A3KGS3 · RGPA2_MOUSE
- ProteinRal GTPase-activating protein subunit alpha-2
- GeneRalgapa2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1872 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalytic subunit of the heterodimeric RalGAP2 complex which acts as a GTPase activator for the Ras-like small GTPases RALA and RALB.
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 | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | nucleus | |
Molecular Function | GTPase activator activity | |
Molecular Function | protein heterodimerization activity | |
Biological Process | activation of GTPase activity | |
Biological Process | Ral protein signal transduction | |
Biological Process | regulation of exocyst localization | |
Biological Process | regulation of protein localization | |
Biological Process | regulation of small GTPase mediated signal transduction |
Keywords
- Molecular function
Names & Taxonomy
Protein names
- Recommended nameRal GTPase-activating protein subunit alpha-2
- 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 accessionA3KGS3
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000286973 | 1-1872 | Ral GTPase-activating protein subunit alpha-2 | |||
Sequence: MFSRRSHGDVKKSTQKVLDPKKDVLTRLKHLRALLDNVDASDLKQFFETNYSQIYFIFYENFITLENSLKLKGNNKSQREELDSILFLFEKILQFLPERIFFRWHYQSIGSTLKKLLHTGNSIKIRCEGIRLFLLWLQALQTNCAEEQVLIFACLVPGFPAVLSSRGPCTLETLINPSPSIVDAKIYPEEITPLLPAISGEKIAEDQTCFFLQILLKYMVIQAASLEWKNKENQDTGFKFLFTLFRKYYLPHLFPSFTKLTNIYKPVLEIPHLRPKPVYVTVTRDNETIYSTKIPYMAARVVFIKWIVTFFLEKKYLTATQNTKNGVDVLPKIIQTVGGGAIQEKVPELDGAGSTEQDKSHSNSSTLSDRRLSNSSLCSIEEEHRTVYEMVQRILLSTRGYVNFVNEVFRQAFLLPSCEISVTRKVVQVYRKWILQNKPVFMEEPDKKDVAQEDADKLGLSETDSKEASSESSGHKRSSSWGRTYSFTSAMSRGCVTEEDNTNVKAGAQAMLQVFLTNAANVFLLEPCAEVPMLLREQVDASKAVLIIFRRMIMELTMNQKTWEQMLQILLRITEAVMQKPKDKHVKDLFAQSLAGLLFRTLIVAWIRANLCVYISRELWDDFLRVLSSLTEWEELITEWSNIMDSLTAVLARTVYGVEMTNLPLDKLSEQKEKKQRGKGCILEPQKGTAVGRSFSLSWRSHPDVTEPMRFRSATTSGAPGVEKARNTVRQKATEVEEFQQAESTAAADCDYLVVGQQQVPRSSSTSDITERLYSDSSQGQKVEHSQNLSSSEPKSVQESKGHVTHEHEGITMLVRRSSSPAELELKDDLQQAHGRCRQRQTSESTGSDTVVGYSNEAELPVSPWQACEEDPDLSTPTDAVADSDARHWLQLSPTDASNLTDSRECLADDCSIIAGGNLTGWHPDSAAVLWRRVLGILGDVNNIQSPKIHAKVFGYLYELWYKLAKIRDNLAISLDNQSSPSPPLLIPPLRMFASWLFKATTLPNEYKEGKLQAYKLICAMMTRRQDVLPNSDFLVHFYLVMHLGLTSEDQDVLNTIIKNCSPRFFSLGLPGFSMLVGDFITAAARVLSTDMLAAPRSEALTLLGSLVCFPNTYQEIPLLQSVPEVSDVVTGAEDVKHYLINILLKNATEEPNECARCIAICSLGVWICEELAQSASHPQVKDAINVIGVTLKFPNKIVAQVACDVLQLLVSYWEKLQMFETALPRKMAEILVATIAFLLPSAEYSSVETDKKFIVSLLLCLLDWCMALPVSALLHPVSTAVLEELHPSRAPLLDYIYRVLHCCVCGSSTYTQQSHYTLTLADLSSTDYDPFLPLANVRNSEPIQYHSSADLGNLLTVEEEKKRRSVELIPLTARMVMAHLVNHLGHYPLSGGPAVLHSLVSENHDNAHVEGTELSSEVFRSPNLQLFVFNDSTLISYLQTPAEGPAGGTSGGSLSDVRVIVRDISGKYSWDGKVLYGPLEGRLAPNGRNPSFQISGWHHHTCGPQKDLFNGEEGDDVLDKLLENIGHTSPECLLPSQLNLNEPSPTPCAMNWDQEKAIMEVILRQSAQEDEYVQRCNSDSSVTVTSQGQPSPVEPRGPFYFCRLLLDDLGMNSWDRRKNFHLLKKNSKLLRELKNLDSRQCRETHKIAVFYIAEGQEDKCSILANERGSQAYEDFVAGLGWEVDLSTHCGFMGGLQRNGSTGQTAPYYATSTVEVIFHVSTRMPSDSDDSLTKKLRHLGNDEVHIVWSEHSRDYRRGIIPTAFGDVSIIIYPMKNHMFFITITKKPEVPFFGPLFDGAIVSGKLLPSLICATCINASRAVKCLIPLYQSFYEERALYLEAIIQNHREVMTFEDFAAQVFSPSPSYSVSGTD | ||||||
Modified residue | 373 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 376 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 379 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 486 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 696 | Phosphoserine; by PKB | ||||
Sequence: S | ||||||
Modified residue | 715 | Phosphothreonine; by PKB | ||||
Sequence: T | ||||||
Modified residue | 819 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 820 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1592 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Abundantly expressed in testis, pancreas, lung, thymus, brown fat, and white fat.
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 350-370 | Disordered | ||||
Sequence: DGAGSTEQDKSHSNSSTLSDR | ||||||
Compositional bias | 356-370 | Polar residues | ||||
Sequence: EQDKSHSNSSTLSDR | ||||||
Compositional bias | 445-473 | Basic and acidic residues | ||||
Sequence: PDKKDVAQEDADKLGLSETDSKEASSESS | ||||||
Region | 445-481 | Disordered | ||||
Sequence: PDKKDVAQEDADKLGLSETDSKEASSESSGHKRSSSW | ||||||
Region | 711-730 | Disordered | ||||
Sequence: FRSATTSGAPGVEKARNTVR | ||||||
Compositional bias | 758-798 | Polar residues | ||||
Sequence: QQVPRSSSTSDITERLYSDSSQGQKVEHSQNLSSSEPKSVQ | ||||||
Region | 758-813 | Disordered | ||||
Sequence: QQVPRSSSTSDITERLYSDSSQGQKVEHSQNLSSSEPKSVQESKGHVTHEHEGITM | ||||||
Compositional bias | 799-813 | Basic and acidic residues | ||||
Sequence: ESKGHVTHEHEGITM | ||||||
Region | 831-851 | Disordered | ||||
Sequence: QQAHGRCRQRQTSESTGSDTV | ||||||
Compositional bias | 836-851 | Polar residues | ||||
Sequence: RCRQRQTSESTGSDTV | ||||||
Domain | 1634-1842 | Rap-GAP | ||||
Sequence: LKNLDSRQCRETHKIAVFYIAEGQEDKCSILANERGSQAYEDFVAGLGWEVDLSTHCGFMGGLQRNGSTGQTAPYYATSTVEVIFHVSTRMPSDSDDSLTKKLRHLGNDEVHIVWSEHSRDYRRGIIPTAFGDVSIIIYPMKNHMFFITITKKPEVPFFGPLFDGAIVSGKLLPSLICATCINASRAVKCLIPLYQSFYEERALYLEAI |
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
A3KGS3-1
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
- Length1,872
- Mass (Da)210,288
- Last updated2007-05-15 v2
- ChecksumCCB0AA23790D863A
A3KGS3-2
- Name2
- Differences from canonical
- 1789-1807: VPFFGPLFDGAIVSGKLLP → LLLKIEKFHSLGPCSMERS
- 1808-1872: Missing
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A2I3BPN8 | A0A2I3BPN8_MOUSE | Ralgapa2 | 1957 | ||
A0A0A0MQD7 | A0A0A0MQD7_MOUSE | Ralgapa2 | 1910 | ||
F7AI67 | F7AI67_MOUSE | Ralgapa2 | 834 | ||
F7CGP0 | F7CGP0_MOUSE | Ralgapa2 | 1567 |
Sequence caution
Features
Showing features for compositional bias, sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 356-370 | Polar residues | ||||
Sequence: EQDKSHSNSSTLSDR | ||||||
Sequence conflict | 436 | in Ref. 2; BAC30146 | ||||
Sequence: Q → R | ||||||
Compositional bias | 445-473 | Basic and acidic residues | ||||
Sequence: PDKKDVAQEDADKLGLSETDSKEASSESS | ||||||
Sequence conflict | 447 | in Ref. 2; BAE34270 | ||||
Sequence: K → E | ||||||
Compositional bias | 758-798 | Polar residues | ||||
Sequence: QQVPRSSSTSDITERLYSDSSQGQKVEHSQNLSSSEPKSVQ | ||||||
Compositional bias | 799-813 | Basic and acidic residues | ||||
Sequence: ESKGHVTHEHEGITM | ||||||
Compositional bias | 836-851 | Polar residues | ||||
Sequence: RCRQRQTSESTGSDTV | ||||||
Sequence conflict | 1511 | in Ref. 4; AAH53994 | ||||
Sequence: N → H | ||||||
Sequence conflict | 1727 | in Ref. 5; BAD32418 | ||||
Sequence: D → V | ||||||
Alternative sequence | VSP_025251 | 1789-1807 | in isoform 2 | |||
Sequence: VPFFGPLFDGAIVSGKLLP → LLLKIEKFHSLGPCSMERS | ||||||
Alternative sequence | VSP_025252 | 1808-1872 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL845273 EMBL· GenBank· DDBJ | CAM46125.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AL845430 EMBL· GenBank· DDBJ | CAM46125.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AL935056 EMBL· GenBank· DDBJ | CAM46125.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AL845273 EMBL· GenBank· DDBJ | CAX15311.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL845430 EMBL· GenBank· DDBJ | CAX15311.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL935056 EMBL· GenBank· DDBJ | CAX15311.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL845430 EMBL· GenBank· DDBJ | CAM46200.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AL845273 EMBL· GenBank· DDBJ | CAM46200.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AL935056 EMBL· GenBank· DDBJ | CAM46200.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AL845430 EMBL· GenBank· DDBJ | CAX15398.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL845273 EMBL· GenBank· DDBJ | CAX15398.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL935056 EMBL· GenBank· DDBJ | CAX15398.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL935056 EMBL· GenBank· DDBJ | CAM46007.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AL845273 EMBL· GenBank· DDBJ | CAM46007.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AL845430 EMBL· GenBank· DDBJ | CAM46007.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AL935056 EMBL· GenBank· DDBJ | CAX15696.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL845273 EMBL· GenBank· DDBJ | CAX15696.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL845430 EMBL· GenBank· DDBJ | CAX15696.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK038838 EMBL· GenBank· DDBJ | BAC30146.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
AK157932 EMBL· GenBank· DDBJ | BAE34270.1 EMBL· GenBank· DDBJ | mRNA | ||
BC053994 EMBL· GenBank· DDBJ | AAH53994.1 EMBL· GenBank· DDBJ | mRNA | ||
BC096528 EMBL· GenBank· DDBJ | AAH96528.1 EMBL· GenBank· DDBJ | mRNA | ||
AK173140 EMBL· GenBank· DDBJ | BAD32418.1 EMBL· GenBank· DDBJ | mRNA |