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Database: UniProt
Entry: A2A935
LinkDB: A2A935
Original site: A2A935 
ID   PRD16_MOUSE             Reviewed;        1275 AA.
AC   A2A935; Q69ZD6; Q6PB79; Q7TPF4;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   10-APR-2019, entry version 100.
DE   RecName: Full=Histone-lysine N-methyltransferase PRDM16 {ECO:0000305};
DE            EC=2.1.1.43 {ECO:0000269|PubMed:22939622};
DE   AltName: Full=PR domain zinc finger protein 16 {ECO:0000305};
DE   AltName: Full=PR domain-containing protein 16 {ECO:0000305};
DE   AltName: Full=Transcription factor MEL1 {ECO:0000305};
DE            Short=MDS1/EVI1-like gene 1 {ECO:0000303|PubMed:12816872};
GN   Name=Prdm16 {ECO:0000312|MGI:MGI:1917923};
GN   Synonyms=Kiaa1675 {ECO:0000305}, Mel1 {ECO:0000303|PubMed:12816872};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Placenta;
RX   PubMed=12816872; DOI=10.1182/blood-2002-12-3944;
RA   Nishikata I., Sasaki H., Iga M., Tateno Y., Imayoshi S., Asou N.,
RA   Nakamura T., Morishita K.;
RT   "A novel EVI1 gene family, MEL1, lacking a PR domain (MEL1S) is
RT   expressed mainly in t(1;3)(p36;q21)-positive AML and blocks G-CSF-
RT   induced myeloid differentiation.";
RL   Blood 102:3323-3332(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 570-1275 (ISOFORM 3).
RC   TISSUE=Pancreatic islet;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [5]
RP   INTERACTION WITH SMAD3, AND DEVELOPMENTAL STAGE.
RX   PubMed=17467076; DOI=10.1016/j.bbamcr.2007.03.016;
RA   Warner D.R., Horn K.H., Mudd L., Webb C.L., Greene R.M., Pisano M.M.;
RT   "PRDM16/MEL1: a novel Smad binding protein expressed in murine
RT   embryonic orofacial tissue.";
RL   Biochim. Biophys. Acta 1773:814-820(2007).
RN   [6]
RP   FUNCTION, INTERACTION WITH PPARGC1A AND PPARGC1B, MUTAGENESIS OF
RP   ARG-996, AND TISSUE SPECIFICITY.
RX   PubMed=17618855; DOI=10.1016/j.cmet.2007.06.001;
RA   Seale P., Kajimura S., Yang W., Chin S., Rohas L.M., Uldry M.,
RA   Tavernier G., Langin D., Spiegelman B.M.;
RT   "Transcriptional control of brown fat determination by PRDM16.";
RL   Cell Metab. 6:38-54(2007).
RN   [7]
RP   FUNCTION, INTERACTION WITH CTBP1; CTBP2; PPARGC1A AND PPARGC1B,
RP   SUBCELLULAR LOCATION, MUTAGENESIS OF 805-ASP-LEU-806, AND REGION.
RX   PubMed=18483224; DOI=10.1101/gad.1666108;
RA   Kajimura S., Seale P., Tomaru T., Erdjument-Bromage H., Cooper M.P.,
RA   Ruas J.L., Chin S., Tempst P., Lazar M.A., Spiegelman B.M.;
RT   "Regulation of the brown and white fat gene programs through a
RT   PRDM16/CtBP transcriptional complex.";
RL   Genes Dev. 22:1397-1409(2008).
RN   [8]
RP   FUNCTION, INTERACTION WITH PPARA AND PPARG, AND DISRUPTION PHENOTYPE.
RX   PubMed=18719582; DOI=10.1038/nature07182;
RA   Seale P., Bjork B., Yang W., Kajimura S., Chin S., Kuang S., Scime A.,
RA   Devarakonda S., Conroe H.M., Erdjument-Bromage H., Tempst P.,
RA   Rudnicki M.A., Beier D.R., Spiegelman B.M.;
RT   "PRDM16 controls a brown fat/skeletal muscle switch.";
RL   Nature 454:961-967(2008).
RN   [9]
RP   FUNCTION, AND INTERACTION WITH CEBPA; CEBPB AND CEBPD.
RX   PubMed=19641492; DOI=10.1038/nature08262;
RA   Kajimura S., Seale P., Kubota K., Lunsford E., Frangioni J.V.,
RA   Gygi S.P., Spiegelman B.M.;
RT   "Initiation of myoblast to brown fat switch by a PRDM16-C/EBP-beta
RT   transcriptional complex.";
RL   Nature 460:1154-1158(2009).
RN   [10]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=22939622; DOI=10.1016/j.cell.2012.06.048;
RA   Pinheiro I., Margueron R., Shukeir N., Eisold M., Fritzsch C.,
RA   Richter F.M., Mittler G., Genoud C., Goyama S., Kurokawa M., Son J.,
RA   Reinberg D., Lachner M., Jenuwein T.;
RT   "Prdm3 and Prdm16 are H3K9me1 methyltransferases required for
RT   mammalian heterochromatin integrity.";
RL   Cell 150:948-960(2012).
RN   [11]
RP   DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX   PubMed=23768516; DOI=10.1016/j.ajhg.2013.05.015;
RA   Arndt A.K., Schafer S., Drenckhahn J.D., Sabeh M.K., Plovie E.R.,
RA   Caliebe A., Klopocki E., Musso G., Werdich A.A., Kalwa H., Heinig M.,
RA   Padera R.F., Wassilew K., Bluhm J., Harnack C., Martitz J.,
RA   Barton P.J., Greutmann M., Berger F., Hubner N., Siebert R.,
RA   Kramer H.H., Cook S.A., MacRae C.A., Klaassen S.;
RT   "Fine mapping of the 1p36 deletion syndrome identifies mutation of
RT   PRDM16 as a cause of cardiomyopathy.";
RL   Am. J. Hum. Genet. 93:67-77(2013).
RN   [12]
RP   INTERACTION WITH ZNF516, AND REGION.
RX   PubMed=25578880; DOI=10.1016/j.molcel.2014.12.005;
RA   Dempersmier J., Sambeat A., Gulyaeva O., Paul S.M., Hudak C.S.,
RA   Raposo H.F., Kwan H.Y., Kang C., Wong R.H., Sul H.S.;
RT   "Cold-inducible Zfp516 activates UCP1 transcription to promote
RT   browning of white fat and development of brown fat.";
RL   Mol. Cell 57:235-246(2015).
CC   -!- FUNCTION: Binds DNA and functions as a transcriptional regulator
CC       (PubMed:18483224). Displays histone methyltransferase activity and
CC       monomethylates 'Lys-9' of histone H3 (H3K9me1) in vitro
CC       (PubMed:22939622). Probably catalyzes the monomethylation of free
CC       histone H3 in the cytoplasm which is then transported to the
CC       nucleus and incorporated into nucleosomes where SUV39H
CC       methyltransferases use it as a substrate to catalyze histone H3
CC       'Lys-9' trimethylation (PubMed:22939622). Likely to be one of the
CC       primary histone methyltransferases along with MECOM/PRDM3 that
CC       direct cytoplasmic H3K9me1 methylation (PubMed:22939622).
CC       Functions in the differentiation of brown adipose tissue (BAT)
CC       which is specialized in dissipating chemical energy in the form of
CC       heat in response to cold or excess feeding while white adipose
CC       tissue (WAT) is specialized in the storage of excess energy and
CC       the control of systemic metabolism (PubMed:17618855,
CC       PubMed:18483224). Together with CEBPB, regulates the
CC       differentiation of myoblastic precursors into brown adipose cells
CC       (PubMed:18719582, PubMed:19641492). Functions as a repressor of
CC       TGF-beta signaling. {ECO:0000269|PubMed:17618855,
CC       ECO:0000269|PubMed:18483224, ECO:0000269|PubMed:18719582,
CC       ECO:0000269|PubMed:19641492, ECO:0000269|PubMed:22939622}.
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:0000269|PubMed:22939622};
CC   -!- SUBUNIT: Interacts with CEBPA, CEBPB and CEBPD; the interaction is
CC       direct (PubMed:19641492). Interacts with PPARG and PPARA; controls
CC       brown adipocytes (PubMed:18719582). Interacts with CTBP1 and
CC       CTBP2; represses the expression of WAT-specific genes
CC       (PubMed:18483224). Interacts with PPARGC1A and PPARGC1B;
CC       interaction with PPARGC1A or PPARGC1B activates the transcription
CC       of BAT-specific gene (PubMed:18483224, PubMed:17618855). Interacts
CC       with HDAC1, SKI and SMAD2; the interaction with SKI promotes the
CC       recruitment of SMAD3-HDAC1 complex on the promoter of TGF-beta
CC       target genes (Probable). Interacts with ZNF516; the interaction is
CC       direct and may play a role in the transcription of brown adipose
CC       tissue-specific gene (PubMed:25578880).
CC       {ECO:0000269|PubMed:17618855, ECO:0000269|PubMed:18483224,
CC       ECO:0000269|PubMed:18719582, ECO:0000269|PubMed:19641492,
CC       ECO:0000269|PubMed:25578880, ECO:0000305|PubMed:17467076}.
CC   -!- INTERACTION:
CC       Q5DW34-1:Ehmt1; NbExp=2; IntAct=EBI-16080455, EBI-16080518;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18483224}.
CC       Cytoplasm {ECO:0000250|UniProtKB:Q9HAZ2}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=A2A935-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A2A935-2; Sequence=VSP_038066, VSP_038067, VSP_038068,
CC                                  VSP_038069;
CC         Note=No experimental confirmation available.;
CC       Name=3;
CC         IsoId=A2A935-3; Sequence=VSP_038067;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Enriched in BAT compared to WAT. Detected in
CC       heart, lung, kidney and brain. Expressed in nuclei of
CC       cardiomyocytes. {ECO:0000269|PubMed:17618855,
CC       ECO:0000269|PubMed:23768516}.
CC   -!- DEVELOPMENTAL STAGE: Expressed at 12.5 dpc, 13.5 dpc and 14.5 dpc.
CC       Expressed in orofacial tissues, heart, liver, brain and limb bud.
CC       At 13.5 dpc, expressed throughout the ventricular myocardium,
CC       including endocardium and epicardium.
CC       {ECO:0000269|PubMed:17467076, ECO:0000269|PubMed:23768516}.
CC   -!- DISRUPTION PHENOTYPE: Mice die at birth but embryos display
CC       altered brown adipose tissue differentiation.
CC       {ECO:0000269|PubMed:18719582}.
CC   -!- SIMILARITY: Belongs to the PRDM16 family. {ECO:0000305}.
DR   EMBL; AB078338; BAC79382.1; -; mRNA.
DR   EMBL; AL627226; CAM14956.1; -; Genomic_DNA.
DR   EMBL; AL611950; CAM14956.1; JOINED; Genomic_DNA.
DR   EMBL; AL627123; CAM14956.1; JOINED; Genomic_DNA.
DR   EMBL; AL627127; CAM14956.1; JOINED; Genomic_DNA.
DR   EMBL; AL627226; CAM14959.1; -; Genomic_DNA.
DR   EMBL; AL611950; CAM14959.1; JOINED; Genomic_DNA.
DR   EMBL; AL627123; CAM14959.1; JOINED; Genomic_DNA.
DR   EMBL; AL627127; CAM14959.1; JOINED; Genomic_DNA.
DR   EMBL; AL627123; CAM21844.1; -; Genomic_DNA.
DR   EMBL; AL611950; CAM21844.1; JOINED; Genomic_DNA.
DR   EMBL; AL627127; CAM21844.1; JOINED; Genomic_DNA.
DR   EMBL; AL627226; CAM21844.1; JOINED; Genomic_DNA.
DR   EMBL; AL627123; CAM21845.1; -; Genomic_DNA.
DR   EMBL; AL611950; CAM21845.1; JOINED; Genomic_DNA.
DR   EMBL; AL627127; CAM21845.1; JOINED; Genomic_DNA.
DR   EMBL; AL627226; CAM21845.1; JOINED; Genomic_DNA.
DR   EMBL; AL627127; CAM22275.1; -; Genomic_DNA.
DR   EMBL; AL611950; CAM22275.1; JOINED; Genomic_DNA.
DR   EMBL; AL627123; CAM22275.1; JOINED; Genomic_DNA.
DR   EMBL; AL627226; CAM22275.1; JOINED; Genomic_DNA.
DR   EMBL; AL627127; CAM22278.1; -; Genomic_DNA.
DR   EMBL; AL611950; CAM22278.1; JOINED; Genomic_DNA.
DR   EMBL; AL627123; CAM22278.1; JOINED; Genomic_DNA.
DR   EMBL; AL627226; CAM22278.1; JOINED; Genomic_DNA.
DR   EMBL; AL611950; CAM24998.1; -; Genomic_DNA.
DR   EMBL; AL627123; CAM24998.1; JOINED; Genomic_DNA.
DR   EMBL; AL627127; CAM24998.1; JOINED; Genomic_DNA.
DR   EMBL; AL627226; CAM24998.1; JOINED; Genomic_DNA.
DR   EMBL; AL611950; CAM25001.1; -; Genomic_DNA.
DR   EMBL; AL627123; CAM25001.1; JOINED; Genomic_DNA.
DR   EMBL; AL627127; CAM25001.1; JOINED; Genomic_DNA.
DR   EMBL; AL627226; CAM25001.1; JOINED; Genomic_DNA.
DR   EMBL; BC059838; AAH59838.1; -; mRNA.
DR   EMBL; AK173230; BAD32508.1; -; mRNA.
DR   CCDS; CCDS38989.1; -. [A2A935-1]
DR   CCDS; CCDS71532.1; -. [A2A935-2]
DR   RefSeq; NP_001277955.1; NM_001291026.1.
DR   RefSeq; NP_001277958.1; NM_001291029.1. [A2A935-2]
DR   RefSeq; NP_081780.3; NM_027504.3. [A2A935-1]
DR   RefSeq; XP_006539236.1; XM_006539173.3. [A2A935-3]
DR   UniGene; Mm.257785; -.
DR   ProteinModelPortal; A2A935; -.
DR   SMR; A2A935; -.
DR   BioGrid; 214194; 5.
DR   DIP; DIP-60593N; -.
DR   IntAct; A2A935; 7.
DR   STRING; 10090.ENSMUSP00000030902; -.
DR   iPTMnet; A2A935; -.
DR   PhosphoSitePlus; A2A935; -.
DR   jPOST; A2A935; -.
DR   MaxQB; A2A935; -.
DR   PaxDb; A2A935; -.
DR   PRIDE; A2A935; -.
DR   Ensembl; ENSMUST00000030902; ENSMUSP00000030902; ENSMUSG00000039410. [A2A935-1]
DR   Ensembl; ENSMUST00000070313; ENSMUSP00000064546; ENSMUSG00000039410. [A2A935-2]
DR   GeneID; 70673; -.
DR   KEGG; mmu:70673; -.
DR   UCSC; uc008wbu.1; mouse. [A2A935-1]
DR   UCSC; uc008wbx.1; mouse. [A2A935-2]
DR   CTD; 63976; -.
DR   MGI; MGI:1917923; Prdm16.
DR   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; COG5048; LUCA.
DR   GeneTree; ENSGT00940000160951; -.
DR   HOGENOM; HOG000231144; -.
DR   InParanoid; A2A935; -.
DR   KO; K22410; -.
DR   OMA; GMQEKKM; -.
DR   OrthoDB; 1318335at2759; -.
DR   TreeFam; TF315309; -.
DR   Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR   ChiTaRS; Prdm16; mouse.
DR   PRO; PR:A2A935; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   Bgee; ENSMUSG00000039410; Expressed in 245 organ(s), highest expression level in pes.
DR   ExpressionAtlas; A2A935; baseline and differential.
DR   Genevisible; A2A935; MM.
DR   GO; GO:0016235; C:aggresome; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0017053; C:transcriptional repressor complex; IDA:UniProtKB.
DR   GO; GO:0033613; F:activating transcription factor binding; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0046332; F:SMAD binding; IPI:MGI.
DR   GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR   GO; GO:0050873; P:brown fat cell differentiation; IDA:UniProtKB.
DR   GO; GO:0048468; P:cell development; IC:GOC-OWL.
DR   GO; GO:0030853; P:negative regulation of granulocyte differentiation; ISS:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IMP:MGI.
DR   GO; GO:0022008; P:neurogenesis; IDA:MGI.
DR   GO; GO:0090336; P:positive regulation of brown fat cell differentiation; IMP:MGI.
DR   GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0043457; P:regulation of cellular respiration; IDA:UniProtKB.
DR   GO; GO:0060021; P:roof of mouth development; IMP:MGI.
DR   GO; GO:0035019; P:somatic stem cell population maintenance; IDA:MGI.
DR   GO; GO:0019827; P:stem cell population maintenance; IMP:MGI.
DR   GO; GO:0043586; P:tongue development; IMP:MGI.
DR   GO; GO:0050872; P:white fat cell differentiation; IDA:UniProtKB.
DR   InterPro; IPR030414; PRDM16.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR24393:SF5; PTHR24393:SF5; 1.
DR   Pfam; PF00096; zf-C2H2; 9.
DR   SMART; SM00317; SET; 1.
DR   SMART; SM00355; ZnF_C2H2; 10.
DR   SUPFAM; SSF57667; SSF57667; 5.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; Complete proteome; Cytoplasm;
KW   Differentiation; DNA-binding; Metal-binding; Methyltransferase;
KW   Nucleus; Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Transferase; Zinc; Zinc-finger.
FT   CHAIN         1   1275       Histone-lysine N-methyltransferase
FT                                PRDM16.
FT                                /FTId=PRO_0000384377.
FT   DOMAIN       82    211       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   ZN_FING     230    255       C2H2-type 1; degenerate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT   ZN_FING     282    304       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     310    332       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     338    361       C2H2-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     367    389       C2H2-type 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     395    417       C2H2-type 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     424    446       C2H2-type 7; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT   ZN_FING     951    973       C2H2-type 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     979   1002       C2H2-type 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING    1008   1030       C2H2-type 10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   REGION      680   1038       Interaction with CTBP1, CTBP2 and ZNF516.
FT                                {ECO:0000269|PubMed:18483224}.
FT   REGION      740   1275       Mediates interaction with SKI and
FT                                regulation of TGF-beta signaling.
FT                                {ECO:0000250|UniProtKB:Q9HAZ2}.
FT   COMPBIAS    460    558       Pro-rich.
FT   VAR_SEQ     129    129       E -> EQ (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_038066.
FT   VAR_SEQ     868    868       Y -> YS (in isoform 2 and isoform 3).
FT                                {ECO:0000303|PubMed:15368895,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_038067.
FT   VAR_SEQ    1174   1176       CVE -> HMQ (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_038068.
FT   VAR_SEQ    1177   1275       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_038069.
FT   MUTAGEN     805    806       DL->AS: Loss of interaction with CTBP1
FT                                and CTBP2 and loss of repression of WAT-
FT                                specific genes.
FT                                {ECO:0000269|PubMed:18483224}.
FT   MUTAGEN     996    996       R->Q: Loss of DNA-binding activity but no
FT                                effect on PRDM16-mediated BAT gene
FT                                transcription activation.
FT                                {ECO:0000269|PubMed:17618855}.
FT   CONFLICT      8      8       R -> K (in Ref. 1; BAC79382).
FT                                {ECO:0000305}.
FT   CONFLICT    510    510       A -> T (in Ref. 1; BAC79382).
FT                                {ECO:0000305}.
FT   CONFLICT    706    706       G -> D (in Ref. 1; BAC79382).
FT                                {ECO:0000305}.
FT   CONFLICT    732    732       P -> L (in Ref. 1; BAC79382).
FT                                {ECO:0000305}.
FT   CONFLICT    760    760       R -> Q (in Ref. 1; BAC79382).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1275 AA;  140858 MW;  2F1F6B6C3EBFEC10 CRC64;
     MRSKARARKL AKSDGDVVNN MYEPDPDLLA GQSAEEETED GILSPIPMGP PSPFPTSEDF
     TPKEGSPYEA PVYIPEDIPI PPDFELRESS IPGAGLGIWA KRKMEIGERF GPYVVTPRAA
     LKEADFGWEM LTDTEVSSQE SCIKKQISED LGSEKFCVDA NQAGSGSWLK YIRVACSCDD
     QNLAMCQINE QIYYKVIKDI EPGEELLVHV KEGAYSLGVM APSLDEDPTF RCDECDELFQ
     CRLDLRRHKK YACSSAGAQL YEGLGEELKP EGLGVGSDGQ AHECKDCERM FPNKYSLEQH
     MIVHTEEREY KCDQCPKAFN WKSNLIRHQM SHDSGKRFEC ENCVKVFTDP SNLQRHIRSQ
     HVGARAHACP DCGKTFATSS GLKQHKHIHS TVKPFICEVC HKSYTQFSNL CRHKRMHADC
     RTQIKCKDCG QMFSTTSSLN KHRRFCEGKN HYTPGSIFTP GLPLTPSPMM DKTKPSPTLN
     HGGLGFSEYF PSRPHPGSLP FSAAPPAFPA LTPGFPGIFP PSLYPRPPLL PPTPLLKSPL
     NHAQDAKLPS PLGNPALPLV SAVSNSSQGA TAATGSEEKF DGRLEDAYAE KVKNRSPDMS
     DGSDFEDINT TTGTDLDTTT GTGSDLDSDL DSDRDKGKDK GKPVESKPEF GGASVPPGAM
     NSVAEVPAFY SQHSFFPPPE EQLLTASGAA GDSIKAIASI AEKYFGPGFM SMQEKKLGSL
     PYHSVFPFQF LPNFPHSLYP FTDRALAHNL LVKAEPKSPR DALKVGGPSA ECPFDLTTKP
     KEAKPALLAP KVPLIPSSGE EQPLDLSIGS RARASQNGGG REPRKNHVYG ERKPGVSEGL
     PKVCPAQLPQ QPSLHYAKPS PFFMDPIYRV EKRKVADPVG VLKEKYLRPS PLLFHPQMSA
     IETMTEKLES FAAMKADSGS SLQPLPHHPF NFRSPPPTLS DPILRKGKER YTCRYCGKIF
     PRSANLTRHL RTHTGEQPYR CKYCDRSFSI SSNLQRHVRN IHNKEKPFKC HLCNRCFGQQ
     TNLDRHLKKH EHEGAPVSQH SGVLTNHLGT SASSPTSESD NHALLDEKED SYFSEIRNFI
     ANSEMNQAST RMDKRPEIQD LDSNPPCPGS ASAKPEDVEE EEEEELEEED DDSLAGKSQE
     DTVSPTPEPQ GVYEDEEDEE PPSLTMGFDH TRRCVEERGG GLLALEPTPT FGKGLDLRRA
     AEEAFEVKDV LNSTLDSEVL KQTLYRQAKN QAYAMMLSLS EDTPLHAPSQ SSLDAWLNIT
     GPSSESGAFN PINHL
//
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