Q9JJP9 · UBQL1_RAT

Function

function

Plays an important role in the regulation of different protein degradation mechanisms and pathways including ubiquitin-proteasome system (UPS), autophagy and endoplasmic reticulum-associated protein degradation (ERAD) pathway. Mediates the proteasomal targeting of misfolded or accumulated proteins for degradation by binding (via UBA domain) to their polyubiquitin chains and by interacting (via ubiquitin-like domain) with the subunits of the proteasome. Plays a role in the ERAD pathway via its interaction with ER-localized proteins UBXN4, VCP and HERPUD1 and may form a link between the polyubiquitinated ERAD substrates and the proteasome. Plays a role in unfolded protein response (UPR) by attenuating the induction of UPR-inducible genes, DDTI3/CHOP, HSPA5 and PDIA2 during ER stress. Involved in the regulation of macroautophagy and autophagosome formation; required for maturation of autophagy-related protein LC3 from the cytosolic form LC3-I to the membrane-bound form LC3-II and may assist in the maturation of autophagosomes to autolysosomes by mediating autophagosome-lysosome fusion. Negatively regulates the TICAM1/TRIF-dependent toll-like receptor signaling pathway by decreasing the abundance of TICAM1 via the autophagic pathway. Promotes the ubiquitination and lysosomal degradation of ORAI1, consequently down-regulating the ORAI1-mediated Ca2+ mobilization (By similarity).
Suppresses the maturation and proteasomal degradation of amyloid beta A4 protein (A4) by stimulating the lysine 63 (K63)-linked polyubiquitination. Delays the maturation of A4 by sequestering it in the Golgi apparatus and preventing its transport to the cell surface for subsequent processing (PubMed:22847417).
Promotes the surface expression of GABA-A receptors (PubMed:11528422).
Ubiquitinates BCL2L10 and thereby stabilizes protein abundance (By similarity).

GO annotations

AspectTerm
Cellular Componentaggresome
Cellular Componentautophagosome
Cellular Componentcytoplasm
Cellular Componentcytoplasmic vesicle
Cellular Componentcytosol
Cellular Componentendoplasmic reticulum
Cellular Componentnucleus
Cellular Componentperinuclear region of cytoplasm
Cellular Componentplasma membrane
Cellular Componentproteasome complex
Molecular Functionidentical protein binding
Molecular Functionkinase binding
Molecular Functionpolyubiquitin modification-dependent protein binding
Molecular Functionprotein domain specific binding
Biological Processaggrephagy
Biological Processautophagosome assembly
Biological Processautophagosome maturation
Biological Processcellular response to hypoxia
Biological ProcessERAD pathway
Biological Processmacroautophagy
Biological Processnegative regulation of store-operated calcium channel activity
Biological Processnegative regulation of toll-like receptor 3 signaling pathway
Biological Processpositive regulation of ERAD pathway
Biological Processpositive regulation of protein ubiquitination
Biological Processregulation of macroautophagy
Biological Processregulation of oxidative stress-induced intrinsic apoptotic signaling pathway
Biological Processregulation of protein ubiquitination
Biological Processresponse to endoplasmic reticulum stress
Biological Processubiquitin-dependent protein catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Ubiquilin-1
  • Alternative names
    • Protein linking IAP with cytoskeleton 1 (PLIC-1)

Gene names

    • Name
      Ubqln1
    • Synonyms
      Da41, Plic1

Organism names

  • Taxonomic identifier
  • Strain
    • Sprague-Dawley
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus

Accessions

  • Primary accession
    Q9JJP9
  • Secondary accessions
    • Q6IN34

Proteomes

Organism-specific databases

Subcellular Location

Nucleus
Cytoplasm
Endoplasmic reticulum
Cell membrane
Note: Recruited to the ER during ER-associated protein degradation (ERAD). Colocalizes with PSEN1 in the cell membrane and in cytoplasmic juxtanuclear structures called aggresomes. Colocalizes with ORAI1 and TICAM1 in the autophagosome. Colocalizes with EPS15 and HGS in ubiquitin-rich cytoplasmic aggregates that are not endocytic compartments and with EPS15 also in aggresomes (By similarity).
Detected in neuronal processes and synapses (PubMed:11528422).

Keywords

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylalanine
ChainPRO_00002110102-582Ubiquilin-1

Post-translational modification

Degraded during both macroautophagy and during chaperone-mediated autophagy (CMA).
Phosphorylated.
Ubiquitinated.

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Monomer and homodimer. Heterodimer with UBQLN2. Binds CD47 (By similarity).
Binds NBL1 (PubMed:9303440).
Binds GABRA1, GABRA2, GABRA3, GABRA6, GABRB1, GABRB2 and GABRB3 (PubMed:11528422).
Binds UBE3A, BTRC, P4HB and MTOR. Interacts with the proteasome 19S subunit. Interacts (via ubiquitin-like domain) with TREX1; the interaction is direct and may control TREX1 subcellular location. Forms a complex with UBXN4 and VCP. Interacts (via UBA domain) with UBQLN4 (via ubiquitin-like domain). Found in a complex with UBQLN2 and MAP1LC3A/B/C. The monomeric form interacts with PSEN1 and PSEN2. Interacts with ORAI1. Interacts (via UBA domain) with TICAM1. Interacts with EPS15. Interacts (via UBA domain) with UBA52 and (via ubiquitin-like domain) with PSMD3 and PSMD4. Interacts with HERPUD1. Interacts with MAP1LC3A/B/C in the presence of UBQLN4. Interacts (via ubiquitin-like domain) with EPS15 (via UIM domains) and both the ubiquitinated and non-ubiquitinated forms can interact with EPS15. Interacts (via ubiquitin-like domain) with EPS15L1, HGS (via UIM domain) and STAM2 (via UIM domain) (By similarity).
Interacts with BCL2L10/BCL-B; in the cytoplasm (By similarity).

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain, compositional bias.

TypeIDPosition(s)Description
Region1-26Disordered
Domain28-102Ubiquitin-like
Region102-136Disordered
Region169-422Interaction with UBXN4
Domain173-201STI1 1
Domain203-242STI1 2
Compositional bias285-308Polar residues
Region285-365Disordered
Compositional bias320-353Polar residues
Domain381-428STI1 3
Domain432-464STI1 4
Region481-513Disordered
Compositional bias490-504Polar residues
Domain539-579UBA

Domain

The UBA domain mediates binding to PSEN1 and PSEN2. It also binds ubiquitin with micromolar affinity, independently of polyubiquitin linkage type. Essential for its association with microtubule-associated protein 1 light chain 3 (MAP1LC3).
The ubiquitin-like domain mediates its association with the subunits of the proteasome.
Dimerization is dependent upon the central region of the protein containing the STI1 domains and is independent of its ubiquitin-like and UBA domains.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    582
  • Mass (Da)
    62,072
  • Last updated
    2000-10-01 v1
  • Checksum
    6651E95B09071E5B
MAESAESGGPPGAQDSAADSGPAEPKIMKVTVKTPKEKEEFAVPENSSVQQFKEEISKRFKSHIDQLVLIFAGKILKDQDTLSQHGIHDGLTVHLVIKTQNRPQDNSAQQTNTTGNSVTSSPAPDSNPTSGPAANSSFGLGGLGGLAGLSSLGLNTTNFSELQSQMQRQLLSNPEMMVQIMENPFVQSMLSNPDLMRQLIMANPQMQQLIQRNPEISHMLNNPNIMRQTLELARNPAMMQEMMRNQERDLSNLESIPGGYNALRRMYTDIQEPMLNAAQEQFGGNPFASLVSSPSSAEGTQPSRTENRDPLPNPWAPQTPQSSPASGSTGSTTNTVSTSAGNATSTPAGQGTSGPNLVPGAGASMFNTPGMQSLLQQITENPQLMQNMLSAPYMRSMMQSLSQNPDLAAQMMLNNPLFAGNPQLQEQMRQQLPTFLQQMQNPDTLSAMSNPRAMQALLQIQQGLQTLATEAPGLIPGFTPGLAAGNSGGPAGTTAPSTAPGEDTNPQGGAAEPGHQQFIQQMLQALAGVNPQLQSPEVRFQQQLEQLSAMGFLNREANLQALIATGGDINAAIERLLGSQPS

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A140TAI1A0A140TAI1_RATUbqln1554
A0A8I5ZXD7A0A8I5ZXD7_RATUbqln1582

Features

Showing features for sequence conflict, compositional bias.

TypeIDPosition(s)Description
Sequence conflict63-64in Ref. 3; AA sequence
Sequence conflict224in Ref. 2; AAH72477
Sequence conflict247-249in Ref. 2; AAH72477
Compositional bias285-308Polar residues
Compositional bias320-353Polar residues
Compositional bias490-504Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
D87950
EMBL· GenBank· DDBJ
BAA92267.1
EMBL· GenBank· DDBJ
mRNA
BC072477
EMBL· GenBank· DDBJ
AAH72477.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp