UniProt functional annotation for Q91YL2



	UniProt functional annotation for Q91YL2

UniProt code: Q91YL2.

Organism: Mus musculus (Mouse).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus.

Function: E3 ubiquitin-protein ligase that mediates ubiquitination oF target proteins (By similarity). Depending on the associated E2 ligase, mediates 'Lys-48'- and 'Lys-63'-linked polyubiquitination of substrates (PubMed:23418353). Part of a BAG6-dependent quality control process ensuring that proteins of the secretory pathway that are mislocalized to the cytosol are degraded by the proteasome (By similarity). Probably acts by providing the ubiquitin ligase activity associated with the BAG6 complex and be responsible for ubiquitination of the hydrophobic mislocalized proteins and their targeting to the proteasome (By similarity). May also play a role in the endosomal recycling of IGF2R, the cation-independent mannose-6-phosphate receptor (By similarity). May play a role in the endosomal sorting and degradation of several membrane receptors including EGFR, FLT3, MET and CXCR4, by mediating their ubiquitination (PubMed:23418353). By ubiquitinating CDKN1A/p21 and targeting it for degradation, may also promote cell proliferation (By similarity). May monoubiquitinate AICDA (By similarity). {ECO:0000250|UniProtKB:Q9BV68, ECO:0000269|PubMed:23418353}.

Catalytic activity: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000269|PubMed:23418353};

Pathway: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:23418353}.

Subunit: Interacts with CCDC50, EGFR, FLT3 and SCAMP3 (PubMed:23418353). Interacts with BAG6 (via ubiquitin-like domain); required for BAG6-dependent ubiquitination of proteins mislocalized to the cytosol (By similarity). Interacts with CDKN1A (By similarity). Interacts with AICDA (By similarity). {ECO:0000250|UniProtKB:Q9BV68, ECO:0000269|PubMed:23418353}.

Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9BV68}. Nucleus {ECO:0000250|UniProtKB:Q9BV68}.

Tissue specificity: Detected in B-cells (at protein level). {ECO:0000269|PubMed:23277564}.

Induction: Up-regulated in B-cells that undergo class-switch recombination (at protein level). {ECO:0000269|PubMed:23277564}.

Domain: The C4-type zinc finger is required for interaction with BAG6. {ECO:0000250|UniProtKB:Q9BV68}.

Ptm: Ubiquitinated. May undergo autoubiquitination. {ECO:0000250|UniProtKB:Q9BV68, ECO:0000303|PubMed:23418353}.

Annotations taken from UniProtKB at the EBI.


Organism:		Mus musculus (Mouse).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus.



Function:		E3 ubiquitin-protein ligase that mediates ubiquitination oF target proteins (By similarity). Depending on the associated E2 ligase, mediates 'Lys-48'- and 'Lys-63'-linked polyubiquitination of substrates (PubMed:23418353). Part of a BAG6-dependent quality control process ensuring that proteins of the secretory pathway that are mislocalized to the cytosol are degraded by the proteasome (By similarity). Probably acts by providing the ubiquitin ligase activity associated with the BAG6 complex and be responsible for ubiquitination of the hydrophobic mislocalized proteins and their targeting to the proteasome (By similarity). May also play a role in the endosomal recycling of IGF2R, the cation-independent mannose-6-phosphate receptor (By similarity). May play a role in the endosomal sorting and degradation of several membrane receptors including EGFR, FLT3, MET and CXCR4, by mediating their ubiquitination (PubMed:23418353). By ubiquitinating CDKN1A/p21 and targeting it for degradation, may also promote cell proliferation (By similarity). May monoubiquitinate AICDA (By similarity). {ECO:0000250\|UniProtKB:Q9BV68, ECO:0000269\|PubMed:23418353}.


Catalytic activity:		Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000269\|PubMed:23418353};
Pathway:		Protein modification; protein ubiquitination. {ECO:0000269\|PubMed:23418353}.
Subunit:		Interacts with CCDC50, EGFR, FLT3 and SCAMP3 (PubMed:23418353). Interacts with BAG6 (via ubiquitin-like domain); required for BAG6-dependent ubiquitination of proteins mislocalized to the cytosol (By similarity). Interacts with CDKN1A (By similarity). Interacts with AICDA (By similarity). {ECO:0000250\|UniProtKB:Q9BV68, ECO:0000269\|PubMed:23418353}.
Subcellular location:		Cytoplasm {ECO:0000250\|UniProtKB:Q9BV68}. Nucleus {ECO:0000250\|UniProtKB:Q9BV68}.
Tissue specificity:		Detected in B-cells (at protein level). {ECO:0000269\|PubMed:23277564}.
Induction:		Up-regulated in B-cells that undergo class-switch recombination (at protein level). {ECO:0000269\|PubMed:23277564}.
Domain:		The C4-type zinc finger is required for interaction with BAG6. {ECO:0000250\|UniProtKB:Q9BV68}.
Ptm:		Ubiquitinated. May undergo autoubiquitination. {ECO:0000250\|UniProtKB:Q9BV68, ECO:0000303\|PubMed:23418353}.