Q8N8N0 · RN152_HUMAN
- ProteinE3 ubiquitin-protein ligase RNF152
- GeneRNF152
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids203 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
E3 ubiquitin-protein ligase that acts as a negative regulator of mTORC1 signaling by mediating ubiquitination of RagA/RRAGA and RHEB (PubMed:25936802, PubMed:30514904).
Catalyzes 'Lys-63'-linked polyubiquitination of RagA/RRAGA in response to amino acid starvation, thereby regulating mTORC1 signaling (PubMed:25936802).
Also mediates monoubiquitination of RHEB, promoting its association with the TSC-TBC complex and subsequent inhibition (PubMed:30514904).
Also mediates 'Lys-48'-linked polyubiquitination of target proteins and their subsequent targeting to the proteasome for degradation (PubMed:21203937).
Induces apoptosis when overexpressed (PubMed:21203937).
Catalyzes 'Lys-63'-linked polyubiquitination of RagA/RRAGA in response to amino acid starvation, thereby regulating mTORC1 signaling (PubMed:25936802).
Also mediates monoubiquitination of RHEB, promoting its association with the TSC-TBC complex and subsequent inhibition (PubMed:30514904).
Also mediates 'Lys-48'-linked polyubiquitination of target proteins and their subsequent targeting to the proteasome for degradation (PubMed:21203937).
Induces apoptosis when overexpressed (PubMed:21203937).
Catalytic activity
Pathway
Protein modification; protein ubiquitination.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | lysosomal membrane | |
Cellular Component | lysosome | |
Cellular Component | organelle membrane | |
Molecular Function | metal ion binding | |
Molecular Function | small GTPase binding | |
Molecular Function | ubiquitin protein ligase activity | |
Molecular Function | ubiquitin-protein transferase activity | |
Biological Process | apoptotic process | |
Biological Process | cellular response to amino acid starvation | |
Biological Process | negative regulation of TORC1 signaling | |
Biological Process | positive regulation of autophagy | |
Biological Process | protein K48-linked ubiquitination | |
Biological Process | protein K63-linked ubiquitination | |
Biological Process | protein monoubiquitination | |
Biological Process | protein ubiquitination |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameE3 ubiquitin-protein ligase RNF152
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ8N8N0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Lysosome membrane ; Single-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 167-187 | Helical | ||||
Sequence: SGVCTVILVACVLVFLLGIVL |
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 264 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000056111 | 1-203 | E3 ubiquitin-protein ligase RNF152 | |||
Sequence: METLSQDSLLECQICFNYYSPRRRPKLLDCKHTCCSVCLQQMRTSQKDVRCPWCRGVTKLPPGFSVSQLPDDPEVLAVIAIPHTSEHTPVFIKLPSNGCYMLPLPISKERALLPGDMGCRLLPGSQQKSVTVVTIPAEQQPLQGGAPQEAVEEEQDRRGVVKSSTWSGVCTVILVACVLVFLLGIVLHNMSCISKRFTVISCG |
Post-translational modification
Ubiquitinated. Autoubiquitinated in vitro, leading to its degradation by the proteasome (Probable).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with RRAGA (inactive GDP-bound form); stimulated by amino acid starvation (PubMed:25936802).
Interacts with SEC16A (By similarity).
Interacts with SEC16A (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q8N8N0 | EBP Q15125 | 3 | EBI-2129725, EBI-3915253 | |
BINARY | Q8N8N0 | GJA8 P48165 | 3 | EBI-2129725, EBI-17458373 | |
BINARY | Q8N8N0 | KIR2DL3 P43628 | 3 | EBI-2129725, EBI-8632435 | |
BINARY | Q8N8N0 | LITAF Q99732 | 3 | EBI-2129725, EBI-725647 | |
BINARY | Q8N8N0 | TSPAN12 O95859 | 3 | EBI-2129725, EBI-2466403 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for zinc finger, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Zinc finger | 12-55 | RING-type | ||||
Sequence: CQICFNYYSPRRRPKLLDCKHTCCSVCLQQMRTSQKDVRCPWCR | ||||||
Region | 106-165 | Necessary for interaction with RRAGA | ||||
Sequence: ISKERALLPGDMGCRLLPGSQQKSVTVVTIPAEQQPLQGGAPQEAVEEEQDRRGVVKSST |
Sequence similarities
Belongs to the RNF152 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length203
- Mass (Da)22,357
- Last updated2002-10-01 v1
- Checksum0DFA570D00744BFA
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
K7EMG3 | K7EMG3_HUMAN | RNF152 | 114 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 12 | in Ref. 1; BAG53711 | ||||
Sequence: C → S |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK096495 EMBL· GenBank· DDBJ | BAC04805.1 EMBL· GenBank· DDBJ | mRNA | ||
AK122758 EMBL· GenBank· DDBJ | BAG53711.1 EMBL· GenBank· DDBJ | mRNA | ||
AC105094 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC094004 EMBL· GenBank· DDBJ | AAH94004.1 EMBL· GenBank· DDBJ | mRNA | ||
BC111956 EMBL· GenBank· DDBJ | AAI11957.1 EMBL· GenBank· DDBJ | mRNA |