Q812A2 · SRGP3_MOUSE

  • Protein
    SLIT-ROBO Rho GTPase-activating protein 3
  • Gene
    Srgap3
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

Function

function

GTPase-activating protein for RAC1 and perhaps CDC42, but not for RhoA small GTPase. May attenuate RAC1 signaling in neurons (By similarity).

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 Componentcytoplasm
Cellular Componentglutamatergic synapse
Molecular FunctionGTPase activator activity
Biological Processnegative regulation of cell migration
Biological Processregulation of postsynapse assembly
Biological Processsignal transduction

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    SLIT-ROBO Rho GTPase-activating protein 3
  • Short names
    srGAP3
  • Alternative names
    • Rho GTPase-activating protein 14
    • WAVE-associated Rac GTPase-activating protein (WRP)

Gene names

    • Name
      Srgap3
    • Synonyms
      Arhgap14, Kiaa0411, Srgap2

Organism names

  • Taxonomic identifier
  • Strains
    • BALB/cJ
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q812A2
  • Secondary accessions
    • Q80U09
    • Q8BKP4
    • Q8BLD0
    • Q925I2

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00000567701-1099SLIT-ROBO Rho GTPase-activating protein 3
Modified residue817Phosphoserine
Modified residue820Phosphoserine
Modified residue821Phosphoserine
Modified residue837Phosphoserine
Modified residue858Phosphoserine
Modified residue954Phosphoserine

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Homodimer (Probable). Forms a heterooligomer with SRGAP1 and SRGAP2 through its F-BAR domain. Interacts with WASF1. Probably interacts with ROBO1. Interacts with FASLG (By similarity).

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain, coiled coil, region, compositional bias.

TypeIDPosition(s)Description
Domain19-314F-BAR
Coiled coil352-392
Region470-493Disordered
Domain506-694Rho-GAP
Domain744-803SH3
Compositional bias809-840Polar residues
Region809-846Disordered
Region861-911Disordered
Coiled coil952-987
Region994-1014Disordered
Region1045-1099Disordered
Compositional bias1064-1099Polar residues

Domain

The F-BAR domain mediates oligomerization, binds membranes, and induces plasma membrane protrusions.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,099
  • Mass (Da)
    124,420
  • Last updated
    2003-06-01 v1
  • Checksum
    C033CD7DE43C1B2C
MSSQTKFKKDKEIIAEYEAQIKEIRTQLVEQFKCLEQQSESRLQLLQDLQEFFRRKAEIELEYSRSLEKLAERFSSKIRSSREHQFKKDQYLLSPVNCWYLVLHQTRRESRDHATLNDIFMNNVIVRLSQISEDVIRLFKKSKEIGLQMHEELLKVTNELYTVMKTYHMYHAESISAESKLKEAEKQEEKQFNKSGELSMNLLRHEDRPQRRSSVKKIEKMKEKRQAKYSENKLKCTKARNDYLLNLAATNAAISKYYIHDVSDLIDCCDLGFHASLARTFRTYLSAEYNLETSRHEGLDVIENAVDNLDSRSDKHTVMDMCSQVFCPPLKFEFQPHMGDEVCQVSAQQPVQTELLMRYHQLQSRLATLKIENEEVRKTLDATMQTLQDMLTVEDFDVSDAFQHSRSTESIKSAASETYMSKINIAKRRANQQETEMFYFTKFKEYVNGSNLITKLQAKHDLLKQTLGEGERAECGTTRPPCLPPKPQKMRRPRPLSVYSHKLFNGSMEAFIKDSGQAIPLVAESCIRFINLYGLQQQGIFRVPGSQVEVNDIKNSFERGEDPLVDDQNERDINSVAGVLKLYFRGLENPLFPKERFQDLISTIKLENPADRVHPIQQILITLPRVVIVVMRYLFAFLNHLSQYSDENMMDPYNLAICFGPTLMHIPDGQDPVSCQAHVNEVIKTIIIHHEAIFPSPRELEGPVYEKCMAGGEEYCDSPHSEPGTIDEVDHDNGTEPHTSDEEVEQIEAIAKFDYVGRSPRELSFKKGASLLLYHRASEDWWEGRHNGVDGLIPHQYIVVQDMDDAFSDSLSQKADSEASSGPLLDDKASSKNDLQSPTEHISDYGFGGVMGRVRLRSDGAAIPRRRSGGDTHSPPRGLGPSIDTPPRAAACPSSPHKIPLSRGRIESPEKRRMATFGSAGSINYPDKKALTEGLSMRSTCGSTRHSSLGDHKSLEAEALAEDIEKTMSTALHELRELERQNTVKQAPDVVLDTLEPLKNPPGPISSEPASPLHTIVIRDPDAAMRRSSSSSTEMMTTFKPALSARLAGAQLRPPPMRPVRPVVQHRSSSSSSSGVGSPAVTPTEKMFPNSSSDKSGTM

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
F6QZR7F6QZR7_MOUSESrgap3102
F8VPQ4F8VPQ4_MOUSESrgap31099
E9QN14E9QN14_MOUSESrgap31075

Sequence caution

The sequence AAK52474.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.
The sequence AAK52474.1 differs from that shown. Reason: Frameshift
The sequence BAC34580.1 differs from that shown. Reason: Miscellaneous discrepancy Intron retention.
The sequence BAC65558.1 differs from that shown. Reason: Erroneous initiation Extended N-terminus.
The sequence BAC65558.1 differs from that shown. Reason: Miscellaneous discrepancy Probable cloning artifact. Aberrant splice sites.

Features

Showing features for sequence conflict, compositional bias.

TypeIDPosition(s)Description
Sequence conflict67in Ref. 4; AAK52474
Sequence conflict122in Ref. 4; AAK52474
Sequence conflict523in Ref. 2; BAC65558
Compositional bias809-840Polar residues
Compositional bias1064-1099Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF496547
EMBL· GenBank· DDBJ
AAM46845.1
EMBL· GenBank· DDBJ
mRNA
AK122276
EMBL· GenBank· DDBJ
BAC65558.1
EMBL· GenBank· DDBJ
mRNA Sequence problems.
AK045508
EMBL· GenBank· DDBJ
BAC32400.1
EMBL· GenBank· DDBJ
mRNA
AK051262
EMBL· GenBank· DDBJ
BAC34580.1
EMBL· GenBank· DDBJ
mRNA Sequence problems.
AF338472
EMBL· GenBank· DDBJ
AAK52474.1
EMBL· GenBank· DDBJ
mRNA Frameshift

Genome annotation databases

Similar Proteins

Disclaimer

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