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Q9H3M7

- TXNIP_HUMAN

UniProt

Q9H3M7 - TXNIP_HUMAN

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Protein

Thioredoxin-interacting protein

Gene

TXNIP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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).4 Publications

GO - Molecular functioni

  1. enzyme inhibitor activity Source: Ensembl
  2. ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cellular response to tumor cell Source: UniProtKB
  3. innate immune response Source: Reactome
  4. keratinocyte differentiation Source: UniProtKB
  5. negative regulation of cell division Source: UniProtKB
  6. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  7. nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway Source: Reactome
  8. platelet-derived growth factor receptor signaling pathway Source: Ensembl
  9. positive regulation of apoptotic process Source: Ensembl
  10. protein import into nucleus Source: Ensembl
  11. regulation of cell proliferation Source: Ensembl
  12. response to calcium ion Source: Ensembl
  13. response to drug Source: Ensembl
  14. response to estradiol Source: Ensembl
  15. response to glucose Source: Ensembl
  16. response to hydrogen peroxide Source: Ensembl
  17. response to mechanical stimulus Source: Ensembl
  18. response to progesterone Source: Ensembl
  19. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_75808. The NLRP3 inflammasome.

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin-interacting protein
Alternative name(s):
Thioredoxin-binding protein 2
Vitamin D3 up-regulated protein 1
Gene namesi
Name:TXNIP
Synonyms:VDUP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:16952. TXNIP.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. mitochondrial intermembrane space Source: Ensembl
  4. nucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

PharmGKBiPA38194.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 391391Thioredoxin-interacting proteinPRO_0000250489Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi63 – 63Interchain
Cross-linki212 – 212Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei361 – 3611Phosphoserine1 Publication

Post-translational modificationi

Ubiquitinated; undergoes polyubiquitination catalyzed by ITCH resulting in proteasomal degradation.1 Publication

Keywords - PTMi

Disulfide bond, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9H3M7.
PaxDbiQ9H3M7.
PRIDEiQ9H3M7.

PTM databases

PhosphoSiteiQ9H3M7.

Expressioni

Inductioni

By 1,25-dihydroxyvitamin D-3 and TGFB1. Down-regulated in response to oxidative stress.3 Publications

Gene expression databases

BgeeiQ9H3M7.
CleanExiHS_TXNIP.
ExpressionAtlasiQ9H3M7. differential.
GenevestigatoriQ9H3M7.

Organism-specific databases

HPAiCAB013291.
HPA031085.

Interactioni

Subunit structurei

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 DDIT4.5 Publications

Protein-protein interaction databases

BioGridi115872. 15 interactions.
IntActiQ9H3M7. 7 interactions.
MINTiMINT-1194670.
STRINGi9606.ENSP00000358323.

Structurei

Secondary structure

1
391
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 169Combined sources
Beta strandi20 – 223Combined sources
Beta strandi26 – 349Combined sources
Beta strandi39 – 413Combined sources
Beta strandi43 – 5816Combined sources
Beta strandi61 – 7616Combined sources
Beta strandi79 – 813Combined sources
Beta strandi89 – 913Combined sources
Beta strandi93 – 953Combined sources
Beta strandi97 – 1048Combined sources
Beta strandi111 – 1144Combined sources
Beta strandi116 – 13015Combined sources
Beta strandi137 – 1426Combined sources
Beta strandi144 – 1463Combined sources
Beta strandi148 – 1503Combined sources
Beta strandi160 – 1678Combined sources
Beta strandi177 – 1859Combined sources
Beta strandi187 – 1904Combined sources
Beta strandi194 – 20310Combined sources
Beta strandi205 – 2073Combined sources
Beta strandi209 – 22315Combined sources
Beta strandi226 – 23813Combined sources
Beta strandi246 – 25611Combined sources
Beta strandi269 – 28113Combined sources
Beta strandi288 – 29811Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GEIX-ray1.50A2-149[»]
4GEJX-ray2.90A/B/C/D/E/F/G/H/I/J2-149[»]
4GFXX-ray1.60A4-154[»]
4LL1X-ray2.00A/C3-317[»]
4LL4X-ray2.70A/C3-317[»]
ProteinModelPortaliQ9H3M7.
SMRiQ9H3M7. Positions 7-299.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the arrestin family.Curated

Phylogenomic databases

eggNOGiNOG325116.
GeneTreeiENSGT00550000074356.
HOGENOMiHOG000237328.
HOVERGENiHBG066469.
InParanoidiQ9H3M7.
OMAiSILGCNI.
OrthoDBiEOG7P02HT.
PhylomeDBiQ9H3M7.
TreeFamiTF313650.

Family and domain databases

InterProiIPR011021. Arrestin-like_N.
IPR011022. Arrestin_C-like.
IPR014756. Ig_E-set.
[Graphical view]
PfamiPF02752. Arrestin_C. 1 hit.
PF00339. Arrestin_N. 1 hit.
[Graphical view]
SMARTiSM01017. Arrestin_C. 1 hit.
[Graphical view]
SUPFAMiSSF81296. SSF81296. 2 hits.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9H3M7-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVMFKKIKSF EVVFNDPEKV YGSGEKVAGR VIVEVCEVTR VKAVRILACG
60 70 80 90 100
VAKVLWMQGS QQCKQTSEYL RYEDTLLLED QPTGENEMVI MRPGNKYEYK
110 120 130 140 150
FGFELPQGPL GTSFKGKYGC VDYWVKAFLD RPSQPTQETK KNFEVVDLVD
160 170 180 190 200
VNTPDLMAPV SAKKEKKVSC MFIPDGRVSV SARIDRKGFC EGDEISIHAD
210 220 230 240 250
FENTCSRIVV PKAAIVARHT YLANGQTKVL TQKLSSVRGN HIISGTCASW
260 270 280 290 300
RGKSLRVQKI RPSILGCNIL RVEYSLLIYV SVPGSKKVIL DLPLVIGSRS
310 320 330 340 350
GLSSRTSSMA SRTSSEMSWV DLNIPDTPEA PPCYMDVIPE DHRLESPTTP
360 370 380 390
LLDDMDGSQD SPIFMYAPEF KFMPPPTYTE VDPCILNNNV Q
Length:391
Mass (Da):43,661
Last modified:March 1, 2001 - v1
Checksum:iB0FE2D35D0B0735A
GO
Isoform 2 (identifier: Q9H3M7-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-83: MVMFKKIKSF...DTLLLEDQPT → MPPKHSLSHRCILSVTASLMATRFSFPS

Note: No experimental confirmation available.

Show »
Length:336
Mass (Da):37,319
Checksum:iB93B9E573BEE0996
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti26 – 261K → R in AAB31977. (PubMed:8086474)Curated
Sequence conflicti26 – 261K → R in AAT01927. (PubMed:17603038)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti177 – 1771R → Q.
Corresponds to variant rs6674773 [ dbSNP | Ensembl ].
VAR_048334

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8383MVMFK…EDQPT → MPPKHSLSHRCILSVTASLM ATRFSFPS in isoform 2. 1 PublicationVSP_054401Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S73591 mRNA. Translation: AAB31977.2.
AY594328 mRNA. Translation: AAT01927.2.
AB051901 Genomic DNA. Translation: BAB18859.1.
AK304670 mRNA. Translation: BAG65445.1.
AL138842, AL160282 Genomic DNA. Translation: CAI22351.1.
BC093702 mRNA. Translation: AAH93702.1.
BC093704 mRNA. Translation: AAH93704.1.
AF333001 Genomic DNA. Translation: AAK37514.1.
CCDSiCCDS72876.1. [Q9H3M7-1]
RefSeqiNP_006463.3. NM_006472.4. [Q9H3M7-1]
UniGeneiHs.533977.
Hs.709057.

Genome annotation databases

EnsembliENST00000425134; ENSP00000396322; ENSG00000265972. [Q9H3M7-2]
ENST00000582401; ENSP00000462521; ENSG00000265972. [Q9H3M7-1]
GeneIDi10628.
KEGGihsa:10628.
UCSCiuc001enn.4. human. [Q9H3M7-1]

Polymorphism databases

DMDMi74752618.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S73591 mRNA. Translation: AAB31977.2 .
AY594328 mRNA. Translation: AAT01927.2 .
AB051901 Genomic DNA. Translation: BAB18859.1 .
AK304670 mRNA. Translation: BAG65445.1 .
AL138842 , AL160282 Genomic DNA. Translation: CAI22351.1 .
BC093702 mRNA. Translation: AAH93702.1 .
BC093704 mRNA. Translation: AAH93704.1 .
AF333001 Genomic DNA. Translation: AAK37514.1 .
CCDSi CCDS72876.1. [Q9H3M7-1 ]
RefSeqi NP_006463.3. NM_006472.4. [Q9H3M7-1 ]
UniGenei Hs.533977.
Hs.709057.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4GEI X-ray 1.50 A 2-149 [» ]
4GEJ X-ray 2.90 A/B/C/D/E/F/G/H/I/J 2-149 [» ]
4GFX X-ray 1.60 A 4-154 [» ]
4LL1 X-ray 2.00 A/C 3-317 [» ]
4LL4 X-ray 2.70 A/C 3-317 [» ]
ProteinModelPortali Q9H3M7.
SMRi Q9H3M7. Positions 7-299.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115872. 15 interactions.
IntActi Q9H3M7. 7 interactions.
MINTi MINT-1194670.
STRINGi 9606.ENSP00000358323.

PTM databases

PhosphoSitei Q9H3M7.

Polymorphism databases

DMDMi 74752618.

Proteomic databases

MaxQBi Q9H3M7.
PaxDbi Q9H3M7.
PRIDEi Q9H3M7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000425134 ; ENSP00000396322 ; ENSG00000265972 . [Q9H3M7-2 ]
ENST00000582401 ; ENSP00000462521 ; ENSG00000265972 . [Q9H3M7-1 ]
GeneIDi 10628.
KEGGi hsa:10628.
UCSCi uc001enn.4. human. [Q9H3M7-1 ]

Organism-specific databases

CTDi 10628.
GeneCardsi GC01P145438.
HGNCi HGNC:16952. TXNIP.
HPAi CAB013291.
HPA031085.
MIMi 606599. gene.
neXtProti NX_Q9H3M7.
PharmGKBi PA38194.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG325116.
GeneTreei ENSGT00550000074356.
HOGENOMi HOG000237328.
HOVERGENi HBG066469.
InParanoidi Q9H3M7.
OMAi SILGCNI.
OrthoDBi EOG7P02HT.
PhylomeDBi Q9H3M7.
TreeFami TF313650.

Enzyme and pathway databases

Reactomei REACT_75808. The NLRP3 inflammasome.

Miscellaneous databases

ChiTaRSi TXNIP. human.
GeneWikii TXNIP.
GenomeRNAii 10628.
NextBioi 35477508.
PROi Q9H3M7.
SOURCEi Search...

Gene expression databases

Bgeei Q9H3M7.
CleanExi HS_TXNIP.
ExpressionAtlasi Q9H3M7. differential.
Genevestigatori Q9H3M7.

Family and domain databases

InterProi IPR011021. Arrestin-like_N.
IPR011022. Arrestin_C-like.
IPR014756. Ig_E-set.
[Graphical view ]
Pfami PF02752. Arrestin_C. 1 hit.
PF00339. Arrestin_N. 1 hit.
[Graphical view ]
SMARTi SM01017. Arrestin_C. 1 hit.
[Graphical view ]
SUPFAMi SSF81296. SSF81296. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of a novel cDNA from HL-60 cells treated with 1,25-dihydroxyvitamin D-3."
    Chen K.-S., DeLuca H.F.
    Biochim. Biophys. Acta 1219:26-32(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION.
  2. "Regulation of the bioavailability of thioredoxin in the lens by a specific thioredoxin-binding protein (TBP-2)."
    Liyanage N.P.M., Fernando M.R., Lou M.F.
    Exp. Eye Res. 85:270-279(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH TXN, INDUCTION.
    Tissue: Lens.
  3. "Homo sapiens VDUP1 gene."
    Toyama S.
    Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Uterus.
  5. "The DNA sequence and biological annotation of human chromosome 1."
    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.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  7. "Cloning and characterization of human VDUP1 gene."
    Park J.B.
    Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-38.
  8. "VDUP1 upregulated by TGF-beta1 and 1,25-dihydorxyvitamin D3 inhibits tumor cell growth by blocking cell-cycle progression."
    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.
    Oncogene 22:4035-4046(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION, INTERACTION WITH ZBTB16; ZBTB32 AND HDAC1.
  9. "hnRNP G elicits tumor-suppressive activity in part by upregulating the expression of Txnip."
    Shin K.H., Kim R.H., Kim R.H., Kang M.K., Park N.H.
    Biochem. Biophys. Res. Commun. 372:880-885(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "The ubiquitin ligase itch regulates apoptosis by targeting thioredoxin-interacting protein for ubiquitin-dependent degradation."
    Zhang P., Wang C., Gao K., Wang D., Mao J., An J., Xu C., Wu D., Yu H., Liu J.O., Yu L.
    J. Biol. Chem. 285:8869-8879(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ITCH, UBIQUITINATION BY ITCH.
  12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    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.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "TXNIP potentiates Redd1-induced mTOR suppression through stabilization of Redd1."
    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.
    Oncogene 30:3792-3801(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DDIT4.
  14. "Structure of the N-terminal domain of human thioredoxin-interacting protein."
    Polekhina G., Ascher D.B., Kok S.F., Beckham S., Wilce M., Waltham M.
    Acta Crystallogr. D 69:333-344(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 2-149, SUBUNIT, INTERCHAIN DISULFIDE BOND.

Entry informationi

Entry nameiTXNIP_HUMAN
AccessioniPrimary (citable) accession number: Q9H3M7
Secondary accession number(s): B4E3D3
, Q16226, Q6PML0, Q9BXG9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: March 1, 2001
Last modified: November 26, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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