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STB1A_DANRE
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   03-AUG-2022, entry version 106.
DE   RecName: Full=Histone-lysine N-methyltransferase SETDB1-A;
DE            EC=2.1.1.354 {ECO:0000250|UniProtKB:Q15047};
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   Danionidae; Danioninae; 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., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., 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., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., 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., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
CC   -!- FUNCTION: Histone methyltransferase that specifically trimethylates
CC       'Lys-9' of histone H3. H3 'Lys-9' trimethylation represents a specific
CC       tag for epigenetic transcriptional repression by recruiting HP1 (CBX1,
CC       CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in
CC       euchromatin regions, thereby playing a central role in the silencing of
CC       euchromatic 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 other
CC       tumor-related genes. Also required to maintain a transcriptionally
CC       repressive state of genes in undifferentiated embryonic stem cells
CC       (ESCs). Associates at promoter regions of tumor suppressor genes (TSGs)
CC       leading to their gene silencing (By similarity).
CC       {ECO:0000250|UniProtKB:Q15047}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC         N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:60260, Rhea:RHEA-COMP:15537, Rhea:RHEA-
CC         COMP:15547, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.354;
CC         Evidence={ECO:0000250|UniProtKB:Q15047, ECO:0000255|PROSITE-
CC         ProRule:PRU00906};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC       Note=Associated with non-pericentromeric regions of chromatin. Excluded
CC       from nucleoli and islands of condensed chromatin (By similarity).
CC       {ECO:0000250}.
CC   -!- DOMAIN: In the pre-SET domain, Cys residues bind 3 zinc ions that are
CC       arranged in a triangular cluster; some of these Cys residues contribute
CC       to the binding of two zinc ions within the cluster. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC       superfamily. Histone-lysine methyltransferase family. Suvar3-9
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
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DR   EMBL; CR626935; CAK04995.1; -; Genomic_DNA.
DR   RefSeq; NP_001038232.1; NM_001044767.2.
DR   AlphaFoldDB; 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   GeneTree; ENSGT00940000157471; -.
DR   HOGENOM; CLU_252145_0_0_1; -.
DR   InParanoid; Q1L8U8; -.
DR   OrthoDB; 183716at2759; -.
DR   PhylomeDB; Q1L8U8; -.
DR   TreeFam; TF106411; -.
DR   PRO; PR:Q1L8U8; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 19.
DR   Bgee; ENSDARG00000041243; Expressed in early embryo and 27 other tissues.
DR   ExpressionAtlas; Q1L8U8; baseline.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0046974; F:histone methyltransferase activity (H3-K9 specific); IBA:GO_Central.
DR   GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0070828; P:heterochromatin organization; IBA:GO_Central.
DR   GO; GO:0051567; P:histone H3-K9 methylation; IBA:GO_Central.
DR   GO; GO:0010629; P:negative regulation of gene expression; IBA:GO_Central.
DR   GO; GO:0090309; P:positive regulation of DNA methylation-dependent heterochromatin assembly; ISS:UniProtKB.
DR   GO; GO:0007265; P:Ras protein signal transduction; ISS:UniProtKB.
DR   Gene3D; 2.170.270.10; -; 2.
DR   InterPro; IPR016177; DNA-bd_dom_sf.
DR   InterPro; IPR040880; DUF5604.
DR   InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR   InterPro; IPR007728; Pre-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR041292; Tudor_4.
DR   InterPro; IPR041291; TUDOR_5.
DR   Pfam; PF18300; DUF5604; 1.
DR   Pfam; PF01429; MBD; 1.
DR   Pfam; PF05033; Pre-SET; 1.
DR   Pfam; PF00856; SET; 1.
DR   Pfam; PF18358; Tudor_4; 1.
DR   Pfam; PF18359; Tudor_5; 1.
DR   SMART; SM00391; MBD; 1.
DR   SMART; SM00468; PreSET; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF54171; SSF54171; 1.
DR   SUPFAM; SSF82199; SSF82199; 1.
DR   PROSITE; PS50867; PRE_SET; 1.
DR   PROSITE; PS50280; SET; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator; Chromosome; Metal-binding; Methyltransferase; Nucleus;
KW   Reference proteome; Repeat; Repressor; S-adenosyl-L-methionine;
KW   Transcription; Transcription regulation; Transferase; Zinc.
FT   CHAIN           1..1436
FT                   /note="Histone-lysine N-methyltransferase SETDB1-A"
FT                   /id="PRO_0000281819"
FT   DOMAIN          633..697
FT                   /note="Tudor 1"
FT   DOMAIN          724..780
FT                   /note="Tudor 2"
FT   DOMAIN          938..1009
FT                   /note="MBD"
FT   DOMAIN          1075..1148
FT                   /note="Pre-SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00157"
FT   DOMAIN          1151..1411
FT                   /note="SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   DOMAIN          1420..1436
FT                   /note="Post-SET"
FT   REGION          170..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          250..327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          344..570
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          781..849
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          869..894
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1247..1294
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        270..327
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        357..401
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        417..444
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        455..471
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        472..514
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        524..538
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        539..570
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        797..849
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        869..887
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1251..1294
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1077
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         1077
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         1079
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         1083
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         1083
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         1089
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         1091
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         1129
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         1129
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         1133
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         1135
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         1140
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         1161..1163
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         1201
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   BINDING         1365
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   BINDING         1368..1369
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         1371
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   BINDING         1424
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   BINDING         1426
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   BINDING         1431
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
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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