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Thioredoxin-interacting protein (Thioredoxin-binding protein 2) (Vitamin D3 up-regulated protein 1)

 TXNIP_HUMAN             Reviewed;         391 AA.
Q9H3M7; B4E3D3; Q16226; Q6PML0; Q9BXG9;
03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
30-AUG-2017, entry version 131.
RecName: Full=Thioredoxin-interacting protein;
AltName: Full=Thioredoxin-binding protein 2;
AltName: Full=Vitamin D3 up-regulated protein 1;
Name=TXNIP; Synonyms=VDUP1;
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 INDUCTION.
PubMed=8086474; DOI=10.1016/0167-4781(94)90242-9;
Chen K.-S., DeLuca H.F.;
"Isolation and characterization of a novel cDNA from HL-60 cells
treated with 1,25-dihydroxyvitamin D-3.";
Biochim. Biophys. Acta 1219:26-32(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH
TXN, AND INDUCTION.
TISSUE=Lens;
PubMed=17603038; DOI=10.1016/j.exer.2007.05.001;
Liyanage N.P.M., Fernando M.R., Lou M.F.;
"Regulation of the bioavailability of thioredoxin in the lens by a
specific thioredoxin-binding protein (TBP-2).";
Exp. Eye Res. 85:270-279(2007).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Toyama S.;
"Homo sapiens VDUP1 gene.";
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Uterus;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-38.
Park J.B.;
"Cloning and characterization of human VDUP1 gene.";
Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
[8]
FUNCTION, INDUCTION, AND INTERACTION WITH ZBTB16; ZBTB32 AND HDAC1.
PubMed=12821938; DOI=10.1038/sj.onc.1206610;
Han S.H., Jeon J.H., Ju H.R., Jung U., Kim K.Y., Yoo H.S., Lee Y.H.,
Song K.S., Hwang H.M., Na Y.S., Yang Y., Lee K.N., Choi I.;
"VDUP1 upregulated by TGF-beta1 and 1,25-dihydorxyvitamin D3 inhibits
tumor cell growth by blocking cell-cycle progression.";
Oncogene 22:4035-4046(2003).
[9]
FUNCTION.
PubMed=18541147; DOI=10.1016/j.bbrc.2008.05.175;
Shin K.H., Kim R.H., Kim R.H., Kang M.K., Park N.H.;
"hnRNP G elicits tumor-suppressive activity in part by upregulating
the expression of Txnip.";
Biochem. Biophys. Res. Commun. 372:880-885(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361, 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).
[11]
INTERACTION WITH ITCH, AND UBIQUITINATION BY ITCH.
PubMed=20068034; DOI=10.1074/jbc.M109.063321;
Zhang P., Wang C., Gao K., Wang D., Mao J., An J., Xu C., Wu D.,
Yu H., Liu J.O., Yu L.;
"The ubiquitin ligase itch regulates apoptosis by targeting
thioredoxin-interacting protein for ubiquitin-dependent degradation.";
J. Biol. Chem. 285:8869-8879(2010).
[12]
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).
[13]
FUNCTION, AND INTERACTION WITH DDIT4.
PubMed=21460850; DOI=10.1038/onc.2011.102;
Jin H.O., Seo S.K., Kim Y.S., Woo S.H., Lee K.H., Yi J.Y., Lee S.J.,
Choe T.B., Lee J.H., An S., Hong S.I., Park I.C.;
"TXNIP potentiates Redd1-induced mTOR suppression through
stabilization of Redd1.";
Oncogene 30:3792-3801(2011).
[14]
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).
[15]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 2-149, SUBUNIT, AND
INTERCHAIN DISULFIDE BOND.
PubMed=23519408; DOI=10.1107/S0907444912047099;
Polekhina G., Ascher D.B., Kok S.F., Beckham S., Wilce M., Waltham M.;
"Structure of the N-terminal domain of human thioredoxin-interacting
protein.";
Acta Crystallogr. D 69:333-344(2013).
-!- FUNCTION: May act as an oxidative stress mediator by inhibiting
thioredoxin activity or by limiting its bioavailability. Interacts
with COPS5 and restores COPS5-induced suppression of CDKN1B
stability, blocking the COPS5-mediated translocation of CDKN1B
from the nucleus to the cytoplasm. Functions as a transcriptional
repressor, possibly by acting as a bridge molecule between
transcription factors and corepressor complexes, and over-
expression will induce G0/G1 cell cycle arrest. Required for the
maturation of natural killer cells. Acts as a suppressor of tumor
cell growth. Inhibits the proteasomal degradation of DDIT4, and
thereby contributes to the inhibition of the mammalian target of
rapamycin complex 1 (mTORC1). {ECO:0000269|PubMed:12821938,
ECO:0000269|PubMed:17603038, ECO:0000269|PubMed:18541147,
ECO:0000269|PubMed:21460850}.
-!- SUBUNIT: Homodimer; disulfide-linked. Interacts with
TXN/thioredoxin through its redox-active site. Interacts with
transcriptional repressors ZBTB16, ZBTB32 and HDAC1. Interacts
(via C-terminus) with ITCH (via WW domains). Interacts with DDIT4.
{ECO:0000269|PubMed:12821938, ECO:0000269|PubMed:17603038,
ECO:0000269|PubMed:20068034, ECO:0000269|PubMed:21460850,
ECO:0000269|PubMed:23519408}.
-!- INTERACTION:
O95905:ECD; NbExp=5; IntAct=EBI-1369170, EBI-2557598;
P10599:TXN; NbExp=4; IntAct=EBI-1369170, EBI-594644;
P52735:VAV2; NbExp=2; IntAct=EBI-1369170, EBI-297549;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9H3M7-1; Sequence=Displayed;
Name=2;
IsoId=Q9H3M7-2; Sequence=VSP_054401;
Note=No experimental confirmation available.;
-!- INDUCTION: By 1,25-dihydroxyvitamin D-3 and TGFB1. Down-regulated
in response to oxidative stress. {ECO:0000269|PubMed:12821938,
ECO:0000269|PubMed:17603038, ECO:0000269|PubMed:8086474}.
-!- PTM: Ubiquitinated; undergoes polyubiquitination catalyzed by ITCH
resulting in proteasomal degradation.
{ECO:0000269|PubMed:20068034}.
-!- SIMILARITY: Belongs to the arrestin family. {ECO:0000305}.
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EMBL; S73591; AAB31977.2; -; mRNA.
EMBL; AY594328; AAT01927.2; -; mRNA.
EMBL; AB051901; BAB18859.1; -; Genomic_DNA.
EMBL; AK304670; BAG65445.1; -; mRNA.
EMBL; AL138842; CAI22351.1; -; Genomic_DNA.
EMBL; AL160282; CAI22351.1; JOINED; Genomic_DNA.
EMBL; BC093702; AAH93702.1; -; mRNA.
EMBL; BC093704; AAH93704.1; -; mRNA.
EMBL; AF333001; AAK37514.1; -; Genomic_DNA.
CCDS; CCDS72876.1; -. [Q9H3M7-1]
CCDS; CCDS81368.1; -. [Q9H3M7-2]
RefSeq; NP_001300901.1; NM_001313972.1. [Q9H3M7-2]
RefSeq; NP_006463.3; NM_006472.5. [Q9H3M7-1]
UniGene; Hs.533977; -.
UniGene; Hs.709057; -.
PDB; 4GEI; X-ray; 1.50 A; A=2-149.
PDB; 4GEJ; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J=2-149.
PDB; 4GFX; X-ray; 1.60 A; A=4-154.
PDB; 4LL1; X-ray; 2.00 A; A/C=3-317.
PDB; 4LL4; X-ray; 2.70 A; A/C=3-317.
PDB; 4ROF; X-ray; 2.03 A; C/D=327-338.
PDB; 4ROJ; X-ray; 1.95 A; D/E/F=327-338.
PDB; 5CQ2; X-ray; 1.40 A; B/C=327-338.
PDB; 5DF6; X-ray; 1.78 A; B/C=371-382.
PDB; 5DWS; X-ray; 1.65 A; B/D/F/H=327-338.
PDB; 5DZD; X-ray; 1.57 A; C/D=327-338.
PDBsum; 4GEI; -.
PDBsum; 4GEJ; -.
PDBsum; 4GFX; -.
PDBsum; 4LL1; -.
PDBsum; 4LL4; -.
PDBsum; 4ROF; -.
PDBsum; 4ROJ; -.
PDBsum; 5CQ2; -.
PDBsum; 5DF6; -.
PDBsum; 5DWS; -.
PDBsum; 5DZD; -.
ProteinModelPortal; Q9H3M7; -.
SMR; Q9H3M7; -.
BioGrid; 115872; 43.
IntAct; Q9H3M7; 12.
MINT; MINT-1194670; -.
STRING; 9606.ENSP00000358323; -.
iPTMnet; Q9H3M7; -.
PhosphoSitePlus; Q9H3M7; -.
SwissPalm; Q9H3M7; -.
BioMuta; TXNIP; -.
DMDM; 74752618; -.
EPD; Q9H3M7; -.
MaxQB; Q9H3M7; -.
PaxDb; Q9H3M7; -.
PeptideAtlas; Q9H3M7; -.
PRIDE; Q9H3M7; -.
Ensembl; ENST00000425134; ENSP00000396322; ENSG00000265972. [Q9H3M7-2]
Ensembl; ENST00000582401; ENSP00000462521; ENSG00000265972. [Q9H3M7-1]
GeneID; 10628; -.
KEGG; hsa:10628; -.
UCSC; uc031utq.2; human. [Q9H3M7-1]
CTD; 10628; -.
DisGeNET; 10628; -.
GeneCards; TXNIP; -.
HGNC; HGNC:16952; TXNIP.
HPA; HPA031085; -.
HPA; HPA053694; -.
MIM; 606599; gene.
neXtProt; NX_Q9H3M7; -.
OpenTargets; ENSG00000265972; -.
PharmGKB; PA38194; -.
eggNOG; KOG3780; Eukaryota.
eggNOG; ENOG41102NY; LUCA.
GeneTree; ENSGT00550000074356; -.
HOGENOM; HOG000237328; -.
HOVERGEN; HBG066469; -.
InParanoid; Q9H3M7; -.
KO; K20910; -.
OMA; ISGMCDA; -.
OrthoDB; EOG091G0B0Y; -.
PhylomeDB; Q9H3M7; -.
TreeFam; TF313650; -.
Reactome; R-HSA-844456; The NLRP3 inflammasome.
ChiTaRS; TXNIP; human.
GeneWiki; TXNIP; -.
GenomeRNAi; 10628; -.
PRO; PR:Q9H3M7; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000265972; -.
CleanEx; HS_TXNIP; -.
ExpressionAtlas; Q9H3M7; baseline and differential.
Genevisible; Q9H3M7; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005758; C:mitochondrial intermembrane space; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0004857; F:enzyme inhibitor activity; IEA:Ensembl.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0071228; P:cellular response to tumor cell; IDA:UniProtKB.
GO; GO:0030216; P:keratinocyte differentiation; IDA:UniProtKB.
GO; GO:0051782; P:negative regulation of cell division; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
GO; GO:0006606; P:protein import into nucleus; IEA:Ensembl.
GO; GO:0042127; P:regulation of cell proliferation; IEA:Ensembl.
GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0009749; P:response to glucose; IEA:Ensembl.
GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
GO; GO:0032570; P:response to progesterone; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR011021; Arrestin-like_N.
InterPro; IPR011022; Arrestin_C-like.
InterPro; IPR014756; Ig_E-set.
Pfam; PF02752; Arrestin_C; 1.
Pfam; PF00339; Arrestin_N; 1.
SMART; SM01017; Arrestin_C; 1.
SUPFAM; SSF81296; SSF81296; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell cycle; Complete proteome;
Cytoplasm; Disulfide bond; Isopeptide bond; Phosphoprotein;
Polymorphism; Reference proteome; Transcription;
Transcription regulation; Tumor suppressor; Ubl conjugation.
CHAIN 1 391 Thioredoxin-interacting protein.
/FTId=PRO_0000250489.
MOD_RES 361 361 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
DISULFID 63 63 Interchain.
CROSSLNK 212 212 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:20068034}.
VAR_SEQ 1 83 MVMFKKIKSFEVVFNDPEKVYGSGEKVAGRVIVEVCEVTRV
KAVRILACGVAKVLWMQGSQQCKQTSEYLRYEDTLLLEDQP
T -> MPPKHSLSHRCILSVTASLMATRFSFPS (in
isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054401.
VARIANT 177 177 R -> Q (in dbSNP:rs6674773).
/FTId=VAR_048334.
CONFLICT 26 26 K -> R (in Ref. 1; AAB31977 and 2;
AAT01927). {ECO:0000305}.
STRAND 8 16 {ECO:0000244|PDB:4GEI}.
STRAND 20 22 {ECO:0000244|PDB:4GEI}.
STRAND 26 34 {ECO:0000244|PDB:4GEI}.
STRAND 39 41 {ECO:0000244|PDB:4GEI}.
STRAND 43 58 {ECO:0000244|PDB:4GEI}.
STRAND 61 76 {ECO:0000244|PDB:4GEI}.
STRAND 79 81 {ECO:0000244|PDB:4GEI}.
STRAND 83 85 {ECO:0000244|PDB:4GEJ}.
STRAND 89 91 {ECO:0000244|PDB:4GEI}.
STRAND 93 95 {ECO:0000244|PDB:4LL4}.
STRAND 97 104 {ECO:0000244|PDB:4GEI}.
STRAND 111 114 {ECO:0000244|PDB:4GFX}.
STRAND 116 130 {ECO:0000244|PDB:4GEI}.
STRAND 137 142 {ECO:0000244|PDB:4GEI}.
STRAND 144 146 {ECO:0000244|PDB:4GEI}.
STRAND 148 150 {ECO:0000244|PDB:4GFX}.
STRAND 160 167 {ECO:0000244|PDB:4LL1}.
STRAND 177 185 {ECO:0000244|PDB:4LL1}.
STRAND 187 190 {ECO:0000244|PDB:4LL1}.
STRAND 194 203 {ECO:0000244|PDB:4LL1}.
STRAND 205 207 {ECO:0000244|PDB:4LL1}.
STRAND 209 223 {ECO:0000244|PDB:4LL1}.
STRAND 226 238 {ECO:0000244|PDB:4LL1}.
STRAND 246 256 {ECO:0000244|PDB:4LL1}.
STRAND 269 281 {ECO:0000244|PDB:4LL1}.
STRAND 288 298 {ECO:0000244|PDB:4LL1}.
HELIX 334 337 {ECO:0000244|PDB:5CQ2}.
SEQUENCE 391 AA; 43661 MW; B0FE2D35D0B0735A CRC64;
MVMFKKIKSF EVVFNDPEKV YGSGEKVAGR VIVEVCEVTR VKAVRILACG VAKVLWMQGS
QQCKQTSEYL RYEDTLLLED QPTGENEMVI MRPGNKYEYK FGFELPQGPL GTSFKGKYGC
VDYWVKAFLD RPSQPTQETK KNFEVVDLVD VNTPDLMAPV SAKKEKKVSC MFIPDGRVSV
SARIDRKGFC EGDEISIHAD FENTCSRIVV PKAAIVARHT YLANGQTKVL TQKLSSVRGN
HIISGTCASW RGKSLRVQKI RPSILGCNIL RVEYSLLIYV SVPGSKKVIL DLPLVIGSRS
GLSSRTSSMA SRTSSEMSWV DLNIPDTPEA PPCYMDVIPE DHRLESPTTP LLDDMDGSQD
SPIFMYAPEF KFMPPPTYTE VDPCILNNNV Q


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E1162h ELISA Homo sapiens,Human,Thioredoxin-binding protein 2,Thioredoxin-interacting protein,TXNIP,VDUP1,Vitamin D3 up-regulated protein 1 96T
U1162h CLIA Homo sapiens,Human,Thioredoxin-binding protein 2,Thioredoxin-interacting protein,TXNIP,VDUP1,Vitamin D3 up-regulated protein 1 96T
U1162m CLIA Mouse,Mus musculus,Thioredoxin-interacting protein,Txnip,Vdup1,Vitamin D3 up-regulated protein 1 96T
U1162r CLIA Rat,Rattus norvegicus,Thioredoxin-interacting protein,Txnip,Vdup1,Vitamin D3 up-regulated protein 1 96T
E1162m ELISA Mouse,Mus musculus,Thioredoxin-interacting protein,Txnip,Vdup1,Vitamin D3 up-regulated protein 1 96T
E1162r ELISA Rat,Rattus norvegicus,Thioredoxin-interacting protein,Txnip,Vdup1,Vitamin D3 up-regulated protein 1 96T
E1162m ELISA kit Mouse,Mus musculus,Thioredoxin-interacting protein,Txnip,Vdup1,Vitamin D3 up-regulated protein 1 96T
E1162r ELISA kit Rat,Rattus norvegicus,Thioredoxin-interacting protein,Txnip,Vdup1,Vitamin D3 up-regulated protein 1 96T
E2135Hu Human Thioredoxin-binding protein 2 per Thioredoxin-interacting protein,TBP-2 per TXNIP ELISA kit 48T
E2135Hu Human Thioredoxin-binding protein 2 per Thioredoxin-interacting protein,TBP-2 per TXNIP ELISA kit 96T
E2135Hu Human Thioredoxin-binding protein 2-Thioredoxin-interacting protein,TBP-2-TXNIP ELISA kit 48T
E2135Hu Human Thioredoxin-binding protein 2-Thioredoxin-interacting protein,TBP-2-TXNIP ELISA kit 96T
UB-E21445 Mouse Thioredoxin-binding protein 2 per Thioredoxin-interacting protein(TBP-2 per TXNIP)ELISA Kit 96T
YHB2956Hu Human Thioredoxin-binding protein 2-Thioredoxin-interacting protein,TBP-2-TXNIP ELISA kit 96T
YHB2956Hu Human Thioredoxin-binding protein 2-Thioredoxin-interacting protein,TBP-2-TXNIP ELISA kit 48T
UB-E02230 Human Thioredoxin-binding protein 2 per Thioredoxin-interacting protein(TBP-2 per TXNIP)ELISA Kit 96T
UB-E10464 Rat Thioredoxin-binding protein 2 per Thioredoxin-interacting protein(TBP-2 per TXNIP)ELISA Kit 96T
15-288-22250 Thioredoxin-like protein 2 - PKC-interacting cousin of thioredoxin; PKC-theta-interacting protein; PKCq-interacting protein Polyclonal 0.1 mg
15-288-22250 Thioredoxin-like protein 2 - PKC-interacting cousin of thioredoxin; PKC-theta-interacting protein; PKCq-interacting protein Polyclonal 0.05 mg
EIAAB44637 Endoplasmic reticulum resident protein 46,ER protein 46,ERp46,Mouse,Mus musculus,PC-TRP,Plasma cell-specific thioredoxin-related protein,Thioredoxin domain-containing protein 5,Thioredoxin-like protei
EIAAB44613 14 kDa thioredoxin-related protein,Homo sapiens,Human,Protein 42-9-9,Thioredoxin domain-containing protein 17,Thioredoxin-like protein 5,TRP14,TXNDC17,TXNL5
10-288-22250F Thioredoxin-like protein 2 - PKC-interacting cousin of thioredoxin; PKC-theta-interacting protein; PKCq-interacting protein 0.05 mg
10-288-22250F Thioredoxin-like protein 2 - PKC-interacting cousin of thioredoxin; PKC-theta-interacting protein; PKCq-interacting protein 0.1 mg
EIAAB44614 14 kDa thioredoxin-related protein,Mouse,Mus musculus,Protein 42-9-9,Thioredoxin domain-containing protein 17,Thioredoxin-like protein 5,TRP14,Txndc17,Txnl5


 

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