GenomeNet

Database: UniProt
Entry: E1C5V0
LinkDB: E1C5V0
Original site: E1C5V0 
ID   SMYD2_CHICK             Reviewed;         436 AA.
AC   E1C5V0;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 1.
DT   13-FEB-2019, entry version 45.
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   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
OC   Phasianidae; Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15592404; DOI=10.1038/nature03154;
RA   Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C.,
RA   Ponting C.P., Bork P., Burt D.W., Groenen M.A.M., Delany M.E.,
RA   Dodgson J.B., Chinwalla A.T., Cliften P.F., Clifton S.W.,
RA   Delehaunty K.D., Fronick C., Fulton R.S., Graves T.A., Kremitzki C.,
RA   Layman D., Magrini V., McPherson J.D., Miner T.L., Minx P., Nash W.E.,
RA   Nhan M.N., Nelson J.O., Oddy L.G., Pohl C.S., Randall-Maher J.,
RA   Smith S.M., Wallis J.W., Yang S.-P., Romanov M.N., Rondelli C.M.,
RA   Paton B., Smith J., Morrice D., Daniels L., Tempest H.G.,
RA   Robertson L., Masabanda J.S., Griffin D.K., Vignal A., Fillon V.,
RA   Jacobbson L., Kerje S., Andersson L., Crooijmans R.P., Aerts J.,
RA   van der Poel J.J., Ellegren H., Caldwell R.B., Hubbard S.J.,
RA   Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M., Arakawa H.,
RA   Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA   Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA   Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA   Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S.,
RA   Miller M.M., Inoko H., Shiina T., Kaufman J., Salomonsen J.,
RA   Skjoedt K., Wong G.K.-S., Wang J., Liu B., Wang J., Yu J., Yang H.,
RA   Nefedov M., Koriabine M., Dejong P.J., Goodstadt L., Webber C.,
RA   Dickens N.J., Letunic I., Suyama M., Torrents D., von Mering C.,
RA   Zdobnov E.M., Makova K., Nekrutenko A., Elnitski L., Eswara P.,
RA   King D.C., Yang S.-P., Tyekucheva S., Radakrishnan A., Harris R.S.,
RA   Chiaromonte F., Taylor J., He J., Rijnkels M., Griffiths-Jones S.,
RA   Ureta-Vidal A., Hoffman M.M., Severin J., Searle S.M.J., Law A.S.,
RA   Speed D., Waddington D., Cheng Z., Tuzun E., Eichler E., Bao Z.,
RA   Flicek P., Shteynberg D.D., Brent M.R., Bye J.M., Huckle E.J.,
RA   Chatterji S., Dewey C., Pachter L., Kouranov A., Mourelatos Z.,
RA   Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA   Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA   Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J.,
RA   Betran E., Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G.,
RA   Furey T.S., Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D.,
RA   Eyras E., Castelo R., Abril J.F., Castellano S., Camara F., Parra G.,
RA   Guigo R., Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A.,
RA   Mardis E.R., Wilson R.K.;
RT   "Sequence and comparative analysis of the chicken genome provide
RT   unique perspectives on vertebrate evolution.";
RL   Nature 432:695-716(2004).
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   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
DR   EMBL; AADN02012084; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   UniGene; Gga.2851; -.
DR   SMR; E1C5V0; -.
DR   STRING; 9031.ENSGALP00000015907; -.
DR   PaxDb; E1C5V0; -.
DR   PRIDE; E1C5V0; -.
DR   eggNOG; KOG2084; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   InParanoid; E1C5V0; -.
DR   OrthoDB; 981799at2759; -.
DR   PhylomeDB; E1C5V0; -.
DR   TreeFam; TF106487; -.
DR   Proteomes; UP000000539; 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   3: Inferred from homology;
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    436       N-lysine methyltransferase SMYD2.
FT                                /FTId=PRO_0000405847.
FT   DOMAIN       10    244       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   ZN_FING      55     93       MYND-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00134}.
FT   REGION       20     22       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   REGION      186    188       Peptide substrate binding. {ECO:0000250}.
FT   REGION      209    210       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   REGION      261    263       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   BINDING     140    140       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   BINDING     243    243       Peptide substrate; via carbonyl oxygen.
FT                                {ECO:0000250}.
SQ   SEQUENCE   436 AA;  49947 MW;  F34E3381E2C17F76 CRC64;
     MRSEAVPQPG GLERFASPGK GRGLRALRRY AVGELLFSCP AYTAVLTVSE RGSHCDGCFA
     RKEGLSKCGR CKQAFYCNVE CQKEDWPMHK LECAAMCAFG QNWNPSETVR LTARILAKQK
     IHPERTQSEK LLAVKEFESH LDKLDNEKRE LIQNDIAALH HFYSKHMEYP DNAALVVLFA
     QVNCNGFTIE DEELSHLGSA IFPDVALMNH SCCPNVIVTY KGTLAEVRAV KEIEPGEEVF
     TSYIDLLYPT EDRNDRLRDS YFFTCDCREC TMKEKDKEKL KIRKLNDPPS AEAVRDMIKY
     ARNVIEEFRR AKHYKPPSEL LEICELSLDK MGAVFEDSNV YMLHMMYQAM GVCLYVQDWE
     GALRYGQKII RPYSKHYPSY SLNVASMWLK LGRLYMALEN RPAGDKALKK AIAIMEVAHG
     KDHPYISEIK KELEDH
//
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