GenomeNet

Database: UniProt
Entry: Q5RGL7
LinkDB: Q5RGL7
Original site: Q5RGL7 
ID   SMY2B_DANRE             Reviewed;         434 AA.
AC   Q5RGL7; Q1JPT4;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 2.
DT   13-FEB-2019, entry version 105.
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=smyd2b; ORFNames=si:dkey-121j17.3;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C.,
RA   Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L.,
RA   McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C.,
RA   Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T.,
RA   Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T.,
RA   Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F.,
RA   Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H.,
RA   Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G.,
RA   Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B.,
RA   Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S.,
RA   Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C.,
RA   Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H.,
RA   Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C.,
RA   Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J.,
RA   Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S.,
RA   Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R.,
RA   Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R.,
RA   Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R.,
RA   Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A.,
RA   Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA   Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA   Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S.,
RA   Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J.,
RA   Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C.,
RA   Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H.,
RA   Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J.,
RA   Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the
RT   human genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5RGL7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5RGL7-2; Sequence=VSP_040727;
CC         Note=No experimental confirmation available.;
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAI20605.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; BX855610; CAI20605.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BC116606; AAI16607.1; -; mRNA.
DR   RefSeq; NP_001038756.1; NM_001045291.1. [Q5RGL7-2]
DR   RefSeq; XP_005164480.1; XM_005164423.3. [Q5RGL7-1]
DR   UniGene; Dr.48486; -.
DR   SMR; Q5RGL7; -.
DR   STRING; 7955.ENSDARP00000005268; -.
DR   PaxDb; Q5RGL7; -.
DR   Ensembl; ENSDART00000031759; ENSDARP00000036459; ENSDARG00000005629. [Q5RGL7-2]
DR   Ensembl; ENSDART00000162198; ENSDARP00000133013; ENSDARG00000005629. [Q5RGL7-1]
DR   GeneID; 568616; -.
DR   KEGG; dre:568616; -.
DR   CTD; 568616; -.
DR   ZFIN; ZDB-GENE-041001-201; smyd2b.
DR   eggNOG; KOG2084; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00940000166832; -.
DR   HOGENOM; HOG000007850; -.
DR   HOVERGEN; HBG098536; -.
DR   InParanoid; Q5RGL7; -.
DR   KO; K11426; -.
DR   OrthoDB; 981799at2759; -.
DR   PhylomeDB; Q5RGL7; -.
DR   TreeFam; TF106487; -.
DR   PRO; PR:Q5RGL7; -.
DR   Proteomes; UP000000437; Chromosome 20.
DR   Bgee; ENSDARG00000005629; Expressed in 11 organ(s), highest expression level in embryo.
DR   ExpressionAtlas; Q5RGL7; baseline.
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:0060047; P:heart contraction; IGI:ZFIN.
DR   GO; GO:0007507; P:heart development; IGI:ZFIN.
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   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   Alternative splicing; Chromatin regulator; Complete proteome;
KW   Cytoplasm; Metal-binding; Methyltransferase; Nucleus;
KW   Reference proteome; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase; Zinc; Zinc-finger.
FT   CHAIN         1    434       N-lysine methyltransferase SMYD2-B.
FT                                /FTId=PRO_0000405849.
FT   DOMAIN        8    242       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   ZN_FING      53     91       MYND-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00134}.
FT   REGION       18     20       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   REGION      184    186       Peptide substrate binding. {ECO:0000250}.
FT   REGION      207    208       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   REGION      259    261       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   BINDING     138    138       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   BINDING     241    241       Peptide substrate; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   VAR_SEQ     107    117       Missing (in isoform 2).
FT                                {ECO:0000303|Ref.2}.
FT                                /FTId=VSP_040727.
SQ   SEQUENCE   434 AA;  49630 MW;  EB9BB6A77675D2BA CRC64;
     MMKAEGIPGI EQFASPGKGR GLRVSRAYGV GELLFSCPAY SYVLSVGERG LICEQCFTRK
     KGLAKCGKCK KAFYCNANCQ KKNWPMHKLE CQAMCAFGEN WRPSETVRLV ARIIARLKAQ
     KERSPSEILL LLGEMEAHLE DMDNEKREMT EAHIAGLHQF YSKHLDFPDH QALLTLFSQV
     HCNGFTVEDE ELSNLGLAIF PDIALLNHSC SPNVIVTYRG INAEVRAVKD ISPGQEIYTS
     YIDLLYPTAD RLERLRDMYY FSCDCKECTT KSMDVVKMSV RKRSDEIGEK EIKDMVRYAR
     NSMENFRRAK QDKSPTELLE MCELSIDKMS TVFDDSNVYI LHMMYQAMGI CLFTEDYEGA
     VRYGEKVIKP FTVLYPAYSM NVASMFLKLG RLYIALDRKL AGIDAFQKAL TIMEVVHGKD
     HTYVTELKQE MRDF
//
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