GenomeNet

Database: UniProt
Entry: Q9CWR2
LinkDB: Q9CWR2
Original site: Q9CWR2 
ID   SMYD3_MOUSE             Reviewed;         428 AA.
AC   Q9CWR2; Q6P7V6; Q8BG90;
DT   16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   13-FEB-2019, entry version 121.
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;
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Brain cortex, Embryonic stem cell, and Medulla oblongata;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and FVB/N-3; TISSUE=Brain, and Mammary tumor;
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).
CC   -!- FUNCTION: Histone methyltransferase. Specifically methylates 'Lys-
CC       4' of histone H3, inducing di- and tri-methylation, but not
CC       monomethylation. Also methylates 'Lys-5' of histone H4. Plays an
CC       important role in transcriptional activation as a member of an RNA
CC       polymerase complex. Binds DNA containing 5'-CCCTCC-3' or 5'-
CC       GAGGGG-3' sequences. {ECO:0000250|UniProtKB:Q9H7B4}.
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   -!- ACTIVITY REGULATION: Histone methyltransferase activity strongly
CC       stimulated by HSPCA. {ECO:0000250|UniProtKB:Q9H7B4}.
CC   -!- SUBUNIT: Interacts with HSPCA. Interacts with HELZ. Interacts with
CC       POLR2A; the interaction may be indirect and may be mediated by
CC       HELZ. Interacts with HSP90AA1; this interaction enhances SMYD3
CC       histone-lysine N-methyltransferase.
CC       {ECO:0000250|UniProtKB:Q9H7B4}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H7B4}.
CC       Nucleus {ECO:0000250|UniProtKB:Q9H7B4}. Note=Mainly cytoplasmic
CC       when cells are arrested at G0/G1. Accumulates in the nucleus at S
CC       phase and G2/M. {ECO:0000250|UniProtKB:Q9H7B4}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. {ECO:0000255|PROSITE-ProRule:PRU00907}.
DR   EMBL; AK010447; BAB26947.1; -; mRNA.
DR   EMBL; AK044168; BAC31804.1; -; mRNA.
DR   EMBL; AK046829; BAC32887.1; -; mRNA.
DR   EMBL; BC052431; AAH52431.1; -; mRNA.
DR   EMBL; BC061485; AAH61485.1; -; mRNA.
DR   CCDS; CCDS15560.1; -.
DR   RefSeq; NP_081464.1; NM_027188.3.
DR   RefSeq; XP_006497045.1; XM_006496982.3.
DR   RefSeq; XP_017167700.1; XM_017312211.1.
DR   RefSeq; XP_017167702.1; XM_017312213.1.
DR   UniGene; Mm.222338; -.
DR   ProteinModelPortal; Q9CWR2; -.
DR   SMR; Q9CWR2; -.
DR   BioGrid; 213640; 1.
DR   IntAct; Q9CWR2; 3.
DR   STRING; 10090.ENSMUSP00000117410; -.
DR   iPTMnet; Q9CWR2; -.
DR   PhosphoSitePlus; Q9CWR2; -.
DR   EPD; Q9CWR2; -.
DR   MaxQB; Q9CWR2; -.
DR   PaxDb; Q9CWR2; -.
DR   PRIDE; Q9CWR2; -.
DR   Ensembl; ENSMUST00000128302; ENSMUSP00000117410; ENSMUSG00000055067.
DR   GeneID; 69726; -.
DR   KEGG; mmu:69726; -.
DR   UCSC; uc007dvj.1; mouse.
DR   CTD; 64754; -.
DR   MGI; MGI:1916976; Smyd3.
DR   eggNOG; KOG2084; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00940000156766; -.
DR   HOGENOM; HOG000007850; -.
DR   HOVERGEN; HBG105004; -.
DR   InParanoid; Q9CWR2; -.
DR   KO; K11426; -.
DR   OMA; DVCKVCL; -.
DR   OrthoDB; 981799at2759; -.
DR   PhylomeDB; Q9CWR2; -.
DR   TreeFam; TF106487; -.
DR   BRENDA; 2.1.1.43; 3474.
DR   Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR   ChiTaRS; Smyd3; mouse.
DR   PRO; PR:Q9CWR2; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   Bgee; ENSMUSG00000055067; Expressed in 167 organ(s), highest expression level in embryo.
DR   ExpressionAtlas; Q9CWR2; baseline and differential.
DR   Genevisible; Q9CWR2; MM.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000993; F:RNA polymerase II complex binding; IDA:MGI.
DR   GO; GO:0001162; F:RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0071549; P:cellular response to dexamethasone stimulus; IDA:MGI.
DR   GO; GO:0045184; P:establishment of protein localization; IMP:MGI.
DR   GO; GO:0014904; P:myotube cell development; IMP:MGI.
DR   GO; GO:0006469; P:negative regulation of protein kinase activity; IMP:MGI.
DR   GO; GO:0006334; P:nucleosome assembly; IMP:MGI.
DR   GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:MGI.
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   2: Evidence at transcript level;
KW   Acetylation; Chromatin regulator; Complete proteome; Cytoplasm;
KW   Metal-binding; Methyltransferase; Nucleus; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase; Zinc; Zinc-finger.
FT   CHAIN         1    428       Histone-lysine N-methyltransferase SMYD3.
FT                                /FTId=PRO_0000218313.
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:0000250|UniProtKB:Q9H7B4}.
FT   REGION      205    206       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250|UniProtKB:Q9H7B4}.
FT   REGION      272    428       C-terminal domain; essential for histone
FT                                methyltransferase activity, nuclear
FT                                localization and mediates interaction
FT                                with HSP90AA1.
FT                                {ECO:0000250|UniProtKB:Q9H7B4}.
FT   BINDING     124    124       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   BINDING     132    132       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   BINDING     239    239       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   BINDING     259    259       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   MOD_RES       1      1       N-acetylmethionine.
FT                                {ECO:0000250|UniProtKB:Q9H7B4}.
FT   CONFLICT    318    318       N -> D (in Ref. 2; AAH61485).
FT                                {ECO:0000305}.
SQ   SEQUENCE   428 AA;  49126 MW;  1EC765044E1FB0DA CRC64;
     MEALKVEKFT TANRGNGLRA VAPLRPGELL FRSDPLAYTV CKGSRGVVCD RCLLGKEKLM
     RCSQCRIAKY CSAKCQKKAW PDHRRECSCL KSCKPRYPPD SVRLLGRVIV KLMDEKPSES
     EKLYSFYDLE SNISKLTEDK KEGLRQLAMT FQHFMREEIQ DASQLPPSFD LFEAFAKVIC
     NSFTICNAEM QEVGVGLYPS MSLLNHSCDP NCSIVFNGPH LLLRAVREIE AGEELTICYL
     DMLMTSEERR KQLRDQYCFE CDCIRCQTQD KDADMLTGDE QIWKEVQESL KKIEELKAHW
     KWEQVLALCQ AIINSNSNRL PDINIYQLKV LDCAMDACIN LGMLEEALFY AMRTMEPYRI
     FFPGSHPVRG VQVMKVGKLQ LHQGMFPQAM KNLRLAFDIM KVTHGREHSL IEDLILLLEE
     CDANIRAS
//
DBGET integrated database retrieval system