Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

PR domain zinc finger protein 16 (PR domain-containing protein 16) (Transcription factor MEL1) (MDS1/EVI1-like gene 1)

 PRD16_MOUSE             Reviewed;        1275 AA.
A2A935; Q69ZD6; Q6PB79; Q7TPF4;
22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
05-FEB-2008, sequence version 1.
28-MAR-2018, entry version 90.
RecName: Full=PR domain zinc finger protein 16 {ECO:0000305};
AltName: Full=PR domain-containing protein 16 {ECO:0000305};
AltName: Full=Transcription factor MEL1 {ECO:0000305};
Short=MDS1/EVI1-like gene 1 {ECO:0000303|PubMed:12816872};
Name=Prdm16 {ECO:0000312|MGI:MGI:1917923};
Synonyms=Kiaa1675 {ECO:0000305}, Mel1 {ECO:0000303|PubMed:12816872};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=12816872; DOI=10.1182/blood-2002-12-3944;
Nishikata I., Sasaki H., Iga M., Tateno Y., Imayoshi S., Asou N.,
Nakamura T., Morishita K.;
"A novel EVI1 gene family, MEL1, lacking a PR domain (MEL1S) is
expressed mainly in t(1;3)(p36;q21)-positive AML and blocks G-CSF-
induced myeloid differentiation.";
Blood 102:3323-3332(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 570-1275 (ISOFORM 3).
TISSUE=Pancreatic islet;
PubMed=15368895; DOI=10.1093/dnares/11.3.205;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 11:205-218(2004).
[5]
INTERACTION WITH SMAD3, AND DEVELOPMENTAL STAGE.
PubMed=17467076; DOI=10.1016/j.bbamcr.2007.03.016;
Warner D.R., Horn K.H., Mudd L., Webb C.L., Greene R.M., Pisano M.M.;
"PRDM16/MEL1: a novel Smad binding protein expressed in murine
embryonic orofacial tissue.";
Biochim. Biophys. Acta 1773:814-820(2007).
[6]
FUNCTION, INTERACTION WITH PPARGC1A AND PPARGC1B, MUTAGENESIS OF
ARG-996, AND TISSUE SPECIFICITY.
PubMed=17618855; DOI=10.1016/j.cmet.2007.06.001;
Seale P., Kajimura S., Yang W., Chin S., Rohas L.M., Uldry M.,
Tavernier G., Langin D., Spiegelman B.M.;
"Transcriptional control of brown fat determination by PRDM16.";
Cell Metab. 6:38-54(2007).
[7]
FUNCTION, INTERACTION WITH CTBP1; CTBP2; PPARGC1A AND PPARGC1B,
SUBCELLULAR LOCATION, MUTAGENESIS OF 805-ASP-LEU-806, AND REGION.
PubMed=18483224; DOI=10.1101/gad.1666108;
Kajimura S., Seale P., Tomaru T., Erdjument-Bromage H., Cooper M.P.,
Ruas J.L., Chin S., Tempst P., Lazar M.A., Spiegelman B.M.;
"Regulation of the brown and white fat gene programs through a
PRDM16/CtBP transcriptional complex.";
Genes Dev. 22:1397-1409(2008).
[8]
FUNCTION, INTERACTION WITH PPARA AND PPARG, AND DISRUPTION PHENOTYPE.
PubMed=18719582; DOI=10.1038/nature07182;
Seale P., Bjork B., Yang W., Kajimura S., Chin S., Kuang S., Scime A.,
Devarakonda S., Conroe H.M., Erdjument-Bromage H., Tempst P.,
Rudnicki M.A., Beier D.R., Spiegelman B.M.;
"PRDM16 controls a brown fat/skeletal muscle switch.";
Nature 454:961-967(2008).
[9]
FUNCTION, AND INTERACTION WITH CEBPA; CEBPB AND CEBPD.
PubMed=19641492; DOI=10.1038/nature08262;
Kajimura S., Seale P., Kubota K., Lunsford E., Frangioni J.V.,
Gygi S.P., Spiegelman B.M.;
"Initiation of myoblast to brown fat switch by a PRDM16-C/EBP-beta
transcriptional complex.";
Nature 460:1154-1158(2009).
[10]
DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
PubMed=23768516; DOI=10.1016/j.ajhg.2013.05.015;
Arndt A.K., Schafer S., Drenckhahn J.D., Sabeh M.K., Plovie E.R.,
Caliebe A., Klopocki E., Musso G., Werdich A.A., Kalwa H., Heinig M.,
Padera R.F., Wassilew K., Bluhm J., Harnack C., Martitz J.,
Barton P.J., Greutmann M., Berger F., Hubner N., Siebert R.,
Kramer H.H., Cook S.A., MacRae C.A., Klaassen S.;
"Fine mapping of the 1p36 deletion syndrome identifies mutation of
PRDM16 as a cause of cardiomyopathy.";
Am. J. Hum. Genet. 93:67-77(2013).
[11]
INTERACTION WITH ZNF516, AND REGION.
PubMed=25578880; DOI=10.1016/j.molcel.2014.12.005;
Dempersmier J., Sambeat A., Gulyaeva O., Paul S.M., Hudak C.S.,
Raposo H.F., Kwan H.Y., Kang C., Wong R.H., Sul H.S.;
"Cold-inducible Zfp516 activates UCP1 transcription to promote
browning of white fat and development of brown fat.";
Mol. Cell 57:235-246(2015).
-!- FUNCTION: Binds DNA and functions as a transcriptional regulator.
Functions in the differentiation of brown adipose tissue (BAT)
which is specialized in dissipating chemical energy in the form of
heat in response to cold or excess feeding while white adipose
tissue (WAT) is specialized in the storage of excess energy and
the control of systemic metabolism. Together with CEBPB, regulates
the differentiation of myoblastic precursors into brown adipose
cells. Functions also as a repressor of TGF-beta signaling. May
regulate granulocytes differentiation.
{ECO:0000269|PubMed:17618855, ECO:0000269|PubMed:18483224,
ECO:0000269|PubMed:18719582, ECO:0000269|PubMed:19641492}.
-!- SUBUNIT: Interacts with CEBPA, CEBPB and CEBPD; the interaction is
direct (PubMed:19641492). Interacts with PPARG and PPARA; controls
brown adipocytes (PubMed:18719582). Interacts with CTBP1 and
CTBP2; represses the expression of WAT-specific genes
(PubMed:18483224). Interacts with PPARGC1A and PPARGC1B;
interaction with PPARGC1A or PPARGC1B activates the transcription
of BAT-specific gene (PubMed:17618855, PubMed:18483224). Interacts
with HDAC1, SKI and SMAD2; the interaction with SKI promotes the
recruitment of SMAD3-HDAC1 complex on the promoter of TGF-beta
target genes (Probable). Interacts with ZNF516; the interaction is
direct and may play a role in the transcription of brown adipose
tissue-specific gene (PubMed:25578880).
{ECO:0000250|UniProtKB:A2A935, ECO:0000269|PubMed:17618855,
ECO:0000269|PubMed:18483224, ECO:0000269|PubMed:18719582,
ECO:0000269|PubMed:19641492, ECO:0000269|PubMed:25578880,
ECO:0000305|PubMed:17467076}.
-!- INTERACTION:
Q5DW34-1:Ehmt1; NbExp=2; IntAct=EBI-16080455, EBI-16080518;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18483224}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=A2A935-1; Sequence=Displayed;
Name=2;
IsoId=A2A935-2; Sequence=VSP_038066, VSP_038067, VSP_038068,
VSP_038069;
Note=No experimental confirmation available.;
Name=3;
IsoId=A2A935-3; Sequence=VSP_038067;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Enriched in BAT compared to WAT. Detected in
heart, lung, kidney and brain. Expressed in nuclei of
cardiomyocytes. {ECO:0000269|PubMed:17618855,
ECO:0000269|PubMed:23768516}.
-!- DEVELOPMENTAL STAGE: Expressed at E12.5, E13.5 and E14.5.
Expressed in orofacial tissues, heart, liver, brain and limb bud.
At E13.5, expressed throughout the ventricular myocardium,
including endocardium and epicardium.
{ECO:0000269|PubMed:17467076, ECO:0000269|PubMed:23768516}.
-!- DISRUPTION PHENOTYPE: Mice die at birth but embryos display
altered brown adipose tissue differentiation.
{ECO:0000269|PubMed:18719582}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB078338; BAC79382.1; -; mRNA.
EMBL; AL627226; CAM14956.1; -; Genomic_DNA.
EMBL; AL611950; CAM14956.1; JOINED; Genomic_DNA.
EMBL; AL627123; CAM14956.1; JOINED; Genomic_DNA.
EMBL; AL627127; CAM14956.1; JOINED; Genomic_DNA.
EMBL; AL627226; CAM14959.1; -; Genomic_DNA.
EMBL; AL611950; CAM14959.1; JOINED; Genomic_DNA.
EMBL; AL627123; CAM14959.1; JOINED; Genomic_DNA.
EMBL; AL627127; CAM14959.1; JOINED; Genomic_DNA.
EMBL; AL627123; CAM21844.1; -; Genomic_DNA.
EMBL; AL611950; CAM21844.1; JOINED; Genomic_DNA.
EMBL; AL627127; CAM21844.1; JOINED; Genomic_DNA.
EMBL; AL627226; CAM21844.1; JOINED; Genomic_DNA.
EMBL; AL627123; CAM21845.1; -; Genomic_DNA.
EMBL; AL611950; CAM21845.1; JOINED; Genomic_DNA.
EMBL; AL627127; CAM21845.1; JOINED; Genomic_DNA.
EMBL; AL627226; CAM21845.1; JOINED; Genomic_DNA.
EMBL; AL627127; CAM22275.1; -; Genomic_DNA.
EMBL; AL611950; CAM22275.1; JOINED; Genomic_DNA.
EMBL; AL627123; CAM22275.1; JOINED; Genomic_DNA.
EMBL; AL627226; CAM22275.1; JOINED; Genomic_DNA.
EMBL; AL627127; CAM22278.1; -; Genomic_DNA.
EMBL; AL611950; CAM22278.1; JOINED; Genomic_DNA.
EMBL; AL627123; CAM22278.1; JOINED; Genomic_DNA.
EMBL; AL627226; CAM22278.1; JOINED; Genomic_DNA.
EMBL; AL611950; CAM24998.1; -; Genomic_DNA.
EMBL; AL627123; CAM24998.1; JOINED; Genomic_DNA.
EMBL; AL627127; CAM24998.1; JOINED; Genomic_DNA.
EMBL; AL627226; CAM24998.1; JOINED; Genomic_DNA.
EMBL; AL611950; CAM25001.1; -; Genomic_DNA.
EMBL; AL627123; CAM25001.1; JOINED; Genomic_DNA.
EMBL; AL627127; CAM25001.1; JOINED; Genomic_DNA.
EMBL; AL627226; CAM25001.1; JOINED; Genomic_DNA.
EMBL; BC059838; AAH59838.1; -; mRNA.
EMBL; AK173230; BAD32508.1; -; mRNA.
CCDS; CCDS38989.1; -. [A2A935-1]
CCDS; CCDS71532.1; -. [A2A935-2]
RefSeq; NP_001277955.1; NM_001291026.1.
RefSeq; NP_001277958.1; NM_001291029.1. [A2A935-2]
RefSeq; NP_081780.3; NM_027504.3. [A2A935-1]
RefSeq; XP_006539236.1; XM_006539173.3. [A2A935-3]
UniGene; Mm.257785; -.
ProteinModelPortal; A2A935; -.
SMR; A2A935; -.
BioGrid; 214194; 5.
DIP; DIP-60593N; -.
IntAct; A2A935; 7.
STRING; 10090.ENSMUSP00000030902; -.
iPTMnet; A2A935; -.
PhosphoSitePlus; A2A935; -.
MaxQB; A2A935; -.
PaxDb; A2A935; -.
PRIDE; A2A935; -.
Ensembl; ENSMUST00000030902; ENSMUSP00000030902; ENSMUSG00000039410. [A2A935-1]
Ensembl; ENSMUST00000070313; ENSMUSP00000064546; ENSMUSG00000039410. [A2A935-2]
GeneID; 70673; -.
KEGG; mmu:70673; -.
UCSC; uc008wbu.1; mouse. [A2A935-1]
UCSC; uc008wbx.1; mouse. [A2A935-2]
CTD; 63976; -.
MGI; MGI:1917923; Prdm16.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
GeneTree; ENSGT00900000140928; -.
HOGENOM; HOG000231144; -.
InParanoid; A2A935; -.
KO; K22410; -.
TreeFam; TF315309; -.
Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
ChiTaRS; Prdm16; mouse.
PRO; PR:A2A935; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000039410; -.
ExpressionAtlas; A2A935; baseline and differential.
Genevisible; A2A935; MM.
GO; GO:0016235; C:aggresome; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0017053; C:transcriptional repressor complex; IDA:UniProtKB.
GO; GO:0033613; F:activating transcription factor binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0046332; F:SMAD binding; IPI:MGI.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0050873; P:brown fat cell differentiation; IDA:UniProtKB.
GO; GO:0030853; P:negative regulation of granulocyte differentiation; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IMP:MGI.
GO; GO:0022008; P:neurogenesis; IDA:MGI.
GO; GO:0060021; P:palate development; IMP:MGI.
GO; GO:0090336; P:positive regulation of brown fat cell differentiation; IMP:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0043457; P:regulation of cellular respiration; IDA:UniProtKB.
GO; GO:0035019; P:somatic stem cell population maintenance; IDA:MGI.
GO; GO:0019827; P:stem cell population maintenance; IMP:MGI.
GO; GO:0043586; P:tongue development; IMP:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0050872; P:white fat cell differentiation; IDA:UniProtKB.
InterPro; IPR030414; PRDM16.
InterPro; IPR001214; SET_dom.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
PANTHER; PTHR24393:SF5; PTHR24393:SF5; 1.
SMART; SM00317; SET; 1.
SMART; SM00355; ZnF_C2H2; 10.
SUPFAM; SSF57667; SSF57667; 5.
PROSITE; PS50280; SET; 1.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10.
1: Evidence at protein level;
Activator; Alternative splicing; Complete proteome; Differentiation;
DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat;
Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
CHAIN 1 1275 PR domain zinc finger protein 16.
/FTId=PRO_0000384377.
DOMAIN 82 211 SET. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
ZN_FING 230 255 C2H2-type 1; degenerate.
{ECO:0000255|PROSITE-ProRule:PRU00042}.
ZN_FING 282 304 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 310 332 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 338 361 C2H2-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 367 389 C2H2-type 5. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 395 417 C2H2-type 6. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 424 446 C2H2-type 7; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00042}.
ZN_FING 951 973 C2H2-type 8. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 979 1002 C2H2-type 9. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 1008 1030 C2H2-type 10. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
REGION 680 1038 Interaction with CTBP1, CTBP2 and ZNF516.
{ECO:0000269|PubMed:18483224}.
REGION 740 1275 Mediates interaction with SKI and
regulation of TGF-beta signaling.
{ECO:0000250|UniProtKB:Q9HAZ2}.
COMPBIAS 460 558 Pro-rich.
VAR_SEQ 129 129 E -> EQ (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_038066.
VAR_SEQ 868 868 Y -> YS (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:15368895,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_038067.
VAR_SEQ 1174 1176 CVE -> HMQ (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_038068.
VAR_SEQ 1177 1275 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_038069.
MUTAGEN 805 806 DL->AS: Loss of interaction with CTBP1
and CTBP2 and loss of repression of WAT-
specific genes.
{ECO:0000269|PubMed:18483224}.
MUTAGEN 996 996 R->Q: Loss of DNA-binding activity but no
effect on PRDM16-mediated BAT gene
transcription activation.
{ECO:0000269|PubMed:17618855}.
CONFLICT 8 8 R -> K (in Ref. 1; BAC79382).
{ECO:0000305}.
CONFLICT 510 510 A -> T (in Ref. 1; BAC79382).
{ECO:0000305}.
CONFLICT 706 706 G -> D (in Ref. 1; BAC79382).
{ECO:0000305}.
CONFLICT 732 732 P -> L (in Ref. 1; BAC79382).
{ECO:0000305}.
CONFLICT 760 760 R -> Q (in Ref. 1; BAC79382).
{ECO:0000305}.
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


Related products :

Catalog number Product name Quantity
EIAAB32297 Kiaa1675,MDS1_EVI1-like gene 1,Mel1,Mouse,Mus musculus,PR domain zinc finger protein 16,PR domain-containing protein 16,Prdm16,Transcription factor MEL1
EIAAB32298 Homo sapiens,Human,KIAA1675,MDS1_EVI1-like gene 1,MEL1,PFM13,PR domain zinc finger protein 16,PR domain-containing protein 16,PRDM16,Transcription factor MEL1
25-097 PRDM5 is a transcription factor of the PR-domain protein family. It contains a PR-domain and multiple zinc finger motifs. Transcription factors of the PR-domain family are known to be involved in cell 0.05 mg
EIAAB29957 BTB_POZ domain zinc finger transcription factor,Homo sapiens,Human,PATZ,PATZ1,POZ-, AT hook-, and zinc finger-containing protein 1,Protein kinase A RI subunit alpha-associated protein,RIAZ,ZBTB19,Zinc
EIAAB32305 B lymphocyte-induced maturation protein 1,Beta-interferon gene positive regulatory domain I-binding factor,Blimp1,Blimp-1,Mouse,Mus musculus,PR domain zinc finger protein 1,PR domain-containing protei
EIAAB46816 BTB_POZ domain zinc finger factor HOF,Mouse,Mus musculus,Zbtb20,Zfp288,Zinc finger and BTB domain-containing protein 20,Zinc finger protein 288
EIAAB48064 CtFIN51,Mouse,Mus musculus,Transcription factor RU49,Zfp38,Zfp-38,Zfp-38,Zinc finger and SCAN domain-containing protein 21,Zinc finger protein 38,Zipro1,Znf38,Zscan21
EIAAB29341 Cellular zinc finger anti-NF-kappa-B protein,Homo sapiens,Human,OTU domain-containing protein 7B,OTUD7B,ZA20D1,Zinc finger A20 domain-containing protein 1,Zinc finger protein Cezanne
18-003-42276 Zinc finger and BTB domain-containing protein 7B - Zinc finger protein 67 homolog; Zfp-67; Zinc finger protein Th-POK; T-helper-inducing POZ_Krueppel-like factor; Krueppel-related zinc finger protein 0.1 mg Protein A
EIAAB46861 BOZF1,BOZ-F1,BTB_POZ and zinc-finger domain-containing factor,BTB_POZ and zinc-finger domains factor on chromosome 1,Homo sapiens,Human,ZBTB8A,Zinc finger and BTB domain-containing protein 8A
EIAAB47160 G patch domain-containing protein 6,GPATC6,GPATCH6,Homo sapiens,Human,KIAA1847,ZC3H9,ZC3HDC9,ZGPAT,Zinc finger and G patch domain-containing protein,Zinc finger CCCH domain-containing protein 9,Zinc f
EIAAB46839 Homo sapiens,Human,KIAA0414,ZBTB22B,ZBTB43,Zinc finger and BTB domain-containing protein 22B,Zinc finger and BTB domain-containing protein 43,Zinc finger protein 297B,ZNF297B,ZnF-x
EIAAB32304 Beta-interferon gene positive regulatory domain I-binding factor,BLIMP1,BLIMP-1,Homo sapiens,Human,Positive regulatory domain I-binding factor 1,PR domain zinc finger protein 1,PR domain-containing pr
18-003-44056 PR domain zinc finger protein 1 - PR domain-containing protein 1; Beta-interferon gene positive regulatory domain I-binding factor; BLIMP-1; Positive regulatory domain I-binding factor 1; PRDI-binding 0.1 mg Protein A
EIAAB47194 Homo sapiens,Human,Zf47,ZFP47,Zfp-47,Zinc finger and SCAN domain-containing protein 13,Zinc finger protein 306,Zinc finger protein 309,Zinc finger protein 47 homolog,Zinc finger protein with KRAB and
EIAAB46826 FANCC-interacting protein,Fanconi anemia zinc finger protein,FAZF,Homo sapiens,Human,Testis zinc finger protein,TZFP,ZBTB32,Zinc finger and BTB domain-containing protein 32,Zinc finger protein 538,ZNF
EIAAB46875 Homo sapiens,Human,ZBTB6,ZID,Zinc finger and BTB domain-containing protein 6,Zinc finger protein 482,Zinc finger protein with interaction domain,ZNF482
EIAAB32307 PR domain zinc finger protein 2,PR domain-containing protein 2,Prdm2,Rat,Rattus norvegicus,Retinoblastoma protein-interacting zinc finger protein,Riz,Zinc finger protein RIZ
EIAAB46856 c-Krox,Krueppel-related zinc finger protein cKrox,Mouse,Mus musculus,T-helper-inducing POZ_Krueppel-like factor,Thpok,Zbtb7b,Zfp67,Zfp-67,Zinc finger and BTB domain-containing protein 7B,Zinc finger p
EIAAB46855 hcKrox,Homo sapiens,Human,Krueppel-related zinc finger protein cKrox,T-helper-inducing POZ_Krueppel-like factor,ZBTB15,ZBTB7B,ZFP67,Zfp-67,Zinc finger and BTB domain-containing protein 15,Zinc finger
EIAAB32320 Histone-lysine N-methyltransferase PRDM9,Hst1,Hybrid sterility protein 1,Meiosis-induced factor containing a PR_SET domain and zinc-finger motif,Meisetz,Mouse,Mus musculus,PR domain zinc finger protei
29-021 POGZ appears to be a zinc finger protein containing a transposase domain at the C-terminus. This protein was found to interact with the transcription factor SP1 in a yeast two-hybrid systemThe protein 0.1 mg
EIAAB46817 BING1,Homo sapiens,Human,Protein BING1,ZBTB22,ZBTB22A,Zinc finger and BTB domain-containing protein 22,Zinc finger and BTB domain-containing protein 22A,Zinc finger protein 297,ZNF297
28-888 MDS1 is located at 3q26 170-400 kb upstream (telomeric) of EVI1 in the chromosomal region in which some of the breakpoints 5' of EVI1 have been mapped. MDS1 has been identified as a single gene as wel 0.1 mg
MDS1_MOUSE ELISA Kit FOR MDS1 and EVI1 complex locus protein MDS1; organism: Mouse; gene name: Mecom 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur