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Transcription factor E3 (Class E basic helix-loop-helix protein 33) (bHLHe33)

 TFE3_HUMAN              Reviewed;         575 AA.
P19532; A8MZL6; Q5JU74; Q92757; Q92758; Q99964;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
13-NOV-2007, sequence version 4.
25-OCT-2017, entry version 189.
RecName: Full=Transcription factor E3;
AltName: Full=Class E basic helix-loop-helix protein 33;
Short=bHLHe33;
Name=TFE3; Synonyms=BHLHE33;
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 1), AND CHROMOSOMAL TRANSLOCATION
WITH PSF AND NONO.
PubMed=9393982; DOI=10.1038/sj.onc.1201394;
Clark J., Lu Y.-J., Sidhar S.K., Parker C., Gill S., Smedley D.,
Hamoudi R., Linehan W.M., Shipley J., Cooper C.S.;
"Fusion of splicing factor genes PSF and NonO (p54nrb) to the TFE3
gene in papillary renal cell carcinoma.";
Oncogene 15:2233-2239(1997).
[2]
SEQUENCE REVISION.
Clark J.;
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Amygdala;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-219, AND CHROMOSOMAL
TRANSLOCATION WITH PRCC.
PubMed=8986805; DOI=10.1073/pnas.93.26.15294;
Weterman M.A.J., Wilbrink M., Geurts van Kessel A.;
"Fusion of the transcription factor TFE3 gene to a novel gene, PRCC,
in t(X;1)(p11;q21)-positive papillary renal cell carcinomas.";
Proc. Natl. Acad. Sci. U.S.A. 93:15294-15298(1996).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 149-575, AND CHROMOSOMAL
TRANSLOCATION WITH PRCC.
TISSUE=Monocyte;
PubMed=8872474; DOI=10.1093/hmg/5.9.1333;
Sidhar S.K., Clark J., Gill S., Hamoudi R., Crew A.J., Gwilliam R.,
Ross M., Linehan W.M., Birdsall S., Shipley J., Cooper C.S.;
"The t(X;1)(p11.2;q21.2) translocation in papillary renal cell
carcinoma fuses a novel gene PRCC to the TFE3 transcription factor
gene.";
Hum. Mol. Genet. 5:1333-1338(1996).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 212-575 (ISOFORM 1).
TISSUE=Leukemia;
PubMed=2338243; DOI=10.1101/gad.4.2.167;
Beckmann H., Su L.-K., Kadesch T.;
"TFE3: a helix-loop-helix protein that activates transcription through
the immunoglobulin enhancer muE3 motif.";
Genes Dev. 4:167-179(1990).
[8]
CHROMOSOMAL TRANSLOCATION WITH ASPSCR1.
PubMed=11358836;
Heimann P., El Housni H., Ogur G., Weterman M.A.J., Petty E.M.,
Vassart G.;
"Fusion of a novel gene, RCC17, to the TFE3 gene in
t(X;17)(p11.2;q25.3)-bearing papillary renal cell carcinomas.";
Cancer Res. 61:4130-4135(2001).
[9]
CHROMOSOMAL TRANSLOCATION WITH ASPSCR1, AND INVOLVEMENT IN ASPS.
PubMed=11244503; DOI=10.1038/sj.onc.1204074;
Ladanyi M., Lui M.Y., Antonescu C.R., Krause-Boehm A., Meindl A.,
Argani P., Healey J.H., Ueda T., Yoshikawa H., Meloni-Ehrig A.,
Sorensen P.H.B., Mertens F., Mandahl N., van den Berghe H., Sciot R.,
Dal Cin P., Bridge J.;
"The der(17)t(X;17)(p11;q25) of human alveolar soft part sarcoma fuses
the TFE3 transcription factor gene to ASPL, a novel gene at 17q25.";
Oncogene 20:48-57(2001).
[10]
SUMOYLATION, AND INTERACTION WITH MITF.
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).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-548; SER-556 AND
SER-560, 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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-556 AND SER-568, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-548; SER-556 AND
SER-560, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and 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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-542 AND SER-548, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-339, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Transcription factor that specifically recognizes and
binds E-box sequences (5'-CANNTG-3'). Efficient DNA-binding
requires dimerization with itself or with another MiT/TFE family
member such as TFEB or MITF. In association with TFEB, activates
the expression of CD40L in T-cells, thereby playing a role in T-
cell-dependent antibody responses in activated CD4(+) T-cells and
thymus-dependent humoral immunity. Specifically recognizes the
MUE3 box, a subset of E-boxes, present in the immunoglobulin
enhancer. It also binds very well to a USF/MLTF site.
-!- SUBUNIT: Homodimer and heterodimer; with TFEB or MITF.
-!- INTERACTION:
O15397:IPO8; NbExp=2; IntAct=EBI-1048957, EBI-358808;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P19532-1; Sequence=Displayed;
Name=2;
IsoId=P19532-2; Sequence=VSP_056882, VSP_056883;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous in fetal and adult tissues.
-!- PTM: Sumoylated; does not affect dimerization with MITF.
{ECO:0000269|PubMed:15507434}.
-!- DISEASE: Note=A chromosomal aberration involving TFE3 is found in
patients with alveolar soft part sarcoma. Translocation
t(X;17)(p11;q25) with ASPSCR1 forms a ASPSCR1-TFE3 fusion protein.
{ECO:0000269|PubMed:11358836}.
-!- DISEASE: Note=Chromosomal aberrations involving TFE3 are found in
patients with papillary renal cell carcinoma. Translocation
t(X;1)(p11.2;q21.2) with PRCC; translocation t(X;1)(p11.2;p34)
with PSF; inversion inv(X)(p11.2;q12) that fuses NONO to TFE3.
{ECO:0000269|PubMed:8872474, ECO:0000269|PubMed:8986805}.
-!- SIMILARITY: Belongs to the MiT/TFE family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA35714.1; Type=Frameshift; Positions=557; Evidence={ECO:0000305};
Sequence=CAA65800.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/TFE3ID86.html";
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EMBL; X96717; CAA65478.1; -; mRNA.
EMBL; AL161985; CAI46207.1; -; mRNA.
EMBL; AC146820; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF196779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BX572102; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X99721; CAA68061.1; -; Genomic_DNA.
EMBL; X97160; CAA65800.1; ALT_SEQ; Genomic_DNA.
EMBL; X97161; CAA65800.1; JOINED; Genomic_DNA.
EMBL; X97162; CAA65800.1; JOINED; Genomic_DNA.
EMBL; X51330; CAA35714.1; ALT_SEQ; mRNA.
CCDS; CCDS14315.3; -. [P19532-1]
PIR; A34596; A34596.
RefSeq; NP_001269071.1; NM_001282142.1.
RefSeq; NP_006512.2; NM_006521.5. [P19532-1]
UniGene; Hs.730740; -.
ProteinModelPortal; P19532; -.
SMR; P19532; -.
BioGrid; 112888; 24.
DIP; DIP-50187N; -.
IntAct; P19532; 7.
STRING; 9606.ENSP00000314129; -.
iPTMnet; P19532; -.
PhosphoSitePlus; P19532; -.
DMDM; 160113240; -.
EPD; P19532; -.
MaxQB; P19532; -.
PaxDb; P19532; -.
PeptideAtlas; P19532; -.
PRIDE; P19532; -.
DNASU; 7030; -.
Ensembl; ENST00000315869; ENSP00000314129; ENSG00000068323. [P19532-1]
Ensembl; ENST00000493583; ENSP00000476976; ENSG00000068323. [P19532-2]
GeneID; 7030; -.
KEGG; hsa:7030; -.
UCSC; uc004dmb.5; human. [P19532-1]
CTD; 7030; -.
DisGeNET; 7030; -.
EuPathDB; HostDB:ENSG00000068323.16; -.
GeneCards; TFE3; -.
HGNC; HGNC:11752; TFE3.
HPA; HPA023881; -.
MalaCards; TFE3; -.
MIM; 314310; gene.
neXtProt; NX_P19532; -.
OpenTargets; ENSG00000068323; -.
Orphanet; 163699; Alveolar soft-tissue sarcoma.
Orphanet; 319308; Translocation renal cell carcinoma.
PharmGKB; PA36467; -.
eggNOG; KOG1318; Eukaryota.
eggNOG; ENOG410ZYYV; LUCA.
GeneTree; ENSGT00390000004402; -.
HOGENOM; HOG000231368; -.
HOVERGEN; HBG006768; -.
InParanoid; P19532; -.
KO; K09105; -.
OMA; PGTATFH; -.
OrthoDB; EOG091G0QCO; -.
PhylomeDB; P19532; -.
TreeFam; TF317174; -.
SIGNOR; P19532; -.
ChiTaRS; TFE3; human.
GeneWiki; TFE3; -.
GenomeRNAi; 7030; -.
PRO; PR:P19532; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000068323; -.
CleanEx; HS_TFE3; -.
ExpressionAtlas; P19532; baseline and differential.
Genevisible; P19532; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IMP: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; IEA:Ensembl.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISS:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IEA:Ensembl.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0006959; P:humoral immune response; ISS:UniProtKB.
GO; GO:0045785; P:positive regulation of cell adhesion; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:0045670; P:regulation of osteoclast differentiation; IEA:InterPro.
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; IPR024100; TFE3.
PANTHER; PTHR12565:SF163; PTHR12565:SF163; 1.
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;
Activator; Adaptive immunity; Alternative splicing;
Chromosomal rearrangement; Complete proteome; DNA-binding; Immunity;
Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Polymorphism;
Proto-oncogene; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 575 Transcription factor E3.
/FTId=PRO_0000127471.
DOMAIN 346 399 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
REGION 260 271 Strong transcription activation domain.
{ECO:0000255}.
REGION 409 430 Leucine-zipper.
SITE 178 179 Breakpoint for translocation to form
PRCC-TFE3 oncogene.
SITE 260 261 Breakpoint for translocation to form
ASPSCR1-TFE3 oncogene.
SITE 295 296 Breakpoint for translocation to form
NONO-TFE3, PSF-TFE3 and ASPSCR1-TFE3
oncogenes.
MOD_RES 188 188 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q64092}.
MOD_RES 542 542 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 548 548 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 554 554 Phosphoserine.
{ECO:0000250|UniProtKB:Q64092}.
MOD_RES 556 556 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 560 560 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 568 568 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
CROSSLNK 339 339 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 77 109 SLPISLQATPATPATLSASSSAGGSRTPAMSSS -> RGLQ
DPCHVVIFFIEGLAAAAANAGPGAGAGEA (in isoform
2). {ECO:0000303|PubMed:17974005}.
/FTId=VSP_056882.
VAR_SEQ 110 575 Missing (in isoform 2).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_056883.
VARIANT 96 96 S -> C (in dbSNP:rs5953258).
/FTId=VAR_027501.
VARIANT 313 313 T -> A (in dbSNP:rs3027470).
/FTId=VAR_027502.
CONFLICT 172 172 V -> M (in Ref. 6; CAA65800).
{ECO:0000305}.
CONFLICT 219 219 P -> S (in Ref. 6; CAA65800).
{ECO:0000305}.
CONFLICT 222 222 P -> K (in Ref. 7; CAA35714).
{ECO:0000305}.
CONFLICT 229 229 P -> L (in Ref. 6; CAA65800).
{ECO:0000305}.
CONFLICT 443 443 P -> G (in Ref. 7; CAA35714).
{ECO:0000305}.
CONFLICT 455 455 A -> T (in Ref. 6; CAA65800 and 7;
CAA35714). {ECO:0000305}.
CONFLICT 475 475 A -> R (in Ref. 7; CAA35714).
{ECO:0000305}.
CONFLICT 575 575 S -> M (in Ref. 6; CAA65800).
{ECO:0000305}.
SEQUENCE 575 AA; 61521 MW; EF1F11AB624C6BE1 CRC64;
MSHAAEPARD GVEASAEGPR AVFVLLEERR PADSAQLLSL NSLLPESGIV ADIELENVLD
PDSFYELKSQ PLPLRSSLPI SLQATPATPA TLSASSSAGG SRTPAMSSSS SSRVLLRQQL
MRAQAQEQER RERREQAAAA PFPSPAPASP AISVVGVSAG GHTLSRPPPA QVPREVLKVQ
THLENPTRYH LQQARRQQVK QYLSTTLGPK LASQALTPPP GPASAQPLPA PEAAHTTGPT
GSAPNSPMAL LTIGSSSEKE IDDVIDEIIS LESSYNDEML SYLPGGTTGL QLPSTLPVSG
NLLDVYSSQG VATPAITVSN SCPAELPNIK REISETEAKA LLKERQKKDN HNLIERRRRF
NINDRIKELG TLIPKSSDPE MRWNKGTILK ASVDYIRKLQ KEQQRSKDLE SRQRSLEQAN
RSLQLRIQEL ELQAQIHGLP VPPTPGLLSL ATTSASDSLK PEQLDIEEEG RPGAATFHVG
GGPAQNAPHQ QPPAPPSDAL LDLHFPSDHL GDLGDPFHLG LEDILMEEEE GVVGGLSGGA
LSPLRAASDP LLSSVSPAVS KASSRRSSFS MEEES


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EIAAB42108 bHLHe33,BHLHE33,Class E basic helix-loop-helix protein 33,Homo sapiens,Human,TFE3,Transcription factor E3
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
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
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
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 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
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 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
EIAAB41704 bHLHa24,BHLHA24,Class A basic helix-loop-helix protein 24,Homo sapiens,Human,TCF23,TCF-23,Transcription factor 23
EIAAB42109 bHLHe35,BHLHE35,Class E basic helix-loop-helix protein 35,Homo sapiens,Human,TFEB,Transcription factor EB
EIAAB24839 bHLHe32,BHLHE32,Class E basic helix-loop-helix protein 32,Homo sapiens,Human,Microphthalmia-associated transcription factor,MITF
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


 

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