ID TXNIP_HUMAN Reviewed; 391 AA.
AC Q9H3M7; B4E3D3; Q16226; Q6PML0; Q9BXG9;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 172.
DE RecName: Full=Thioredoxin-interacting protein;
DE AltName: Full=Thioredoxin-binding protein 2;
DE AltName: Full=Vitamin D3 up-regulated protein 1;
GN Name=TXNIP; Synonyms=VDUP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INDUCTION.
RX PubMed=8086474; DOI=10.1016/0167-4781(94)90242-9;
RA Chen K.-S., DeLuca H.F.;
RT "Isolation and characterization of a novel cDNA from HL-60 cells treated
RT with 1,25-dihydroxyvitamin D-3.";
RL Biochim. Biophys. Acta 1219:26-32(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH TXN, AND
RP INDUCTION.
RC TISSUE=Lens;
RX PubMed=17603038; DOI=10.1016/j.exer.2007.05.001;
RA Liyanage N.P.M., Fernando M.R., Lou M.F.;
RT "Regulation of the bioavailability of thioredoxin in the lens by a specific
RT thioredoxin-binding protein (TBP-2).";
RL Exp. Eye Res. 85:270-279(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Toyama S.;
RT "Homo sapiens VDUP1 gene.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-38.
RA Park J.B.;
RT "Cloning and characterization of human VDUP1 gene.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION, INDUCTION, AND INTERACTION WITH ZBTB16; ZBTB32 AND HDAC1.
RX PubMed=12821938; DOI=10.1038/sj.onc.1206610;
RA Han S.H., Jeon J.H., Ju H.R., Jung U., Kim K.Y., Yoo H.S., Lee Y.H.,
RA Song K.S., Hwang H.M., Na Y.S., Yang Y., Lee K.N., Choi I.;
RT "VDUP1 upregulated by TGF-beta1 and 1,25-dihydorxyvitamin D3 inhibits tumor
RT cell growth by blocking cell-cycle progression.";
RL Oncogene 22:4035-4046(2003).
RN [9]
RP FUNCTION.
RX PubMed=18541147; DOI=10.1016/j.bbrc.2008.05.175;
RA Shin K.H., Kim R.H., Kim R.H., Kang M.K., Park N.H.;
RT "hnRNP G elicits tumor-suppressive activity in part by upregulating the
RT expression of Txnip.";
RL Biochem. Biophys. Res. Commun. 372:880-885(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP INTERACTION WITH ITCH, AND UBIQUITINATION BY ITCH.
RX PubMed=20068034; DOI=10.1074/jbc.m109.063321;
RA Zhang P., Wang C., Gao K., Wang D., Mao J., An J., Xu C., Wu D., Yu H.,
RA Liu J.O., Yu L.;
RT "The ubiquitin ligase itch regulates apoptosis by targeting thioredoxin-
RT interacting protein for ubiquitin-dependent degradation.";
RL J. Biol. Chem. 285:8869-8879(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP FUNCTION, AND INTERACTION WITH DDIT4.
RX PubMed=21460850; DOI=10.1038/onc.2011.102;
RA Jin H.O., Seo S.K., Kim Y.S., Woo S.H., Lee K.H., Yi J.Y., Lee S.J.,
RA Choe T.B., Lee J.H., An S., Hong S.I., Park I.C.;
RT "TXNIP potentiates Redd1-induced mTOR suppression through stabilization of
RT Redd1.";
RL Oncogene 30:3792-3801(2011).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 2-149, SUBUNIT, AND INTERCHAIN
RP DISULFIDE BOND.
RX PubMed=23519408; DOI=10.1107/s0907444912047099;
RA Polekhina G., Ascher D.B., Kok S.F., Beckham S., Wilce M., Waltham M.;
RT "Structure of the N-terminal domain of human thioredoxin-interacting
RT protein.";
RL Acta Crystallogr. D 69:333-344(2013).
CC -!- FUNCTION: May act as an oxidative stress mediator by inhibiting
CC thioredoxin activity or by limiting its bioavailability. Interacts with
CC COPS5 and restores COPS5-induced suppression of CDKN1B stability,
CC blocking the COPS5-mediated translocation of CDKN1B from the nucleus to
CC the cytoplasm. Functions as a transcriptional repressor, possibly by
CC acting as a bridge molecule between transcription factors and
CC corepressor complexes, and over-expression will induce G0/G1 cell cycle
CC arrest. Required for the maturation of natural killer cells. Acts as a
CC suppressor of tumor cell growth. Inhibits the proteasomal degradation
CC of DDIT4, and thereby contributes to the inhibition of the mammalian
CC target of rapamycin complex 1 (mTORC1). {ECO:0000269|PubMed:12821938,
CC ECO:0000269|PubMed:17603038, ECO:0000269|PubMed:18541147,
CC ECO:0000269|PubMed:21460850}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with TXN/thioredoxin
CC through its redox-active site. Interacts with transcriptional
CC repressors ZBTB16, ZBTB32 and HDAC1. Interacts (via C-terminus) with
CC ITCH (via WW domains). Interacts with DDIT4.
CC {ECO:0000269|PubMed:12821938, ECO:0000269|PubMed:17603038,
CC ECO:0000269|PubMed:20068034, ECO:0000269|PubMed:21460850,
CC ECO:0000269|PubMed:23519408}.
CC -!- INTERACTION:
CC Q9H3M7; O95905: ECD; NbExp=5; IntAct=EBI-1369170, EBI-2557598;
CC Q9H3M7; P10599: TXN; NbExp=8; IntAct=EBI-1369170, EBI-594644;
CC Q9H3M7; P52735: VAV2; NbExp=2; IntAct=EBI-1369170, EBI-297549;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H3M7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H3M7-2; Sequence=VSP_054401;
CC -!- INDUCTION: By 1,25-dihydroxyvitamin D-3 and TGFB1. Down-regulated in
CC response to oxidative stress. {ECO:0000269|PubMed:12821938,
CC ECO:0000269|PubMed:17603038, ECO:0000269|PubMed:8086474}.
CC -!- PTM: Ubiquitinated; undergoes polyubiquitination catalyzed by ITCH
CC resulting in proteasomal degradation. {ECO:0000269|PubMed:20068034}.
CC -!- SIMILARITY: Belongs to the arrestin family. {ECO:0000305}.
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DR EMBL; S73591; AAB31977.2; -; mRNA.
DR EMBL; AY594328; AAT01927.2; -; mRNA.
DR EMBL; AB051901; BAB18859.1; -; Genomic_DNA.
DR EMBL; AK304670; BAG65445.1; -; mRNA.
DR EMBL; AL138842; CAI22351.1; -; Genomic_DNA.
DR EMBL; AL160282; CAI22351.1; JOINED; Genomic_DNA.
DR EMBL; BC093702; AAH93702.1; -; mRNA.
DR EMBL; BC093704; AAH93704.1; -; mRNA.
DR EMBL; AF333001; AAK37514.1; -; Genomic_DNA.
DR CCDS; CCDS72876.1; -. [Q9H3M7-1]
DR CCDS; CCDS81368.1; -. [Q9H3M7-2]
DR RefSeq; NP_001300901.1; NM_001313972.1. [Q9H3M7-2]
DR RefSeq; NP_006463.3; NM_006472.5. [Q9H3M7-1]
DR PDB; 4GEI; X-ray; 1.50 A; A=2-149.
DR PDB; 4GEJ; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J=2-149.
DR PDB; 4GFX; X-ray; 1.60 A; A=4-154.
DR PDB; 4LL1; X-ray; 2.00 A; A/C=3-317.
DR PDB; 4LL4; X-ray; 2.70 A; A/C=3-317.
DR PDB; 4ROF; X-ray; 2.03 A; C/D=327-338.
DR PDB; 4ROJ; X-ray; 1.95 A; D/E/F=327-338.
DR PDB; 5CQ2; X-ray; 1.40 A; B/C=327-338.
DR PDB; 5DF6; X-ray; 1.78 A; B/C=371-382.
DR PDB; 5DWS; X-ray; 1.65 A; B/D/F/H=327-338.
DR PDB; 5DZD; X-ray; 1.57 A; C/D=327-338.
DR PDBsum; 4GEI; -.
DR PDBsum; 4GEJ; -.
DR PDBsum; 4GFX; -.
DR PDBsum; 4LL1; -.
DR PDBsum; 4LL4; -.
DR PDBsum; 4ROF; -.
DR PDBsum; 4ROJ; -.
DR PDBsum; 5CQ2; -.
DR PDBsum; 5DF6; -.
DR PDBsum; 5DWS; -.
DR PDBsum; 5DZD; -.
DR AlphaFoldDB; Q9H3M7; -.
DR SMR; Q9H3M7; -.
DR BioGRID; 115872; 176.
DR IntAct; Q9H3M7; 28.
DR MINT; Q9H3M7; -.
DR STRING; 9606.ENSP00000462521; -.
DR TCDB; 8.A.136.1.14; the alpha/beta-arrestin (arrb) family.
DR GlyGen; Q9H3M7; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q9H3M7; -.
DR PhosphoSitePlus; Q9H3M7; -.
DR SwissPalm; Q9H3M7; -.
DR BioMuta; TXNIP; -.
DR DMDM; 74752618; -.
DR EPD; Q9H3M7; -.
DR jPOST; Q9H3M7; -.
DR MassIVE; Q9H3M7; -.
DR MaxQB; Q9H3M7; -.
DR PaxDb; 9606-ENSP00000462521; -.
DR PeptideAtlas; Q9H3M7; -.
DR ProteomicsDB; 80731; -. [Q9H3M7-1]
DR Pumba; Q9H3M7; -.
DR Antibodypedia; 73170; 426 antibodies from 35 providers.
DR DNASU; 10628; -.
DR Ensembl; ENST00000425134.2; ENSP00000396322.2; ENSG00000265972.6. [Q9H3M7-2]
DR Ensembl; ENST00000582401.6; ENSP00000462521.1; ENSG00000265972.6. [Q9H3M7-1]
DR GeneID; 10628; -.
DR KEGG; hsa:10628; -.
DR MANE-Select; ENST00000582401.6; ENSP00000462521.1; NM_006472.6; NP_006463.3.
DR UCSC; uc031utq.2; human. [Q9H3M7-1]
DR AGR; HGNC:16952; -.
DR CTD; 10628; -.
DR DisGeNET; 10628; -.
DR GeneCards; TXNIP; -.
DR HGNC; HGNC:16952; TXNIP.
DR HPA; ENSG00000265972; Low tissue specificity.
DR MIM; 606599; gene.
DR neXtProt; NX_Q9H3M7; -.
DR OpenTargets; ENSG00000265972; -.
DR PharmGKB; PA38194; -.
DR VEuPathDB; HostDB:ENSG00000265972; -.
DR eggNOG; KOG3780; Eukaryota.
DR GeneTree; ENSGT00940000158522; -.
DR HOGENOM; CLU_039221_1_1_1; -.
DR InParanoid; Q9H3M7; -.
DR OMA; GPQQCKQ; -.
DR OrthoDB; 22053at2759; -.
DR PhylomeDB; Q9H3M7; -.
DR TreeFam; TF313650; -.
DR PathwayCommons; Q9H3M7; -.
DR Reactome; R-HSA-844456; The NLRP3 inflammasome.
DR Reactome; R-HSA-9617629; Regulation of FOXO transcriptional activity by acetylation.
DR Reactome; R-HSA-9660826; Purinergic signaling in leishmaniasis infection.
DR Reactome; R-HSA-9707564; Cytoprotection by HMOX1.
DR SignaLink; Q9H3M7; -.
DR SIGNOR; Q9H3M7; -.
DR BioGRID-ORCS; 10628; 16 hits in 1161 CRISPR screens.
DR ChiTaRS; TXNIP; human.
DR GeneWiki; TXNIP; -.
DR GenomeRNAi; 10628; -.
DR Pharos; Q9H3M7; Tbio.
DR PRO; PR:Q9H3M7; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9H3M7; Protein.
DR Bgee; ENSG00000265972; Expressed in right lung and 209 other cell types or tissues.
DR Genevisible; Q9H3M7; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0004857; F:enzyme inhibitor activity; IEA:Ensembl.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0140052; P:cellular response to oxidised low-density lipoprotein particle stimulus; TAS:ARUK-UCL.
DR GO; GO:0071228; P:cellular response to tumor cell; IDA:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; TAS:ARUK-UCL.
DR GO; GO:0030216; P:keratinocyte differentiation; IDA:UniProtKB.
DR GO; GO:0051782; P:negative regulation of cell division; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0006606; P:protein import into nucleus; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IBA:GO_Central.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0009749; P:response to glucose; IEA:Ensembl.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0032570; P:response to progesterone; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR Gene3D; 2.60.40.640; -; 2.
DR InterPro; IPR014752; Arrestin-like_C.
DR InterPro; IPR011021; Arrestin-like_N.
DR InterPro; IPR011022; Arrestin_C-like.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR11188; ARRESTIN DOMAIN CONTAINING PROTEIN; 1.
DR PANTHER; PTHR11188:SF14; THIOREDOXIN-INTERACTING PROTEIN; 1.
DR Pfam; PF02752; Arrestin_C; 1.
DR Pfam; PF00339; Arrestin_N; 1.
DR SMART; SM01017; Arrestin_C; 1.
DR SUPFAM; SSF81296; E set domains; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cytoplasm; Disulfide bond;
KW Isopeptide bond; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Tumor suppressor; Ubl conjugation.
FT CHAIN 1..391
FT /note="Thioredoxin-interacting protein"
FT /id="PRO_0000250489"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT DISULFID 63
FT /note="Interchain"
FT CROSSLNK 212
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:20068034"
FT VAR_SEQ 1..83
FT /note="MVMFKKIKSFEVVFNDPEKVYGSGEKVAGRVIVEVCEVTRVKAVRILACGVA
FT KVLWMQGSQQCKQTSEYLRYEDTLLLEDQPT -> MPPKHSLSHRCILSVTASLMATRF
FT SFPS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054401"
FT VARIANT 177
FT /note="R -> Q (in dbSNP:rs6674773)"
FT /id="VAR_048334"
FT CONFLICT 26
FT /note="K -> R (in Ref. 1; AAB31977 and 2; AAT01927)"
FT /evidence="ECO:0000305"
FT STRAND 8..16
FT /evidence="ECO:0007829|PDB:4GEI"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:4GEI"
FT STRAND 26..34
FT /evidence="ECO:0007829|PDB:4GEI"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:4GEI"
FT STRAND 43..58
FT /evidence="ECO:0007829|PDB:4GEI"
FT STRAND 61..76
FT /evidence="ECO:0007829|PDB:4GEI"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:4GEI"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:4GEJ"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:4GEI"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:4LL4"
FT STRAND 97..104
FT /evidence="ECO:0007829|PDB:4GEI"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:4GFX"
FT STRAND 116..130
FT /evidence="ECO:0007829|PDB:4GEI"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:4GEI"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:4GEI"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:4GFX"
FT STRAND 160..167
FT /evidence="ECO:0007829|PDB:4LL1"
FT STRAND 177..185
FT /evidence="ECO:0007829|PDB:4LL1"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:4LL1"
FT STRAND 194..203
FT /evidence="ECO:0007829|PDB:4LL1"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:4LL1"
FT STRAND 209..223
FT /evidence="ECO:0007829|PDB:4LL1"
FT STRAND 226..238
FT /evidence="ECO:0007829|PDB:4LL1"
FT STRAND 246..256
FT /evidence="ECO:0007829|PDB:4LL1"
FT STRAND 269..281
FT /evidence="ECO:0007829|PDB:4LL1"
FT STRAND 288..298
FT /evidence="ECO:0007829|PDB:4LL1"
FT HELIX 334..337
FT /evidence="ECO:0007829|PDB:5CQ2"
SQ 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
//
