Q08E39 · SPY2_BOVIN

  • Protein
    Protein sprouty homolog 2
  • Gene
    SPRY2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    3/5

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).

Features

Showing features for site.

131520406080100120140160180200220240260280300
TypeIDPosition(s)Description
Site144-145Cleavage; by FAP

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytosol
Cellular Componentmicrotubule
Cellular Componentruffle membrane
Biological Processanimal organ development
Biological Processnegative regulation of epithelial to mesenchymal transition
Biological Processnegative regulation of ERK1 and ERK2 cascade
Biological Processnegative regulation of fibroblast growth factor receptor signaling pathway
Biological Processnegative regulation of lens fiber cell differentiation
Biological Processnegative regulation of protein ubiquitination
Biological Processnegative regulation of Ras protein signal transduction
Biological Processnegative regulation of transforming growth factor beta receptor signaling pathway

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Protein sprouty homolog 2
  • Short names
    Spry-2

Gene names

    • Name
      SPRY2

Organism names

  • Taxonomic identifier
  • Strain
    • Hereford
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos

Accessions

  • Primary accession
    Q08E39

Proteomes

Organism-specific databases

Subcellular Location

Note: Associated with microtubules in unstimulated cells but is translocated to the membrane ruffles in cells stimulated with EGF (epidermal growth factor).

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00002952991-315Protein sprouty homolog 2

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).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for compositional bias, region, domain.

TypeIDPosition(s)Description
Compositional bias1-18Polar residues
Region1-38Disordered
Region51-140Disordered
Compositional bias73-87Basic and acidic residues
Compositional bias106-140Polar residues
Region118-315Required for interaction with CAV1
Domain177-291SPR
Region178-315Required for interaction with TESK1

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 status
    Complete
  • Length
    315
  • Mass (Da)
    34,569
  • Last updated
    2006-10-31 v1
  • Checksum
    27AE6A0AC0A5D592
MEARAQSGSGSQPLLQAPRDSGRQRGEPDPRDALPQQVHVLSLDQIRAIRNTNEYTEGPTVLPRAGLKPAPRPTAQHKHERLHGLPEPRQPSRPQHPPAHPSARASLARSISTVSSGSRSSTRTSTSSSSSEQRLLGSSFSSGPLADRIIRVQPKSELKPGELKPLSKEDVGLHAYKCEDCGKCKCKECTYPRPLPSDWICDKQCLCSAQNVIDYGTCVCCVKGLFYHCSNDDEDNCADNPCSCSQSHCCTRWSAMGVMSLFLPCLWCYLPAKGCLKLCQGCYDRVNRPGCRCKNSNTVCCKVPTVPPRNFEKPT

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0AAA9SRX0A0AAA9SRX0_BOVINSPRY2294

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-18Polar residues
Compositional bias73-87Basic and acidic residues
Compositional bias106-140Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BC123435
EMBL· GenBank· DDBJ
AAI23436.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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