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Database: UniProt
Entry: Q08BR4
LinkDB: Q08BR4
Original site: Q08BR4 
ID   STB1B_DANRE             Reviewed;        1216 AA.
AC   Q08BR4; Q06ZW4;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   05-DEC-2018, entry version 81.
DE   RecName: Full=Histone-lysine N-methyltransferase SETDB1-B;
DE            EC=2.1.1.43;
DE   AltName: Full=SET domain bifurcated 1B;
GN   Name=setdb1b; ORFNames=zgc:152899;
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 MRNA] OF 1-1204.
RC   STRAIN=AB;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 373-1216.
RC   TISSUE=Kidney marrow;
RX   PubMed=15520368; DOI=10.1073/pnas.0407241101;
RA   Song H.-D., Sun X.-J., Deng M., Zhang G.-W., Zhou Y., Wu X.-Y.,
RA   Sheng Y., Chen Y., Ruan Z., Jiang C.-L., Fan H.-Y., Zon L.I.,
RA   Kanki J.P., Liu T.X., Look A.T., Chen Z.;
RT   "Hematopoietic gene expression profile in zebrafish kidney marrow.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:16240-16245(2004).
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         Evidence={ECO:0000255|PROSITE-ProRule:PRU00906};
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:PRU00906}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI24602.1; Type=Frameshift; Positions=874; Evidence={ECO:0000305};
DR   EMBL; BC124601; AAI24602.1; ALT_FRAME; mRNA.
DR   EMBL; DQ358103; ABC88478.1; -; mRNA.
DR   UniGene; Dr.106645; -.
DR   UniGene; Dr.74521; -.
DR   ProteinModelPortal; Q08BR4; -.
DR   SMR; Q08BR4; -.
DR   STRING; 7955.ENSDARP00000082796; -.
DR   PaxDb; Q08BR4; -.
DR   PRIDE; Q08BR4; -.
DR   ZFIN; ZDB-GENE-061013-224; setdb1b.
DR   eggNOG; KOG1141; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   HOGENOM; HOG000154292; -.
DR   HOVERGEN; HBG061013; -.
DR   InParanoid; Q08BR4; -.
DR   PhylomeDB; Q08BR4; -.
DR   PRO; PR:Q08BR4; -.
DR   Proteomes; UP000000437; Unplaced.
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; IPR025796; Hist-Lys_N-MeTrfase_SETDB1.
DR   InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR007728; Pre-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR002999; Tudor.
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   SMART; SM00333; TUDOR; 2.
DR   SUPFAM; SSF54171; SSF54171; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50867; PRE_SET; 1.
DR   PROSITE; PS51573; SAM_MT43_SUVAR39_1; 1.
DR   PROSITE; PS50280; SET; 1.
PE   2: Evidence at transcript level;
KW   Chromatin regulator; Chromosome; Coiled coil; Complete proteome;
KW   Metal-binding; Methyltransferase; Nucleus; Reference proteome; Repeat;
KW   Repressor; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase; Zinc.
FT   CHAIN         1   1216       Histone-lysine N-methyltransferase
FT                                SETDB1-B.
FT                                /FTId=PRO_0000281820.
FT   DOMAIN      266    329       Tudor 1.
FT   DOMAIN      356    412       Tudor 2.
FT   DOMAIN      595    666       MBD.
FT   DOMAIN      728    801       Pre-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00157}.
FT   DOMAIN      804   1179       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN     1188   1204       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   REGION      814    816       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   REGION     1136   1137       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   COILED       38     61       {ECO:0000255}.
FT   METAL       730    730       Zinc 1. {ECO:0000250}.
FT   METAL       730    730       Zinc 2. {ECO:0000250}.
FT   METAL       732    732       Zinc 1. {ECO:0000250}.
FT   METAL       736    736       Zinc 1. {ECO:0000250}.
FT   METAL       736    736       Zinc 3. {ECO:0000250}.
FT   METAL       742    742       Zinc 1. {ECO:0000250}.
FT   METAL       744    744       Zinc 2. {ECO:0000250}.
FT   METAL       782    782       Zinc 2. {ECO:0000250}.
FT   METAL       782    782       Zinc 3. {ECO:0000250}.
FT   METAL       786    786       Zinc 2. {ECO:0000250}.
FT   METAL       788    788       Zinc 3. {ECO:0000250}.
FT   METAL       793    793       Zinc 3. {ECO:0000250}.
FT   METAL      1139   1139       Zinc 4. {ECO:0000250}.
FT   METAL      1192   1192       Zinc 4. {ECO:0000250}.
FT   METAL      1194   1194       Zinc 4. {ECO:0000250}.
FT   METAL      1199   1199       Zinc 4. {ECO:0000250}.
FT   BINDING     852    852       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   BINDING     854    854       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   BINDING    1133   1133       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
SQ   SEQUENCE   1216 AA;  135811 MW;  44C38E80B5941AAD CRC64;
     MEMELEPELE EELGVSLDEL RKWIEEQVDS SEAVQKRKAD LEQLQEWVEQ REKEVADIDA
     LCSNASESVV QCEALVKEVY SNMGLVYRES SSDDEGGKAN PSEVIEIDDD DDDDVIAVGC
     LVPPKKSLTQ AKDPALKEAS AALQRTSQQV QNLAQTVNRT AQSGVTTPVK TGGPPGQGPL
     AVPAVFMSSA PRNTPTQPNP NIKQDSIKIN MTLLGKKRTK TWHRGTLVAI KQVGNNLKYK
     VRFENKGKSL LSGNHVAFEY HPTLERLFVG ARVVARYKDG NQVWLYAGVV AEMPNSKNRM
     RFLIFFDDGY ASYVGLPELY PICRPLKKTW EDIEDASCRD FIEEYITSYP NRPMVLLKPG
     QIIKTEWEGT WWKSRVEEVD GSLVKMLFLD DKRSEWIYRG STRLEPMFNL KMNTANSQEK
     KMAGQQRQRP NMGALRTKGP VVQYTSDNSA AASTGGGAAT PGTPTRPVAP QPAGPPQPSR
     TESPSFKSQM AKKSTGQLAL QPRQGMPSDL QPKPIINALQ TNTSRLFLLQ SGPVHTLTPI
     TPAPQTVQTA ISTYTNERVP QEPSYQAPND RLFYLTHNCS PECLKRIRPT RPNLHRGRNP
     LLTPLLYEFR RMTGRRRLNR KMSFHVIYKS PCGLSLRNMT EIQRYLFQTQ CDFIFLEMFC
     LDPYVLVDRR FQPQRPFYFI RDITSGREDI PLSCVNEIDN TPPPSVAYSK ERIPEDGVYI
     NTSADFLVGC DCTDGCRDKS KCSCHQLTLQ ATGCTPGGQI NPNAGYHYKR LDECLPTGIY
     ECNKRCRCNM QMCTNRLVQH GLQVRLQLFK TQNKGWGIRC LDDIAKGSFV CIYAGKILTD
     DFADKEGLEM GDEYFANLDH IESVENFKEG YESEAHCSDS EGSGVDMSRV KLPASSRHGK
     SNKMEERNSS TTGKSQDDSS EESDDEKDDD SNEDDSDSSD DTFVKDTYYT TSSVWRSYTT
     RRQAKGLKEE SQDSKDGMSV SAGEDRKPPH MPEETGKSKV ASWLTNQSST SANQSVKVEG
     GIKTEKKDVM TLSDSDDVQT ISSGSDDNKE REKKTQAVVK RQVAVKSTRG IALKSHSMMV
     KSGGGGAGGG GSGPSHGHGG GGGDNGPKNT RLFFDGEESC YIIDAKLEGN LGRYLNHSCS
     PNLFVQNVFV DTHDLRFPWV AFFASKRIRA GTELTWDYNY EVGSVEGKEL LCCCGSTECR
     GRLLQIIKTE WEGTWW
//
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