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

Microphthalmia-associated transcription factor (Class E basic helix-loop-helix protein 32) (bHLHe32)

 MITF_HUMAN              Reviewed;         526 AA.
O75030; B4DJL2; D3K197; E9PFN0; Q14841; Q9P2V0; Q9P2V1; Q9P2V2;
Q9P2Y8;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
21-FEB-2001, sequence version 2.
25-OCT-2017, entry version 184.
RecName: Full=Microphthalmia-associated transcription factor;
AltName: Full=Class E basic helix-loop-helix protein 32;
Short=bHLHe32;
Name=MITF; Synonyms=BHLHE32;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A2), NUCLEOTIDE SEQUENCE [MRNA] OF
1-35 (ISOFORMS H1/H2), FUNCTION, TISSUE SPECIFICITY, AND INVOLVEMENT
IN WS2-OA.
TISSUE=Kidney;
PubMed=9647758; DOI=10.1006/bbrc.1998.8838;
Amae S., Fuse N., Yasumoto K., Sato S., Yajima I., Yamamoto H.,
Udono T., Durlu Y.K., Tamai M., Takahashi K., Shibahara S.;
"Identification of a novel isoform of microphthalmia-associated
transcription factor that is enriched in retinal pigment epithelium.";
Biochem. Biophys. Res. Commun. 247:710-715(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM M1).
TISSUE=Skin;
PubMed=8069297; DOI=10.1093/hmg/3.4.553;
Tachibana M., Perez-Jurado L.A., Nakayama A., Hodgkinson C.A., Li X.,
Schneider M., Miki T., Fex J., Francke U., Arnheiter H.;
"Cloning of MITF, the human homolog of the mouse microphthalmia gene
and assignment to chromosome 3p14.1-p12.3.";
Hum. Mol. Genet. 3:553-557(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MDEL), AND TISSUE SPECIFICITY.
PubMed=20163701; DOI=10.1186/1741-7015-8-14;
Wang Y., Radfar S., Liu S., Riker A.I., Khong H.T.;
"Mitf-Mdel, a novel melanocyte/melanoma-specific isoform of
microphthalmia-associated transcription factor-M, as a candidate
biomarker for melanoma.";
BMC Med. 8:14-14(2010).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A2).
TISSUE=Uterus;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 12).
TISSUE=Thalamus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS M1 AND M2).
TISSUE=Skin;
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).
[8]
PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS A1/A2; B1/B2;
H1/H2 AND M1/M2).
PubMed=10760582; DOI=10.1016/S0167-4781(00)00051-8;
Udono T., Yasumoto K., Takeda K., Amae S., Watanabe K., Saito H.,
Fuse N., Tachibana M., Takahashi K., Tamai M., Shibahara S.;
"Structural organization of the human microphthalmia-associated
transcription factor gene containing four alternative promoters.";
Biochim. Biophys. Acta 1491:205-219(2000).
[9]
ALTERNATIVE SPLICING (ISOFORM C1/C2).
TISSUE=Kidney;
PubMed=10578055; DOI=10.1093/oxfordjournals.jbchem.a022548;
Fuse N., Yasumoto K., Takeda K., Amae S., Yoshizawa M., Udono T.,
Takahashi K., Tamai M., Tomita Y., Tachibana M., Shibahara S.;
"Molecular cloning of cDNA encoding a novel microphthalmia-associated
transcription factor isoform with a distinct amino-terminus.";
J. Biochem. 126:1043-1051(1999).
[10]
PHOSPHORYLATION AT SER-180 AND SER-516, UBIQUITINATION, AND
MUTAGENESIS OF SER-180 AND SER-516.
PubMed=10673502;
Wu M., Hemesath T.J., Takemoto C.M., Horstmann M.A., Wells A.G.,
Price E.R., Fisher D.Z., Fisher D.E.;
"c-Kit triggers dual phosphorylations, which couple activation and
degradation of the essential melanocyte factor Mi.";
Genes Dev. 14:301-312(2000).
[11]
FUNCTION, MUTAGENESIS OF SER-405, AND PHOSPHORYLATION AT SER-405.
PubMed=10587587; DOI=10.1093/hmg/9.1.125;
Takeda K., Takemoto C., Kobayashi I., Watanabe A., Nobukuni Y.,
Fisher D.E., Tachibana M.;
"Ser298 of MITF, a mutation site in Waardenburg syndrome type 2, is a
phosphorylation site with functional significance.";
Hum. Mol. Genet. 9:125-132(2000).
[12]
INTERACTION WITH KARS.
PubMed=14975237; DOI=10.1016/S1074-7613(04)00020-2;
Lee Y.N., Nechushtan H., Figov N., Razin E.;
"The function of lysyl-tRNA synthetase and Ap4A as signaling
regulators of MITF activity in FcepsilonRI-activated mast cells.";
Immunity 20:145-151(2004).
[13]
SUMOYLATION AT LYS-289 AND LYS-423, AND MUTAGENESIS OF LYS-289 AND
LYS-423.
PubMed=15507434; DOI=10.1074/jbc.M411757200;
Miller A.J., Levy C., Davis I.J., Razin E., Fisher D.E.;
"Sumoylation of MITF and its related family members TFE3 and TFEB.";
J. Biol. Chem. 280:146-155(2005).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-414, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-414, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-491, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
IDENTIFICATION IN A COMPLEX WITH HINT1 AND CTNNB1, AND FUNCTION.
PubMed=22647378; DOI=10.4161/cc.20765;
Genovese G., Ghosh P., Li H., Rettino A., Sioletic S., Cittadini A.,
Sgambato A.;
"The tumor suppressor HINT1 regulates MITF and beta-catenin
transcriptional activity in melanoma cells.";
Cell Cycle 11:2206-2215(2012).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-414, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN COMMAD, VARIANTS COMMAD
ASN-313; ARG-324 DEL AND GLY-324, AND CHARACTERIZATION OF VARIANTS
COMMAD ASN-313 AND ARG-324 DEL.
PubMed=27889061; DOI=10.1016/j.ajhg.2016.11.004;
George A., Zand D.J., Hufnagel R.B., Sharma R., Sergeev Y.V.,
Legare J.M., Rice G.M., Scott Schwoerer J.A., Rius M., Tetri L.,
Gamm D.M., Bharti K., Brooks B.P.;
"Biallelic mutations in MITF cause coloboma, osteopetrosis,
microphthalmia, macrocephaly, albinism, and deafness.";
Am. J. Hum. Genet. 99:1388-1394(2016).
[20]
INVOLVEMENT IN DISEASE, AND VARIANT LYS-425.
PubMed=27680874; DOI=10.1210/jc.2016-2103;
Castro-Vega L.J., Kiando S.R., Burnichon N., Buffet A., Amar L.,
Simian C., Berdelou A., Galan P., Schlumberger M., Bouatia-Naji N.,
Favier J., Bressac-de Paillerets B., Gimenez-Roqueplo A.P.;
"The MITF, p.E318K Variant, as a Risk Factor for Pheochromocytoma and
Paraganglioma.";
J. Clin. Endocrinol. Metab. 101:4764-4768(2016).
[21]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 357-403, SUBUNIT, AND COILED
COIL.
PubMed=24631970; DOI=10.1016/J.JSB.2014.03.002;
Kukenshoner T., Wohlwend D., Niemoller C., Dondapati P., Speck J.,
Adeniran A.V., Nieth A., Gerhardt S., Einsle O., Muller K.M.,
Arndt K.M.;
"Improving coiled coil stability while maintaining specificity by a
bacterial hitchhiker selection system.";
J. Struct. Biol. 186:335-348(2014).
[22]
VARIANTS WS2A LYS-310; ARG-324 DEL; PRO-357; ASP-385 AND PRO-405.
PubMed=8589691; DOI=10.1093/hmg/4.11.2131;
Tassabehji M., Newton V.E., Liu X.-Z., Brady A., Donnai D.,
Krajewska-Walasek M., Murday V., Norman A., Obersztyn E., Reardon W.,
Rice J.C., Trembath R., Wieacker P., Whiteford M., Winter R.,
Read A.P.;
"The mutational spectrum in Waardenburg syndrome.";
Hum. Mol. Genet. 4:2131-2137(1995).
[23]
VARIANT TADS LYS-317.
TISSUE=Blood;
PubMed=10851256; DOI=10.1136/jmg.37.6.446;
Smith S.D., Kelley P.M., Kenyon J.B., Hoover D.;
"Tietz syndrome (hypopigmentation/deafness) caused by mutation of
MITF.";
J. Med. Genet. 37:446-448(2000).
[24]
INVOLVEMENT IN CMM8, AND VARIANT CMM8 LYS-425.
PubMed=22012259; DOI=10.1038/nature10539;
Bertolotto C., Lesueur F., Giuliano S., Strub T., de Lichy M.,
Bille K., Dessen P., d'Hayer B., Mohamdi H., Remenieras A., Maubec E.,
de la Fouchardiere A., Molinie V., Vabres P., Dalle S., Poulalhon N.,
Martin-Denavit T., Thomas L., Andry-Benzaquen P., Dupin N.,
Boitier F., Rossi A., Perrot J.L., Labeille B., Robert C.,
Escudier B., Caron O., Brugieres L., Saule S., Gardie B., Gad S.,
Richard S., Couturier J., Teh B.T., Ghiorzo P., Pastorino L., Puig S.,
Badenas C., Olsson H., Ingvar C., Rouleau E., Lidereau R.,
Bahadoran P., Vielh P., Corda E., Blanche H., Zelenika D., Galan P.,
Aubin F., Bachollet B., Becuwe C., Berthet P., Bignon Y.J.,
Bonadona V., Bonafe J.L., Bonnet-Dupeyron M.N., Cambazard F.,
Chevrant-Breton J., Coupier I., Dalac S., Demange L., d'Incan M.,
Dugast C., Faivre L., Vincent-Fetita L., Gauthier-Villars M.,
Gilbert B., Grange F., Grob J.J., Humbert P., Janin N., Joly P.,
Kerob D., Lasset C., Leroux D., Levang J., Limacher J.M.,
Livideanu C., Longy M., Lortholary A., Stoppa-Lyonnet D., Mansard S.,
Mansuy L., Marrou K., Mateus C., Maugard C., Meyer N., Nogues C.,
Souteyrand P., Venat-Bouvet L., Zattara H., Chaudru V., Lenoir G.M.,
Lathrop M., Davidson I., Avril M.F., Demenais F., Ballotti R.,
Bressac-de Paillerets B.;
"A SUMOylation-defective MITF germline mutation predisposes to
melanoma and renal carcinoma.";
Nature 480:94-98(2011).
[25]
INVOLVEMENT IN CMM8, VARIANT CMM8 LYS-425, AND CHARACTERIZATION OF
VARIANT CMM8 LYS-425.
PubMed=22080950; DOI=10.1038/nature10630;
Yokoyama S., Woods S.L., Boyle G.M., Aoude L.G., MacGregor S.,
Zismann V., Gartside M., Cust A.E., Haq R., Harland M., Taylor J.C.,
Duffy D.L., Holohan K., Dutton-Regester K., Palmer J.M., Bonazzi V.,
Stark M.S., Symmons J., Law M.H., Schmidt C., Lanagan C., O'Connor L.,
Holland E.A., Schmid H., Maskiell J.A., Jetann J., Ferguson M.,
Jenkins M.A., Kefford R.F., Giles G.G., Armstrong B.K., Aitken J.F.,
Hopper J.L., Whiteman D.C., Pharoah P.D., Easton D.F., Dunning A.M.,
Newton-Bishop J.A., Montgomery G.W., Martin N.G., Mann G.J.,
Bishop D.T., Tsao H., Trent J.M., Fisher D.E., Hayward N.K.,
Brown K.M.;
"A novel recurrent mutation in MITF predisposes to familial and
sporadic melanoma.";
Nature 480:99-103(2011).
[26]
VARIANT WS2A THR-294.
PubMed=28236341; DOI=10.1002/humu.23206;
Issa S., Bondurand N., Faubert E., Poisson S., Lecerf L., Nitschke P.,
Deggouj N., Loundon N., Jonard L., David A., Sznajer Y., Blanchet P.,
Marlin S., Pingault V.;
"EDNRB mutations cause Waardenburg syndrome type II in the
heterozygous state.";
Hum. Mutat. 38:581-593(2017).
-!- FUNCTION: Transcription factor that regulates the expression of
genes with essential roles in cell differentiation, proliferation
and survival. Binds to M-boxes (5'-TCATGTG-3') and symmetrical DNA
sequences (E-boxes) (5'-CACGTG-3') found in the promoters of
target genes, such as BCL2 and tyrosinase (TYR). Plays an
important role in melanocyte development by regulating the
expression of tyrosinase (TYR) and tyrosinase-related protein 1
(TYRP1). Plays a critical role in the differentiation of various
cell types, such as neural crest-derived melanocytes, mast cells,
osteoclasts and optic cup-derived retinal pigment epithelium.
{ECO:0000269|PubMed:10587587, ECO:0000269|PubMed:22647378,
ECO:0000269|PubMed:27889061, ECO:0000269|PubMed:9647758}.
-!- SUBUNIT: Homodimer or heterodimer; dimerization is mediated via
the coiled coil region (PubMed:24631970). Efficient DNA binding
requires dimerization with another bHLH protein. Binds DNA in the
form of homodimer or heterodimer with either TFE3, TFEB or TFEC.
Interacts with KARS (PubMed:14975237). Identified in a complex
with HINT1 and CTNNB1 (PubMed:22647378).
{ECO:0000269|PubMed:14975237, ECO:0000269|PubMed:22647378,
ECO:0000269|PubMed:24631970}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27889061}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=12;
Comment=The X2-type isoforms differ from the X1-type isoforms by
the absence of a 6 residue insert.;
Name=A1;
IsoId=O75030-1; Sequence=Displayed;
Name=A2;
IsoId=O75030-2; Sequence=VSP_002128;
Name=B1;
IsoId=O75030-3; Sequence=VSP_002124;
Name=B2;
IsoId=O75030-4; Sequence=VSP_002124, VSP_002128;
Name=C1;
IsoId=O75030-5; Sequence=VSP_002125;
Name=C2;
IsoId=O75030-6; Sequence=VSP_002125, VSP_002128;
Name=H1;
IsoId=O75030-7; Sequence=VSP_002126;
Name=H2;
IsoId=O75030-8; Sequence=VSP_002126, VSP_002128;
Name=M1;
IsoId=O75030-9; Sequence=VSP_002127;
Name=M2;
IsoId=O75030-10; Sequence=VSP_002127, VSP_002128;
Name=Mdel;
IsoId=O75030-11; Sequence=VSP_002127, VSP_045178, VSP_045179;
Name=12;
IsoId=O75030-12; Sequence=VSP_046438, VSP_045179;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Isoform M is exclusively expressed in
melanocytes and melanoma cells. Isoform A and isoform H are widely
expressed in many cell types including melanocytes and retinal
pigment epithelium (RPE). Isoform C is expressed in many cell
types including RPE but not in melanocyte-lineage cells. Isoform
Mdel is widely expressed in melanocytes, melanoma cell lines and
tissues, but almost undetectable in non-melanoma cell lines.
{ECO:0000269|PubMed:20163701, ECO:0000269|PubMed:9647758}.
-!- DOMAIN: The leucine zipper region is part of a larger coiled coil.
{ECO:0000305|PubMed:24631970}.
-!- PTM: Phosphorylation at Ser-405 significantly enhances the ability
to bind the tyrosinase promoter. Phosphorylated at Ser-180 and
Ser-516 following KIT signaling, trigerring a short live
activation: Phosphorylation at Ser-180 and Ser-516 by MAPK and
RPS6KA1, respectively, activate the transcription factor activity
but also promote ubiquitination and subsequent degradation by the
proteasome. {ECO:0000269|PubMed:10587587,
ECO:0000269|PubMed:10673502}.
-!- PTM: Ubiquitinated following phosphorylation at Ser-180, leading
to subsequent degradation by the proteasome. Deubiquitinated by
USP13, preventing its degradation. {ECO:0000269|PubMed:10673502}.
-!- DISEASE: Waardenburg syndrome 2A (WS2A) [MIM:193510]: WS2 is a
genetically heterogeneous, autosomal dominant disorder
characterized by sensorineural deafness, pigmentary disturbances,
and absence of dystopia canthorum. The frequency of deafness is
higher in WS2 than in WS1. {ECO:0000269|PubMed:28236341,
ECO:0000269|PubMed:8589691}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Waardenburg syndrome 2, with ocular albinism, autosomal
recessive (WS2-OA) [MIM:103470]: A disorder characterized by the
association of features typical of Waardenburg syndrome type 2
with ocular albinism. Patients manifest reduced visual acuity,
albinotic fundus, deafness, hypomelanosis.
{ECO:0000269|PubMed:9647758}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Tietz albinism-deafness syndrome (TADS) [MIM:103500]: An
autosomal dominant disorder characterized by generalized
hypopigmentation and congenital, bilateral, profound sensorineural
deafness. {ECO:0000269|PubMed:10851256}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- DISEASE: Melanoma, cutaneous malignant 8 (CMM8) [MIM:614456]: A
malignant neoplasm of melanocytes, arising de novo or from a pre-
existing benign nevus, which occurs most often in the skin but
also may involve other sites. {ECO:0000269|PubMed:22012259,
ECO:0000269|PubMed:22080950}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- DISEASE: Coloboma, osteopetrosis, microphthalmia, macrocephaly,
albinism, and deafness (COMMAD) [MIM:617306]: An autosomal
recessive syndrome characterized by severe microphthalmia,
profound congenital sensorineural hearing loss, lack of pigment in
the hair, skin, and eyes, macrocephaly, facial dysmorphism, and
osteopetrosis. {ECO:0000269|PubMed:27889061}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
An allelic combination involving at least one dominant-negative
mutation, inherited in a recessive manner, represents the
underlying molecular mechanism leading to COMMAD syndrome.
{ECO:0000269|PubMed:27889061}.
-!- DISEASE: Note=Variations affecting this gene are associated with
susceptibility to pheochromocytomas and paragangliomas, rare
neural crest-derived tumors with an approximate incidence of
1:300,000/year. {ECO:0000269|PubMed:27680874}.
-!- SIMILARITY: Belongs to the MiT/TFE family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB006909; BAA32288.1; -; mRNA.
EMBL; AB006989; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; Z29678; CAA82775.1; -; mRNA.
EMBL; GU355676; ADB90411.1; -; mRNA.
EMBL; AL110195; CAB53672.1; -; mRNA.
EMBL; AK296129; BAG58874.1; -; mRNA.
EMBL; AC099326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC104445; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC104449; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC124915; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC026961; AAH26961.1; -; mRNA.
EMBL; BC065243; AAH65243.1; -; mRNA.
EMBL; AF034755; AAC39639.1; -; Genomic_DNA.
EMBL; AB032359; BAA95208.1; -; Genomic_DNA.
EMBL; AB032358; BAA95207.1; -; Genomic_DNA.
EMBL; AB032357; BAA95206.1; -; Genomic_DNA.
EMBL; AB009608; BAA95209.1; ALT_TERM; Genomic_DNA.
CCDS; CCDS2913.1; -. [O75030-9]
CCDS; CCDS43106.1; -. [O75030-2]
CCDS; CCDS43107.1; -. [O75030-10]
CCDS; CCDS46865.1; -. [O75030-8]
CCDS; CCDS46866.2; -. [O75030-11]
CCDS; CCDS54607.1; -. [O75030-12]
PIR; I38024; I38024.
PIR; T14752; T14752.
RefSeq; NP_000239.1; NM_000248.3. [O75030-9]
RefSeq; NP_001171896.1; NM_001184967.1. [O75030-12]
RefSeq; NP_006713.1; NM_006722.2. [O75030-6]
RefSeq; NP_937801.1; NM_198158.2. [O75030-10]
RefSeq; NP_937802.1; NM_198159.2. [O75030-2]
RefSeq; NP_937820.1; NM_198177.2. [O75030-8]
RefSeq; NP_937821.2; NM_198178.2. [O75030-11]
RefSeq; XP_005264811.1; XM_005264754.1. [O75030-1]
RefSeq; XP_005264812.1; XM_005264755.3. [O75030-7]
RefSeq; XP_016861933.1; XM_017006444.1. [O75030-5]
RefSeq; XP_016861937.1; XM_017006448.1. [O75030-12]
UniGene; Hs.166017; -.
UniGene; Hs.618266; -.
PDB; 4C7N; X-ray; 2.10 A; A=357-403.
PDBsum; 4C7N; -.
ProteinModelPortal; O75030; -.
SMR; O75030; -.
BioGrid; 110432; 27.
DIP; DIP-59573N; -.
IntAct; O75030; 7.
MINT; MINT-7997258; -.
STRING; 9606.ENSP00000295600; -.
ChEMBL; CHEMBL1741165; -.
iPTMnet; O75030; -.
PhosphoSitePlus; O75030; -.
BioMuta; MITF; -.
MaxQB; O75030; -.
PaxDb; O75030; -.
PeptideAtlas; O75030; -.
PRIDE; O75030; -.
Ensembl; ENST00000314557; ENSP00000324246; ENSG00000187098. [O75030-10]
Ensembl; ENST00000314589; ENSP00000324443; ENSG00000187098. [O75030-8]
Ensembl; ENST00000328528; ENSP00000327867; ENSG00000187098. [O75030-6]
Ensembl; ENST00000352241; ENSP00000295600; ENSG00000187098. [O75030-2]
Ensembl; ENST00000394351; ENSP00000377880; ENSG00000187098. [O75030-9]
Ensembl; ENST00000448226; ENSP00000391803; ENSG00000187098. [O75030-1]
Ensembl; ENST00000472437; ENSP00000418845; ENSG00000187098. [O75030-12]
Ensembl; ENST00000531774; ENSP00000435909; ENSG00000187098. [O75030-11]
GeneID; 4286; -.
KEGG; hsa:4286; -.
UCSC; uc003dnz.4; human. [O75030-1]
CTD; 4286; -.
DisGeNET; 4286; -.
EuPathDB; HostDB:ENSG00000187098.14; -.
GeneCards; MITF; -.
HGNC; HGNC:7105; MITF.
HPA; CAB002578; -.
HPA; HPA003259; -.
MalaCards; MITF; -.
MIM; 103470; phenotype.
MIM; 103500; phenotype.
MIM; 156845; gene.
MIM; 193510; phenotype.
MIM; 614456; phenotype.
MIM; 617306; phenotype.
neXtProt; NX_O75030; -.
OpenTargets; ENSG00000187098; -.
Orphanet; 404511; Clear cell papillary renal cell carcinoma.
Orphanet; 293822; MITF-related melanoma and renal cell carcinoma predisposition syndrome.
Orphanet; 352740; Ocular albinism with congenital sensorineural deafness.
Orphanet; 319298; Papillary renal cell carcinoma.
Orphanet; 42665; Tietz syndrome.
Orphanet; 895; Waardenburg syndrome type 2.
PharmGKB; PA30823; -.
eggNOG; KOG1318; Eukaryota.
eggNOG; ENOG4110SME; LUCA.
GeneTree; ENSGT00390000004402; -.
HOGENOM; HOG000231368; -.
HOVERGEN; HBG006768; -.
InParanoid; O75030; -.
KO; K09455; -.
OMA; MEDTDHA; -.
OrthoDB; EOG091G0QCO; -.
PhylomeDB; O75030; -.
TreeFam; TF317174; -.
Reactome; R-HSA-3232118; SUMOylation of transcription factors.
SignaLink; O75030; -.
SIGNOR; O75030; -.
GeneWiki; Microphthalmia-associated_transcription_factor; -.
GenomeRNAi; 4286; -.
PMAP-CutDB; O75030; -.
PRO; PR:O75030; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000187098; -.
CleanEx; HS_MITF; -.
ExpressionAtlas; O75030; baseline and differential.
Genevisible; O75030; HS.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0070888; F:E-box binding; IDA:UniProtKB.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:UniProtKB.
GO; GO:0001227; F:transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding; NAS:BHF-UCL.
GO; GO:0030318; P:melanocyte differentiation; IBA:GO_Central.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:2000144; P:positive regulation of DNA-templated transcription, initiation; IDA:CACAO.
GO; GO:0010628; P:positive regulation of gene expression; IDA:CACAO.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0006461; P:protein complex assembly; IDA:UniProtKB.
GO; GO:0016925; P:protein sumoylation; TAS:Reactome.
GO; GO:2001141; P:regulation of RNA biosynthetic process; IDA:CACAO.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
CDD; cd00083; HLH; 1.
Gene3D; 4.10.280.10; -; 1.
InterPro; IPR011598; bHLH_dom.
InterPro; IPR036638; HLH_DNA-bd_sf.
InterPro; IPR021802; MiT/TFE_C.
InterPro; IPR031867; MiT/TFE_N.
InterPro; IPR030532; MITF.
PANTHER; PTHR12565:SF91; PTHR12565:SF91; 2.
Pfam; PF11851; DUF3371; 1.
Pfam; PF00010; HLH; 1.
Pfam; PF15951; MITF_TFEB_C_3_N; 1.
SMART; SM00353; HLH; 1.
SUPFAM; SSF47459; SSF47459; 1.
PROSITE; PS50888; BHLH; 1.
1: Evidence at protein level;
3D-structure; Activator; Albinism; Alternative splicing; Coiled coil;
Complete proteome; Deafness; Developmental protein; Disease mutation;
DNA-binding; Isopeptide bond; Microphthalmia; Nucleus; Osteopetrosis;
Phosphoprotein; Polymorphism; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation; Waardenburg syndrome.
CHAIN 1 526 Microphthalmia-associated transcription
factor.
/FTId=PRO_0000127276.
DOMAIN 311 364 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
REGION 224 295 Transactivation.
REGION 374 395 Leucine-zipper.
{ECO:0000305|PubMed:24631970}.
REGION 401 431 DNA binding regulation.
COILED 355 402 {ECO:0000305|PubMed:24631970}.
MOD_RES 180 180 Phosphoserine; by MAPK.
{ECO:0000269|PubMed:10673502}.
MOD_RES 405 405 Phosphoserine; by GSK3.
{ECO:0000269|PubMed:10587587}.
MOD_RES 414 414 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 491 491 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 516 516 Phosphoserine; by RPS6KA1.
{ECO:0000269|PubMed:10673502}.
CROSSLNK 289 289 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:15507434}.
CROSSLNK 423 423 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:15507434}.
VAR_SEQ 1 118 MQSESGIVPDFEVGEEFHEEPKTYYELKSQPLKSSSSAEHP
GASKPPISSSSMTSRILLRQQLMREQMQEQERREQQQKLQA
AQFMQQRVPVSQTPAINVSVPTTLPSATQVPMEVLK -> M
LEMLEYNHYQ (in isoform M1, isoform M2 and
isoform Mdel).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:20163701,
ECO:0000303|PubMed:8069297}.
/FTId=VSP_002127.
VAR_SEQ 1 52 Missing (in isoform 12).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046438.
VAR_SEQ 1 35 MQSESGIVPDFEVGEEFHEEPKTYYELKSQPLKSS -> ME
ALRVQMFMPCSFESLYL (in isoform H1 and
isoform H2). {ECO:0000305}.
/FTId=VSP_002126.
VAR_SEQ 1 34 MQSESGIVPDFEVGEEFHEEPKTYYELKSQPLKS -> MLY
AFWFSH (in isoform B1 and isoform B2).
{ECO:0000305}.
/FTId=VSP_002124.
VAR_SEQ 1 34 MQSESGIVPDFEVGEEFHEEPKTYYELKSQPLKS -> MGH
LENTSVVFPRAIFSLCEKETRKLTLCLFSR (in
isoform C1 and isoform C2).
{ECO:0000305}.
/FTId=VSP_002125.
VAR_SEQ 139 194 Missing (in isoform Mdel).
{ECO:0000303|PubMed:20163701}.
/FTId=VSP_045178.
VAR_SEQ 293 298 Missing (in isoform Mdel and isoform 12).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:20163701}.
/FTId=VSP_045179.
VAR_SEQ 294 299 Missing (in isoform A2, isoform B2,
isoform C2, isoform H2 and isoform M2).
{ECO:0000303|PubMed:11230166,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9647758}.
/FTId=VSP_002128.
VARIANT 294 294 A -> T (in WS2A; unknown pathological
significance).
{ECO:0000269|PubMed:28236341}.
/FTId=VAR_078311.
VARIANT 310 310 R -> K (in WS2A; unknown pathological
significance).
{ECO:0000269|PubMed:8589691}.
/FTId=VAR_010297.
VARIANT 313 313 K -> N (in COMMAD; has both cytoplasmic
and nuclear localization; decreased
binding to M-box or E-box DNA sequences).
{ECO:0000269|PubMed:27889061}.
/FTId=VAR_077922.
VARIANT 317 317 N -> K (in TADS; dbSNP:rs104893745).
{ECO:0000269|PubMed:10851256}.
/FTId=VAR_010298.
VARIANT 324 324 R -> G (in COMMAD).
{ECO:0000269|PubMed:27889061}.
/FTId=VAR_077923.
VARIANT 324 324 Missing (in WS2A and COMMAD; does not
localize to the nucleus; does not bind M-
box or E-box DNA sequences; loss of
function in transcriptional regulation;
dominant negative effect).
{ECO:0000269|PubMed:27889061,
ECO:0000269|PubMed:8589691}.
/FTId=VAR_010299.
VARIANT 357 357 S -> P (in WS2A; dbSNP:rs104893744).
{ECO:0000269|PubMed:8589691}.
/FTId=VAR_010300.
VARIANT 385 385 N -> D (in WS2A).
{ECO:0000269|PubMed:8589691}.
/FTId=VAR_010301.
VARIANT 405 405 S -> P (in WS2A; dbSNP:rs104893747).
{ECO:0000269|PubMed:8589691}.
/FTId=VAR_010302.
VARIANT 425 425 E -> K (in CMM8; associated with disease
susceptibility; also associated with
pheochromocytomas and paragangliomas
susceptibility; results in impaired
sumoylation; dbSNP:rs149617956).
{ECO:0000269|PubMed:22012259,
ECO:0000269|PubMed:22080950,
ECO:0000269|PubMed:27680874}.
/FTId=VAR_067367.
MUTAGEN 180 180 S->A: Abolishes both transcription factor
activity and ubiquitination, leading to
an inert and stable protein; when
associated with A-516.
{ECO:0000269|PubMed:10673502}.
MUTAGEN 289 289 K->R: Loss of sumoylation; when
associated with R-423.
{ECO:0000269|PubMed:15507434}.
MUTAGEN 405 405 S->A,P: Loss of phosphorylation and
function. {ECO:0000269|PubMed:10587587}.
MUTAGEN 423 423 K->R: Loss of sumoylation; when
associated with R-289.
{ECO:0000269|PubMed:15507434}.
MUTAGEN 516 516 S->A: Abolishes both transcription factor
activity and ubiquitination, leading to
an inert and stable protein; when
associated with A-180.
{ECO:0000269|PubMed:10673502}.
CONFLICT 241 241 I -> T (in Ref. 5; BAG58874).
{ECO:0000305}.
HELIX 357 401 {ECO:0000244|PDB:4C7N}.
SEQUENCE 526 AA; 58795 MW; 136EBED3044C1986 CRC64;
MQSESGIVPD FEVGEEFHEE PKTYYELKSQ PLKSSSSAEH PGASKPPISS SSMTSRILLR
QQLMREQMQE QERREQQQKL QAAQFMQQRV PVSQTPAINV SVPTTLPSAT QVPMEVLKVQ
THLENPTKYH IQQAQRQQVK QYLSTTLANK HANQVLSLPC PNQPGDHVMP PVPGSSAPNS
PMAMLTLNSN CEKEGFYKFE EQNRAESECP GMNTHSRASC MQMDDVIDDI ISLESSYNEE
ILGLMDPALQ MANTLPVSGN LIDLYGNQGL PPPGLTISNS CPANLPNIKR ELTACIFPTE
SEARALAKER QKKDNHNLIE RRRRFNINDR IKELGTLIPK SNDPDMRWNK GTILKASVDY
IRKLQREQQR AKELENRQKK LEHANRHLLL RIQELEMQAR AHGLSLIPST GLCSPDLVNR
IIKQEPVLEN CSQDLLQHHA DLTCTTTLDL TDGTITFNNN LGTGTEANQA YSVPTKMGSK
LEDILMDDTL SPVGVTDPLL SSVSPGASKT SSRRSSMSME ETEHTC


Related products :

Catalog number Product name Quantity
EIAAB24839 bHLHe32,BHLHE32,Class E basic helix-loop-helix protein 32,Homo sapiens,Human,Microphthalmia-associated transcription factor,MITF
EIAAB37697 Basic helix-loop-helix transcription factor scleraxis,bHLHa41,BHLHA41,bHLHa48,Class A basic helix-loop-helix protein 41,Class A basic helix-loop-helix protein 48,Homo sapiens,Human,SCX,SCXA
EIAAB28828 bHLHb7,BHLHB7,bHLHe20,BHLHE20,Class B basic helix-loop-helix protein 7,Class E basic helix-loop-helix protein 20,Homo sapiens,Human,OLIG3,Oligo3,Oligodendrocyte transcription factor 3
EIAAB28821 bHLHb6,BHLHB6,bHLHe21,BHLHE21,Class B basic helix-loop-helix protein 6,Class E basic helix-loop-helix protein 21,Homo sapiens,Human,OLIG1,Oligo1,Oligodendrocyte transcription factor 1
EIAAB28826 bHLHb1,BHLHB1,bHLHe19,BHLHE19,Class B basic helix-loop-helix protein 1,Class E basic helix-loop-helix protein 19,Homo sapiens,Human,OLIG2,Oligo2,Oligodendrocyte transcription factor 2,PRKCBP2,Protein
U2004h CLIA Basic-helix-loop-helix-PAS protein MOP2,bHLHe73,BHLHE73,Class E basic helix-loop-helix protein 73,Endothelial PAS domain-containing protein 1,EPAS1,EPAS-1,HIF-1-alpha-like factor,HIF2A,HIF-2-alph 96T
E2004h ELISA Basic-helix-loop-helix-PAS protein MOP2,bHLHe73,BHLHE73,Class E basic helix-loop-helix protein 73,Endothelial PAS domain-containing protein 1,EPAS1,EPAS-1,HIF-1-alpha-like factor,HIF2A,HIF-2-alp 96T
U2004h CLIA kit Basic-helix-loop-helix-PAS protein MOP2,bHLHe73,BHLHE73,Class E basic helix-loop-helix protein 73,Endothelial PAS domain-containing protein 1,EPAS1,EPAS-1,HIF-1-alpha-like factor,HIF2A,HIF-2 96T
E2004h ELISA kit Basic-helix-loop-helix-PAS protein MOP2,bHLHe73,BHLHE73,Class E basic helix-loop-helix protein 73,Endothelial PAS domain-containing protein 1,EPAS1,EPAS-1,HIF-1-alpha-like factor,HIF2A,HIF- 96T
U0798h CLIA ARNT-interacting protein,Basic-helix-loop-helix-PAS protein MOP1,bHLHe78,BHLHE78,Class E basic helix-loop-helix protein 78,HIF1A,HIF-1-alpha,HIF1-alpha,Homo sapiens,Human,Hypoxia-inducible factor 96T
EIAAB27132 bHLHa6,BHLHA6,Class A basic helix-loop-helix protein 6,Homo sapiens,Human,NeuroD3,NEUROD3,NEUROG1,Neurogenic basic-helix-loop-helix protein,Neurogenic differentiation factor 3,Neurogenin-1,NGN,NGN1,NG
E0798h ELISA ARNT-interacting protein,Basic-helix-loop-helix-PAS protein MOP1,bHLHe78,BHLHE78,Class E basic helix-loop-helix protein 78,HIF1A,HIF-1-alpha,HIF1-alpha,Homo sapiens,Human,Hypoxia-inducible facto 96T
E0798h ELISA kit ARNT-interacting protein,Basic-helix-loop-helix-PAS protein MOP1,bHLHe78,BHLHE78,Class E basic helix-loop-helix protein 78,HIF1A,HIF-1-alpha,HIF1-alpha,Homo sapiens,Human,Hypoxia-inducible 96T
EIAAB14718 Basic helix-loop-helix protein N-twist,bHLHa31,BHLHA31,Class A basic helix-loop-helix protein 31,Fer3-like protein,FERD3L,Homo sapiens,Human,NATO3,Nephew of atonal 3,Neuronal twist,NTWIST
E0255h ELISA ATH1,ATOH1,bHLHa14,BHLHA14,Class A basic helix-loop-helix protein 14,hATH1,Helix-loop-helix protein hATH-1,Homo sapiens,Human,Protein atonal homolog 1 96T
U0255h CLIA ATH1,ATOH1,bHLHa14,BHLHA14,Class A basic helix-loop-helix protein 14,hATH1,Helix-loop-helix protein hATH-1,Homo sapiens,Human,Protein atonal homolog 1 96T
E0255h ELISA kit ATH1,ATOH1,bHLHa14,BHLHA14,Class A basic helix-loop-helix protein 14,hATH1,Helix-loop-helix protein hATH-1,Homo sapiens,Human,Protein atonal homolog 1 96T
EIAAB42114 bHLHe34,BHLHE34,Class E basic helix-loop-helix protein 34,Homo sapiens,hTFEC-L,Human,TCFEC,TFEC,TFE-C,TFECL,Transcription factor EC,Transcription factor EC-like
25-061 ATOH1 belongs to the basic helix-loop-helix (BHLH) family of transcription factors. It activates E-box dependent transcription along with E47.This protein belongs to the basic helix-loop-helix (BHLH) 0.05 mg
EIAAB42109 bHLHe35,BHLHE35,Class E basic helix-loop-helix protein 35,Homo sapiens,Human,TFEB,Transcription factor EB
EIAAB41704 bHLHa24,BHLHA24,Class A basic helix-loop-helix protein 24,Homo sapiens,Human,TCF23,TCF-23,Transcription factor 23
EIAAB42108 bHLHe33,BHLHE33,Class E basic helix-loop-helix protein 33,Homo sapiens,Human,TFE3,Transcription factor E3
EIAAB32965 bHLH transcription factor p48,bHLHa29,BHLHA29,Class A basic helix-loop-helix protein 29,Homo sapiens,Human,p48 DNA-binding subunit of transcription factor PTF1,Pancreas transcription factor 1 subunit
EIAAB45447 bHLHb11,BHLHB11,Class B basic helix-loop-helix protein 11,Homo sapiens,Human,Major late transcription factor 1,Upstream stimulatory factor 1,USF,USF1
EIAAB41701 bHLHa23,BHLHA23,Capsulin,Class A basic helix-loop-helix protein 23,Epicardin,Homo sapiens,Human,POD1,Pod-1,Podocyte-expressed 1,TCF21,TCF-21,Transcription factor 21


 

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