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N-lysine methyltransferase SMYD2 (EC 2.1.1.-) (Histone methyltransferase SMYD2) (EC 2.1.1.43) (SET and MYND domain-containing protein 2)

 SMYD2_PIG               Reviewed;         433 AA.
C3RZA1;
08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
16-JUN-2009, sequence version 1.
28-MAR-2018, entry version 46.
RecName: Full=N-lysine methyltransferase SMYD2;
EC=2.1.1.-;
AltName: Full=Histone methyltransferase SMYD2;
EC=2.1.1.43;
AltName: Full=SET and MYND domain-containing protein 2;
Name=SMYD2;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
PubMed=19133938; DOI=10.1111/j.1365-2052.2008.01818.x;
Peng Y.B., Yerle M., Liu B.;
"Mapping and expression analyses during porcine foetal muscle
development of 12 genes involved in histone modifications.";
Anim. Genet. 40:242-246(2009).
-!- FUNCTION: Protein-lysine N-methyltransferase that methylates both
histones and non-histone proteins, including p53/TP53 and RB1.
Specifically methylates histone H3 'Lys-4' (H3K4me) and
dimethylates histone H3 'Lys-36' (H3K36me2). Shows even higher
methyltransferase activity on p53/TP53. Monomethylates 'Lys-370'
of p53/TP53, leading to decreased DNA-binding activity and
subsequent transcriptional regulation activity of p53/TP53.
Monomethylates RB1 at 'Lys-860' (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
-!- SUBUNIT: Interacts with RNA polymerase II and HELZ. Interacts with
SIN3A and HDAC1. Interacts (via MYND-type zinc finger) with
EPB41L3. Interacts (via SET domain) with p53/TP53. Interacts with
RB1 and HSP90AA1 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Nucleus
{ECO:0000250}.
-!- DEVELOPMENTAL STAGE: During fetal muscle development, expression
increases from 33 to 90 dpc. {ECO:0000269|PubMed:19133938}.
-!- SIMILARITY: Belongs to the class V-like SAM-binding
methyltransferase superfamily. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
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EMBL; EU661943; ACH71265.1; -; mRNA.
RefSeq; NP_001153563.1; NM_001160091.1.
UniGene; Ssc.13656; -.
STRING; 9823.ENSSSCP00000016522; -.
PaxDb; C3RZA1; -.
PRIDE; C3RZA1; -.
GeneID; 100294706; -.
KEGG; ssc:100294706; -.
CTD; 56950; -.
eggNOG; KOG2084; Eukaryota.
eggNOG; COG2940; LUCA.
HOGENOM; HOG000007850; -.
InParanoid; C3RZA1; -.
KO; K11426; -.
Proteomes; UP000008227; Unplaced.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016279; F:protein-lysine N-methyltransferase activity; ISS:UniProtKB.
GO; GO:0000993; F:RNA polymerase II core binding; ISS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0018027; P:peptidyl-lysine dimethylation; ISS:UniProtKB.
GO; GO:0018026; P:peptidyl-lysine monomethylation; ISS:UniProtKB.
GO; GO:0043516; P:regulation of DNA damage response, signal transduction by p53 class mediator; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.25.40.10; -; 1.
InterPro; IPR001214; SET_dom.
InterPro; IPR011990; TPR-like_helical_dom_sf.
InterPro; IPR002893; Znf_MYND.
Pfam; PF00856; SET; 1.
Pfam; PF01753; zf-MYND; 1.
SMART; SM00317; SET; 1.
SUPFAM; SSF48452; SSF48452; 1.
PROSITE; PS50280; SET; 1.
PROSITE; PS01360; ZF_MYND_1; 1.
PROSITE; PS50865; ZF_MYND_2; 1.
2: Evidence at transcript level;
Chromatin regulator; Complete proteome; Cytoplasm; Metal-binding;
Methyltransferase; Nucleus; Reference proteome;
S-adenosyl-L-methionine; Transcription; Transcription regulation;
Transferase; Zinc; Zinc-finger.
CHAIN 1 433 N-lysine methyltransferase SMYD2.
/FTId=PRO_0000405846.
DOMAIN 7 241 SET. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
ZN_FING 52 90 MYND-type. {ECO:0000255|PROSITE-
ProRule:PRU00134}.
REGION 17 19 S-adenosyl-L-methionine binding.
{ECO:0000250}.
REGION 183 185 Peptide substrate binding. {ECO:0000250}.
REGION 206 207 S-adenosyl-L-methionine binding.
{ECO:0000250}.
REGION 258 260 S-adenosyl-L-methionine binding.
{ECO:0000250}.
BINDING 137 137 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00190}.
BINDING 240 240 Peptide substrate; via carbonyl oxygen.
{ECO:0000250}.
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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