GenomeNet

Database: UniProt
Entry: P97443
LinkDB: P97443
Original site: P97443 
ID   SMYD1_MOUSE             Reviewed;         490 AA.
AC   P97443; P97442; P97444; Q6DFW7;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 3.
DT   13-FEB-2019, entry version 136.
DE   RecName: Full=Histone-lysine N-methyltransferase Smyd1;
DE            EC=2.1.1.43;
DE   AltName: Full=CD8b-opposite;
DE   AltName: Full=SET and MYND domain-containing protein 1;
DE   AltName: Full=Zinc finger protein BOP;
DE            Short=m-BOP;
GN   Name=Smyd1; Synonyms=Bop;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), TISSUE SPECIFICITY,
RP   AND VARIANTS ARG-95; LEU-160 AND THR-344.
RC   STRAIN=BALB/cJ {ECO:0000269|PubMed:9013956}, and
RC   C57BL/6J {ECO:0000269|PubMed:9013956};
RC   TISSUE=Skeletal muscle {ECO:0000269|PubMed:9013956}, and
RC   Spleen {ECO:0000269|PubMed:9013956};
RX   PubMed=9013956;
RA   Hwang I., Gottlieb P.D.;
RT   "The Bop gene adjacent to the mouse CD8b gene encodes distinct zinc-
RT   finger proteins expressed in CTLs and in muscle.";
RL   J. Immunol. 158:1165-1174(1997).
RN   [2] {ECO:0000305}
RP   SEQUENCE REVISION TO N-TERMINUS.
RA   Gottlieb P.D., Hwang I.;
RL   Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Heart;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFOFRM 1).
RC   STRAIN=C57BL/6J; TISSUE=Eye;
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   [6] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION
RP   WITH HDAC1; HDAC2 AND HDAC3.
RX   PubMed=11923873; DOI=10.1038/ng866;
RA   Gottlieb P.D., Pierce S.A., Sims R.J. III, Yamagishi H., Weihe E.K.,
RA   Harriss J.V., Maika S.D., Kuziel W.A., King H.L., Olson E.N.,
RA   Nakagawa O., Srivastava D.;
RT   "Bop encodes a muscle-restricted protein containing MYND and SET
RT   domains and is essential for cardiac differentiation and
RT   morphogenesis.";
RL   Nat. Genet. 31:25-32(2002).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Heart;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH
RP   S-ADENOSYL-ORNITHINE, CATALYTIC ACTIVITY, ZINC-BINDING SITES,
RP   FUNCTION, AND INTERACTION WITH NACA ISOFORM SKNAC.
RX   PubMed=20943667; DOI=10.1074/jbc.M110.168187;
RA   Sirinupong N., Brunzelle J., Ye J., Pirzada A., Nico L., Yang Z.;
RT   "Crystal structure of cardiac-specific histone methyltransferase SmyD1
RT   reveals unusual active site architecture.";
RL   J. Biol. Chem. 285:40635-40644(2010).
CC   -!- FUNCTION: Methylates histone H3 at 'Lys-4' (H3K4me). Acts as a
CC       transcriptional repressor. Essential for cardiomyocyte
CC       differentiation and cardiac morphogenesis.
CC       {ECO:0000269|PubMed:11923873, ECO:0000269|PubMed:20943667}.
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:20943667};
CC   -!- SUBUNIT: Interacts with HDAC1, HDAC2 and HDAC3. Interacts (via
CC       MYND-type zinc finger) with NACA isoform skNAC.
CC       {ECO:0000269|PubMed:11923873, ECO:0000269|PubMed:20943667}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11923873}.
CC       Nucleus {ECO:0000269|PubMed:11923873}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=ISKM-BOP1 {ECO:0000269|PubMed:9013956};
CC         IsoId=P97443-1; Sequence=Displayed;
CC       Name=2; Synonyms=SKM-BOP2 {ECO:0000269|PubMed:9013956};
CC         IsoId=P97443-2; Sequence=VSP_050403, VSP_050404;
CC       Name=3; Synonyms=T-BOP {ECO:0000269|PubMed:9013956};
CC         IsoId=P97443-3; Sequence=VSP_050402;
CC   -!- TISSUE SPECIFICITY: Expressed in cardiac and skeletal muscle,
CC       lymphocytes and thymus. {ECO:0000269|PubMed:11923873,
CC       ECO:0000269|PubMed:9013956}.
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   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC53021.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=AAC53022.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
DR   EMBL; U76371; AAC53020.1; -; mRNA.
DR   EMBL; U76373; AAC53021.2; ALT_INIT; mRNA.
DR   EMBL; U76374; AAC53022.2; ALT_INIT; mRNA.
DR   EMBL; AK142252; BAE24995.1; -; mRNA.
DR   EMBL; CH466523; EDK98934.1; -; Genomic_DNA.
DR   EMBL; BC076601; AAH76601.1; -; mRNA.
DR   CCDS; CCDS20227.2; -. [P97443-2]
DR   CCDS; CCDS51805.1; -. [P97443-1]
DR   RefSeq; NP_001153599.1; NM_001160127.1. [P97443-1]
DR   RefSeq; NP_033892.2; NM_009762.2. [P97443-2]
DR   UniGene; Mm.234274; -.
DR   UniGene; Mm.440892; -.
DR   PDB; 3N71; X-ray; 2.30 A; A=1-490.
DR   PDBsum; 3N71; -.
DR   ProteinModelPortal; P97443; -.
DR   SMR; P97443; -.
DR   BioGrid; 198379; 5.
DR   ELM; P97443; -.
DR   IntAct; P97443; 2.
DR   MINT; P97443; -.
DR   STRING; 10090.ENSMUSP00000073911; -.
DR   iPTMnet; P97443; -.
DR   PhosphoSitePlus; P97443; -.
DR   MaxQB; P97443; -.
DR   PaxDb; P97443; -.
DR   PRIDE; P97443; -.
DR   Ensembl; ENSMUST00000074301; ENSMUSP00000073911; ENSMUSG00000055027. [P97443-1]
DR   Ensembl; ENSMUST00000114186; ENSMUSP00000109824; ENSMUSG00000055027. [P97443-2]
DR   GeneID; 12180; -.
DR   KEGG; mmu:12180; -.
DR   UCSC; uc009cgj.2; mouse. [P97443-1]
DR   CTD; 150572; -.
DR   MGI; MGI:104790; Smyd1.
DR   eggNOG; KOG2084; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00940000156114; -.
DR   HOGENOM; HOG000050244; -.
DR   HOVERGEN; HBG054953; -.
DR   InParanoid; P97443; -.
DR   KO; K11426; -.
DR   OMA; GIFPNLC; -.
DR   OrthoDB; 981799at2759; -.
DR   PhylomeDB; P97443; -.
DR   TreeFam; TF106487; -.
DR   ChiTaRS; Smyd1; mouse.
DR   EvolutionaryTrace; P97443; -.
DR   PRO; PR:P97443; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   Bgee; ENSMUSG00000055027; Expressed in 198 organ(s), highest expression level in skeletal muscle tissue.
DR   ExpressionAtlas; P97443; baseline and differential.
DR   Genevisible; P97443; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
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; IDA:MGI.
DR   GO; GO:0006338; P:chromatin remodeling; IPI:MGI.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
DR   GO; GO:0045663; P:positive regulation of myoblast differentiation; ISO:MGI.
DR   GO; GO:0010831; P:positive regulation of myotube differentiation; ISO:MGI.
DR   GO; GO:0035914; P:skeletal muscle cell differentiation; IMP:MGI.
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   3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
KW   DNA-binding; Metal-binding; Methyltransferase; Nucleus; Polymorphism;
KW   Reference proteome; 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_0000218308.
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   REGION      205    206       S-adenosyl-L-methionine binding.
FT   REGION      270    272       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   METAL       208    208       Zinc.
FT   METAL       274    274       Zinc.
FT   METAL       276    276       Zinc.
FT   METAL       279    279       Zinc.
FT   BINDING     135    135       S-adenosyl-L-methionine.
FT   VAR_SEQ       6     45       MENVEVFTSEGKGRGLKATKEFWAADVIFAERAYSAVVFD
FT                                -> MKNGEACGGWQ (in isoform 3).
FT                                {ECO:0000303|PubMed:9013956}.
FT                                /FTId=VSP_050402.
FT   VAR_SEQ     220    220       N -> K (in isoform 2).
FT                                {ECO:0000303|PubMed:9013956}.
FT                                /FTId=VSP_050403.
FT   VAR_SEQ     221    233       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:9013956}.
FT                                /FTId=VSP_050404.
FT   VARIANT      95     95       K -> R (in strain: C57BL/6).
FT                                {ECO:0000269|PubMed:9013956}.
FT   VARIANT     160    160       P -> L (in strain: C57BL/6).
FT                                {ECO:0000269|PubMed:9013956}.
FT   VARIANT     344    344       A -> T (in strain: C57BL/6).
FT                                {ECO:0000269|PubMed:9013956}.
FT   STRAND        9     13       {ECO:0000244|PDB:3N71}.
FT   STRAND       15     17       {ECO:0000244|PDB:3N71}.
FT   STRAND       19     25       {ECO:0000244|PDB:3N71}.
FT   STRAND       32     36       {ECO:0000244|PDB:3N71}.
FT   STRAND       39     43       {ECO:0000244|PDB:3N71}.
FT   HELIX        45     47       {ECO:0000244|PDB:3N71}.
FT   TURN         48     50       {ECO:0000244|PDB:3N71}.
FT   TURN         53     55       {ECO:0000244|PDB:3N71}.
FT   TURN         66     68       {ECO:0000244|PDB:3N71}.
FT   STRAND       72     75       {ECO:0000244|PDB:3N71}.
FT   HELIX        76     96       {ECO:0000244|PDB:3N71}.
FT   HELIX       102    116       {ECO:0000244|PDB:3N71}.
FT   STRAND      119    121       {ECO:0000244|PDB:3N71}.
FT   STRAND      126    128       {ECO:0000244|PDB:3N71}.
FT   HELIX       129    131       {ECO:0000244|PDB:3N71}.
FT   HELIX       136    138       {ECO:0000244|PDB:3N71}.
FT   HELIX       141    157       {ECO:0000244|PDB:3N71}.
FT   HELIX       167    178       {ECO:0000244|PDB:3N71}.
FT   STRAND      181    185       {ECO:0000244|PDB:3N71}.
FT   STRAND      191    197       {ECO:0000244|PDB:3N71}.
FT   HELIX       201    203       {ECO:0000244|PDB:3N71}.
FT   STRAND      211    217       {ECO:0000244|PDB:3N71}.
FT   STRAND      222    224       {ECO:0000244|PDB:3N71}.
FT   HELIX       228    230       {ECO:0000244|PDB:3N71}.
FT   STRAND      233    240       {ECO:0000244|PDB:3N71}.
FT   HELIX       259    270       {ECO:0000244|PDB:3N71}.
FT   HELIX       277    281       {ECO:0000244|PDB:3N71}.
FT   TURN        282    284       {ECO:0000244|PDB:3N71}.
FT   HELIX       285    288       {ECO:0000244|PDB:3N71}.
FT   STRAND      293    295       {ECO:0000244|PDB:3N71}.
FT   HELIX       299    320       {ECO:0000244|PDB:3N71}.
FT   TURN        321    323       {ECO:0000244|PDB:3N71}.
FT   HELIX       325    339       {ECO:0000244|PDB:3N71}.
FT   TURN        340    342       {ECO:0000244|PDB:3N71}.
FT   HELIX       348    363       {ECO:0000244|PDB:3N71}.
FT   HELIX       367    384       {ECO:0000244|PDB:3N71}.
FT   HELIX       390    405       {ECO:0000244|PDB:3N71}.
FT   HELIX       409    426       {ECO:0000244|PDB:3N71}.
FT   HELIX       432    465       {ECO:0000244|PDB:3N71}.
SQ   SEQUENCE   490 AA;  56496 MW;  5D18208678771CBE CRC64;
     MTIGSMENVE VFTSEGKGRG LKATKEFWAA DVIFAERAYS AVVFDSLINF VCHTCFKRQE
     KLHRCGQCKF AHYCDRTCQK DAWLNHKNEC AAIKKYGKVP NENIRLAARI MWRVEREGTG
     LTEGCLVSVD DLQNHVEHFG EEEQKELRVD VDTFLQYWPP QSQQFSMQYI SHIFGVINCN
     GFTLSDQRGL QAVGVGIFPN LGLVNHDCWP NCTVIFNNGN HEAVKSMFHT QMRIELRALG
     KISEGEELTV SYIDFLHLSE ERRRQLKKQY YFDCSCEHCQ KGLKDDLFLA AKEDPKPSQE
     VVKEMIQFSK DTLEKIDKAR SEGLYHEVVK LCRECLEKQE PVFADTNLYV LRLLSIASEV
     LSYLQAYEEA SHYARRMVDG YMKLYHHNNA QLGMAVMRAG LTNWHAGHIE VGHGMICKAY
     AILLVTHGPS HPITKDLEAM RMQTEMELRM FRQNEFMYHK MREAALNNQP MQVMAEPSNE
     PAPALFHKKQ
//
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