UBQLN1

From Wikipedia, the free encyclopedia
Jump to: navigation, search
Ubiquilin 1
Protein UBQLN1 PDB 2JY5.png
Rendering based on PDB 2JY5.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols UBQLN1 ; DA41; DSK2; PLIC-1; UBQN; XDRP1
External IDs OMIM605046 MGI1860276 HomoloGene40881 GeneCards: UBQLN1 Gene
Orthologs
Species Human Mouse
Entrez 29979 56085
Ensembl ENSG00000135018 ENSMUSG00000005312
UniProt Q9UMX0 Q8R317
RefSeq (mRNA) NM_013438 NM_026842
RefSeq (protein) NP_038466 NP_081118
Location (UCSC) Chr 9:
86.27 – 86.32 Mb
Chr 13:
58.18 – 58.22 Mb
PubMed search [1] [2]

Ubiquilin-1 is a protein that in humans is encoded by the UBQLN1 gene.[1][2][3]

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 Disease[edit]

Ubiquilin 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 Non-human Proteins[edit]

Human ubiquitin (ubiquilin) shares high degree of similarity with related proteins in yeast, rat and frog.

Interactions[edit]

UBQLN1 has been shown to interact with

References[edit]

  1. ^ Ozaki T, Hishiki T, Toyama Y, Yuasa S, Nakagawara A, Sakiyama S (Oct 1997). "Identification of a new cellular protein that can interact specifically with DAN". DNA Cell Biol 16 (8): 985–91. doi:10.1089/dna.1997.16.985. PMID 9303440. 
  2. ^ Hanaoka E, Ozaki T, Ohira M, Nakamura Y, Suzuki M, Takahashi E, Moriya H, Nakagawara A, Sakiyama S (Jul 2000). "Molecular cloning and expression analysis of the human DA41 gene and its mapping to chromosome 9q21.2-q21.3". J Hum Genet 45 (3): 188–91. doi:10.1007/s100380050209. PMID 10807547. 
  3. ^ a b "Entrez Gene: UBQLN1 ubiquilin 1". 
  4. ^ a b Stieren ES, El Ayadi A, Xiao Y, Siller E, Landsverk ML, Oberhauser AF, Barral JM, Boehning D (August 2011). "Ubiquilin-1 Is a Molecular Chaperone for the Amyloid Precursor Protein". J Biol Chem 286 (41): 35689–98. doi:10.1074/jbc.M111.243147. PMC 3195644. PMID 21852239. Lay summaryScience Daily. 
  5. ^ Kim TY, Kim E, Yoon SK, Yoon JB (May 2008). "Herp enhances ER-associated protein degradation by recruiting ubiquilins". Biochem. Biophys. Res. Commun. 369 (2): 741–6. doi:10.1016/j.bbrc.2008.02.086. PMID 18307982. 
  6. ^ Wu S, Mikhailov A, Kallo-Hosein H, Hara K, Yonezawa K, Avruch J (January 2002). "Characterization of ubiquilin 1, an mTOR-interacting protein". Biochim. Biophys. Acta 1542 (1–3): 41–56. doi:10.1016/S0167-4889(01)00164-1. PMID 11853878. 
  7. ^ Ko HS, Uehara T, Nomura Y (September 2002). "Role of ubiquilin associated with protein-disulfide isomerase in the endoplasmic reticulum in stress-induced apoptotic cell death". J. Biol. Chem. 277 (38): 35386–92. doi:10.1074/jbc.M203412200. PMID 12095988. 
  8. ^ a b Mah AL, Perry G, Smith MA, Monteiro MJ (November 2000). "Identification of Ubiquilin, a Novel Presenilin Interactor That Increases Presenilin Protein Accumulation". J. Cell Biol. 151 (4): 847–62. doi:10.1083/jcb.151.4.847. PMC 2169435. PMID 11076969. 
  9. ^ Kleijnen MF, Shih AH, Zhou P, Kumar S, Soccio RE, Kedersha NL, Gill G, Howley PM (August 2000). "The hPLIC proteins may provide a link between the ubiquitination machinery and the proteasome". Mol. Cell 6 (2): 409–19. doi:10.1016/S1097-2765(00)00040-X. PMID 10983987. 

Further reading[edit]