Q8TEC5 · SH3R2_HUMAN
- ProteinE3 ubiquitin-protein ligase SH3RF2
- GeneSH3RF2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids729 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Has E3 ubiquitin-protein ligase activity (PubMed:24130170).
Acts as an anti-apoptotic regulator of the JNK pathway by ubiquitinating and promoting the degradation of SH3RF1, a scaffold protein that is required for pro-apoptotic JNK activation (PubMed:22128169).
Facilitates TNF-alpha-mediated recruitment of adapter proteins TRADD and RIPK1 to TNFRSF1A and regulates PAK4 protein stability via inhibition of its ubiquitin-mediated proteasomal degradation (PubMed:24130170).
Inhibits PPP1CA phosphatase activity (PubMed:19389623, PubMed:19945436).
Acts as an anti-apoptotic regulator of the JNK pathway by ubiquitinating and promoting the degradation of SH3RF1, a scaffold protein that is required for pro-apoptotic JNK activation (PubMed:22128169).
Facilitates TNF-alpha-mediated recruitment of adapter proteins TRADD and RIPK1 to TNFRSF1A and regulates PAK4 protein stability via inhibition of its ubiquitin-mediated proteasomal degradation (PubMed:24130170).
Inhibits PPP1CA phosphatase activity (PubMed:19389623, PubMed:19945436).
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 | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | metal ion binding | |
Molecular Function | phosphatase binding | |
Molecular Function | protein phosphatase 1 binding | |
Molecular Function | protein phosphatase inhibitor activity | |
Molecular Function | ubiquitin protein ligase activity | |
Biological Process | negative regulation of apoptotic process | |
Biological Process | negative regulation of JNK cascade | |
Biological Process | negative regulation of protein ubiquitination | |
Biological Process | positive regulation of cell migration | |
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 SH3RF2
- 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 accessionQ8TEC5
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_052118 | 16 | in dbSNP:rs34739859 | |||
Sequence: F → S | ||||||
Natural variant | VAR_052119 | 174 | in dbSNP:rs34942619 | |||
Sequence: F → V | ||||||
Natural variant | VAR_029788 | 267 | in dbSNP:rs758037 | |||
Sequence: R → C | ||||||
Natural variant | VAR_052120 | 477 | in dbSNP:rs35165046 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_029789 | 592 | in dbSNP:rs2962525 | |||
Sequence: W → R | ||||||
Mutagenesis | 643 | Significant loss of interaction with PPP1CA. Significant loss of interaction with PPP1CA; when associated with G-645. | ||||
Sequence: V → G | ||||||
Mutagenesis | 645 | Significant loss of interaction with PPP1CA. Significant loss of interaction with PPP1CA; when associated with G-643. | ||||
Sequence: F → G | ||||||
Natural variant | VAR_029790 | 687 | in dbSNP:rs11435 | |||
Sequence: V → I | ||||||
Natural variant | VAR_029791 | 710 | in dbSNP:rs1056149 | |||
Sequence: G → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 969 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_0000269512 | 1-729 | UniProt | E3 ubiquitin-protein ligase SH3RF2 | |||
Sequence: MDDLTLLDLLECPVCFEKLDVTAKVLPCQHTFCKPCLQRVFKAHKELRCPECRTPVFSNIEALPANLLLVRLLDGVRSGQSSGRGGSFRRPGTMTLQDGRKSRTNPRRLQASPFRLVPNVRIHMDGVPRAKALCNYRGQNPGDLRFNKGDIILLRRQLDENWYQGEINGISGNFPASSVEVIKQLPQPPPLCRALYNFDLRGKDKSENQDCLTFLKDDIITVISRVDENWAEGKLGDKVGIFPILFVEPNLTARHLLEKNKGRQSSRTKNLSLVSSSSRGNTSTLRRGPGSRRKVPGQFSITTALNTLNRMVHSPSGRHMVEISTPVLISSSNPSVITQPMEKADVPSSCVGQVSTYHPAPVSPGHSTAVVSLPGSQQHLSANMFVALHSYSAHGPDELDLQKGEGVRVLGKCQDGWLRGVSLVTGRVGIFPNNYVIPIFRKTSSFPDSRSPGLYTTWTLSTSSVSSQGSISEGDPRQSRPFKSVFVPTAIVNPVRSTAGPGTLGQGSLRKGRSSMRKNGSLQRPLQSGIPTLVVGSLRRSPTMVLRPQQFQFYQPQGIPSSPSAVVVEMGSKPALTGEPALTCISRGSEAWIHSAASSLIMEDKEIPIKSEPLPKPPASAPPSILVKPENSRNGIEKQVKTVRFQNYSPPPTKHYTSHPTSGKPEQPATLKASQPEAASLGPEMTVLFAHRSGCHSGQQTDLRRKSALGKATTLVSTASGTQTVFPSK | |||||||
Modified residue (large scale data) | 112 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 508 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 649 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 649 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Autoubiquitinated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Heart (at protein level). Up-regulated in colon cancer tissues as compared to normal colon tissues (at protein level). Testis. In the heart, present in the apex, left atrium, right atrium, left ventricle and right ventricle, but not in the aorta.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with FASLG and PPP1CA (PubMed:19389623, PubMed:19807924, PubMed:19945436).
Interacts with PAK4 and TNFRSF1A (PubMed:24130170).
Interacts with DLK1, MAP3K10/MLK2, MAPK8IP1/JIP1, MAPK8IP2/JIP2 and MAPK8IP3/JIP3. Interacts with RAC1 (both active GTP- or inactive GDP-bound forms) (By similarity).
Interacts with PAK4 and TNFRSF1A (PubMed:24130170).
Interacts with DLK1, MAP3K10/MLK2, MAPK8IP1/JIP1, MAPK8IP2/JIP2 and MAPK8IP3/JIP3. Interacts with RAC1 (both active GTP- or inactive GDP-bound forms) (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q8TEC5 | AKAP8L Q9ULX6 | 3 | EBI-2130111, EBI-357530 | |
BINARY | Q8TEC5 | AMOTL2 Q9Y2J4 | 4 | EBI-2130111, EBI-746752 | |
BINARY | Q8TEC5 | BAG4 O95429 | 3 | EBI-2130111, EBI-2949658 | |
BINARY | Q8TEC5 | BANP Q8N9N5 | 3 | EBI-2130111, EBI-744695 | |
BINARY | Q8TEC5 | CCDC102B Q68D86 | 3 | EBI-2130111, EBI-10171570 | |
BINARY | Q8TEC5 | CYSRT1 A8MQ03 | 3 | EBI-2130111, EBI-3867333 | |
BINARY | Q8TEC5 | EFS O43281-2 | 3 | EBI-2130111, EBI-11525448 | |
BINARY | Q8TEC5 | GOLGA2 Q08379 | 4 | EBI-2130111, EBI-618309 | |
BINARY | Q8TEC5 | MTUS2 Q5JR59-3 | 4 | EBI-2130111, EBI-11522433 | |
BINARY | Q8TEC5 | NEK6 Q9HC98-4 | 3 | EBI-2130111, EBI-11750983 | |
BINARY | Q8TEC5 | PPP1CA P62136 | 3 | EBI-2130111, EBI-357253 | |
BINARY | Q8TEC5 | VPS37C A5D8V6 | 3 | EBI-2130111, EBI-2559305 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for zinc finger, region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Zinc finger | 12-53 | RING-type | ||||
Sequence: CPVCFEKLDVTAKVLPCQHTFCKPCLQRVFKAHKELRCPECR | ||||||
Region | 78-105 | Disordered | ||||
Sequence: SGQSSGRGGSFRRPGTMTLQDGRKSRTN | ||||||
Domain | 125-184 | SH3 1 | ||||
Sequence: DGVPRAKALCNYRGQNPGDLRFNKGDIILLRRQLDENWYQGEINGISGNFPASSVEVIKQ | ||||||
Domain | 187-252 | SH3 2 | ||||
Sequence: QPPPLCRALYNFDLRGKDKSENQDCLTFLKDDIITVISRVDENWAEGKLGDKVGIFPILFVEPNLT | ||||||
Region | 258-297 | Disordered | ||||
Sequence: EKNKGRQSSRTKNLSLVSSSSRGNTSTLRRGPGSRRKVPG | ||||||
Compositional bias | 266-288 | Polar residues | ||||
Sequence: SRTKNLSLVSSSSRGNTSTLRRG | ||||||
Region | 370-459 | Interaction with PAK4 | ||||
Sequence: VVSLPGSQQHLSANMFVALHSYSAHGPDELDLQKGEGVRVLGKCQDGWLRGVSLVTGRVGIFPNNYVIPIFRKTSSFPDSRSPGLYTTWT | ||||||
Domain | 380-441 | SH3 3 | ||||
Sequence: LSANMFVALHSYSAHGPDELDLQKGEGVRVLGKCQDGWLRGVSLVTGRVGIFPNNYVIPIFR | ||||||
Region | 497-526 | Disordered | ||||
Sequence: STAGPGTLGQGSLRKGRSSMRKNGSLQRPL | ||||||
Compositional bias | 499-526 | Polar residues | ||||
Sequence: AGPGTLGQGSLRKGRSSMRKNGSLQRPL | ||||||
Region | 610-677 | Disordered | ||||
Sequence: KSEPLPKPPASAPPSILVKPENSRNGIEKQVKTVRFQNYSPPPTKHYTSHPTSGKPEQPATLKASQPE | ||||||
Compositional bias | 636-669 | Polar residues | ||||
Sequence: IEKQVKTVRFQNYSPPPTKHYTSHPTSGKPEQPA | ||||||
Region | 641-646 | Interaction with PPP1CA | ||||
Sequence: KTVRFQ |
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 & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q8TEC5-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length729
- Mass (Da)79,320
- Last updated2010-05-18 v3
- ChecksumF85CCC0188DA8477
Q8TEC5-2
- Name2
Q8TEC5-3
- Name3
- Differences from canonical
- 1-543: Missing
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_022058 | 1-508 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_040662 | 1-543 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 148 | in Ref. 2; BAB85025 | ||||
Sequence: K → R | ||||||
Sequence conflict | 168 | in Ref. 2; BAB85025 | ||||
Sequence: N → S | ||||||
Compositional bias | 266-288 | Polar residues | ||||
Sequence: SRTKNLSLVSSSSRGNTSTLRRG | ||||||
Compositional bias | 499-526 | Polar residues | ||||
Sequence: AGPGTLGQGSLRKGRSSMRKNGSLQRPL | ||||||
Alternative sequence | VSP_022059 | 509-519 | in isoform 2 | |||
Sequence: LRKGRSSMRKN → MRKSKWWQRD | ||||||
Compositional bias | 636-669 | Polar residues | ||||
Sequence: IEKQVKTVRFQNYSPPPTKHYTSHPTSGKPEQPA |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK058046 EMBL· GenBank· DDBJ | BAB71639.1 EMBL· GenBank· DDBJ | mRNA | ||
AK074234 EMBL· GenBank· DDBJ | BAB85025.1 EMBL· GenBank· DDBJ | mRNA | Different termination. | |
AK292576 EMBL· GenBank· DDBJ | BAF85265.1 EMBL· GenBank· DDBJ | mRNA | ||
AC005216 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC005351 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC011359 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC091887 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC031650 EMBL· GenBank· DDBJ | AAH31650.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC073914 EMBL· GenBank· DDBJ | AAH73914.1 EMBL· GenBank· DDBJ | mRNA | ||
BC125106 EMBL· GenBank· DDBJ | AAI25107.1 EMBL· GenBank· DDBJ | mRNA |