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Reviewed, UniProtKB/Swiss-Prot Q9H3M7 (TXNIP_HUMAN)

Last modified November 24, 2009. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Thioredoxin-interacting protein
Alternative name(s):
    Vitamin D3 up-regulated protein 1
    Thioredoxin-binding protein 2
Gene names
Name: TXNIP
Synonyms: VDUP1
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length391 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

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. Ref.2 Ref.7

Subunit structure

Interacts with TXN/thioredoxin through its redox-active site. Interacts with transcriptional repressors ZBTB16, ZBTB32 and HDAC1. Ref.2 Ref.7

Subcellular location

Cytoplasm By similarity.

Induction

By 1,25-dihydroxyvitamin D-3 and TGFB1. Down-regulated in response to oxidative stress. Ref.2 Ref.7 Ref.1

Sequence similarities

Belongs to the arrestin family.

Ontologies

Keywords
   Biological processCell cycle
Transcription
Transcription regulation
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

keratinocyte differentiation

Inferred from direct assay. Source: UniProtKB

regulation of transcription

Inferred from electronic annotation. Source: UniProtKB-KW

transcription

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionprotein binding

Inferred from physical interaction. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TXNP105992EBI-1369170,EBI-594644

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 391391Thioredoxin-interacting protein
PRO_0000250489

Amino acid modifications

Modified residue3491Phosphothreonine Ref.9
Modified residue3611Phosphoserine Ref.9
Cross-link212Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.8

Natural variations

Natural variant1771R → Q: dbSNP rs6674773.
VAR_048334

Experimental info

Sequence conflict261K → R in AAB31977. Ref.1
Sequence conflict261K → R in AAT01927. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9H3M7-1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: B0FE2D35D0B0735A

FASTA39143,661
        10         20         30         40         50         60 
MVMFKKIKSF EVVFNDPEKV YGSGEKVAGR VIVEVCEVTR VKAVRILACG VAKVLWMQGS 

        70         80         90        100        110        120 
QQCKQTSEYL RYEDTLLLED QPTGENEMVI MRPGNKYEYK FGFELPQGPL GTSFKGKYGC 

       130        140        150        160        170        180 
VDYWVKAFLD RPSQPTQETK KNFEVVDLVD VNTPDLMAPV SAKKEKKVSC MFIPDGRVSV 

       190        200        210        220        230        240 
SARIDRKGFC EGDEISIHAD FENTCSRIVV PKAAIVARHT YLANGQTKVL TQKLSSVRGN 

       250        260        270        280        290        300 
HIISGTCASW RGKSLRVQKI RPSILGCNIL RVEYSLLIYV SVPGSKKVIL DLPLVIGSRS 

       310        320        330        340        350        360 
GLSSRTSSMA SRTSSEMSWV DLNIPDTPEA PPCYMDVIPE DHRLESPTTP LLDDMDGSQD 

       370        380        390 
SPIFMYAPEF KFMPPPTYTE VDPCILNNNV Q 

« Hide

References

« Hide 'large scale' references
[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: 8086474] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], 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: 17603038] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], 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]"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. expand/collapse author list , 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: 16710414] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[6]"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.
[7]"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: 12821938] [Abstract]
Cited for: FUNCTION, INDUCTION, INTERACTION WITH ZBTB16; ZBTB32 AND HDAC1.
[8]"Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry."
Meierhofer D., Wang X., Huang L., Kaiser P.
J. Proteome Res. 7:4566-4576(2008) [PubMed: 18781797] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-212, MASS SPECTROMETRY.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-349 AND SER-361, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

S73591 mRNA. Translation: AAB31977.2.
AY594328 mRNA. Translation: AAT01927.2.
AB051901 Genomic DNA. Translation: BAB18859.1.
AL138842, AL160282 Genomic DNA. Translation: CAI22351.1.
BC093702 mRNA. Translation: AAH93702.1.
BC093704 mRNA. Translation: AAH93704.1.
AF333001 Genomic DNA. Translation: AAK37514.1.
IPIIPI00007956.
RefSeqNP_006463.3.
UniGeneHs.533977

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ9H3M7. 1 interaction.
STRINGQ9H3M7.

PTM databases

PhosphoSiteQ9H3M7.

Proteomic databases

PRIDEQ9H3M7.

Genome annotation databases

EnsemblENST00000369317; ENSP00000358323; ENSG00000117289; Homo sapiens. [Genome view]
GeneID10628.
KEGGhsa:10628.
UCSCuc001enn.2. human.

Organism-specific databases

CTD10628.
GeneCardsGC01P144149.
HGNCHGNC:16952. TXNIP.
HPACAB013291.
MIM606599. gene.
PharmGKBPA38194.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ9H3M7.
OMAEAPPCYM
OrthoDBEOG9258D1

Gene expression databases

ArrayExpressQ9H3M7.
BgeeQ9H3M7.
CleanExHS_TXNIP.
GenevestigatorQ9H3M7.
GermOnlineENSG00000117289. Homo sapiens.

Family and domain databases

InterProIPR011022. Arrestin-like_C.
IPR011021. Arrestin-like_N.
IPR014756. Ig_E-set.
[Graphical view]
PfamPF02752. Arrestin_C. 1 hit.
PF00339. Arrestin_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio40381.
SOURCESearch...

Entry information

Entry nameTXNIP_HUMAN
AccessionPrimary (citable) accession number: Q9H3M7
Secondary accession number(s): Q16226, Q6PML0, Q9BXG9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: March 1, 2001
Last modified: November 24, 2009
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

Relevant documents

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents