Q812A2 · SRGP3_MOUSE
- ProteinSLIT-ROBO Rho GTPase-activating protein 3
- GeneSrgap3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1099 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
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 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 | cytoplasm | |
Cellular Component | glutamatergic synapse | |
Molecular Function | GTPase activator activity | |
Biological Process | negative regulation of cell migration | |
Biological Process | regulation of postsynapse assembly | |
Biological Process | signal transduction |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSLIT-ROBO Rho GTPase-activating protein 3
- Short namessrGAP3
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ812A2
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000056770 | 1-1099 | SLIT-ROBO Rho GTPase-activating protein 3 | |||
Sequence: MSSQTKFKKDKEIIAEYEAQIKEIRTQLVEQFKCLEQQSESRLQLLQDLQEFFRRKAEIELEYSRSLEKLAERFSSKIRSSREHQFKKDQYLLSPVNCWYLVLHQTRRESRDHATLNDIFMNNVIVRLSQISEDVIRLFKKSKEIGLQMHEELLKVTNELYTVMKTYHMYHAESISAESKLKEAEKQEEKQFNKSGELSMNLLRHEDRPQRRSSVKKIEKMKEKRQAKYSENKLKCTKARNDYLLNLAATNAAISKYYIHDVSDLIDCCDLGFHASLARTFRTYLSAEYNLETSRHEGLDVIENAVDNLDSRSDKHTVMDMCSQVFCPPLKFEFQPHMGDEVCQVSAQQPVQTELLMRYHQLQSRLATLKIENEEVRKTLDATMQTLQDMLTVEDFDVSDAFQHSRSTESIKSAASETYMSKINIAKRRANQQETEMFYFTKFKEYVNGSNLITKLQAKHDLLKQTLGEGERAECGTTRPPCLPPKPQKMRRPRPLSVYSHKLFNGSMEAFIKDSGQAIPLVAESCIRFINLYGLQQQGIFRVPGSQVEVNDIKNSFERGEDPLVDDQNERDINSVAGVLKLYFRGLENPLFPKERFQDLISTIKLENPADRVHPIQQILITLPRVVIVVMRYLFAFLNHLSQYSDENMMDPYNLAICFGPTLMHIPDGQDPVSCQAHVNEVIKTIIIHHEAIFPSPRELEGPVYEKCMAGGEEYCDSPHSEPGTIDEVDHDNGTEPHTSDEEVEQIEAIAKFDYVGRSPRELSFKKGASLLLYHRASEDWWEGRHNGVDGLIPHQYIVVQDMDDAFSDSLSQKADSEASSGPLLDDKASSKNDLQSPTEHISDYGFGGVMGRVRLRSDGAAIPRRRSGGDTHSPPRGLGPSIDTPPRAAACPSSPHKIPLSRGRIESPEKRRMATFGSAGSINYPDKKALTEGLSMRSTCGSTRHSSLGDHKSLEAEALAEDIEKTMSTALHELRELERQNTVKQAPDVVLDTLEPLKNPPGPISSEPASPLHTIVIRDPDAAMRRSSSSSTEMMTTFKPALSARLAGAQLRPPPMRPVRPVVQHRSSSSSSSGVGSPAVTPTEKMFPNSSSDKSGTM | ||||||
Modified residue | 817 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 820 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 821 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 837 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 858 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 954 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for domain, coiled coil, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 19-314 | F-BAR | ||||
Sequence: AQIKEIRTQLVEQFKCLEQQSESRLQLLQDLQEFFRRKAEIELEYSRSLEKLAERFSSKIRSSREHQFKKDQYLLSPVNCWYLVLHQTRRESRDHATLNDIFMNNVIVRLSQISEDVIRLFKKSKEIGLQMHEELLKVTNELYTVMKTYHMYHAESISAESKLKEAEKQEEKQFNKSGELSMNLLRHEDRPQRRSSVKKIEKMKEKRQAKYSENKLKCTKARNDYLLNLAATNAAISKYYIHDVSDLIDCCDLGFHASLARTFRTYLSAEYNLETSRHEGLDVIENAVDNLDSRSD | ||||||
Coiled coil | 352-392 | |||||
Sequence: QTELLMRYHQLQSRLATLKIENEEVRKTLDATMQTLQDMLT | ||||||
Region | 470-493 | Disordered | ||||
Sequence: GERAECGTTRPPCLPPKPQKMRRP | ||||||
Domain | 506-694 | Rho-GAP | ||||
Sequence: GSMEAFIKDSGQAIPLVAESCIRFINLYGLQQQGIFRVPGSQVEVNDIKNSFERGEDPLVDDQNERDINSVAGVLKLYFRGLENPLFPKERFQDLISTIKLENPADRVHPIQQILITLPRVVIVVMRYLFAFLNHLSQYSDENMMDPYNLAICFGPTLMHIPDGQDPVSCQAHVNEVIKTIIIHHEAIF | ||||||
Domain | 744-803 | SH3 | ||||
Sequence: VEQIEAIAKFDYVGRSPRELSFKKGASLLLYHRASEDWWEGRHNGVDGLIPHQYIVVQDM | ||||||
Compositional bias | 809-840 | Polar residues | ||||
Sequence: DSLSQKADSEASSGPLLDDKASSKNDLQSPTE | ||||||
Region | 809-846 | Disordered | ||||
Sequence: DSLSQKADSEASSGPLLDDKASSKNDLQSPTEHISDYG | ||||||
Region | 861-911 | Disordered | ||||
Sequence: AAIPRRRSGGDTHSPPRGLGPSIDTPPRAAACPSSPHKIPLSRGRIESPEK | ||||||
Coiled coil | 952-987 | |||||
Sequence: HKSLEAEALAEDIEKTMSTALHELRELERQNTVKQA | ||||||
Region | 994-1014 | Disordered | ||||
Sequence: TLEPLKNPPGPISSEPASPLH | ||||||
Region | 1045-1099 | Disordered | ||||
Sequence: ARLAGAQLRPPPMRPVRPVVQHRSSSSSSSGVGSPAVTPTEKMFPNSSSDKSGTM | ||||||
Compositional bias | 1064-1099 | Polar residues | ||||
Sequence: VQHRSSSSSSSGVGSPAVTPTEKMFPNSSSDKSGTM |
Domain
The F-BAR domain mediates oligomerization, binds membranes, and induces plasma membrane protrusions.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,099
- Mass (Da)124,420
- Last updated2003-06-01 v1
- ChecksumC033CD7DE43C1B2C
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 67 | in Ref. 4; AAK52474 | ||||
Sequence: L → V | ||||||
Sequence conflict | 122 | in Ref. 4; AAK52474 | ||||
Sequence: N → T | ||||||
Sequence conflict | 523 | in Ref. 2; BAC65558 | ||||
Sequence: A → V | ||||||
Compositional bias | 809-840 | Polar residues | ||||
Sequence: DSLSQKADSEASSGPLLDDKASSKNDLQSPTE | ||||||
Compositional bias | 1064-1099 | Polar residues | ||||
Sequence: VQHRSSSSSSSGVGSPAVTPTEKMFPNSSSDKSGTM |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |