
CC       methyltransferase activity on p53/TP53. Monomethylates 'Lys-370'
CC       of p53/TP53, leading to decreased DNA-binding activity and
CC       subsequent transcriptional regulation activity of p53/TP53.
CC       Monomethylates RB1 at 'Lys-860'. {ECO:0000269|PubMed:17108971,
CC       ECO:0000269|PubMed:17805299, ECO:0000269|PubMed:18065756,
CC       ECO:0000269|PubMed:20870719, ECO:0000269|PubMed:21782458,
CC       ECO:0000269|PubMed:21880715}.
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:18065756,
CC         ECO:0000269|PubMed:21782458, ECO:0000269|PubMed:21880715};
CC   -!- SUBUNIT: Interacts with RNA polymerase II and HELZ. Interacts with
CC       SIN3A and HDAC1 (By similarity). Interacts (via MYND-type zinc
CC       finger) with EPB41L3. Interacts (via SET domain) with p53/TP53.
CC       Interacts with RB1 and HSP90AA1. {ECO:0000250,
CC       ECO:0000269|PubMed:17108971, ECO:0000269|PubMed:18065756,
CC       ECO:0000269|PubMed:20870719, ECO:0000269|PubMed:21724641}.
CC   -!- INTERACTION:
CC       P04637:TP53; NbExp=6; IntAct=EBI-1055671, EBI-366083;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Nucleus
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9NRG4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NRG4-2; Sequence=VSP_056005;
CC         Note=No experimental confirmation available.;
CC   -!- INDUCTION: Expression is repressed by CEBPA.
CC       {ECO:0000269|PubMed:17242690}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/SMYD2ID47098ch1q32.html";
DR   EMBL; AF226053; AAF86953.1; -; mRNA.
DR   EMBL; AK313868; BAG36596.1; -; mRNA.
DR   EMBL; AL929236; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC017080; AAH17080.2; -; mRNA.
DR   EMBL; BC098276; AAH98276.1; -; mRNA.
DR   EMBL; BC098133; AAH98133.1; -; mRNA.
DR   EMBL; BC098305; AAH98305.1; -; mRNA.
DR   EMBL; BC098335; AAH98335.1; -; mRNA.
DR   CCDS; CCDS31022.1; -. [Q9NRG4-1]
DR   RefSeq; NP_064582.2; NM_020197.2. [Q9NRG4-1]
DR   UniGene; Hs.66170; -.
DR   PDB; 3RIB; X-ray; 2.79 A; A/B=1-433.
DR   PDB; 3S7B; X-ray; 2.42 A; A=1-433.
DR   PDB; 3S7D; X-ray; 2.30 A; A=1-433.
DR   PDB; 3S7F; X-ray; 2.85 A; A=1-433.
DR   PDB; 3S7J; X-ray; 3.04 A; A=1-433.
DR   PDB; 3TG4; X-ray; 2.00 A; A=1-433.
DR   PDB; 3TG5; X-ray; 2.30 A; A=1-433.
DR   PDB; 4O6F; X-ray; 2.82 A; A=1-433.
DR   PDB; 4WUY; X-ray; 1.63 A; A=1-433.
DR   PDB; 4YND; X-ray; 2.79 A; A=1-433.
DR   PDB; 5ARF; X-ray; 1.92 A; A=2-433.
DR   PDB; 5ARG; X-ray; 1.99 A; A=2-433.
DR   PDB; 5KJK; X-ray; 1.93 A; A=5-433.
DR   PDB; 5KJL; X-ray; 2.70 A; A=5-433.
DR   PDB; 5KJM; X-ray; 2.19 A; A=5-433.
DR   PDB; 5KJN; X-ray; 2.72 A; A=5-433.
DR   PDB; 5V3H; X-ray; 2.69 A; A=1-433.
DR   PDB; 5WCG; X-ray; 2.02 A; A=1-433.
DR   PDB; 6CBX; X-ray; 1.94 A; A/B=1-433.
DR   PDB; 6CBY; X-ray; 2.55 A; A/B=1-433.
DR   PDB; 6MON; X-ray; 2.71 A; A/B=5-433.
DR   PDBsum; 3RIB; -.
DR   PDBsum; 3S7B; -.
DR   PDBsum; 3S7D; -.
DR   PDBsum; 3S7F; -.
DR   PDBsum; 3S7J; -.
DR   PDBsum; 3TG4; -.
DR   PDBsum; 3TG5; -.
DR   PDBsum; 4O6F; -.
DR   PDBsum; 4WUY; -.
DR   PDBsum; 4YND; -.
DR   PDBsum; 5ARF; -.
DR   PDBsum; 5ARG; -.
DR   PDBsum; 5KJK; -.
DR   PDBsum; 5KJL; -.
DR   PDBsum; 5KJM; -.
DR   PDBsum; 5KJN; -.
DR   PDBsum; 5V3H; -.
DR   PDBsum; 5WCG; -.
DR   PDBsum; 6CBX; -.
DR   PDBsum; 6CBY; -.
DR   PDBsum; 6MON; -.
DR   ProteinModelPortal; Q9NRG4; -.
DR   SMR; Q9NRG4; -.
DR   BioGrid; 121274; 27.
DR   DIP; DIP-50202N; -.
DR   IntAct; Q9NRG4; 6.
DR   MINT; Q9NRG4; -.
DR   STRING; 9606.ENSP00000355924; -.
DR   BindingDB; Q9NRG4; -.
DR   ChEMBL; CHEMBL2169716; -.
DR   GuidetoPHARMACOLOGY; 2714; -.
DR   iPTMnet; Q9NRG4; -.
DR   PhosphoSitePlus; Q9NRG4; -.
DR   BioMuta; SMYD2; -.
DR   DMDM; 90185234; -.
DR   EPD; Q9NRG4; -.
DR   jPOST; Q9NRG4; -.
DR   MaxQB; Q9NRG4; -.
DR   PaxDb; Q9NRG4; -.
DR   PeptideAtlas; Q9NRG4; -.
DR   PRIDE; Q9NRG4; -.
DR   ProteomicsDB; 82355; -.
DR   Ensembl; ENST00000366957; ENSP00000355924; ENSG00000143499. [Q9NRG4-1]
DR   GeneID; 56950; -.
DR   KEGG; hsa:56950; -.
DR   UCSC; uc057pjy.1; human. [Q9NRG4-1]
DR   CTD; 56950; -.
DR   DisGeNET; 56950; -.
DR   EuPathDB; HostDB:ENSG00000143499.13; -.
DR   GeneCards; SMYD2; -.
DR   HGNC; HGNC:20982; SMYD2.
DR   HPA; HPA029023; -.
DR   MIM; 610663; gene.
DR   neXtProt; NX_Q9NRG4; -.
DR   OpenTargets; ENSG00000143499; -.
DR   PharmGKB; PA134930268; -.
DR   eggNOG; KOG2084; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00940000157082; -.
DR   HOGENOM; HOG000007850; -.
DR   HOVERGEN; HBG098536; -.
DR   InParanoid; Q9NRG4; -.
DR   KO; K11426; -.
DR   OMA; AVQEIHP; -.
DR   OrthoDB; 981799at2759; -.
DR   PhylomeDB; Q9NRG4; -.
DR   TreeFam; TF106487; -.
DR   Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
DR   Reactome; R-HSA-6804760; Regulation of TP53 Activity through Methylation.
DR   ChiTaRS; SMYD2; human.
DR   GenomeRNAi; 56950; -.
DR   PRO; PR:Q9NRG4; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   Bgee; ENSG00000143499; Expressed in 227 organ(s), highest expression level in left ventricle myocardium.
DR   ExpressionAtlas; Q9NRG4; baseline and differential.
DR   Genevisible; Q9NRG4; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); ISS:UniProtKB.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; TAS:Reactome.
DR   GO; GO:0016278; F:lysine N-methyltransferase activity; TAS:Reactome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0002039; F:p53 binding; IPI:UniProtKB.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0000993; F:RNA polymerase II complex binding; ISS:UniProtKB.
DR   GO; GO:0007507; P:heart development; IEA:Ensembl.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR   GO; GO:0018027; P:peptidyl-lysine dimethylation; ISS:UniProtKB.
DR   GO; GO:0018026; P:peptidyl-lysine monomethylation; IDA:UniProtKB.
DR   GO; GO:0043516; P:regulation of DNA damage response, signal transduction by p53 class mediator; IMP:UniProtKB.
DR   GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
DR   Gene3D; 1.25.40.10; -; 1.
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   SUPFAM; SSF48452; SSF48452; 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; Alternative splicing; Chromatin regulator;
KW   Complete proteome; Cytoplasm; Metal-binding; Methyltransferase;
KW   Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase; Zinc; Zinc-finger.
FT   CHAIN         1    433       N-lysine methyltransferase SMYD2.
FT                                /FTId=PRO_0000218309.
FT   DOMAIN        7    241       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   ZN_FING      52     90       MYND-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00134}.
FT   REGION       17     19       S-adenosyl-L-methionine binding.
FT   REGION      183    185       Peptide substrate binding.
FT   REGION      206    207       S-adenosyl-L-methionine binding.
FT   REGION      258    260       S-adenosyl-L-methionine binding.
FT   BINDING     137    137       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190,
FT                                ECO:0000269|PubMed:21724641}.
FT   BINDING     240    240       Peptide substrate; via carbonyl oxygen.
FT   MOD_RES     283    283       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   VAR_SEQ     273    433       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_056005.
FT   VARIANT     165    165       G -> E (in dbSNP:rs1134647).
FT                                {ECO:0000269|PubMed:14702039,
FT                                ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|Ref.1}.
FT                                /FTId=VAR_023442.
FT   VARIANT     430    430       I -> M (in dbSNP:rs11120301).
FT                                /FTId=VAR_052991.
FT   MUTAGEN     187    187       E->K: Abolishes methyltransferase
FT                                activity on p53/TP53.
FT                                {ECO:0000269|PubMed:21880715}.
FT   MUTAGEN     189    189       E->K: Strongly reduces methyltransferase
FT                                activity on p53/TP53.
FT                                {ECO:0000269|PubMed:21880715}.
FT   MUTAGEN     190    190       E->K: Strongly reduces methyltransferase
FT                                activity on p53/TP53.
FT                                {ECO:0000269|PubMed:21880715}.
FT   MUTAGEN     207    207       H->A: Abolishes methyltransferase
FT                                activity. {ECO:0000269|PubMed:17108971}.
FT   MUTAGEN     240    240       Y->F: Abolishes methyltransferase
FT                                activity. {ECO:0000269|PubMed:20870719,
FT                                ECO:0000269|PubMed:21782458}.
FT   MUTAGEN     245    245       Y->F: Strongly reduces methyltransferase
FT                                activity on p53/TP53.
FT                                {ECO:0000269|PubMed:21880715}.
FT   MUTAGEN     252    252       D->R: Slightly reduces methyltransferase
FT                                activity on p53/TP53.
FT                                {ECO:0000269|PubMed:21880715}.
FT   MUTAGEN     253    253       R->Q: No effect on methyltransferase
FT                                activity on p53/TP53.
FT                                {ECO:0000269|PubMed:21880715}.
FT   MUTAGEN     306    306       R->E: No effect on methyltransferase
FT                                activity on p53/TP53.
FT                                {ECO:0000269|PubMed:21880715}.
FT   MUTAGEN     374    374       Y->A: Abolishes methyltransferase
FT                                activity on p53/TP53.
FT                                {ECO:0000269|PubMed:21880715}.
FT   MUTAGEN     429    429       E->K: Reduces methyltransferase activity
FT                                on p53/TP53.
FT                                {ECO:0000269|PubMed:21880715}.
FT   MUTAGEN     431    431       E->K: Strongly reduces methyltransferase
FT                                activity on p53/TP53.
FT                                {ECO:0000269|PubMed:21880715}.
FT   HELIX         1      4       {ECO:0000244|PDB:5V3H}.
FT   TURN          5      8       {ECO:0000244|PDB:5V3H}.
FT   STRAND        9     14       {ECO:0000244|PDB:4WUY}.
FT   TURN         15     17       {ECO:0000244|PDB:4WUY}.
FT   STRAND       18     25       {ECO:0000244|PDB:4WUY}.
FT   STRAND       32     37       {ECO:0000244|PDB:4WUY}.
FT   STRAND       39     43       {ECO:0000244|PDB:4WUY}.
FT   HELIX        45     47       {ECO:0000244|PDB:4WUY}.
FT   TURN         48     50       {ECO:0000244|PDB:6CBX}.
FT   TURN         53     55       {ECO:0000244|PDB:4WUY}.
FT   TURN         66     68       {ECO:0000244|PDB:4WUY}.
FT   STRAND       72     75       {ECO:0000244|PDB:4WUY}.
FT   HELIX        76     86       {ECO:0000244|PDB:4WUY}.
FT   TURN         87     89       {ECO:0000244|PDB:4WUY}.
FT   HELIX        90     96       {ECO:0000244|PDB:4WUY}.
FT   HELIX        97     99       {ECO:0000244|PDB:4WUY}.
FT   HELIX       104    118       {ECO:0000244|PDB:4WUY}.
FT   HELIX       124    126       {ECO:0000244|PDB:6CBX}.
FT   STRAND      127    129       {ECO:0000244|PDB:3RIB}.
FT   HELIX       131    133       {ECO:0000244|PDB:4WUY}.
FT   HELIX       138    140       {ECO:0000244|PDB:4WUY}.
FT   HELIX       143    164       {ECO:0000244|PDB:4WUY}.
FT   HELIX       169    182       {ECO:0000244|PDB:4WUY}.
FT   STRAND      184    187       {ECO:0000244|PDB:4WUY}.
FT   STRAND      193    198       {ECO:0000244|PDB:4WUY}.
FT   HELIX       200    203       {ECO:0000244|PDB:4WUY}.
FT   STRAND      205    207       {ECO:0000244|PDB:5ARF}.
FT   STRAND      212    218       {ECO:0000244|PDB:4WUY}.
FT   STRAND      221    228       {ECO:0000244|PDB:4WUY}.
FT   STRAND      235    238       {ECO:0000244|PDB:6CBY}.
FT   STRAND      243    245       {ECO:0000244|PDB:5KJL}.
FT   HELIX       247    258       {ECO:0000244|PDB:4WUY}.
FT   HELIX       265    269       {ECO:0000244|PDB:4WUY}.
FT   HELIX       273    276       {ECO:0000244|PDB:4WUY}.
FT   HELIX       288    305       {ECO:0000244|PDB:4WUY}.
FT   TURN        309    311       {ECO:0000244|PDB:5ARF}.
FT   HELIX       318    329       {ECO:0000244|PDB:4WUY}.
FT   HELIX       337    353       {ECO:0000244|PDB:4WUY}.
FT   HELIX       356    373       {ECO:0000244|PDB:4WUY}.
FT   HELIX       379    394       {ECO:0000244|PDB:4WUY}.
FT   HELIX       398    415       {ECO:0000244|PDB:4WUY}.
FT   TURN        416    419       {ECO:0000244|PDB:5KJL}.
FT   HELIX       421    432       {ECO:0000244|PDB:4WUY}.
SQ   SEQUENCE   433 AA;  49688 MW;  3EEA5B8417870F5D CRC64;
     MRAEGLGGLE RFCSPGKGRG LRALQPFQVG DLLFSCPAYA YVLTVNERGN HCEYCFTRKE
     GLSKCGRCKQ AFYCNVECQK EDWPMHKLEC SPMVVFGENW NPSETVRLTA RILAKQKIHP
     ERTPSEKLLA VKEFESHLDK LDNEKKDLIQ SDIAALHHFY SKHLGFPDND SLVVLFAQVN
     CNGFTIEDEE LSHLGSAIFP DVALMNHSCC PNVIVTYKGT LAEVRAVQEI KPGEEVFTSY
     IDLLYPTEDR NDRLRDSYFF TCECQECTTK DKDKAKVEIR KLSDPPKAEA IRDMVRYARN
     VIEEFRRAKH YKSPSELLEI CELSQEKMSS VFEDSNVYML HMMYQAMGVC LYMQDWEGAL
     QYGQKIIKPY SKHYPLYSLN VASMWLKLGR LYMGLEHKAA GEKALKKAIA IMEVAHGKDH
     PYISEIKQEI ESH
//
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