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Zinc finger homeobox protein 3 (AT motif-binding factor 1) (AT-binding transcription factor 1) (Alpha-fetoprotein enhancer-binding protein) (Zinc finger homeodomain protein 3) (ZFH-3)

 ZFHX3_MOUSE             Reviewed;        3726 AA.
Q61329;
18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
18-JUL-2018, entry version 159.
RecName: Full=Zinc finger homeobox protein 3;
AltName: Full=AT motif-binding factor 1;
AltName: Full=AT-binding transcription factor 1;
AltName: Full=Alpha-fetoprotein enhancer-binding protein;
AltName: Full=Zinc finger homeodomain protein 3;
Short=ZFH-3;
Name=Zfhx3; Synonyms=Atbf1;
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].
STRAIN=BALB/MK X ICR; TISSUE=Brain;
PubMed=8654949; DOI=10.1016/0378-1119(95)00740-7;
Ido A., Miura Y., Watanabe M., Sakai M., Inoue Y., Miki T.,
Hashimoto T., Morinaga T., Nishi S., Tamaoki T.;
"Cloning of the cDNA encoding the mouse ATBF1 transcription factor.";
Gene 168:227-231(1996).
[2]
INTERACTION WITH FNBP3.
PubMed=9171351; DOI=10.1093/emboj/16.9.2376;
Bedford M.T., Chan D.C., Leder P.;
"FBP WW domains and the Abl SH3 domain bind to a specific class of
proline-rich ligands.";
EMBO J. 16:2376-2383(1997).
[3]
TISSUE SPECIFICITY.
PubMed=11312261; DOI=10.1074/jbc.M010378200;
Berry F.B., Miura Y., Mihara K., Kaspar P., Sakata N.,
Hashimoto-Tamaoki T., Tamaoki T.;
"Positive and negative regulation of myogenic differentiation of C2C12
cells by isoforms of the multiple homeodomain zinc finger
transcription factor ATBF1.";
J. Biol. Chem. 276:25057-25065(2001).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2904, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, and Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[5]
PHOSPHORYLATION AT SER-1600; SER-2634; SER-2795; SER-2804; SER-2900;
SER-3434; SER-3443; SER-3616 AND SER-3700, IDENTIFICATION BY MASS
SPECTROMETRY, AND PROTEOLYTIC PROCESSING.
PubMed=23022192; DOI=10.1016/j.bbrc.2012.09.092;
Zhang S., Kim T.S., Dong Y., Kanazawa S., Kawaguchi M., Gao N.,
Minato H., Takegami T., Nojima T., Asai K., Miura Y.;
"AT motif binding factor 1 (ATBF1) is highly phosphorylated in
embryonic brain and protected from cleavage by calpain-1.";
Biochem. Biophys. Res. Commun. 427:537-541(2012).
[6]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, AND
MUTAGENESIS OF VAL-1963.
PubMed=26232227; DOI=10.1016/j.cell.2015.06.060;
Parsons M.J., Brancaccio M., Sethi S., Maywood E.S., Satija R.,
Edwards J.K., Jagannath A., Couch Y., Finelli M.J., Smyllie N.J.,
Esapa C., Butler R., Barnard A.R., Chesham J.E., Saito S., Joynson G.,
Wells S., Foster R.G., Oliver P.L., Simon M.M., Mallon A.M.,
Hastings M.H., Nolan P.M.;
"The regulatory factor ZFHX3 modifies circadian function in SCN via an
AT motif-driven axis.";
Cell 162:607-621(2015).
-!- FUNCTION: Transcriptional regulator which can act as an activator
or a repressor. Inhibits the enhancer element of the AFP gene by
binding to its AT-rich core sequence. In concert with SMAD-
dependent TGF-beta signaling can repress the transcription of AFP
via its interaction with SMAD2/3 (By similarity). Regulates the
circadian locomotor rhythms via transcriptional activation of
neuropeptidergic genes which are essential for intercellular
synchrony and rhythm amplitude in the suprachiasmatic nucleus
(SCN) of the brain (PubMed:26232227). Regulator of myoblasts
differentiation through the binding to the AT-rich sequence of
MYF6 promoter and promoter repression. Down-regulates the MUC5AC
promoter in gastric cancer. In association with RUNX3, upregulates
CDKN1A promoter activity following TGF-beta stimulation (By
similarity). {ECO:0000250|UniProtKB:Q15911,
ECO:0000269|PubMed:26232227}.
-!- SUBUNIT: Interacts with ALKBH4 and PIAS3 (By similarity).
Interacts with FNBP3. Interacts with ESR1, RUNX3, TRIM25, SMAD2
and SMAD3 (By similarity). {ECO:0000250|UniProtKB:Q15911,
ECO:0000269|PubMed:9171351}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15911}.
Cytoplasm {ECO:0000250|UniProtKB:Q15911}. Note=Translocates from
the cytoplasm to the nucleus following TGF-beta stimulation.
Expressed in nuclear body (NB)-like dots in the nucleus some of
which overlap or closely associate with PML body.
{ECO:0000250|UniProtKB:Q15911}.
-!- TISSUE SPECIFICITY: Expressed in suprachiasmatic nucleus (SCN) of
the brain (at protein level). Expressed in skeletal muscle. Levels
of expression are high in myoblasts but low in differentiated
muscle. {ECO:0000269|PubMed:11312261,
ECO:0000269|PubMed:26232227}.
-!- PTM: Phosphorylated at Ser-2634 in embryonic and adult brain.
Phosphorylated at Ser-1600, Ser-2795, Ser-2804, Ser-2900, Ser-
3434, Ser-3443, Ser-3616 and Ser-3700 in the embryonic brain only.
Hpyerphosphorylated in embryonic brain and phosphorylation
decreases its sensitivity to calpain-mediated proteolysis.
{ECO:0000269|PubMed:23022192}.
-!- PTM: Adult brain-derived ZFHX3 is sensitive, but embryonic brain-
derived ZFHX3 is resistant to calpain 1-mediated proteolysis.
{ECO:0000269|PubMed:23022192}.
-!- PTM: Ubiquitinated, leading to its proteasomal degradation.
{ECO:0000250|UniProtKB:Q15911}.
-!- PTM: Nuclear localization is essential for its sumoylation.
{ECO:0000250|UniProtKB:Q15911}.
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EMBL; D26046; BAA05046.1; -; mRNA.
UniGene; Mm.416972; -.
UniGene; Mm.477670; -.
ProteinModelPortal; Q61329; -.
IntAct; Q61329; 2.
MINT; Q61329; -.
STRING; 10090.ENSMUSP00000044612; -.
iPTMnet; Q61329; -.
PhosphoSitePlus; Q61329; -.
MaxQB; Q61329; -.
PaxDb; Q61329; -.
PeptideAtlas; Q61329; -.
PRIDE; Q61329; -.
MGI; MGI:99948; Zfhx3.
eggNOG; KOG1146; Eukaryota.
eggNOG; ENOG410XYHC; LUCA.
HOGENOM; HOG000155777; -.
HOVERGEN; HBG050606; -.
InParanoid; Q61329; -.
PhylomeDB; Q61329; -.
ChiTaRS; Zfhx3; mouse.
PRO; PR:Q61329; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_ZFHX3; -.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005739; C:mitochondrion; HDA:MGI.
GO; GO:0016604; C:nuclear body; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005667; C:transcription factor complex; ISO:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISO:MGI.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0032922; P:circadian regulation of gene expression; IMP:UniProtKB.
GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
GO; GO:0045662; P:negative regulation of myoblast differentiation; ISO:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0045663; P:positive regulation of myoblast differentiation; ISO:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:1904059; P:regulation of locomotor rhythm; IMP:UniProtKB.
GO; GO:0071559; P:response to transforming growth factor beta; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00086; homeodomain; 4.
InterPro; IPR009057; Homeobox-like_sf.
InterPro; IPR017970; Homeobox_CS.
InterPro; IPR001356; Homeobox_dom.
InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
Pfam; PF00046; Homeobox; 4.
SMART; SM00389; HOX; 4.
SMART; SM00355; ZnF_C2H2; 23.
SMART; SM00451; ZnF_U1; 7.
SUPFAM; SSF46689; SSF46689; 4.
SUPFAM; SSF57667; SSF57667; 8.
PROSITE; PS00027; HOMEOBOX_1; 2.
PROSITE; PS50071; HOMEOBOX_2; 4.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 15.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
1: Evidence at protein level;
Activator; Complete proteome; Cytoplasm; DNA-binding; Homeobox;
Isopeptide bond; Metal-binding; Myogenesis; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 3726 Zinc finger homeobox protein 3.
/FTId=PRO_0000046931.
ZN_FING 79 103 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 282 305 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 641 664 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 672 695 C2H2-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 727 751 C2H2-type 5. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 805 829 C2H2-type 6; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00042}.
ZN_FING 946 969 C2H2-type 7; degenerate.
{ECO:0000255|PROSITE-ProRule:PRU00042}.
ZN_FING 985 1009 C2H2-type 8; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00042}.
ZN_FING 1041 1065 C2H2-type 9; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00042}.
ZN_FING 1089 1113 C2H2-type 10; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00042}.
ZN_FING 1233 1256 C2H2-type 11; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00042}.
ZN_FING 1262 1285 C2H2-type 12. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 1370 1395 C2H2-type 13. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 1411 1433 C2H2-type 14. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 1439 1462 C2H2-type 15. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 1555 1579 C2H2-type 16. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 1606 1630 C2H2-type 17. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 1990 2013 C2H2-type 18. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
DNA_BIND 2152 2211 Homeobox 1. {ECO:0000255|PROSITE-
ProRule:PRU00108}.
DNA_BIND 2249 2308 Homeobox 2. {ECO:0000255|PROSITE-
ProRule:PRU00108}.
ZN_FING 2335 2358 C2H2-type 19; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00042}.
ZN_FING 2539 2561 C2H2-type 20. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
DNA_BIND 2650 2709 Homeobox 3. {ECO:0000255|PROSITE-
ProRule:PRU00108}.
ZN_FING 2720 2743 C2H2-type 21. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
DNA_BIND 2952 3011 Homeobox 4. {ECO:0000255|PROSITE-
ProRule:PRU00108}.
ZN_FING 3032 3056 C2H2-type 22. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 3552 3576 C2H2-type 23. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
MOTIF 2624 2626 Nuclear localization signal.
{ECO:0000250|UniProtKB:Q15911}.
COMPBIAS 461 491 Poly-Glu.
COMPBIAS 771 785 Poly-Ala.
COMPBIAS 1314 1317 Poly-Ala.
COMPBIAS 1734 1748 Poly-Gln.
COMPBIAS 1794 1799 Poly-Gln.
COMPBIAS 1856 1863 Poly-Gln.
COMPBIAS 2044 2059 Poly-Pro.
COMPBIAS 2405 2408 Poly-Ala.
COMPBIAS 3216 3220 Poly-Pro.
COMPBIAS 3380 3409 Poly-Gln.
COMPBIAS 3412 3420 Poly-Gln.
COMPBIAS 3534 3550 Poly-Gly.
COMPBIAS 3620 3623 Poly-Pro.
COMPBIAS 3659 3662 Poly-Ser.
MOD_RES 426 426 Phosphoserine.
{ECO:0000250|UniProtKB:Q15911}.
MOD_RES 428 428 Phosphothreonine.
{ECO:0000250|UniProtKB:Q15911}.
MOD_RES 535 535 Phosphoserine.
{ECO:0000250|UniProtKB:Q15911}.
MOD_RES 573 573 Phosphoserine.
{ECO:0000250|UniProtKB:Q15911}.
MOD_RES 1207 1207 Phosphoserine.
{ECO:0000250|UniProtKB:Q15911}.
MOD_RES 1600 1600 Phosphoserine.
{ECO:0000269|PubMed:23022192}.
MOD_RES 2634 2634 Phosphoserine.
{ECO:0000269|PubMed:23022192}.
MOD_RES 2795 2795 Phosphoserine.
{ECO:0000269|PubMed:23022192}.
MOD_RES 2804 2804 Phosphoserine.
{ECO:0000269|PubMed:23022192}.
MOD_RES 2900 2900 Phosphoserine.
{ECO:0000269|PubMed:23022192}.
MOD_RES 2904 2904 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 3434 3434 Phosphoserine.
{ECO:0000269|PubMed:23022192}.
MOD_RES 3443 3443 Phosphoserine.
{ECO:0000269|PubMed:23022192}.
MOD_RES 3457 3457 Phosphoserine.
{ECO:0000250|UniProtKB:Q15911}.
MOD_RES 3616 3616 Phosphoserine.
{ECO:0000269|PubMed:23022192}.
MOD_RES 3700 3700 Phosphoserine.
{ECO:0000269|PubMed:23022192}.
CROSSLNK 2356 2356 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000250|UniProtKB:Q15911}.
CROSSLNK 2815 2815 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:Q15911}.
CROSSLNK 2815 2815 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q15911}.
CROSSLNK 3262 3262 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000250|UniProtKB:Q15911}.
MUTAGEN 1963 1963 V->F: In short circuit/sci mutant;
shorter circadian period, homozygous
lethality during embryonic development
and diminished ability to activate the
transcription of circadian-related
neuropeptides.
{ECO:0000269|PubMed:26232227}.
SEQUENCE 3726 AA; 406570 MW; 915ACBE588A72C98 CRC64;
MEGCDSPVVS GKDNGCGIPQ HRQWTELNSA HLPDKPSSME QPTGESHGPL DSLRAPFNER
LADSSTSAGP PAEPASKEVS CNECSASFSS LQTYMEHHCP GTHPPPALRE ESASDTSEEG
EEESDVENLA GEIVYQPDGS AYIVESLSQL AQSGAACGSS SGSGAVPSLF LNSLPGVGGK
QGDPSCAAPV YPQIINTSHI ASSFGKWFEG SDPAFPNTSA LAGLSPVLHS FRVFDVRHKS
NKDYLNSDGS AKSSCVSKDV PNNVDLSKFD GFVLYGKRKP ILMCFLCKLS FGYVRSFVTH
AVHDHRMTLS EEERKLLSNK NISAIIQGIG KDKEPLVSFL EPKNKNFQHP LVSTGNLIGP
GHSFYGKFSG IRMEGEEALP AVAAAGPEQP QAGLLTPSTL LNLGGLTSSV LKTPITSVPL
GPLASSPTKS SEGKDSGAAE GDKQESGGHQ DCFSEKVEPA EEEEAEEEEE EEEEAEEEEE
EEEEEEEEEE EASKGLFPND LEEELEDSPS EESGPPAGGT TKKDLALSNP SISNSPLMPN
VLQTLSRGPA STTSNSASNF VVFDGANRRS RLSFNSEGVR ANVAEGRRLD FADESANKDS
ATAPEPNEST EGDDGGFVPH HQHAGSLCEL GVGESPSGSG VECPKCDTVL GSSRSLGGHM
TMMHSRNSCK TLKCPKCNWH YKYQQTLEAH MKEKHPEPGG SCVYCKSGQP HPRLARGESY
TCGYKPFRCE VCNYSTTTKG NLSIHMQSDK HLNNMQNLQN GGGEQVFSHS AGAAAAAAAA
AAAAANIGSS WGAPSPTKPK TKPTWRCEVC DYETNVARNL RIHMTSEKHM HNMMLLQQNM
TQIQHNRHLG LGSLPSPAEA ELYQYYLAQN MNLPNLKMDS TASDAQFMMS GFQLDPTGPM
AAMTPALVGG EIPLDMRLGG GQLVSEELMN LGESFIQTND PSLKLFQCAV CNKFTTDNLD
MLGLHMNVER SLSEDEWKAV MGDSYQCKLC RYNTQLKANF QLHCKTDKHV QKYQLVAHIK
EGGKANEWRL KCVAIGNPVH LKCNACDYYT NSLEKLRLHT VNSRHEASLK LYKHLQQHES
GVEGESCYYH CVLCNYSTKA KLNLIQHVRS MKHQRSESLR KLQRLQKGLP EEDEDLGQIF
TIRRCPSTDP EEPVEDAEGP SEASADPEEL AKDQGSGSEE GQSKRAASSS QAEKELTDSP
ATTKRTSFPG SSETPLSSKR PKASEEIKPE QMYQCPYCKY SNADVNRLRV HAMTQHSVQP
LLRCPLCQDM LNNKIHLQLH LTHLHSVAPD CVEKLIMTVT APEMVMPSSM FLPAAAADRD
GNSTLEEVGK QPEASEDPGK NILPPASMEH GGDLKPTSAD PSCGREDSGF LCWKKGCNQV
FKTSATLQTH FNEVHAKRPQ LPVSDRHVYK YRCNQCSLAF KTIEKLQLHS QYHVIRAATM
CCLCQRSFRT FQALKKHLET SHLELSEADI QQLYGGLLAN GDLLAMGDPT LAEDHTIIVE
EDKEEESDLE DKQSPTGSDS GSVQEDSGSE PKRALPFRKG PNFTMEKFLD PSRPYKCTVC
KESFTQKNIL LVHYNSVSHL HKLKRALQES ATGQPEPTSS PDNKPFKCNT CNVAYSQSST
LEIHMRSVLH QTKARAAKLE AASGNSNGTG NSGGVSLSSS TPSPVGSSGA NNTFTATNPS
SAAMAPSVNA LSQVPPESVV MPPLGNPISA NIASPSEPKE ANRKKLADMI ASRQQQQQQQ
QQQQQQAQTL AQAQAQVQAH LQQELQQQAA LIQSQLFNPT LLPHFPMTTE TLLQLQQQQH
LLFPFYIPSA EFQLNPEVSL PVTSGALTLT GSGPGLLEDL KVQVQIPQQS HQQILQQQQQ
QSQLSLSQSH SALLQPSQHP EKKNKVVIKE KDKESQRERE GPEGAEGNTG PQESLPDASK
AKEKKDLAPG GGSEGTMLPP RIASDARGNA TKALLENFGF ELVIQYNENK QKAQKKNGKA
EQGGESLEKL ECDSCGKLFS NILILKSHQE HVHQNYFPFK QLERFAKQYR EHYDKLYPLR
PQTPEPPPPP PPPPPPPLPT APPQPASAPA IPASAPPITS PTIAPAQPSV PLTQLSMPME
LPIFSPLMMQ TMPLQTLPAQ LPPQLGPVEP LPADLAQLYQ HQLNPTLLQQ QNKRPRTRIT
DDQLRVLRQY FDINNSPSEE QIKEMADKSG LPQKVIKHWF RNTLFKERQR NKDSPYNFSN
PPITSLEELK IDSRPPSPEP QKQEYWGSKR SSRTRFTDYQ LRVLQDFFDA NAYPKDDEFE
QLSNLLNLPT RVIVVWFQNA RQKARKNYEN QGEGKDGERR ELTNDRYIRT SNLNYQCKKC
SLVFQRIFDL IKHQKKLCYK DEDEEGQDDS QNEDSMDAME ILTPTSSSCS TPMPSQAYST
PAPSAAAANT APSAFLQLTA ETDELATFNS KAEASDEKPK QADPPSAQPN QTQEKQGQPK
PEMQQQLEQL EQKTNAPQPK LPQPAAPSLP QPPPQAPPPQ CPLPQSSPSP SQLSHLPLKP
LHTSTPQQLA NLPPQLIPYQ CDQCKLAFPS FEHWQEHQQL HFLSAQNQFI HPQFLDRSLD
MPFMLFDPSN PLLASQLLSG AIPQIPASSA TSPSTPTSTM NTLKRKLEEK ASASPGENDS
GTGGEEPQRD KRLRTTITPE QLEILYQKYL LDSNPTRKML DHIAHEVGLK KRVVQVWFQN
TRARERKGQF RAVGPAQAHR RCPFCRALFK AKTALEAHIR SRHWHEAKRA GYNLTLSAML
LDCDGGLQMK GDIFDGTSFS HLPPSSSDGQ GVPLSPVSKT MELSPRTLLS PSSIKVEGIE
DFESPSMSSV NLNFDQTKLD NDDCSSVNTA ITDTTTGDEG NADNDSATGI ATETKSSAPN
EGLTKAAMMA MSEYEDRLSS GLVSPAPSFY SKEYDNEGTV DYSETSSLAD PCSPSPGASG
SAGKSGDGGD RPGQKRFRTQ MTNLQLKVLK SCFNDYRTPT MLECEVLGND IGLPKRVVQV
WFQNARAKEK KSKLSMAKHF GINQTSYEGP KTECTLCGIK YSARLSVRDH IFSQQHISKV
KDTIGSQLDK EKEYFDPATV RQLMAQQELD RIKKANEVLG LAAQQQGMFD NAPLQALNLP
TTYPALQGIP PVLLPGLNRP SLPGFTPANT ALTSPKPNLM GLPSTTVPSP GLPTSGLPNK
PSSASLSSPT PAQATMAMAP QPPPQPQQPQ PPVQQPPPPP AAQQIPAPQL TPQQQRKDKD
GEKGKEKEKA HKGKGEPLPV PKKEKGEAPP AGTGTISAPL PAMEYAVDPA QLQALQAALT
SDPTALLTSQ FLPYFVPGFS PYYAPQIPGA LQSGYLQPMY GMEGLFPYSP ALSRPLMGLS
PGSLLQQYQQ YQQSLQEAIQ QQQQQQQQQQ QQQQQQQRQL QQQQQQQQQK VQQQQQQQQQ
PKASQTPVPQ GAASPDKDPA KESPKPEEQK NVPRELSPLL PKPPEEPEAE SKSASADSLC
DPFIVPKVQY KLVCRKCQAG FGDEEAARSH LKSLCCFGQS VVNLQEMVLH VPTGSGGGGG
GGGGSGGGGG SYHCLACESA LCGEEALSQH LESALHKHRT ITRAARNAKE HPSLLPHSAC
FPDPSTASTS QSAAHSNDSP PPPSAAPSSS ASPHASRKSW PPVGSRASAA KPPSFPPLSS
SSTVTSSSCS TSGVQPSMPT DDYSEESDTD LSQKSDGPAS PVEGPKDPSC PKDSGLTSVG
TDTFRL


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EIAAB47360 GC-box-binding zinc finger protein 1,GZP1,Homo sapiens,Human,Transcription factor ZBP-99,ZBP99,Zinc finger DNA-binding protein 99,Zinc finger protein 281,ZNF281
EIAAB47268 Beta enolase repressor factor 1,G-rich box-binding protein,Mouse,Mus musculus,Transcription factor BFCOL1,Transcription factor ZBP-89,Zbp89,Zfp148,Zinc finger DNA-binding protein 89,Zinc finger protei
EIAAB35961 FINB,Finger protein in nuclear bodies,Homo sapiens,Human,Raf-responsive zinc finger protein LZ321,Ras-responsive element-binding protein 1,RREB1,RREB-1,Zep-1,Zinc finger motif enhancer-binding protein
EIAAB47027 Delta EF1,MEB1,Mouse,Mus musculus,Tcf8,TCF-8,Transcription factor 8,Zeb1,Zfhx1a,Zfx1a,Zfx1ha,Zinc finger E-box-binding homeobox 1,Zinc finger homeobox protein 1a
EIAAB47029 AREB6,Homo sapiens,Human,Negative regulator of IL2,NIL-2-A zinc finger protein,TCF8,TCF-8,Transcription factor 8,ZEB1,Zinc finger E-box-binding homeobox 1
20-372-60303 zinc finger E-box binding homeobox 1 (ZEB1) - Mouse monoclonal anti-human TCF8 antibody; Transcription factor 8; NIL-2-A zinc finger protein; Negative regulator of IL2 Monoclonal 0.1 mg
EIAAB47671 Homo sapiens,Human,KIAA1221,ZEP2,Zep-2,Zinc finger motif enhancer-binding protein 2,Zinc finger protein 644,ZNF644
EIAAB47269 Rat,Rattus norvegicus,Transcription factor ZBP-89,Zbp89,Zfp148,Zinc finger DNA-binding protein 89,Zinc finger protein 148,Znf148
EIAAB47266 Homo sapiens,Human,Transcription factor ZBP-89,ZBP89,Zinc finger DNA-binding protein 89,Zinc finger protein 148,ZNF148
EIAAB47267 Bos taurus,Bovine,Transcription factor ZBP-89,ZBP89,Zinc finger DNA-binding protein 89,Zinc finger protein 148,ZNF148
EIAAB37990 BBP,Homo sapiens,Human,Mammalian branch point-binding protein,mBBP,SF1,Splicing factor 1,Transcription factor ZFM1,ZFM1,Zinc finger gene in MEN1 locus,Zinc finger protein 162,ZNF162
EIAAB37989 BBP,CW17,Mammalian branch point-binding protein,mBBP,Mouse,Mus musculus,mZFM,Sf1,Splicing factor 1,Transcription factor ZFM1,Zfm1,Zfp162,Zinc finger gene in MEN1 locus,Zinc finger protein 162
EIAAB47026 Chicken,Delta EF1,Delta-crystallin enhancer-binding factor,Gallus gallus,TCF8,TCF-8,Transcription factor 8,ZEB1,Zinc finger E-box-binding homeobox 1
31-162 Transcription Factor AREB6 _ transcription factor 8 _zinc finger homeodomain enhancer-binding protein inhibits interleukin-2 (IL-2) gene expression. May be responsible for transcriptional repression o 0.05 mg
EIAAB46813 LP-1,Mouse,Mus musculus,Polyomavirus late initiator promoter-binding protein,Zbtb17,Zfp100,Zfp-100,Zinc finger and BTB domain-containing protein 17,Zinc finger protein 100,Zinc finger protein 151,Zinc
EIAAB47033 Alpha A-CRYBP1,Alpha A-crystallin-binding protein 1,Alpha A-crystallin-binding protein I,Cryabp1,Hivep1,Mouse,Mus musculus,Transcription factor alphaA-CRYBP1,Zinc finger protein 40,Znf40
EIAAB47030 Mouse,Mus musculus,Sip1,Smad-interacting protein 1,Zeb2,Zfhx1b,Zfx1b,Zinc finger E-box-binding homeobox 2,Zinc finger homeobox protein 1b
EIAAB47031 Homo sapiens,HRIHFB2411,Human,KIAA0569,SIP1,Smad-interacting protein 1,SMADIP1,ZEB2,ZFHX1B,ZFX1B,Zinc finger E-box-binding homeobox 2,Zinc finger homeobox protein 1b
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
18-003-42715 Zinc finger and BTB domain-containing protein 7A - Leukemia_lymphoma-related factor; Factor that binds to inducer of short transcripts protein 1; Factor binding IST protein 1; FBI-1; HIV-1 1st-binding 0.1 mg Protein A
EIAAB47355 Homo sapiens,Human,Neurotrophin receptor-interacting factor homolog,SP2114,Zf2,Zinc finger protein 274,Zinc finger protein HFB101,Zinc finger protein with KRAB and SCAN domains 19,Zinc finger protein
EIAAB47457 Early B-cell factor-associated zinc finger protein,Ebfaz,Kiaa0760,Mouse,Mus musculus,Nur12,Oaz,Olf1_EBF-associated zinc finger protein,Smad- and Olf-interacting zinc finger protein,Zfp423,Zinc finger


 

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