O43295 · SRGP3_HUMAN
- ProteinSLIT-ROBO Rho GTPase-activating protein 3
- GeneSRGAP3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1099 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
GTPase-activating protein for RAC1 and perhaps Cdc42, but not for RhoA small GTPase. May attenuate RAC1 signaling in neurons.
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 | cytosol | |
Cellular Component | postsynapse | |
Molecular Function | GTPase activator activity | |
Biological Process | negative regulation of cell migration | |
Biological Process | regulation of small GTPase mediated signal transduction | |
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
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO43295
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Disease & Variants
Involvement in disease
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_035550 | 623 | in a breast cancer sample; somatic mutation | |||
Sequence: L → I | ||||||
Natural variant | VAR_049159 | 628 | in dbSNP:rs2271207 | |||
Sequence: I → V |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,146 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, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000056769 | 1-1099 | UniProt | SLIT-ROBO Rho GTPase-activating protein 3 | |||
Sequence: MSSQTKFKKDKEIIAEYEAQIKEIRTQLVEQFKCLEQQSESRLQLLQDLQEFFRRKAEIELEYSRSLEKLAERFSSKIRSSREHQFKKDQYLLSPVNCWYLVLHQTRRESRDHATLNDIFMNNVIVRLSQISEDVIRLFKKSKEIGLQMHEELLKVTNELYTVMKTYHMYHAESISAESKLKEAEKQEEKQFNKSGDLSMNLLRHEDRPQRRSSVKKIEKMKEKRQAKYSENKLKCTKARNDYLLNLAATNAAISKYYIHDVSDLIDCCDLGFHASLARTFRTYLSAEYNLETSRHEGLDVIENAVDNLDSRSDKHTVMDMCNQVFCPPLKFEFQPHMGDEVCQVSAQQPVQTELLMRYHQLQSRLATLKIENEEVRKTLDATMQTLQDMLTVEDFDVSDAFQHSRSTESVKSAASETYMSKINIAKRRANQQETEMFYFTKFKEYVNGSNLITKLQAKHDLLKQTLGEGERAECGTTRPPCLPPKPQKMRRPRPLSVYSHKLFNGSMEAFIKDSGQAIPLVVESCIRYINLYGLQQQGIFRVPGSQVEVNDIKNSFERGEDPLVDDQNERDINSVAGVLKLYFRGLENPLFPKERFQDLISTIKLENPAERVHQIQQILVTLPRVVIVVMRYLFAFLNHLSQYSDENMMDPYNLAICFGPTLMHIPDGQDPVSCQAHINEVIKTIIIHHEAIFPSPRELEGPVYEKCMAGGEEYCDSPHSEPGAIDEVDHDNGTEPHTSDEEVEQIEAIAKFDYMGRSPRELSFKKGASLLLYHRASEDWWEGRHNGVDGLIPHQYIVVQDMDDAFSDSLSQKADSEASSGPLLDDKASSKNDLQSPTEHISDYGFGGVMGRVRLRSDGAAIPRRRSGGDTHSPPRGLGPSIDTPPRAAACPSSPHKIPLTRGRIESPEKRRMATFGSAGSINYPDKKALSEGHSMRSTCGSTRHSSLGDHKSLEAEALAEDIEKTMSTALHELRELERQNTVKQAPDVVLDTLEPLKNPPGPVSSEPASPLHTIVIRDPDAAMRRSSSSSTEMMTTFKPALSARLAGAQLRPPPMRPVRPVVQHRSSSSSSSGVGSPAVTPTEKMFPNSSADKSGTM | |||||||
Modified residue | 817 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 820 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 821 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 837 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 837 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 858 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 858 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 868 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 872 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 874 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 895 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 919 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 954 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 954 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1070 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Highly expressed in adult and fetal brain. Expressed at low levels in kidney. Isoform 3 is expressed in the kidney but is absent in the brain.
Gene expression databases
Organism-specific 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.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | O43295 | Amph O08838 | 3 | EBI-368166, EBI-80080 | |
BINARY | O43295 | GRB2 P62993 | 2 | EBI-368166, EBI-401755 | |
BINARY | O43295 | HTT P42858 | 4 | EBI-368166, EBI-466029 | |
XENO | O43295 | Sh3gl1 O35964 | 3 | EBI-368166, EBI-1149235 | |
XENO | O43295 | Sh3gl2 O35179 | 3 | EBI-368166, EBI-1149197 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, coiled coil, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 19-314 | F-BAR | ||||
Sequence: AQIKEIRTQLVEQFKCLEQQSESRLQLLQDLQEFFRRKAEIELEYSRSLEKLAERFSSKIRSSREHQFKKDQYLLSPVNCWYLVLHQTRRESRDHATLNDIFMNNVIVRLSQISEDVIRLFKKSKEIGLQMHEELLKVTNELYTVMKTYHMYHAESISAESKLKEAEKQEEKQFNKSGDLSMNLLRHEDRPQRRSSVKKIEKMKEKRQAKYSENKLKCTKARNDYLLNLAATNAAISKYYIHDVSDLIDCCDLGFHASLARTFRTYLSAEYNLETSRHEGLDVIENAVDNLDSRSD | ||||||
Region | 205-225 | Disordered | ||||
Sequence: HEDRPQRRSSVKKIEKMKEKR | ||||||
Coiled coil | 352-392 | |||||
Sequence: QTELLMRYHQLQSRLATLKIENEEVRKTLDATMQTLQDMLT | ||||||
Region | 471-493 | Disordered | ||||
Sequence: ERAECGTTRPPCLPPKPQKMRRP | ||||||
Domain | 482-670 | Rho-GAP | ||||
Sequence: CLPPKPQKMRRPRPLSVYSHKLFNGSMEAFIKDSGQAIPLVVESCIRYINLYGLQQQGIFRVPGSQVEVNDIKNSFERGEDPLVDDQNERDINSVAGVLKLYFRGLENPLFPKERFQDLISTIKLENPAERVHQIQQILVTLPRVVIVVMRYLFAFLNHLSQYSDENMMDPYNLAICFGPTLMHIPDGQ | ||||||
Domain | 744-803 | SH3 | ||||
Sequence: VEQIEAIAKFDYMGRSPRELSFKKGASLLLYHRASEDWWEGRHNGVDGLIPHQYIVVQDM | ||||||
Compositional bias | 809-840 | Polar residues | ||||
Sequence: DSLSQKADSEASSGPLLDDKASSKNDLQSPTE | ||||||
Region | 809-847 | Disordered | ||||
Sequence: DSLSQKADSEASSGPLLDDKASSKNDLQSPTEHISDYGF | ||||||
Region | 861-911 | Disordered | ||||
Sequence: AAIPRRRSGGDTHSPPRGLGPSIDTPPRAAACPSSPHKIPLTRGRIESPEK | ||||||
Region | 926-950 | Disordered | ||||
Sequence: PDKKALSEGHSMRSTCGSTRHSSLG | ||||||
Coiled coil | 952-987 | |||||
Sequence: HKSLEAEALAEDIEKTMSTALHELRELERQNTVKQA | ||||||
Region | 995-1099 | Disordered | ||||
Sequence: LEPLKNPPGPVSSEPASPLHTIVIRDPDAAMRRSSSSSTEMMTTFKPALSARLAGAQLRPPPMRPVRPVVQHRSSSSSSSGVGSPAVTPTEKMFPNSSADKSGTM | ||||||
Compositional bias | 1025-1039 | Polar residues | ||||
Sequence: MRRSSSSSTEMMTTF | ||||||
Compositional bias | 1064-1099 | Polar residues | ||||
Sequence: VQHRSSSSSSSGVGSPAVTPTEKMFPNSSADKSGTM |
Domain
The F-BAR domain mediates oligomerization, binds membranes, and induces plasma membrane protrusions.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
O43295-1
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
- SynonymsMEGAPa, srGAP3a
- Length1,099
- Mass (Da)124,504
- Last updated2004-06-07 v3
- Checksum2D1BA2D338E1BF13
O43295-2
- Name2
- SynonymsMEGAPb, srGAP3b
- Differences from canonical
- 480-513: PPCLPPKPQKMRRPRPLSVYSHKLFNGSMEAFIK → GRRNARTRNQ
O43295-3
- Name3
- SynonymsMEGAPc, srGAP3c
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_010582 | 480-489 | in isoform 3 | |||
Sequence: PPCLPPKPQK → IQDKLYRL | ||||||
Alternative sequence | VSP_010581 | 480-513 | in isoform 2 | |||
Sequence: PPCLPPKPQKMRRPRPLSVYSHKLFNGSMEAFIK → GRRNARTRNQ | ||||||
Alternative sequence | VSP_010583 | 490-1099 | in isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 809-840 | Polar residues | ||||
Sequence: DSLSQKADSEASSGPLLDDKASSKNDLQSPTE | ||||||
Compositional bias | 1025-1039 | Polar residues | ||||
Sequence: MRRSSSSSTEMMTTF | ||||||
Compositional bias | 1064-1099 | Polar residues | ||||
Sequence: VQHRSSSSSSSGVGSPAVTPTEKMFPNSSADKSGTM |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF464189 EMBL· GenBank· DDBJ | AAN57784.1 EMBL· GenBank· DDBJ | mRNA | ||
AF427144 EMBL· GenBank· DDBJ | AAN07095.1 EMBL· GenBank· DDBJ | mRNA | ||
AB007871 EMBL· GenBank· DDBJ | BAA24841.2 EMBL· GenBank· DDBJ | mRNA |