Biology:UBQLN1

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A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

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

Ubiquilins contain two domains, an 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.

Functions

Ubiquilin-1 is associated with protein degradation and aggregation of misfolded proteins, and may be involved in neurodegenerative diseases.[4][5] Ubiquilin-1 has been reported to act as a molecular chaperone for amyloid precursor protein (APP), a protein associated with Alzheimer's disease.[6]

Ubiquilin-1 was first identified through its interactions with presenilins.[7] Two transcript variants encoding different isoforms have been found for this gene.[3]

Related proteins

Human UBQLN1 shares a high degree of similarity with related ubiquilins including UBQLN2 and UBQLN4.[8]

Interactions

UBQLN1 has been shown to interact with

References

  1. "Identification of a new cellular protein that can interact specifically with DAN". DNA and Cell Biology 16 (8): 985–91. August 1997. doi:10.1089/dna.1997.16.985. PMID 9303440. 
  2. "Molecular cloning and expression analysis of the human DA41 gene and its mapping to chromosome 9q21.2-q21.3". Journal of Human Genetics 45 (3): 188–91. Jul 2000. doi:10.1007/s100380050209. PMID 10807547. 
  3. 3.0 3.1 "Entrez Gene: UBQLN1 ubiquilin 1". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=29979. 
  4. "Emerging role of Alzheimer's disease-associated ubiquilin-1 in protein aggregation". Biochemical Society Transactions 38 (Pt 1): 150–5. February 2010. doi:10.1042/BST0380150. PMID 20074050. 
  5. "An emerging role for Ubiquilin 1 in regulating protein quality control system and in disease pathogenesis". Discovery Medicine 8 (40): 18–22. June 2009. PMID 19772837. 
  6. "Ubiquilin-1 is a molecular chaperone for the amyloid precursor protein". The Journal of Biological Chemistry 286 (41): 35689–98. October 2011. doi:10.1074/jbc.M111.243147. PMID 21852239. 
    • "Alzheimer's brains found to have lower levels of key protein". ScienceDaily (Press release). September 1, 2011.
  7. "Identification of ubiquilin, a novel presenilin interactor that increases presenilin protein accumulation". The Journal of Cell Biology 151 (4): 847–62. November 2000. doi:10.1083/jcb.151.4.847. PMID 11076969. 
  8. "The ubiquilin gene family: evolutionary patterns and functional insights". BMC Evolutionary Biology 14: 63. March 2014. doi:10.1186/1471-2148-14-63. PMID 24674348. 
  9. "Herp enhances ER-associated protein degradation by recruiting ubiquilins". Biochemical and Biophysical Research Communications 369 (2): 741–6. May 2008. doi:10.1016/j.bbrc.2008.02.086. PMID 18307982. 
  10. "Characterization of ubiquilin 1, an mTOR-interacting protein". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1542 (1–3): 41–56. January 2002. doi:10.1016/S0167-4889(01)00164-1. PMID 11853878. 
  11. "Role of ubiquilin associated with protein-disulfide isomerase in the endoplasmic reticulum in stress-induced apoptotic cell death". The Journal of Biological Chemistry 277 (38): 35386–92. September 2002. doi:10.1074/jbc.M203412200. PMID 12095988. 
  12. 12.0 12.1 "Identification of ubiquilin, a novel presenilin interactor that increases presenilin protein accumulation". The Journal of Cell Biology 151 (4): 847–62. November 2000. doi:10.1083/jcb.151.4.847. PMID 11076969. 
  13. "The hPLIC proteins may provide a link between the ubiquitination machinery and the proteasome". Molecular Cell 6 (2): 409–19. August 2000. doi:10.1016/S1097-2765(00)00040-X. PMID 10983987. 
  14. "A proteome-scale map of the human interactome network". Cell 159 (5): 1212–1226. November 2014. doi:10.1016/j.cell.2014.10.050. PMID 25416956. 

Further reading