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Q9H3M7

- TXNIP_HUMAN

UniProt

Q9H3M7 - TXNIP_HUMAN

Protein

Thioredoxin-interacting protein

Gene

TXNIP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    3. 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

    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

    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

    ArrayExpressiQ9H3M7.
    BgeeiQ9H3M7.
    CleanExiHS_TXNIP.
    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. 13 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 – 169
    Beta strandi20 – 223
    Beta strandi26 – 349
    Beta strandi39 – 413
    Beta strandi43 – 5816
    Beta strandi61 – 7616
    Beta strandi79 – 813
    Beta strandi89 – 913
    Beta strandi93 – 953
    Beta strandi97 – 1048
    Beta strandi111 – 1144
    Beta strandi116 – 13015
    Beta strandi137 – 1426
    Beta strandi144 – 1463
    Beta strandi148 – 1503
    Beta strandi160 – 1678
    Beta strandi177 – 1859
    Beta strandi187 – 1904
    Beta strandi194 – 20310
    Beta strandi205 – 2073
    Beta strandi209 – 22315
    Beta strandi226 – 23813
    Beta strandi246 – 25611
    Beta strandi269 – 28113
    Beta strandi288 – 29811

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MVMFKKIKSF EVVFNDPEKV YGSGEKVAGR VIVEVCEVTR VKAVRILACG    50
    VAKVLWMQGS QQCKQTSEYL RYEDTLLLED QPTGENEMVI MRPGNKYEYK 100
    FGFELPQGPL GTSFKGKYGC VDYWVKAFLD RPSQPTQETK KNFEVVDLVD 150
    VNTPDLMAPV SAKKEKKVSC MFIPDGRVSV SARIDRKGFC EGDEISIHAD 200
    FENTCSRIVV PKAAIVARHT YLANGQTKVL TQKLSSVRGN HIISGTCASW 250
    RGKSLRVQKI RPSILGCNIL RVEYSLLIYV SVPGSKKVIL DLPLVIGSRS 300
    GLSSRTSSMA SRTSSEMSWV DLNIPDTPEA PPCYMDVIPE DHRLESPTTP 350
    LLDDMDGSQD SPIFMYAPEF KFMPPPTYTE VDPCILNNNV Q 391
    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:
    EMBL
    GenBank
    DDBJ
    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.
    CCDSiCCDS913.1. [Q9H3M7-1]
    RefSeqiNP_006463.3. NM_006472.4. [Q9H3M7-1]
    UniGeneiHs.533977.
    Hs.709057.

    Genome annotation databases

    EnsembliENST00000582401; 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:
    EMBL
    GenBank
    DDBJ
    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 CCDS913.1. [Q9H3M7-1 ]
    RefSeqi NP_006463.3. NM_006472.4. [Q9H3M7-1 ]
    UniGenei Hs.533977.
    Hs.709057.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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. 13 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 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.
    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

    ArrayExpressi Q9H3M7.
    Bgeei Q9H3M7.
    CleanExi HS_TXNIP.
    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

    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: October 1, 2014
    This is version 104 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

    Dasty 3