Gene Ontology annotation through association of InterPro records with GO terms
Gene Ontology annotation based on Enzyme Commission mapping
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniPathway vocabulary mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Combined Automated Annotation using Multiple IEA Methods
Falcon deep research report for human PEX2
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Deep research synthesis of 2024 reviews confirms PEX2 as a subunit of the heterotrimeric PEX2/PEX10/PEX12 membrane-embedded RING E3 ubiquitin ligase complex that monoubiquitinates PEX5 at Cys11 for receptor recycling, and polyubiquitinates receptors for RADAR-pathway degradation.
"PEX2 is one of three **RING-finger peroxins** (PEX2/PEX10/PEX12) that form a **membrane-embedded E3 ubiquitin ligase** complex required for ubiquitination of the import receptors"
Defective PEX gene products correlate with the protein import, biochemical abnormalities, and phenotypic heterogeneity in peroxisome biogenesis disorders.
Molecular anatomy of the peroxin Pex12p: ring finger domain is essential for Pex12p function and interacts with the peroxisome-targeting signal type 1-receptor Pex5p and a ring peroxin, Pex10p.
Two different targeting signals direct human peroxisomal membrane protein 22 to peroxisomes.
The peroxisomal membrane targeting elements of human peroxin 2 (PEX2).
A human gene responsible for Zellweger syndrome that affects peroxisome assembly.
The parafibromin tumor suppressor protein inhibits cell proliferation by repression of the c-myc proto-oncogene.
Defining the membrane proteome of NK cells.
The peroxisomal receptor Pex19p forms a helical mPTS recognition domain.
PEX14 is required for microtubule-based peroxisome motility in human cells.
Distinct modes of ubiquitination of peroxisome-targeting signal type 1 (PTS1) receptor Pex5p regulate PTS1 protein import.
ATM functions at the peroxisome to induce pexophagy in response to ROS.
PEX2 is the E3 ubiquitin ligase required for pexophagy during starvation.
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PEX2 specifically (not PEX10 or PEX12) ubiquitinates PEX5 and PMP70 during amino acid starvation
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PEX2 overexpression induces pexophagy via NBR1-dependent autophagy
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PEX2 protein levels regulated by mTORC1 pathway
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Validated in vivo in protein-restricted mice
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Peroxisomal β-oxidation acts as a sensor for intracellular fatty acids and regulates lipolysis.
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PEX2 polyubiquitinates ATGL at K92 via K48-linkage for proteasomal degradation
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PEX2 acts as ROS sensor with disulfide bond-mediated protein stabilization
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Peroxisomal beta-oxidation derived ROS regulate PEX2 protein levels
A peroxisomal ubiquitin ligase complex forms a retrotranslocation channel.
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Cryo-EM structure of PEX2/PEX10/PEX12 complex reveals retrotranslocation channel
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Each subunit contributes 5 TM segments forming open channel pore
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RING finger domains form cytosolic tower above channel for receptor ubiquitination
Restoration of PEX2 peroxisome assembly defects by overexpression of PMP70.
PEX2:PEX10:PEX12 binds PEX5S,L (in PEX5S:PEX13:PEX14) and Ub:UBE2D1,2,3
PEX2:PEX10:PEX12 monoubiquitinates PEX5S,L at cysteine-11
Cargo of PEX5S,L translocates from the cytosol to the peroxisomal matrix
PEX5S,L:Cargo binds PEX13:PEX14:PEX2:PEX10:PEX12 (Docking and Translocation Module)
PEX2:PEX10:PEX12 monoubiquitinates PEX5L at cysteine-11
PEX1:PEX6:PEX26:ZFAND6 dissociates Ub:PEX5L and PEX7 from PEX14:PEX13:PEX2:PEX10:PEX12 and translocates PEX5L and PEX7 from the peroxisomal membrane to the cytosol
Cargo of PEX5L:PEX7 translocates from the cytosol to the peroxisomal matrix
PEX2:PEX10:PEX12:Ub:PEX5L:PEX7:PEX13:PEX14 binds PEX1:PEX6:PEX26 and ZFAND6
PEX2:PEX10:PEX12 binds PEX5L (in PEX5L:PEX7:PEX13:PEX14:PEX2:PEX10:PEX12) and Ub:UBE2D1,2,3
PEX2:PEX10:PEX12:Ub:PEX5S,L:PEX13:PEX14 binds PEX1:PEX6:PEX26 and ZFAND6
PEX3:PEX19:class I PMP dissociates
PEX19:class I PMP binds PEX3
PEX19 binds class I peroxisomal membrane proteins