UBQLN1

Protein-coding gene in the species Homo sapiens


title: "UBQLN1" type: doc version: 1 created: 2026-02-28 author: "Wikipedia contributors" status: active scope: public description: "Protein-coding gene in the species Homo sapiens" topic_path: "uncategorized" source: "https://en.wikipedia.org/wiki/UBQLN1" license: "CC BY-SA 4.0" wikipedia_page_id: 0 wikipedia_revision_id: 0

::summary Protein-coding gene in the species Homo sapiens ::

Ubiquilin-1 is a protein that in humans is encoded by the UBQLN1 gene.

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. Ubiquilin-1 has been reported to act as a molecular chaperone for amyloid precursor protein (APP), a protein associated with Alzheimer's disease.

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

Related proteins

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

Interactions

UBQLN1 has been shown to interact with

References

References

  1. (August 1997). "Identification of a new cellular protein that can interact specifically with DAN". DNA and Cell Biology.
  2. (Jul 2000). "Molecular cloning and expression analysis of the human DA41 gene and its mapping to chromosome 9q21.2-q21.3". Journal of Human Genetics.
  3. "Entrez Gene: UBQLN1 ubiquilin 1".
  4. (February 2010). "Emerging role of Alzheimer's disease-associated ubiquilin-1 in protein aggregation". Biochemical Society Transactions.
  5. (June 2009). "An emerging role for Ubiquilin 1 in regulating protein quality control system and in disease pathogenesis". Discovery Medicine.
  6. (November 2000). "Identification of ubiquilin, a novel presenilin interactor that increases presenilin protein accumulation". The Journal of Cell Biology.
  7. (March 2014). "The ubiquilin gene family: evolutionary patterns and functional insights". BMC Evolutionary Biology.
  8. (May 2008). "Herp enhances ER-associated protein degradation by recruiting ubiquilins". Biochemical and Biophysical Research Communications.
  9. (January 2002). "Characterization of ubiquilin 1, an mTOR-interacting protein". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research.
  10. (September 2002). "Role of ubiquilin associated with protein-disulfide isomerase in the endoplasmic reticulum in stress-induced apoptotic cell death". The Journal of Biological Chemistry.
  11. (November 2000). "Identification of ubiquilin, a novel presenilin interactor that increases presenilin protein accumulation". The Journal of Cell Biology.
  12. (August 2000). "The hPLIC proteins may provide a link between the ubiquitination machinery and the proteasome". Molecular Cell.
  13. (November 2014). "A proteome-scale map of the human interactome network". Cell.

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