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Database: UniProt/SWISS-PROT
Entry: SETB2_XENLA
LinkDB: SETB2_XENLA
Original site: SETB2_XENLA 
ID   SETB2_XENLA             Reviewed;         703 AA.
AC   Q6YI93; B7ZRV6;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
DT   30-AUG-2017, entry version 75.
DE   RecName: Full=Histone-lysine N-methyltransferase SETDB2;
DE            EC=2.1.1.43;
DE   AltName: Full=Chronic lymphocytic leukemia deletion region gene 8 protein homolog;
DE   AltName: Full=SET domain bifurcated 2;
GN   Name=setdb2; Synonyms=clld8;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Ruzov A., Meehan R.;
RT   "Molecular cloning and analysis of the expression of SET-domain
RT   putative histone methyltransferase CLLD8 in Xenopus laevis.";
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Oocyte;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Histone methyltransferase involved in left-right axis
CC       specification in early development and mitosis. Specifically
CC       trimethylates 'Lys-9' of histone H3 (H3K9me3). H3K9me3 is a
CC       specific tag for epigenetic transcriptional repression that
CC       recruits HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated
CC       histones. Contributes to H3K9me3 in both the interspersed
CC       repetitive elements and centromere-associated repeats. Plays a
CC       role in chromosome condensation and segregation during mitosis (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
CC       S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome
CC       {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. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN61106.1; Type=Frameshift; Positions=695; Evidence={ECO:0000305};
DR   EMBL; AY145835; AAN61106.1; ALT_FRAME; mRNA.
DR   EMBL; BC170303; AAI70303.1; -; mRNA.
DR   RefSeq; NP_001082765.1; NM_001089296.1.
DR   UniGene; Xl.29790; -.
DR   MaxQB; Q6YI93; -.
DR   GeneID; 398711; -.
DR   KEGG; xla:398711; -.
DR   CTD; 398711; -.
DR   Xenbase; XB-GENE-1219036; setdb2.
DR   HOVERGEN; HBG106688; -.
DR   KO; K18494; -.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0046974; F:histone methyltransferase activity (H3-K9 specific); ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB.
DR   GO; GO:0001947; P:heart looping; ISS:UniProtKB.
DR   GO; GO:0051567; P:histone H3-K9 methylation; ISS:UniProtKB.
DR   GO; GO:0070986; P:left/right axis specification; ISS:UniProtKB.
DR   GO; GO:0000278; P:mitotic cell cycle; ISS:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   InterPro; IPR016177; DNA-bd_dom.
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   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; PS50868; POST_SET; 1.
DR   PROSITE; PS50867; PRE_SET; 1.
DR   PROSITE; PS50280; SET; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Chromatin regulator; Chromosome;
KW   Developmental protein; Metal-binding; Methyltransferase; Mitosis;
KW   Nucleus; S-adenosyl-L-methionine; Transferase; Zinc.
FT   CHAIN         1    703       Histone-lysine N-methyltransferase
FT                                SETDB2.
FT                                /FTId=PRO_0000281825.
FT   DOMAIN      178    248       MBD.
FT   DOMAIN      310    384       Pre-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00157}.
FT   DOMAIN      387    678       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   REGION      397    399       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   REGION      635    636       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   METAL       312    312       Zinc 1. {ECO:0000250}.
FT   METAL       312    312       Zinc 2. {ECO:0000250}.
FT   METAL       314    314       Zinc 1. {ECO:0000250}.
FT   METAL       318    318       Zinc 1. {ECO:0000250}.
FT   METAL       318    318       Zinc 3. {ECO:0000250}.
FT   METAL       324    324       Zinc 1. {ECO:0000250}.
FT   METAL       326    326       Zinc 2. {ECO:0000250}.
FT   METAL       365    365       Zinc 2. {ECO:0000250}.
FT   METAL       365    365       Zinc 3. {ECO:0000250}.
FT   METAL       369    369       Zinc 2. {ECO:0000250}.
FT   METAL       371    371       Zinc 3. {ECO:0000250}.
FT   METAL       376    376       Zinc 3. {ECO:0000250}.
FT   METAL       638    638       Zinc 4. {ECO:0000250}.
FT   METAL       691    691       Zinc 4. {ECO:0000250}.
FT   METAL       693    693       Zinc 4. {ECO:0000250}.
FT   METAL       698    698       Zinc 4. {ECO:0000250}.
FT   BINDING     632    632       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   CONFLICT     97     97       K -> Q (in Ref. 1; AAN61106).
FT                                {ECO:0000305}.
FT   CONFLICT    175    175       S -> P (in Ref. 1; AAN61106).
FT                                {ECO:0000305}.
SQ   SEQUENCE   703 AA;  78698 MW;  12D86C32892B5325 CRC64;
     MEQSANARQS TLRSRTQELN TLSVLSKDVS LEDAKKYWKD RQADGKVDWI FEKVLNKLKI
     LWQKIKDGSA TNLEYVRAVI LVNEAGNLEE DLEEDLKEDT DTIHIDIHKE NEVQENTDCS
     PERKEDTCLN LNTDCGTDVS GSEPECNSTV SPPAAERVYF GNHSCGPSCL SGINSFLFTK
     GNPLQLPISC DFQRCHLKIN SPDDLSHILY KAPCGRSLRD YDEVHSYLTE TGCHFLAVDN
     FSFNNHVRLD SNSSFNQGIV QDCDISNDVE SVPVAFSNEI DNTRPSNFIY RKTSWPPGYS
     LNNFTDIFVK CCNCTDGCLD ILTCSCLQLT AQAFTKCMES SLGIGPLGYK HKRLQEPIPT
     GLYECNVSCK CDRMLCQNRV VQHGLKLRLQ VFKTNTKGWG VRCLDDVDKG TFVCIYAGRI
     LIRTADCTVK STPDDSVACG NEDHEDSTST CALILSKRKR KTSHSDSEVT VMHTNPYSMR
     SHGLSVHRLS NTFSPRQARS GEREFSLQPL RRPKTKTSML QKRRRQLIEE GACTVQNSSE
     EEGPTPPQSP EQKSSAGTKI QRNENSDETA SGYVSEESSS SVISGGHPLE KPISKFKSKL
     NKTTVYLSTS PEQTCEENLH FLDASKEGNV GRFLNHSCCP NLFVQQVFVD THQKCFPWVA
     FFTNSVVKAG TELTWDYSYD IGTAADQEIQ CLCGQKTCKN KVV
//
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