UniProt Accession

 TXNIP_HUMAN; Q9H3M7; Q16226; Q6PML0; Q9BXG9 

Genbank Protein ID

 S73591; AY594328; AB051901; AL138842; AL160282; BC093702; BC093704; AF333001 

Genbank Nucleotide ID

 AAB31977.2; AAT01927.2; BAB18859.1; CAI22351.1; CAI22351.1; AAH93702.1; AAH93704.1; AAK37514.1 

Protein Name

 Thioredoxin-interacting protein 

Protein Synonyms/Alias

 Thioredoxin-binding protein 2; Vitamin D3 up-regulated protein 1 

Gene Name

 TXNIP 

Gene Synonyms/Alias

 VDUP1 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
26	KVYGSGEKVAGRVIV	ubiquitination	[1, 2, 3, 4, 5, 6, 7]
96	VIMRPGNKYEYKFGF	ubiquitination	[7]
100	PGNKYEYKFGFELPQ	ubiquitination	[7]
115	GPLGTSFKGKYGCVD	ubiquitination	[1, 2, 7]
163	LMAPVSAKKEKKVSC	ubiquitination	[7]
167	VSAKKEKKVSCMFIP	ubiquitination	[2]
212	CSRIVVPKAAIVARH	ubiquitination	[1, 2, 7, 8]
228	YLANGQTKVLTQKLS	ubiquitination	[1, 7]
233	QTKVLTQKLSSVRGN	ubiquitination	[1, 2, 4]
287	VSVPGSKKVILDLPL	ubiquitination	[1, 7]

Reference

 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [4] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [5] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [6] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [7] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [8] Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry.
 Meierhofer D, Wang X, Huang L, Kaiser P.
 J Proteome Res. 2008 Oct;7(10):4566-76. [PMID: 18781797] 

Functional Description

 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). 

Sequence Annotation

 MOD_RES 361 361 Phosphoserine.
 CROSSLNK 212 212 Glycyl lysine isopeptide (Lys-Gly)  

Keyword

 3D-structure; Cell cycle; Complete proteome; Cytoplasm; Isopeptide bond; Phosphoprotein; Polymorphism; Reference proteome; Transcription; Transcription regulation; Tumor suppressor; Ubl conjugation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 391 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005758; C:mitochondrial intermembrane space; IEA:Compara.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0004857; F:enzyme inhibitor activity; IEA:Compara.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0071228; P:cellular response to tumor cell; IDA:UniProtKB.
 GO:0045087; P:innate immune response; TAS:Reactome.
 GO:0030216; P:keratinocyte differentiation; IDA:UniProtKB.
 GO:0051782; P:negative regulation of cell division; IDA:UniProtKB.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Compara.
 GO:0035872; P:nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway; TAS:Reactome.
 GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IEA:Compara.
 GO:0043065; P:positive regulation of apoptotic process; IEA:Compara.
 GO:0006606; P:protein import into nucleus; IEA:Compara.
 GO:0042127; P:regulation of cell proliferation; IEA:Compara.
 GO:0051592; P:response to calcium ion; IEA:Compara.
 GO:0042493; P:response to drug; IEA:Compara.
 GO:0032355; P:response to estradiol stimulus; IEA:Compara.
 GO:0009749; P:response to glucose stimulus; IEA:Compara.
 GO:0042542; P:response to hydrogen peroxide; IEA:Compara.
 GO:0009612; P:response to mechanical stimulus; IEA:Compara.
 GO:0032570; P:response to progesterone stimulus; IEA:Compara.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 

Interpro

 IPR011021; Arrestin-like_N.
 IPR011022; Arrestin_C-like.
 IPR014756; Ig_E-set. 

Pfam

 PF02752; Arrestin_C
 PF00339; Arrestin_N 

SMART

 SM01017; Arrestin_C 

PROSITE

  

PRINTS