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Database: UniProt
Entry: Q6GN68
LinkDB: Q6GN68
Original site: Q6GN68 
ID   SMY2B_XENLA             Reviewed;         430 AA.
AC   Q6GN68;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   13-FEB-2019, entry version 73.
DE   RecName: Full=N-lysine methyltransferase SMYD2-B;
DE            EC=2.1.1.-;
DE   AltName: Full=Histone methyltransferase SMYD2-B;
DE            EC=2.1.1.43;
DE   AltName: Full=SET and MYND domain-containing protein 2B;
GN   Name=smyd2-b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=19003161; DOI=10.1007/s10616-008-9128-1;
RA   Kawamura S., Yoshigai E., Kuhara S., Tashiro K.;
RT   "smyd1 and smyd2 are expressed in muscle tissue in Xenopus laevis.";
RL   Cytotechnology 57:161-168(2008).
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   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Nucleus
CC       {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Expressed from stage 2, indicating it is
CC       expressed maternally. Expression is persistent through stage 40.
CC       {ECO:0000269|PubMed:19003161}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
DR   EMBL; BC073650; AAH73650.1; -; mRNA.
DR   RefSeq; NP_001085986.1; NM_001092517.1.
DR   UniGene; Xl.29550; -.
DR   ProteinModelPortal; Q6GN68; -.
DR   SMR; Q6GN68; -.
DR   MaxQB; Q6GN68; -.
DR   GeneID; 444415; -.
DR   KEGG; xla:444415; -.
DR   CTD; 444415; -.
DR   Xenbase; XB-GENE-17330768; smyd2.
DR   HOVERGEN; HBG098536; -.
DR   KO; K11426; -.
DR   OrthoDB; 981799at2759; -.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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:0016279; F:protein-lysine N-methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0000993; F:RNA polymerase II complex binding; ISS:UniProtKB.
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   SMART; SM00317; SET; 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   2: Evidence at transcript level;
KW   Chromatin regulator; Cytoplasm; Metal-binding; Methyltransferase;
KW   Nucleus; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase; Zinc; Zinc-finger.
FT   CHAIN         1    430       N-lysine methyltransferase SMYD2-B.
FT                                /FTId=PRO_0000405851.
FT   DOMAIN        5    239       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   ZN_FING      50     88       MYND-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00134}.
FT   REGION       15     17       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   REGION      181    183       Peptide substrate binding. {ECO:0000250}.
FT   REGION      204    205       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   REGION      256    258       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   BINDING     135    135       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   BINDING     238    238       Peptide substrate; via carbonyl oxygen.
FT                                {ECO:0000250}.
SQ   SEQUENCE   430 AA;  49119 MW;  43A35362BF585337 CRC64;
     MGQPEGLERF DSPGKGRGLK ATRSFALGEL LFSCPAYTYV LTDNERGNHC DFCFTRKEGL
     SKCGKCKQAF YCNVDCQKGD WPMHKLECSS MCSSGQNWCP SETVRLTARI LAKQKTQTER
     TASERFMSVK EFESHLSKLD NEKKELIEND ISALHRFYSK NVHNCDNAAL EFLFAQVNCN
     GFTIEDEELS HLGSAIFPDV ALMNHSCCPN VIVTYKGTVA EVRAVQEIHA GEEVFTSYID
     LLYPTEDRND RLKDSYFFSC DCRECSTKQK DPAKLELRKL SDPPSPQTVR DMITYARNVV
     EEFRRAKHYK TPSELLEICE LSLDKMGSVF VDSNVYMLHM MYQAMGVCLY MQDWEGALKY
     GEKIIKPYSK HYPAYSLNVA SMWLKLGRLY MGLEKNTIGT KALKKALAIM EIAHGPDHYY
     IAEIKKELEL
//
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