TXNIP

TXNIP
PDBに登録されている構造
PDBオルソログ検索: RCSB PDBe PDBj
PDBのIDコード一覧

4GEI, 4GEJ, 4GFX, 4LL1, 4LL4, 4ROF, 4ROJ, 5CQ2, 5DF6, 5DWS, 5DZD

識別子
記号TXNIP, thioredoxin interacting protein, EST01027, HHCPA78, THIF, VDUP1, ARRDC6
外部IDOMIM: 606599 MGI: 1889549 HomoloGene: 38186 GeneCards: TXNIP
遺伝子の位置 (ヒト)
1番染色体 (ヒト)
染色体1番染色体 (ヒト)[1]
1番染色体 (ヒト)
TXNIP遺伝子の位置
TXNIP遺伝子の位置
バンドデータ無し開始点145,992,435 bp[1]
終点145,996,579 bp[1]
遺伝子の位置 (マウス)
3番染色体 (マウス)
染色体3番染色体 (マウス)[2]
3番染色体 (マウス)
TXNIP遺伝子の位置
TXNIP遺伝子の位置
バンドデータ無し開始点96,465,273 bp[2]
終点96,469,199 bp[2]
RNA発現パターン




さらなる参照発現データ
遺伝子オントロジー
分子機能• enzyme inhibitor activity
• 血漿タンパク結合
• ubiquitin protein ligase binding
細胞の構成要素• 細胞質
• 細胞質基質
• mitochondrial intermembrane space
• 細胞核
生物学的プロセス• cellular response to tumor cell
• エストラジオールへの反応
• negative regulation of catalytic activity
• regulation of transcription, DNA-templated
• protein import into nucleus
• response to progesterone
• response to mechanical stimulus
• negative regulation of transcription by RNA polymerase II
• response to glucose
• 酸化ストレスへの反応
• transcription, DNA-templated
• keratinocyte differentiation
• response to calcium ion
• negative regulation of cell division
• regulation of cell population proliferation
• positive regulation of apoptotic process
• 細胞周期
• platelet-derived growth factor receptor signaling pathway
• 過酸化水素への反応
• シグナル伝達
出典:Amigo / QuickGO
オルソログ
種ヒトマウス
Entrez

10628

56338

Ensembl

ENSG00000265972

ENSMUSG00000038393

UniProt

Q9H3M7

Q8BG60

RefSeq
(mRNA)

NM_006472
NM_001313972

NM_001009935
NM_023719

RefSeq
(タンパク質)

NP_001300901
NP_006463

NP_001009935
NP_076208

場所
(UCSC)		Chr 1: 145.99 – 146 MbChr 1: 96.47 – 96.47 Mb
PubMed検索[3][4]
ウィキデータ
閲覧/編集 ヒト閲覧/編集 マウス

チオレドキシン相互作用タンパク質（英: Thioredoxin-interacting protein, TXNIP）は、ヒト TXNIP 遺伝子にコードされているタンパク質である[5][6]。

チオレドキシン結合タンパク質2（英: Thioredoxin-binding protein 2, TBP-2）やビタミンD3上向き制御タンパク質1（英: Vitamin D3 up-regulated protein 1, VDUP-1）としても知られている。

相互作用

TXNIPは、チオレドキシン[7]およびZBTB32（英語版）[8]と相互作用することが示されている。

脚注

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000265972 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000038393 - Ensembl, May 2017
  3. ^ Human PubMed Reference:
  4. ^ Mouse PubMed Reference:
  5. ^ Chen KS, DeLuca HF (Oct 1994). “Isolation and characterization of a novel cDNA from HL-60 cells treated with 1,25-dihydroxyvitamin D-3”. Biochim. Biophys. Acta 1219 (1): 26–32. PMID 8086474. 
  6. ^ “Entrez Gene: TXNIP thioredoxin interacting protein”. 2011年6月3日閲覧。
  7. ^ Nishiyama, A; Matsui M, Iwata S, Hirota K, Masutani H, Nakamura H, Takagi Y, Sono H, Gon Y, Yodoi J (Jul. 1999), “Identification of thioredoxin-binding protein-2/vitamin D(3) up-regulated protein 1 as a negative regulator of thioredoxin function and expression”, J. Biol. Chem. (UNITED STATES) 274 (31): 21645–50, doi:10.1074/jbc.274.31.21645, ISSN 0021-9258, PMID 10419473 
  8. ^ Han, Seung Hyun; Jeon Jun Ho, Ju Hyang Ran, Jung Uhee, Kim Kun Young, Yoo Hyang Sook, Lee Young Ho, Song Kyu Sang, Hwang Ho Myeung, Na Yoon Sook, Yang Young, Lee Kee Nyung, Choi Inpyo (Jun. 2003), “VDUP1 upregulated by TGF-beta1 and 1,25-dihydorxyvitamin D3 inhibits tumor cell growth by blocking cell-cycle progression”, Oncogene (England) 22 (26): 4035–46, doi:10.1038/sj.onc.1206610, ISSN 0950-9232, PMID 12821938 

推薦文献

  • Nishiyama A, Matsui M, Iwata S, et al. (1999). “Identification of thioredoxin-binding protein-2/vitamin D(3) up-regulated protein 1 as a negative regulator of thioredoxin function and expression.”. J. Biol. Chem. 274 (31): 21645–50. doi:10.1074/jbc.274.31.21645. PMID 10419473. 
  • Ludwig DL, Kotanides H, Le T, et al. (2001). “Cloning, genetic characterization, and chromosomal mapping of the mouse VDUP1 gene.”. Gene 269 (1-2): 103–12. doi:10.1016/S0378-1119(01)00455-3. PMID 11376942. 
  • Bodnar JS, Chatterjee A, Castellani LW, et al. (2002). “Positional cloning of the combined hyperlipidemia gene Hyplip1.”. Nat. Genet. 30 (1): 110–6. doi:10.1038/ng811. PMC 2846781. PMID 11753387. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2846781/. 
  • Joguchi A, Otsuka I, Minagawa S, et al. (2002). “Overexpression of VDUP1 mRNA sensitizes HeLa cells to paraquat.”. Biochem. Biophys. Res. Commun. 293 (1): 293–7. doi:10.1016/S0006-291X(02)00208-5. PMID 12054598. 
  • Butler LM, Zhou X, Xu WS, et al. (2002). “The histone deacetylase inhibitor SAHA arrests cancer cell growth, up-regulates thioredoxin-binding protein-2, and down-regulates thioredoxin.”. Proc. Natl. Acad. Sci. U.S.A. 99 (18): 11700–5. doi:10.1073/pnas.182372299. PMC 129332. PMID 12189205. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC129332/. 
  • Schulze PC, De Keulenaer GW, Yoshioka J, et al. (2002). “Vitamin D3-upregulated protein-1 (VDUP-1) regulates redox-dependent vascular smooth muscle cell proliferation through interaction with thioredoxin.”. Circ. Res. 91 (8): 689–95. doi:10.1161/01.RES.0000037982.55074.F6. PMID 12386145. 
  • Han SH, Jeon JH, Ju HR, et al. (2003). “VDUP1 upregulated by TGF-beta1 and 1,25-dihydorxyvitamin D3 inhibits tumor cell growth by blocking cell-cycle progression.”. Oncogene 22 (26): 4035–46. doi:10.1038/sj.onc.1206610. PMID 12821938. 
  • Champliaud MF, Viel A, Baden HP (2003). “The expression of vitamin D-upregulated protein 1 in skin and its interaction with sciellin in cultured keratinocytes.”. J. Invest. Dermatol. 121 (4): 781–5. doi:10.1046/j.1523-1747.2003.12539.x. PMID 14632196. 
  • Kim KY, Shin SM, Kim JK, et al. (2004). “Heat shock factor regulates VDUP1 gene expression.”. Biochem. Biophys. Res. Commun. 315 (2): 369–75. doi:10.1016/j.bbrc.2004.01.047. PMID 14766217. 
  • Schulze PC, Yoshioka J, Takahashi T, et al. (2004). “Hyperglycemia promotes oxidative stress through inhibition of thioredoxin function by thioredoxin-interacting protein.”. J. Biol. Chem. 279 (29): 30369–74. doi:10.1074/jbc.M400549200. PMID 15128745. 
  • Coon H, Singh N, Dunn D, et al. (2004). “TXNIP gene not associated with familial combined hyperlipidemia in the NHLBI Family Heart Study.”. Atherosclerosis 174 (2): 357–62. doi:10.1016/j.atherosclerosis.2004.02.004. PMID 15136067. 
  • Nishinaka Y, Masutani H, Oka S, et al. (2004). “Importin alpha1 (Rch1) mediates nuclear translocation of thioredoxin-binding protein-2/vitamin D(3)-up-regulated protein 1.”. J. Biol. Chem. 279 (36): 37559–65. doi:10.1074/jbc.M405473200. PMID 15234975. 
  • Aitken CJ, Hodge JM, Nishinaka Y, et al. (2005). “Regulation of human osteoclast differentiation by thioredoxin binding protein-2 and redox-sensitive signaling.”. J. Bone Miner. Res. 19 (12): 2057–64. doi:10.1359/JBMR.040913. PMID 15537450. 
  • Yamawaki H, Pan S, Lee RT, Berk BC (2005). “Fluid shear stress inhibits vascular inflammation by decreasing thioredoxin-interacting protein in endothelial cells.”. J. Clin. Invest. 115 (3): 733–8. doi:10.1172/JCI200523001. PMC 546457. PMID 15696199. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC546457/. 
  • Minn AH, Hafele C, Shalev A (2005). “Thioredoxin-interacting protein is stimulated by glucose through a carbohydrate response element and induces beta-cell apoptosis.”. Endocrinology 146 (5): 2397–405. doi:10.1210/en.2004-1378. PMID 15705778. 
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