GenomeNet

Database: UniProt
Entry: C3RZA1
LinkDB: C3RZA1
Original site: C3RZA1 
ID   SMYD2_PIG               Reviewed;         433 AA.
AC   C3RZA1;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   13-FEB-2019, entry version 51.
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   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC   Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX   PubMed=19133938; DOI=10.1111/j.1365-2052.2008.01818.x;
RA   Peng Y.B., Yerle M., Liu B.;
RT   "Mapping and expression analyses during porcine foetal muscle
RT   development of 12 genes involved in histone modifications.";
RL   Anim. Genet. 40:242-246(2009).
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   -!- DEVELOPMENTAL STAGE: During fetal muscle development, expression
CC       increases from 33 to 90 dpc. {ECO:0000269|PubMed:19133938}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
DR   EMBL; EU661943; ACH71265.1; -; mRNA.
DR   RefSeq; NP_001153563.1; NM_001160091.1.
DR   UniGene; Ssc.13656; -.
DR   STRING; 9823.ENSSSCP00000016522; -.
DR   PaxDb; C3RZA1; -.
DR   PRIDE; C3RZA1; -.
DR   GeneID; 100294706; -.
DR   KEGG; ssc:100294706; -.
DR   CTD; 56950; -.
DR   eggNOG; KOG2084; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   HOGENOM; HOG000007850; -.
DR   InParanoid; C3RZA1; -.
DR   KO; K11426; -.
DR   OrthoDB; 981799at2759; -.
DR   Proteomes; UP000008227; Unplaced.
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; Complete proteome; Cytoplasm; Metal-binding;
KW   Methyltransferase; Nucleus; 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_0000405846.
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}.
SQ   SEQUENCE   433 AA;  49870 MW;  D38765A5889BE160 CRC64;
     MRAEGDGGLE RFCSPGKGRG LRALQPFQVG DLLFSCPAYA YVLTVNERGN HCEFCFARKE
     GLSKCGRCKQ AFYCNVECQK EDWPMHKLEC SPMVVFGENW NPSETVRLTA RILAKQKIHP
     ERTPSEKLLA VKEFESHLDK LDNEKRDLIQ SDIAALHHFY SKHLEFPDSD SLVVLFAQVN
     CNGFTIEDEE LSHLGSXIFP DVALMNHSCC PNVIVTYKGT LAEVRAVQEI HPGEEVFTSY
     IDLLYPTEDR NDRLRDSYFF TCECQECTTK DKDKAKVEIR KLNDPPKAEA IRDMVRYARN
     VIEEFRRAKH YKSPSELLEI CELSQEKMSC VFEDSNVYML HMMYQAMGVC LYMQDWEGAL
     RYGQKIIQPY SKHYPLYSLN VASMWLKLGR LYMGLENKAA GERALRKAIA IMEVAHGKDH
     PYISEIKQEI ESH
//
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