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SMYD2_RAT
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   03-AUG-2022, entry version 116.
DE   RecName: Full=N-lysine methyltransferase SMYD2;
DE            EC=2.1.1.- {ECO:0000250|UniProtKB:Q9NRG4};
DE   AltName: Full=Histone methyltransferase SMYD2;
DE            EC=2.1.1.354 {ECO:0000250|UniProtKB:Q9NRG4};
DE   AltName: Full=SET and MYND domain-containing protein 2;
GN   Name=Smyd2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   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., Williams S.C.;
RT   "Gene discovery in the hamster: a comparative genomics approach for gene
RT   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 BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   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 trimethylates histone H3 'Lys-4' (H3K4me3) in vivo. The
CC       activity requires interaction with HSP90alpha. Shows even higher
CC       methyltransferase activity on p53/TP53. Monomethylates 'Lys-370' of
CC       p53/TP53, leading to decreased DNA-binding activity and subsequent
CC       transcriptional regulation activity of p53/TP53. Monomethylates RB1 at
CC       'Lys-860'. {ECO:0000250|UniProtKB:Q9NRG4}.
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:0000250|UniProtKB:Q9NRG4};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[protein] + S-adenosyl-L-methionine = H(+) + N(6)-
CC         methyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:51736, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13053,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929;
CC         Evidence={ECO:0000250|UniProtKB:Q9NRG4};
CC   -!- SUBUNIT: Interacts with RNA polymerase II and HELZ. Interacts with
CC       SIN3A and HDAC1. Interacts (via MYND-type zinc finger) with EPB41L3.
CC       Interacts (via SET domain) with p53/TP53. Interacts with RB1 and
CC       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 methyltransferase
CC       superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
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DR   EMBL; BK001057; DAA01315.1; -; mRNA.
DR   RefSeq; NP_996733.1; NM_206851.1.
DR   AlphaFoldDB; 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   GeneTree; ENSGT00940000157082; -.
DR   HOGENOM; CLU_018406_0_0_1; -.
DR   InParanoid; Q7M6Z3; -.
DR   OMA; HYKAPPS; -.
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 skeletal muscle tissue and 20 other tissues.
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:0018024; F:histone-lysine N-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0002039; F:p53 binding; ISO:RGD.
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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0007507; P:heart development; IEP:RGD.
DR   GO; GO:0034968; P:histone lysine methylation; IBA:GO_Central.
DR   GO; GO:0016571; P:histone methylation; ISO: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   CDD; cd19202; SET_SMYD2; 1.
DR   Gene3D; 1.25.40.10; -; 1.
DR   Gene3D; 2.170.270.10; -; 1.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR044419; SMYD2_SET.
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   SUPFAM; SSF82199; SSF82199; 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; Cytoplasm; Metal-binding; Methyltransferase; Nucleus;
KW   Phosphoprotein; Reference proteome; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..433
FT                   /note="N-lysine methyltransferase SMYD2"
FT                   /id="PRO_0000218311"
FT   DOMAIN          7..241
FT                   /note="SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   ZN_FING         52..90
FT                   /note="MYND-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         17..19
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
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         55
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
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         68
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         74
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         78
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         86
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         90
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         137
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   BINDING         206..207
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         258..260
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         283
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|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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