Q8TEJ3 · SH3R3_HUMAN
- ProteinE3 ubiquitin-protein ligase SH3RF3
- GeneSH3RF3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids882 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Has E3 ubiquitin-protein ligase activity.
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 | |
---|---|---|
Molecular Function | metal ion binding | |
Molecular Function | ubiquitin protein ligase activity | |
Biological Process | positive regulation of JNK cascade | |
Biological Process | positive regulation of proteasomal ubiquitin-dependent protein catabolic process | |
Biological Process | protein autoubiquitination | |
Biological Process | protein ubiquitination |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameE3 ubiquitin-protein ligase SH3RF3
- 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 accessionQ8TEJ3
- Secondary accessions
Proteomes
Organism-specific databases
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 73 | Significant reduction in autoubiquitination; when associated with A-75. | ||||
Sequence: C → A | ||||||
Mutagenesis | 75 | Significant reduction in autoubiquitination; when associated with A-73. | ||||
Sequence: H → A | ||||||
Mutagenesis | 403 | Significant loss of interaction with RAC1; alone or when associated with P-404 and A-406. | ||||
Sequence: I → N | ||||||
Mutagenesis | 404 | Reduced JNK activation. Significant loss of interaction with RAC1; alone or when associated with N-403 and A-406. | ||||
Sequence: S → P | ||||||
Mutagenesis | 406 | Significant loss of interaction with RAC1; when associated with N-403 and P-404. | ||||
Sequence: P → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 986 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, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000284883 | 1-882 | UniProt | E3 ubiquitin-protein ligase SH3RF3 | |||
Sequence: MLLGASWLCASKAAAAAAQSEGDEDRPGERRRRRAAATAAGAGEDMDESSLLDLLECSVCLERLDTTAKVLPCQHTFCRRCLESIVCSRHELRCPECRILVGCGVDELPANILLVRLLDGIRQRPRAGTSPGGSPPARPIPGQSAAPTLAGGGGGAAGSTPGSPVFLSAAAGSTAGSLRELATSRTAPAAKNPCLLPYGKALYSYEGKEPGDLKFNKGDIIVLRRKVDEQWYHGELHGTQGFLPASYIQCIQPLPHAPPQGKALYDFEMKDKDQDKDCLTFTKDEILTVLRRVDENWAEGMLGDKIGIFPLLYVELNDSAKQLIEMDKPCPAAASSCNASLPSDSGAVASVAPSPTLSSSGAVSAFQRRVDGKKNTKKRHSFTALSVTHRSSQAASHRHSMEISAPVLISSSDPRAAARIGDLAHLSCAAPTQDVSSSAGSTPTAVPRAASVSGEQGTPPKVQLPLNVYLALYAYKPQKSDELELHKGEMYRVLEKCQDGWFKGASLRTGVSGVFPGNYVTPVSRVPAGGAGPPRNNVVGGSPLAKGITTTMHPGSGSLSSLATATRPALPITTPQAHAQHPTASPPTGSCLRHSAQPTASQARSTISTAAHSAAQAQDRPTATVSPLRTQNSPSRLPATSLRPHSVVSPQHSHQPPVQMCPRPAIPLTSAASAITPPNVSAANLNGEAGGGPIGVLSTSSPTNTGCKLDEKKSEKKEKKSGLLKLLAGASTKKKSRSPPSVSPTHDPQVAVDALLQGAVGPEVSSLSIHGRAGSCPIESEMQGAMGMEPLHRKAGSLDLNFTSPSRQAPLSMAAIRPEPKLLPRERYRVVVSYPPQSEAEIELKEGDIVFVHKKREDGWYKGTLQRNGRTGLFPGSFVESF | |||||||
Modified residue (large scale data) | 381 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 400 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 400 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 458 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 736 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 743 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 797 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 797 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 803 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 804 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 881 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Autoubiquitinated.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts (via SH3 domain 3) with PAK2 (PubMed:16374509).
Interacts with RAC1 (GTP-bound form) (PubMed:20696164).
Interacts with RAC1 (GTP-bound form) (PubMed:20696164).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q8TEJ3 | PAK2 Q13177 | 2 | EBI-7975674, EBI-1045887 | |
BINARY | Q8TEJ3 | RAC1 P63000 | 6 | EBI-7975674, EBI-413628 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, zinc finger, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 18-42 | Disordered | ||||
Sequence: AQSEGDEDRPGERRRRRAAATAAGA | ||||||
Compositional bias | 22-38 | Basic and acidic residues | ||||
Sequence: GDEDRPGERRRRRAAAT | ||||||
Zinc finger | 57-98 | RING-type | ||||
Sequence: CSVCLERLDTTAKVLPCQHTFCRRCLESIVCSRHELRCPECR | ||||||
Region | 124-159 | Disordered | ||||
Sequence: RPRAGTSPGGSPPARPIPGQSAAPTLAGGGGGAAGS | ||||||
Domain | 194-253 | SH3 1 | ||||
Sequence: CLLPYGKALYSYEGKEPGDLKFNKGDIIVLRRKVDEQWYHGELHGTQGFLPASYIQCIQP | ||||||
Domain | 256-319 | SH3 2 | ||||
Sequence: HAPPQGKALYDFEMKDKDQDKDCLTFTKDEILTVLRRVDENWAEGMLGDKIGIFPLLYVELNDS | ||||||
Region | 368-399 | Disordered | ||||
Sequence: RRVDGKKNTKKRHSFTALSVTHRSSQAASHRH | ||||||
Region | 369-439 | Interaction with RAC1 | ||||
Sequence: RVDGKKNTKKRHSFTALSVTHRSSQAASHRHSMEISAPVLISSSDPRAAARIGDLAHLSCAAPTQDVSSSA | ||||||
Compositional bias | 385-399 | Polar residues | ||||
Sequence: LSVTHRSSQAASHRH | ||||||
Region | 433-458 | Disordered | ||||
Sequence: QDVSSSAGSTPTAVPRAASVSGEQGT | ||||||
Domain | 464-525 | SH3 3 | ||||
Sequence: LPLNVYLALYAYKPQKSDELELHKGEMYRVLEKCQDGWFKGASLRTGVSGVFPGNYVTPVSR | ||||||
Compositional bias | 575-656 | Polar residues | ||||
Sequence: PQAHAQHPTASPPTGSCLRHSAQPTASQARSTISTAAHSAAQAQDRPTATVSPLRTQNSPSRLPATSLRPHSVVSPQHSHQP | ||||||
Region | 575-664 | Disordered | ||||
Sequence: PQAHAQHPTASPPTGSCLRHSAQPTASQARSTISTAAHSAAQAQDRPTATVSPLRTQNSPSRLPATSLRPHSVVSPQHSHQPPVQMCPRP | ||||||
Region | 693-747 | Disordered | ||||
Sequence: PIGVLSTSSPTNTGCKLDEKKSEKKEKKSGLLKLLAGASTKKKSRSPPSVSPTHD | ||||||
Compositional bias | 708-723 | Basic and acidic residues | ||||
Sequence: KLDEKKSEKKEKKSGL | ||||||
Domain | 823-882 | SH3 4 | ||||
Sequence: LPRERYRVVVSYPPQSEAEIELKEGDIVFVHKKREDGWYKGTLQRNGRTGLFPGSFVESF |
Domain
The RING finger domain is required for ubiquitin ligase activity and autoubiquitination.
Sequence similarities
Belongs to the SH3RF family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length882
- Mass (Da)92,776
- Last updated2007-05-01 v2
- Checksum07DF961AF2C80A08
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 22-38 | Basic and acidic residues | ||||
Sequence: GDEDRPGERRRRRAAAT | ||||||
Compositional bias | 385-399 | Polar residues | ||||
Sequence: LSVTHRSSQAASHRH | ||||||
Compositional bias | 575-656 | Polar residues | ||||
Sequence: PQAHAQHPTASPPTGSCLRHSAQPTASQARSTISTAAHSAAQAQDRPTATVSPLRTQNSPSRLPATSLRPHSVVSPQHSHQP | ||||||
Compositional bias | 708-723 | Basic and acidic residues | ||||
Sequence: KLDEKKSEKKEKKSGL |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC010906 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC140485 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC139850 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC109344 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
DQ307286 EMBL· GenBank· DDBJ | ABC25188.1 EMBL· GenBank· DDBJ | mRNA | ||
AK074131 EMBL· GenBank· DDBJ | BAB84957.1 EMBL· GenBank· DDBJ | mRNA | ||
AL831825 EMBL· GenBank· DDBJ | CAD38539.1 EMBL· GenBank· DDBJ | mRNA |