Q08E39 · SPY2_BOVIN
- ProteinProtein sprouty homolog 2
- GeneSPRY2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids315 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
function
Antagonist of fibroblast growth factor (FGF) pathways via inhibition of FGF-mediated phosphorylation of ERK1/2 (By similarity).
Thereby acts as an antagonist of FGF-induced retinal lens fiber differentiation, may inhibit limb bud outgrowth and may negatively modulate respiratory organogenesis (By similarity).
Inhibits TGFB-induced epithelial-to-mesenchymal transition in retinal lens epithelial cells (By similarity).
Inhibits CBL/C-CBL-mediated EGFR ubiquitination (By similarity).
Thereby acts as an antagonist of FGF-induced retinal lens fiber differentiation, may inhibit limb bud outgrowth and may negatively modulate respiratory organogenesis (By similarity).
Inhibits TGFB-induced epithelial-to-mesenchymal transition in retinal lens epithelial cells (By similarity).
Inhibits CBL/C-CBL-mediated EGFR ubiquitination (By similarity).
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 144-145 | Cleavage; by FAP | ||||
Sequence: PL |
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 | cytosol | |
Cellular Component | microtubule | |
Cellular Component | ruffle membrane | |
Biological Process | animal organ development | |
Biological Process | negative regulation of epithelial to mesenchymal transition | |
Biological Process | negative regulation of ERK1 and ERK2 cascade | |
Biological Process | negative regulation of fibroblast growth factor receptor signaling pathway | |
Biological Process | negative regulation of lens fiber cell differentiation | |
Biological Process | negative regulation of protein ubiquitination | |
Biological Process | negative regulation of Ras protein signal transduction | |
Biological Process | negative regulation of transforming growth factor beta receptor signaling pathway |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein sprouty homolog 2
- Short namesSpry-2
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos
Accessions
- Primary accessionQ08E39
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Associated with microtubules in unstimulated cells but is translocated to the membrane ruffles in cells stimulated with EGF (epidermal growth factor).
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000295299 | 1-315 | Protein sprouty homolog 2 | |||
Sequence: MEARAQSGSGSQPLLQAPRDSGRQRGEPDPRDALPQQVHVLSLDQIRAIRNTNEYTEGPTVLPRAGLKPAPRPTAQHKHERLHGLPEPRQPSRPQHPPAHPSARASLARSISTVSSGSRSSTRTSTSSSSSEQRLLGSSFSSGPLADRIIRVQPKSELKPGELKPLSKEDVGLHAYKCEDCGKCKCKECTYPRPLPSDWICDKQCLCSAQNVIDYGTCVCCVKGLFYHCSNDDEDNCADNPCSCSQSHCCTRWSAMGVMSLFLPCLWCYLPAKGCLKLCQGCYDRVNRPGCRCKNSNTVCCKVPTVPPRNFEKPT |
Post-translational modification
Cleaved at Pro-144 by the prolyl endopeptidase FAP (seprase) activity (in vitro).
Proteomic databases
Expression
Gene expression databases
Interaction
Subunit
Forms heterodimers with SPRY1 (By similarity).
Forms a tripartite complex containing GAB1, METTL13 and SPRY2 (By similarity).
Within the complex interacts with METTL13 (By similarity).
Interacts with RAF1 (By similarity).
Interacts (via C-terminus) with TESK1 (via C-terminus); the interaction disrupts SPRY2 interaction with GRB2, potentially via disruption of SPRY2 serine dephosphorylation (By similarity).
Interacts with PPP2R1A/PP2A-A and PPP2CA/PP2A-C; the interaction with PPP2CA/PP2A-C is inhibited by interaction with TESK1, possibly by vesicular sequestration of SPRY2 (By similarity).
Inhibition of the interaction with the serine/threonine-protein phosphatase 2A (PP2A) holoenzyme results in loss of PP2A-mediated dephosphorylation, resulting in the loss of SPRY2 interaction with GRB2 (By similarity).
Interacts with GRB2 (By similarity).
Interacts with CBL/C-CBL; the interaction inhibits CBL-mediated ubiquitination of EGFR (By similarity).
Interacts (via C-terminus) with CAV1 (via C-terminus) (By similarity).
Forms a tripartite complex containing GAB1, METTL13 and SPRY2 (By similarity).
Within the complex interacts with METTL13 (By similarity).
Interacts with RAF1 (By similarity).
Interacts (via C-terminus) with TESK1 (via C-terminus); the interaction disrupts SPRY2 interaction with GRB2, potentially via disruption of SPRY2 serine dephosphorylation (By similarity).
Interacts with PPP2R1A/PP2A-A and PPP2CA/PP2A-C; the interaction with PPP2CA/PP2A-C is inhibited by interaction with TESK1, possibly by vesicular sequestration of SPRY2 (By similarity).
Inhibition of the interaction with the serine/threonine-protein phosphatase 2A (PP2A) holoenzyme results in loss of PP2A-mediated dephosphorylation, resulting in the loss of SPRY2 interaction with GRB2 (By similarity).
Interacts with GRB2 (By similarity).
Interacts with CBL/C-CBL; the interaction inhibits CBL-mediated ubiquitination of EGFR (By similarity).
Interacts (via C-terminus) with CAV1 (via C-terminus) (By similarity).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-18 | Polar residues | ||||
Sequence: MEARAQSGSGSQPLLQAP | ||||||
Region | 1-38 | Disordered | ||||
Sequence: MEARAQSGSGSQPLLQAPRDSGRQRGEPDPRDALPQQV | ||||||
Region | 51-140 | Disordered | ||||
Sequence: NTNEYTEGPTVLPRAGLKPAPRPTAQHKHERLHGLPEPRQPSRPQHPPAHPSARASLARSISTVSSGSRSSTRTSTSSSSSEQRLLGSSF | ||||||
Compositional bias | 73-87 | Basic and acidic residues | ||||
Sequence: PTAQHKHERLHGLPE | ||||||
Compositional bias | 106-140 | Polar residues | ||||
Sequence: SLARSISTVSSGSRSSTRTSTSSSSSEQRLLGSSF | ||||||
Region | 118-315 | Required for interaction with CAV1 | ||||
Sequence: SRSSTRTSTSSSSSEQRLLGSSFSSGPLADRIIRVQPKSELKPGELKPLSKEDVGLHAYKCEDCGKCKCKECTYPRPLPSDWICDKQCLCSAQNVIDYGTCVCCVKGLFYHCSNDDEDNCADNPCSCSQSHCCTRWSAMGVMSLFLPCLWCYLPAKGCLKLCQGCYDRVNRPGCRCKNSNTVCCKVPTVPPRNFEKPT | ||||||
Domain | 177-291 | SPR | ||||
Sequence: KCEDCGKCKCKECTYPRPLPSDWICDKQCLCSAQNVIDYGTCVCCVKGLFYHCSNDDEDNCADNPCSCSQSHCCTRWSAMGVMSLFLPCLWCYLPAKGCLKLCQGCYDRVNRPGC | ||||||
Region | 178-315 | Required for interaction with TESK1 | ||||
Sequence: CEDCGKCKCKECTYPRPLPSDWICDKQCLCSAQNVIDYGTCVCCVKGLFYHCSNDDEDNCADNPCSCSQSHCCTRWSAMGVMSLFLPCLWCYLPAKGCLKLCQGCYDRVNRPGCRCKNSNTVCCKVPTVPPRNFEKPT |
Domain
The Cys-rich domain is responsible for the localization of the protein to the membrane ruffles.
Sequence similarities
Belongs to the sprouty family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length315
- Mass (Da)34,569
- Last updated2006-10-31 v1
- Checksum27AE6A0AC0A5D592
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0AAA9SRX0 | A0AAA9SRX0_BOVIN | SPRY2 | 294 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-18 | Polar residues | ||||
Sequence: MEARAQSGSGSQPLLQAP | ||||||
Compositional bias | 73-87 | Basic and acidic residues | ||||
Sequence: PTAQHKHERLHGLPE | ||||||
Compositional bias | 106-140 | Polar residues | ||||
Sequence: SLARSISTVSSGSRSSTRTSTSSSSSEQRLLGSSF |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BC123435 EMBL· GenBank· DDBJ | AAI23436.1 EMBL· GenBank· DDBJ | mRNA |