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Database: UniProt
Entry: Q7M6Z3
LinkDB: Q7M6Z3
Original site: Q7M6Z3 
ID   SMYD2_RAT               Reviewed;         433 AA.
AC   Q7M6Z3;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   13-FEB-2019, entry version 105.
DE   RecName: Full=N-lysine methyltransferase SMYD2;
DE            EC=2.1.1.-;
DE   AltName: Full=Histone methyltransferase SMYD2;
DE            EC=2.1.1.43;
DE   AltName: Full=SET and MYND domain-containing protein 2;
GN   Name=Smyd2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=12783626; DOI=10.1186/1471-2164-4-22;
RA   Oduru S., Campbell J.L., Karri S., Hendry W.J., Khan S.A.,
RA   Williams S.C.;
RT   "Gene discovery in the hamster: a comparative genomics approach for
RT   gene annotation by sequencing of hamster testis cDNAs.";
RL   BMC Genomics 4:22-22(2003).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
RA   Lundby C., Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14
RT   different rat organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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' (By similarity). {ECO:0000250}.
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 RNA polymerase II and HELZ. Interacts with
CC       SIN3A and HDAC1. Interacts (via MYND-type zinc finger) with
CC       EPB41L3. Interacts (via SET domain) with p53/TP53. Interacts with
CC       RB1 and HSP90AA1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Nucleus
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
DR   EMBL; BK001057; DAA01315.1; -; mRNA.
DR   RefSeq; NP_996733.1; NM_206851.1.
DR   UniGene; Rn.7052; -.
DR   ProteinModelPortal; Q7M6Z3; -.
DR   SMR; Q7M6Z3; -.
DR   STRING; 10116.ENSRNOP00000004783; -.
DR   iPTMnet; Q7M6Z3; -.
DR   PhosphoSitePlus; Q7M6Z3; -.
DR   jPOST; Q7M6Z3; -.
DR   PaxDb; Q7M6Z3; -.
DR   PRIDE; Q7M6Z3; -.
DR   Ensembl; ENSRNOT00000004783; ENSRNOP00000004783; ENSRNOG00000003583.
DR   GeneID; 289372; -.
DR   KEGG; rno:289372; -.
DR   CTD; 56950; -.
DR   RGD; 727785; Smyd2.
DR   eggNOG; KOG2084; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00940000157082; -.
DR   HOGENOM; HOG000007850; -.
DR   HOVERGEN; HBG098536; -.
DR   InParanoid; Q7M6Z3; -.
DR   KO; K11426; -.
DR   OMA; AVQEIHP; -.
DR   OrthoDB; 981799at2759; -.
DR   PhylomeDB; Q7M6Z3; -.
DR   TreeFam; TF106487; -.
DR   Reactome; R-RNO-3214841; PKMTs methylate histone lysines.
DR   Reactome; R-RNO-6804760; Regulation of TP53 Activity through Methylation.
DR   PRO; PR:Q7M6Z3; -.
DR   Proteomes; UP000002494; Chromosome 13.
DR   Bgee; ENSRNOG00000003583; Expressed in 10 organ(s), highest expression level in skeletal muscle tissue.
DR   Genevisible; Q7M6Z3; RN.
DR   GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR   GO; GO:0005829; C:cytosol; IDA:RGD.
DR   GO; GO:0005634; C:nucleus; IDA:RGD.
DR   GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0002039; F:p53 binding; IEA:Ensembl.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0000993; F:RNA polymerase II complex binding; ISS:UniProtKB.
DR   GO; GO:0007507; P:heart development; IEP:RGD.
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; ISS:UniProtKB.
DR   GO; GO:0018027; P:peptidyl-lysine dimethylation; ISS:UniProtKB.
DR   GO; GO:0018026; P:peptidyl-lysine monomethylation; ISS:UniProtKB.
DR   GO; GO:0043516; P:regulation of DNA damage response, signal transduction by p53 class mediator; ISS:UniProtKB.
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   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   Chromatin regulator; Complete proteome; Cytoplasm; Metal-binding;
KW   Methyltransferase; Nucleus; Phosphoprotein; 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_0000218311.
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                                {ECO:0000250}.
FT   REGION      183    185       Peptide substrate binding. {ECO:0000250}.
FT   REGION      206    207       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   REGION      258    260       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   BINDING     137    137       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   BINDING     240    240       Peptide substrate; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   MOD_RES     283    283       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
SQ   SEQUENCE   433 AA;  49648 MW;  7CE05492B8CA1578 CRC64;
     MRAEARGGLE RFCSAGKGRG LRALRPFHVG DLLFSCPAYA CVLTVGERGH HCECCFARKE
     GLSKCGRCKQ AFYCDVECQK EDWPLHKLEC SSMVVFGENW NPSETVRLTA RILAKQKMHP
     ERTPSEKLLA VREFESHLDK LDNEKKDLIQ SDIAALHQFY SKHLEFPDHS SLVVLFAQVN
     CNGFTIEDEE LSHLGSAIFP DVALMNHSCC PNVIVTYKGT LAEVRAVQEI HPGDEVFTSY
     IDLLYPTEDR NDRLRDSYFF TCECRECTTK DKDKAKVEIR KLSNPPQAEA IRDMVRYARN
     VIEEFRRAKH YKSPSELLEI CELSQEKMSS VFEDSNVYML HMMYQAMGVC LYMQDWEGAL
     KYGQKIIKPY SKHYPVYSLN VASMWLKLGR LYMGLENKAA GEKALKKAIA IMEIAHGKDH
     PYISEIKQEI ESH
//
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