词条 | UBQLN1 |
释义 |
Ubiquilins contain a N-terminal ubiquitin-like domain and a C-terminal ubiquitin-associated domain. They physically associate with both proteasomes and ubiquitin ligases, and thus are thought to functionally link the ubiquitination machinery to the proteasome to effect in vivo protein degradation. Possible Role In Preventing Alzheimers DiseaseUbiquilin has also been shown to modulate accumulation of presenilin proteins, and is found in lesions associated with Alzheimer's and Parkinson's disease. Two transcript variants encoding different isoforms have been found for this gene.[3] Higher levels of ubiquilin-1 in the brain decreased malformation of the APP molecule which plays a key role in triggering Alzheimers disease.[4] Conversely, lower levels of ubiquilin-1 in the brain were associated with increased malformation of APP.[4] Similarity to Other ProteinsHuman UBQLN1 shares a high degree of similarity with related ubiquilins including UBQLN2 and UBQLN4.[5] InteractionsUBQLN1 has been shown to interact with
References1. ^{{cite journal | vauthors = Ozaki T, Hishiki T, Toyama Y, Yuasa S, Nakagawara A, Sakiyama S | title = Identification of a new cellular protein that can interact specifically with DAN | journal = DNA Cell Biol | volume = 16 | issue = 8 | pages = 985–91 |date=Oct 1997 | pmid = 9303440 | pmc = | doi =10.1089/dna.1997.16.985 }} 2. ^{{cite journal | vauthors = Hanaoka E, Ozaki T, Ohira M, Nakamura Y, Suzuki M, Takahashi E, Moriya H, Nakagawara A, Sakiyama S | title = Molecular cloning and expression analysis of the human DA41 gene and its mapping to chromosome 9q21.2-q21.3 | journal = J Hum Genet | volume = 45 | issue = 3 | pages = 188–91 |date=Jul 2000 | pmid = 10807547 | pmc = | doi = 10.1007/s100380050209 }} 3. ^1 {{cite web | title = Entrez Gene: UBQLN1 ubiquilin 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=29979| accessdate = }} 4. ^1 {{cite journal | vauthors = Stieren ES, El Ayadi A, Xiao Y, Siller E, Landsverk ML, Oberhauser AF, Barral JM, Boehning D | title = Ubiquilin-1 Is a Molecular Chaperone for the Amyloid Precursor Protein | journal = J Biol Chem | volume = 286| issue = 41| pages = 35689–98|date=August 2011 | pmid = 21852239 | doi = 10.1074/jbc.M111.243147 | laysummary = https://www.sciencedaily.com/releases/2011/09/110901112537.htm | laysource = Science Daily | pmc=3195644}} 5. ^{{cite journal | author = Marín I | title = The ubiquilin gene family: evolutionary patterns and functional insights | journal = BMC Evol Biol | volume = 14| pages = 63 | date=March 2014 | pmid = 24674348 | doi = 10.1186/1471-2148-14-63 | pmc=4230246}} 6. ^{{cite journal | vauthors = Kim TY, Kim E, Yoon SK, Yoon JB | title = Herp enhances ER-associated protein degradation by recruiting ubiquilins | journal = Biochem. Biophys. Res. Commun. | volume = 369 | issue = 2 | pages = 741–6 |date=May 2008 | pmid = 18307982 | doi = 10.1016/j.bbrc.2008.02.086 }} 7. ^{{cite journal | vauthors = Wu S, Mikhailov A, Kallo-Hosein H, Hara K, Yonezawa K, Avruch J | title = Characterization of ubiquilin 1, an mTOR-interacting protein | journal = Biochim. Biophys. Acta | volume = 1542 | issue = 1–3 | pages = 41–56 |date=January 2002 | pmid = 11853878 | doi = 10.1016/S0167-4889(01)00164-1 }} 8. ^{{cite journal | vauthors = Ko HS, Uehara T, Nomura Y | title = Role of ubiquilin associated with protein-disulfide isomerase in the endoplasmic reticulum in stress-induced apoptotic cell death | journal = J. Biol. Chem. | volume = 277 | issue = 38 | pages = 35386–92 |date=September 2002 | pmid = 12095988 | doi = 10.1074/jbc.M203412200 }} 9. ^1 {{cite journal | vauthors = Mah AL, Perry G, Smith MA, Monteiro MJ | title = Identification of Ubiquilin, a Novel Presenilin Interactor That Increases Presenilin Protein Accumulation | journal = J. Cell Biol. | volume = 151 | issue = 4 | pages = 847–62 |date=November 2000 | pmid = 11076969 | pmc = 2169435 | doi = 10.1083/jcb.151.4.847 }} 10. ^{{cite journal | vauthors = Kleijnen MF, Shih AH, Zhou P, Kumar S, Soccio RE, Kedersha NL, Gill G, Howley PM | title = The hPLIC proteins may provide a link between the ubiquitination machinery and the proteasome | journal = Mol. Cell | volume = 6 | issue = 2 | pages = 409–19 |date=August 2000 | pmid = 10983987 | doi = 10.1016/S1097-2765(00)00040-X }} 11. ^{{cite journal | pmid = 25416956 | doi=10.1016/j.cell.2014.10.050 | pmc=4266588 | volume=159 | title=A proteome-scale map of the human interactome network | year=2014 | journal=Cell | pages=1212–26 | vauthors=Rolland T, Taşan M, Charloteaux B, Pevzner SJ, Zhong Q, Sahni N, Yi S, Lemmens I, Fontanillo C, Mosca R, Kamburov A, Ghiassian SD, Yang X, Ghamsari L, Balcha D, Begg BE, Braun P, Brehme M, Broly MP, Carvunis AR, Convery-Zupan D, Corominas R, Coulombe-Huntington J, Dann E, Dreze M, Dricot A, Fan C, Franzosa E, Gebreab F, Gutierrez BJ, Hardy MF, Jin M, Kang S, Kiros R, Lin GN, Luck K, MacWilliams A, Menche J, Murray RR, Palagi A, Poulin MM, Rambout X, Rasla J, Reichert P, Romero V, Ruyssinck E, Sahalie JM, Scholz A, Shah AA, Sharma A, Shen Y, Spirohn K, Tam S, Tejeda AO, Trigg SA, Twizere JC, Vega K, Walsh J, Cusick ME, Xia Y, Barabási AL, Iakoucheva LM, Aloy P, De Las RJ, Tavernier J, Calderwood MA, Hill DE, Hao T, Roth FP, Vidal M}} Further reading{{refbegin | 2}}
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