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 27-MAR-2024, entry version 188.
DE RecName: Full=Histone-lysine N-methyltransferase SMYD3;
DE EC=2.1.1.354 {ECO:0000255|PROSITE-ProRule:PRU00907, ECO:0000269|PubMed:15235609, ECO:0000269|PubMed:22419068};
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 AND
RP 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 proliferation of
RT 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [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., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., 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., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., 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., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (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 project:
RT 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., Buerckstuemmer T.,
RA 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., Zmoos A.F.,
RA McDevitt P., Sinnamon R., Le B., Mas G., Annan R., Sage J., Garcia B.A.,
RA Tummino P.J., Gozani O., Kruger R.G.;
RT "Smyd3 regulates cancer cell phenotypes and catalyzes histone H4 lysine 5
RT methylation.";
RL Epigenetics 7:340-343(2012).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT 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 BY
RP 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 LOCATION.
RX PubMed=25738358; DOI=10.18632/oncotarget.2970;
RA Brown M.A., Foreman K., Harriss J., Das C., Zhu L., Edwards M., Shaaban S.,
RA Tucker H.;
RT "C-terminal domain of SMYD3 serves as a unique HSP90-regulated motif in
RT 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 in
RT complex with S-adenosyl-L-methionine.";
RL Submitted (APR-2010) to the PDB data bank.
CC -!- FUNCTION: Histone methyltransferase. Specifically methylates 'Lys-4' of
CC histone H3, inducing di- and tri-methylation, but not monomethylation
CC (PubMed:15235609, PubMed:22419068). Also methylates 'Lys-5' of histone
CC H4 (PubMed:22419068). Plays an important role in transcriptional
CC activation as a member of an RNA polymerase complex (PubMed:15235609).
CC Binds DNA containing 5'-CCCTCC-3' or 5'-GAGGGG-3' sequences
CC (PubMed:15235609). {ECO:0000269|PubMed:15235609,
CC ECO:0000269|PubMed:22419068}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60260, Rhea:RHEA-COMP:15537, Rhea:RHEA-
CC COMP:15547, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.354;
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 HELZ
CC (PubMed:15235609). Interacts with POLR2A; the interaction may be
CC indirect and may be mediated by HELZ (PubMed:15235609). Interacts with
CC HSP90AA1; this interaction enhances SMYD3 histone-lysine N-
CC methyltransferase (PubMed:25738358). {ECO:0000269|PubMed:15235609,
CC ECO:0000269|PubMed:25738358}.
CC -!- INTERACTION:
CC Q9H7B4; Q9H0L4: CSTF2T; NbExp=3; IntAct=EBI-347919, EBI-747012;
CC Q9H7B4; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-347919, EBI-744099;
CC Q9H7B4; Q13064: MKRN3; NbExp=3; IntAct=EBI-347919, EBI-2340269;
CC Q9H7B4; Q7Z3B4: NUP54; NbExp=3; IntAct=EBI-347919, EBI-741048;
CC Q9H7B4; Q16512: PKN1; NbExp=3; IntAct=EBI-347919, EBI-602382;
CC Q9H7B4; Q92529: SHC3; NbExp=3; IntAct=EBI-347919, EBI-79084;
CC Q9H7B4; Q15915: ZIC1; NbExp=3; IntAct=EBI-347919, EBI-11963196;
CC Q9H7B4-1; Q9Y2U5: MAP3K2; NbExp=3; IntAct=EBI-16204880, EBI-357393;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15235609}. Nucleus
CC {ECO:0000269|PubMed:15235609, ECO:0000269|PubMed:25738358}. Note=Mainly
CC cytoplasmic when cells are arrested at G0/G1. Accumulates in the
CC nucleus at S phase and 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 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 methyltransferase
CC superfamily. Histone-lysine methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU00907}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="https://atlasgeneticsoncology.org/gene/46100/SMYD3";
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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 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 PDB; 6IJL; X-ray; 2.35 A; A=1-428.
DR PDB; 6O9O; X-ray; 1.59 A; A=1-428.
DR PDB; 6P6G; X-ray; 1.59 A; A=1-428.
DR PDB; 6P6K; X-ray; 1.55 A; A=1-428.
DR PDB; 6P7Z; X-ray; 1.19 A; A=1-428.
DR PDB; 6PAF; X-ray; 1.24 A; A=1-428.
DR PDB; 6YUH; X-ray; 1.93 A; A=3-427.
DR PDB; 6ZRB; X-ray; 1.55 A; A=1-428.
DR PDB; 7BJ1; X-ray; 1.61 A; A=1-428.
DR PDB; 7O2A; X-ray; 1.57 A; A=1-428.
DR PDB; 7O2B; X-ray; 2.03 A; A=1-428.
DR PDB; 7O2C; X-ray; 1.52 A; A=1-428.
DR PDB; 7QLB; X-ray; 1.80 A; A=1-428.
DR PDB; 7QNR; X-ray; 1.57 A; A=1-428.
DR PDB; 7QNU; X-ray; 1.64 A; A=1-428.
DR PDB; 8OWO; X-ray; 1.80 A; A=1-428.
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 PDBsum; 6IJL; -.
DR PDBsum; 6O9O; -.
DR PDBsum; 6P6G; -.
DR PDBsum; 6P6K; -.
DR PDBsum; 6P7Z; -.
DR PDBsum; 6PAF; -.
DR PDBsum; 6YUH; -.
DR PDBsum; 6ZRB; -.
DR PDBsum; 7BJ1; -.
DR PDBsum; 7O2A; -.
DR PDBsum; 7O2B; -.
DR PDBsum; 7O2C; -.
DR PDBsum; 7QLB; -.
DR PDBsum; 7QNR; -.
DR PDBsum; 7QNU; -.
DR PDBsum; 8OWO; -.
DR AlphaFoldDB; Q9H7B4; -.
DR SMR; Q9H7B4; -.
DR BioGRID; 122268; 70.
DR DIP; DIP-32653N; -.
DR IntAct; Q9H7B4; 46.
DR MINT; Q9H7B4; -.
DR STRING; 9606.ENSP00000419184; -.
DR BindingDB; Q9H7B4; -.
DR ChEMBL; CHEMBL2321643; -.
DR GlyGen; Q9H7B4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H7B4; -.
DR MetOSite; Q9H7B4; -.
DR PhosphoSitePlus; Q9H7B4; -.
DR SwissPalm; Q9H7B4; -.
DR BioMuta; SMYD3; -.
DR DMDM; 212276523; -.
DR EPD; Q9H7B4; -.
DR jPOST; Q9H7B4; -.
DR MassIVE; Q9H7B4; -.
DR MaxQB; Q9H7B4; -.
DR PaxDb; 9606-ENSP00000419184; -.
DR PeptideAtlas; Q9H7B4; -.
DR ProteomicsDB; 81096; -. [Q9H7B4-1]
DR ProteomicsDB; 81097; -. [Q9H7B4-2]
DR ProteomicsDB; 81098; -. [Q9H7B4-3]
DR Pumba; Q9H7B4; -.
DR ABCD; Q9H7B4; 9 sequenced antibodies.
DR Antibodypedia; 34720; 338 antibodies from 37 providers.
DR DNASU; 64754; -.
DR Ensembl; ENST00000490107.6; ENSP00000419184.2; ENSG00000185420.19. [Q9H7B4-1]
DR Ensembl; ENST00000630181.2; ENSP00000487434.1; ENSG00000185420.19. [Q9H7B4-3]
DR GeneID; 64754; -.
DR KEGG; hsa:64754; -.
DR MANE-Select; ENST00000490107.6; ENSP00000419184.2; NM_001167740.2; NP_001161212.1.
DR UCSC; uc001ibl.4; human. [Q9H7B4-1]
DR AGR; HGNC:15513; -.
DR CTD; 64754; -.
DR DisGeNET; 64754; -.
DR GeneCards; SMYD3; -.
DR HGNC; HGNC:15513; SMYD3.
DR HPA; ENSG00000185420; Low tissue specificity.
DR MIM; 608783; gene.
DR neXtProt; NX_Q9H7B4; -.
DR OpenTargets; ENSG00000185420; -.
DR PharmGKB; PA37972; -.
DR VEuPathDB; HostDB:ENSG00000185420; -.
DR eggNOG; KOG2084; Eukaryota.
DR GeneTree; ENSGT00940000156766; -.
DR InParanoid; Q9H7B4; -.
DR OMA; LHMKLGK; -.
DR OrthoDB; 166337at2759; -.
DR PhylomeDB; Q9H7B4; -.
DR TreeFam; TF106487; -.
DR BioCyc; MetaCyc:HS11979-MONOMER; -.
DR BRENDA; 2.1.1.354; 2681.
DR PathwayCommons; Q9H7B4; -.
DR Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
DR SignaLink; Q9H7B4; -.
DR BioGRID-ORCS; 64754; 16 hits in 1177 CRISPR screens.
DR ChiTaRS; SMYD3; human.
DR EvolutionaryTrace; Q9H7B4; -.
DR GeneWiki; SMYD3; -.
DR GenomeRNAi; 64754; -.
DR Pharos; Q9H7B4; Tchem.
DR PRO; PR:Q9H7B4; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9H7B4; Protein.
DR Bgee; ENSG00000185420; Expressed in corpus epididymis and 170 other cell types or tissues.
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:0140954; F:histone H3K36 dimethyltransferase activity; ISS:UniProtKB.
DR GO; GO:0140999; F:histone H3K4 trimethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0140939; F:histone H4 methyltransferase activity; IMP:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
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:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
DR GO; GO:0045184; P:establishment of protein localization; IEA:Ensembl.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0014904; P:myotube cell development; 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 CDD; cd19203; SET_SMYD3; 1.
DR Gene3D; 1.10.220.160; -; 1.
DR Gene3D; 1.25.40.970; -; 1.
DR Gene3D; 6.10.140.2220; -; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR025805; Hist-Lys_N-MeTrfase_SMYD3.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR044420; SMYD3_SET.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR002893; Znf_MYND.
DR PANTHER; PTHR12197; HISTONE-LYSINE N-METHYLTRANSFERASE SMYD; 1.
DR PANTHER; PTHR12197:SF288; HISTONE-LYSINE N-METHYLTRANSFERASE SMYD3; 1.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF01753; zf-MYND; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SET domain; 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 Cytoplasm; Metal-binding; Methyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; S-adenosyl-L-methionine; Transferase; Zinc;
KW Zinc-finger.
FT CHAIN 1..428
FT /note="Histone-lysine N-methyltransferase SMYD3"
FT /id="PRO_0000218312"
FT DOMAIN 4..240
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT ZN_FING 49..87
FT /note="MYND-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT REGION 272..428
FT /note="C-terminal domain; essential for histone
FT methyltransferase activity, nuclear localization and
FT mediates interaction with HSP90AA1"
FT /evidence="ECO:0000269|PubMed:25738358"
FT BINDING 14..16
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|Ref.12"
FT BINDING 49
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 52
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 124
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190,
FT ECO:0000269|Ref.12"
FT BINDING 132
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190,
FT ECO:0000269|Ref.12"
FT BINDING 181
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190,
FT ECO:0000269|Ref.12"
FT BINDING 205..206
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|Ref.12"
FT BINDING 239
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190,
FT ECO:0000269|Ref.12"
FT BINDING 259
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190,
FT ECO:0000269|Ref.12"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 22
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..170
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_012416"
FT VAR_SEQ 1..59
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_035601"
FT VAR_SEQ 171..176
FT /note="LFEAFA -> MEEEEE (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_012417"
FT CONFLICT 13
FT /note="K -> N (in Ref. 1; BAB86333 and 6; AAH31010)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="K -> R (in Ref. 6; AAH31010)"
FT /evidence="ECO:0000305"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:6P7Z"
FT STRAND 12..22
FT /evidence="ECO:0007829|PDB:6P7Z"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:6P7Z"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:6P7Z"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:6P7Z"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:6PAF"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:6P7Z"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:6P7Z"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:6P7Z"
FT HELIX 73..92
FT /evidence="ECO:0007829|PDB:6P7Z"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:7O2C"
FT HELIX 100..114
FT /evidence="ECO:0007829|PDB:6P7Z"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:6P7Z"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:6P7Z"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:6P7Z"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:6P7Z"
FT HELIX 138..154
FT /evidence="ECO:0007829|PDB:6P7Z"
FT TURN 155..158
FT /evidence="ECO:0007829|PDB:6P7Z"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:6P7Z"
FT HELIX 171..181
FT /evidence="ECO:0007829|PDB:6P7Z"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:6P7Z"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:6P7Z"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:6P7Z"
FT STRAND 211..217
FT /evidence="ECO:0007829|PDB:6P7Z"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:6P7Z"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:6P7Z"
FT HELIX 246..257
FT /evidence="ECO:0007829|PDB:6P7Z"
FT HELIX 264..268
FT /evidence="ECO:0007829|PDB:6P7Z"
FT TURN 269..271
FT /evidence="ECO:0007829|PDB:6P7Z"
FT HELIX 272..275
FT /evidence="ECO:0007829|PDB:6P7Z"
FT HELIX 280..298
FT /evidence="ECO:0007829|PDB:6P7Z"
FT HELIX 302..313
FT /evidence="ECO:0007829|PDB:6P7Z"
FT TURN 316..319
FT /evidence="ECO:0007829|PDB:5HQ8"
FT HELIX 325..341
FT /evidence="ECO:0007829|PDB:6P7Z"
FT HELIX 344..361
FT /evidence="ECO:0007829|PDB:6P7Z"
FT HELIX 367..382
FT /evidence="ECO:0007829|PDB:6P7Z"
FT HELIX 386..403
FT /evidence="ECO:0007829|PDB:6P7Z"
FT TURN 404..407
FT /evidence="ECO:0007829|PDB:3OXF"
FT HELIX 409..426
FT /evidence="ECO:0007829|PDB:6P7Z"
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
//
