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Database: UniProt
Entry: Q1L8U8
LinkDB: Q1L8U8
Original site: Q1L8U8 
ID   STB1A_DANRE             Reviewed;        1436 AA.
AC   Q1L8U8;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   13-FEB-2019, entry version 94.
DE   RecName: Full=Histone-lysine N-methyltransferase SETDB1-A;
DE            EC=2.1.1.43;
DE   AltName: Full=SET domain bifurcated 1A;
GN   Name=setdb1a; ORFNames=si:ch211-81a5.6;
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).
CC   -!- FUNCTION: Histone methyltransferase that specifically
CC       trimethylates 'Lys-9' of histone H3. H3 'Lys-9' trimethylation
CC       represents a specific tag for epigenetic transcriptional
CC       repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to
CC       methylated histones. Mainly functions in euchromatin regions,
CC       thereby playing a central role in the silencing of euchromatic
CC       genes. H3 'Lys-9' trimethylation is coordinated with DNA
CC       methylation. Plays a role in promoter hypermethylation and
CC       transcriptional silencing of tumor suppressor genes (TSGs) or
CC       other tumor-related genes. Also required to maintain a
CC       transcriptionally repressive state of genes in undifferentiated
CC       embryonic stem cells (ESCs). Associates at promoter regions of
CC       tumor suppressor genes (TSGs) leading to their gene silencing (By
CC       similarity). {ECO:0000250|UniProtKB:Q15047}.
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: Nucleus {ECO:0000250}. Chromosome
CC       {ECO:0000250}. Note=Associated with non-pericentromeric regions of
CC       chromatin. Excluded from nucleoli and islands of condensed
CC       chromatin (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: In the pre-SET domain, Cys residues bind 3 zinc ions that
CC       are arranged in a triangular cluster; some of these Cys residues
CC       contribute to the binding of two zinc ions within the cluster.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. Suvar3-9 subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
DR   EMBL; CR626935; CAK04995.1; -; Genomic_DNA.
DR   RefSeq; NP_001038232.1; NM_001044767.2.
DR   UniGene; Dr.77930; -.
DR   ProteinModelPortal; Q1L8U8; -.
DR   SMR; Q1L8U8; -.
DR   STRING; 7955.ENSDARP00000060441; -.
DR   PaxDb; Q1L8U8; -.
DR   PRIDE; Q1L8U8; -.
DR   Ensembl; ENSDART00000060442; ENSDARP00000060441; ENSDARG00000041243.
DR   Ensembl; ENSDART00000088336; ENSDARP00000082769; ENSDARG00000041243.
DR   GeneID; 553292; -.
DR   KEGG; dre:553292; -.
DR   CTD; 553292; -.
DR   ZFIN; ZDB-GENE-030131-2421; setdb1a.
DR   eggNOG; KOG1141; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00940000157471; -.
DR   InParanoid; Q1L8U8; -.
DR   KO; K11421; -.
DR   OrthoDB; 183716at2759; -.
DR   PhylomeDB; Q1L8U8; -.
DR   TreeFam; TF106411; -.
DR   PRO; PR:Q1L8U8; -.
DR   Proteomes; UP000000437; Chromosome 19.
DR   Bgee; ENSDARG00000041243; Expressed in 29 organ(s), highest expression level in mature ovarian follicle.
DR   ExpressionAtlas; Q1L8U8; baseline.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0090309; P:positive regulation of methylation-dependent chromatin silencing; ISS:UniProtKB.
DR   GO; GO:0007265; P:Ras protein signal transduction; ISS:UniProtKB.
DR   InterPro; IPR016177; DNA-bd_dom_sf.
DR   InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR   InterPro; IPR007728; Pre-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   Pfam; PF01429; MBD; 1.
DR   Pfam; PF05033; Pre-SET; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00391; MBD; 1.
DR   SMART; SM00468; PreSET; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF54171; SSF54171; 1.
DR   PROSITE; PS50867; PRE_SET; 1.
DR   PROSITE; PS50280; SET; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator; Chromosome; Complete proteome; Metal-binding;
KW   Methyltransferase; Nucleus; Reference proteome; Repeat; Repressor;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase; Zinc.
FT   CHAIN         1   1436       Histone-lysine N-methyltransferase
FT                                SETDB1-A.
FT                                /FTId=PRO_0000281819.
FT   DOMAIN      633    697       Tudor 1.
FT   DOMAIN      724    780       Tudor 2.
FT   DOMAIN      938   1009       MBD.
FT   DOMAIN     1075   1148       Pre-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00157}.
FT   DOMAIN     1151   1411       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN     1420   1436       Post-SET.
FT   REGION     1161   1163       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   REGION     1368   1369       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   METAL      1077   1077       Zinc 1. {ECO:0000250}.
FT   METAL      1077   1077       Zinc 2. {ECO:0000250}.
FT   METAL      1079   1079       Zinc 1. {ECO:0000250}.
FT   METAL      1083   1083       Zinc 1. {ECO:0000250}.
FT   METAL      1083   1083       Zinc 3. {ECO:0000250}.
FT   METAL      1089   1089       Zinc 1. {ECO:0000250}.
FT   METAL      1091   1091       Zinc 2. {ECO:0000250}.
FT   METAL      1129   1129       Zinc 2. {ECO:0000250}.
FT   METAL      1129   1129       Zinc 3. {ECO:0000250}.
FT   METAL      1133   1133       Zinc 2. {ECO:0000250}.
FT   METAL      1135   1135       Zinc 3. {ECO:0000250}.
FT   METAL      1140   1140       Zinc 3. {ECO:0000250}.
FT   METAL      1371   1371       Zinc 4. {ECO:0000250}.
FT   METAL      1424   1424       Zinc 4. {ECO:0000250}.
FT   METAL      1426   1426       Zinc 4. {ECO:0000250}.
FT   METAL      1431   1431       Zinc 4. {ECO:0000250}.
FT   BINDING    1201   1201       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   BINDING    1365   1365       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
SQ   SEQUENCE   1436 AA;  160025 MW;  9C4174768AA95B5B CRC64;
     MSREKDDENL LRMTKDDLQR WIQAEVERNP HLMQRREQLA QVEEWVKQKE RDSTCTRLLY
     SNACESVLEC ESVMKGLYAL LGLDYRDEDS EEEGGGGQPH DVIQIADDEA ERRGNVICNG
     EDDDNDDLVV IDLGATKETL EPMLEKVTVA IQKSSKLVQD LVQMVSKTSM GATSPLSTSS
     SDINRPSSSS TPEIVRPESV TPKLEITNSI TIVKTESLSS VPKISSLFNS SEQCKSIADH
     DSYFKPTIKT EPEWTPLTPW EDSESSPFEK LIKTESQSTD VTPSVMTPNK QPELLSFQST
     TKIKPEPQST QANTELSSPP SNSKLLENHN SLSIAAIKNE SQLKASVSEV DLLESDSEQS
     DNAATKTRFK PSEVTASSKL KSSGDHNSAS ASLNRTDPKV RPVTPSGTPP PSKSPPAVDN
     TASVETNQTD SELPTETPVE ESTLPSNPKE AVIMSDAEST DKTEKPQTRK KSSKPSVTTT
     SPESRLTSSK SPPVTKTSST QKETARAQSP SDSIDESADM EDSPDEPSNS PTESPTKTPD
     KTTRNDAPAK PSKAKKSSKH SSSESSKTLK EIKLKVGAAV LGKKRHNHWS RGTVQEVETE
     DDGNTYKVEF KKGKTIVLSA NHVAAYKPPS LKDLYIGCRV VASAKSENGK SLYNAGVMVE
     LPERKNRMRF LVFFDDGLAT YLALPDLYFV CKQTKKVWRE IKDESSRKQV KDYLQVYPNP
     IAVVLRLGQE TKAVRNGQFE DCTVLQLDGS LVQICYKNDK QKEWIYKGSD KLEHILTIKN
     RHKQHSHKKH HSPEGKTQSS QPKTLHSSKS ASTSTSSANV SPVSSDSVSP ARVTRQSDKT
     KTSISPQKIM SPAFQPKVVL QKISLPSSIS PAARVSNSNT NSSLISAKRP APDEEEDEYF
     SEDEVEVLEQ EQNKSVYLHQ RCCPACLEEV RPHQVDIHHG KNPLLIPLLF KFRRMTARRR
     IDGKLFFHIF YRSPCGRSLC DMQEVQDYLF ETRCDFLFLE MFCMDPFVLV NRARPPSTTT
     GQPHLYLPDI SEGKEVMPVP CVNEVDNTLA PNVTYTKDRV PARGVFINTS SDFMVGCDCT
     DGCRDRSKCA CHKLTIEATS LCTGGPVDVS AGYTHKRLPT SLPTGVYECN PLCRCDPRMC
     SNRLVQHGMQ LRLELFMTQH KGWGIRCKDD VPKGTFVCVF TGKIVNEDKM NEDDTMSGNE
     YLANLDFIEG VEKLKEGYES EAYCSDTEVE SSKKTITMKT GPLLKNSLYK EDSSSGEEPM
     EVDTAKDKVK VHDKPLGERK LPNKPHETPK DTQKKISELR KNDGQESSGP KRCFAIKSFQ
     RRVKPLESTE AQKEKTKTPK NTRGLFNDED ACYIIDARQE GNLGRYINHS CSPNLFVQNV
     FVDTHDLRFP WVAFFASKRI KAGTELTWDY NYEVGSVEGK VLLCCCGSLR CTGRLL
//
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