GenomeNet

Database: UniProt
Entry: Q8NB12
LinkDB: Q8NB12
Original site: Q8NB12 
ID   SMYD1_HUMAN             Reviewed;         490 AA.
AC   Q8NB12; A0AV30; A6NE13;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   13-FEB-2019, entry version 131.
DE   RecName: Full=Histone-lysine N-methyltransferase SMYD1;
DE            EC=2.1.1.43;
DE   AltName: Full=SET and MYND domain-containing protein 1;
GN   Name=SMYD1;
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 {ECO:0000312|EMBL:BAC03732.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Skeletal muscle;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 4.";
RL   Nature 434:724-731(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   TISSUE SPECIFICITY, AND INDUCTION BY SRF.
RX   PubMed=19783823; DOI=10.1093/nar/gkp773;
RA   Li D., Niu Z., Yu W., Qian Y., Wang Q., Li Q., Yi Z., Luo J., Wu X.,
RA   Wang Y., Schwartz R.J., Liu M.;
RT   "SMYD1, the myogenic activator, is a direct target of serum response
RT   factor and myogenin.";
RL   Nucleic Acids Res. 37:7059-7071(2009).
CC   -!- FUNCTION: Methylates histone H3 at 'Lys-4' (H3K4me), seems able to
CC       perform both mono-, di-, and trimethylation. Acts as a
CC       transcriptional repressor. Essential for cardiomyocyte
CC       differentiation and cardiac morphogenesis.
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   -!- SUBUNIT: Interacts with HDAC1, HDAC2 and HDAC3. Interacts (via
CC       MYND-type zinc finger) with NACA isoform skNAC (By similarity).
CC       {ECO:0000250}.
CC   -!- INTERACTION:
CC       P30520:ADSS; NbExp=2; IntAct=EBI-8463848, EBI-1042898;
CC       O14503:BHLHE40; NbExp=5; IntAct=EBI-8463848, EBI-711810;
CC       Q9H8W3:FAM204A; NbExp=3; IntAct=EBI-8463848, EBI-8465160;
CC       Q8IX15-3:HOMEZ; NbExp=3; IntAct=EBI-8463848, EBI-10172004;
CC       A7E2Y1:MYH7B; NbExp=2; IntAct=EBI-8463848, EBI-2880253;
CC       Q9BQ04:RBM4B; NbExp=2; IntAct=EBI-8463848, EBI-715531;
CC       Q9BVJ6:UTP14A; NbExp=3; IntAct=EBI-8463848, EBI-473284;
CC       Q8NCP5:ZBTB44; NbExp=3; IntAct=EBI-8463848, EBI-5658292;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expression seems mostly restricted to heart
CC       and skeletal muscle. {ECO:0000269|PubMed:19783823}.
CC   -!- INDUCTION: By serum response factor SRF and myogenin. SRF binds to
CC       the CArG site and MYOG binds to the E-box element on SMYD1
CC       promoter. {ECO:0000269|PubMed:19783823}.
CC   -!- DOMAIN: The SET domain is split between the S-sequence (residues
CC       1-49) and the core SET domain (residues 181-258), however the two
CC       segments still come together to form a conserved SET domain fold.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
DR   EMBL; AK091724; BAC03732.1; -; mRNA.
DR   EMBL; AL832035; CAI46139.1; -; mRNA.
DR   EMBL; AC092836; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC126191; AAI26192.1; -; mRNA.
DR   CCDS; CCDS33240.1; -.
DR   RefSeq; NP_938015.1; NM_198274.3.
DR   UniGene; Hs.516176; -.
DR   ProteinModelPortal; Q8NB12; -.
DR   SMR; Q8NB12; -.
DR   BioGrid; 127308; 18.
DR   IntAct; Q8NB12; 42.
DR   MINT; Q8NB12; -.
DR   STRING; 9606.ENSP00000393453; -.
DR   iPTMnet; Q8NB12; -.
DR   PhosphoSitePlus; Q8NB12; -.
DR   BioMuta; SMYD1; -.
DR   DMDM; 34925329; -.
DR   jPOST; Q8NB12; -.
DR   PaxDb; Q8NB12; -.
DR   PeptideAtlas; Q8NB12; -.
DR   PRIDE; Q8NB12; -.
DR   ProteomicsDB; 72714; -.
DR   DNASU; 150572; -.
DR   Ensembl; ENST00000419482; ENSP00000393453; ENSG00000115593.
DR   GeneID; 150572; -.
DR   KEGG; hsa:150572; -.
DR   UCSC; uc002ssr.4; human.
DR   CTD; 150572; -.
DR   DisGeNET; 150572; -.
DR   EuPathDB; HostDB:ENSG00000115593.14; -.
DR   GeneCards; SMYD1; -.
DR   HGNC; HGNC:20986; SMYD1.
DR   HPA; HPA062282; -.
DR   MIM; 606846; gene.
DR   neXtProt; NX_Q8NB12; -.
DR   OpenTargets; ENSG00000115593; -.
DR   PharmGKB; PA134862943; -.
DR   eggNOG; KOG2084; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00940000156114; -.
DR   HOGENOM; HOG000050244; -.
DR   HOVERGEN; HBG054953; -.
DR   InParanoid; Q8NB12; -.
DR   KO; K11426; -.
DR   OMA; GIFPNLC; -.
DR   OrthoDB; 981799at2759; -.
DR   PhylomeDB; Q8NB12; -.
DR   TreeFam; TF106487; -.
DR   GenomeRNAi; 150572; -.
DR   PRO; PR:Q8NB12; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   Bgee; ENSG00000115593; Expressed in 110 organ(s), highest expression level in quadriceps femoris.
DR   ExpressionAtlas; Q8NB12; baseline and differential.
DR   Genevisible; Q8NB12; HS.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl.
DR   GO; GO:0006338; P:chromatin remodeling; IEA:Ensembl.
DR   GO; GO:0007507; P:heart development; IEA:Ensembl.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl.
DR   GO; GO:0045663; P:positive regulation of myoblast differentiation; IDA:BHF-UCL.
DR   GO; GO:0010831; P:positive regulation of myotube differentiation; IDA:BHF-UCL.
DR   GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl.
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   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   Complete proteome; Cytoplasm; DNA-binding; Metal-binding;
KW   Methyltransferase; Nucleus; Polymorphism; Reference proteome;
KW   Repressor; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase; Zinc; Zinc-finger.
FT   CHAIN         1    490       Histone-lysine N-methyltransferase SMYD1.
FT                                /FTId=PRO_0000218307.
FT   DOMAIN        7    253       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                                {ECO:0000250}.
FT   REGION      205    206       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   REGION      270    272       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   METAL       208    208       Zinc. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   METAL       274    274       Zinc. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   METAL       276    276       Zinc. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   METAL       279    279       Zinc. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   BINDING     135    135       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   VARIANT     164    164       Q -> P (in dbSNP:rs1542087).
FT                                /FTId=VAR_052990.
SQ   SEQUENCE   490 AA;  56617 MW;  1AE2FAE62D2B28C6 CRC64;
     MTIGRMENVE VFTAEGKGRG LKATKEFWAA DIIFAERAYS AVVFDSLVNF VCHTCFKRQE
     KLHRCGQCKF AHYCDRTCQK DAWLNHKNEC SAIKRYGKVP NENIRLAARI MWRVEREGTG
     LTEGCLVSVD DLQNHVEHFG EEEQKDLRVD VDTFLQYWPP QSQQFSMQYI SHIFGVINCN
     GFTLSDQRGL QAVGVGIFPN LGLVNHDCWP NCTVIFNNGN HEAVKSMFHT QMRIELRALG
     KISEGEELTV SYIDFLNVSE ERKRQLKKQY YFDCTCEHCQ KKLKDDLFLG VKDNPKPSQE
     VVKEMIQFSK DTLEKIDKAR SEGLYHEVVK LCRECLEKQE PVFADTNIYM LRMLSIVSEV
     LSYLQAFEEA SFYARRMVDG YMKLYHPNNA QLGMAVMRAG LTNWHAGNIE VGHGMICKAY
     AILLVTHGPS HPITKDLEAM RVQTEMELRM FRQNEFMYYK MREAALNNQP MQVMAEPSNE
     PSPALFHKKQ
//
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