A6X8Z5 · RHG31_MOUSE
- ProteinRho GTPase-activating protein 31
- GeneArhgap31
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1425 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Functions as a GTPase-activating protein (GAP) for RAC1 and CDC42. Required for cell spreading, polarized lamellipodia formation and cell migration.
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 | focal adhesion | |
Cellular Component | lamellipodium | |
Molecular Function | GTPase activator activity | |
Molecular Function | SH3 domain binding | |
Biological Process | small GTPase-mediated signal transduction |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRho GTPase-activating protein 31
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionA6X8Z5
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 56 | 70% reduction of GAP activity; when associated with V-169. | ||||
Sequence: R → A | ||||||
Mutagenesis | 169 | 70% reduction of GAP activity; when associated with A-56. | ||||
Sequence: N → V |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 96 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000320115 | 1-1425 | Rho GTPase-activating protein 31 | |||
Sequence: MKNKGAKQKLKRKGAASAFGCDLTEYLESSGQDVPYVLKSCAEFIETHGIVDGIYRLSGITSNIQRLRQEFGSDQCPDLTREVYLQDIHCVGSLCKLYFRELPNPLLTYELYEKFTEAVSHRPEEGQLARIQNVILELPPPHYRTLEYLIRHLAHIASFSSKTNMHARNLALVWAPNLLRSKKIEATICNGDAAFLAVRVQQVVIEFILNHADQIFNGGAPGALQQDESRTITKSLTLPALSLPMKLVSLEEAQARSLATNHPARKERRENSLPEIVPPPFHTVLELPDNKRKLSSKSKKWKSIFNLGRSGSDSKSKLSRNGSVFVRGQRLSVEKATIRPAKSMDSLCSVPVEGKENKGNFSRTVTTGGFFIPATKMHASSTGSSCDLSKEGEWGQEGMPAGAEGGCEVGGQIRPLPEQLKVFRPIGDPESEQSAPKLLGMFYTSSDSPGKSVFTSSLFQMEPSPRHQRKALNISEPFAVSVPLRVSAVISTNSTPCRTPPKELQSLSSLEEFSFQGSESGGWPEEEKPLGAESFPGSVTKKAATEDTKPEPEVPGRAECSQSPPLDPGTQVEKKTLHVSLGSQVSKEAEKRPKAEKVMEESQGASQPKPSTPQESLGAGTEPLILHEMDEEDLAQALIWPEIQQELKIIESEEEFSSLPPAAQKTSPIPESSPAPFPFPEAPGSLPSSSAPREVWTRDAANQSIQEAAILTDREKLEPVCSLLESESQQELSPDPASLAPLEMLLFEKVSSPARIEIGGPRNLSPPLTPAPPPPTPLEEEPEVLLSKEGPDREDAARDSRTDVYTEQPTPKESPGIPTPCQREEAIASPNEKQNARHAVPENKGPGLPSPTKEVDIIPQEEGGAPHSAQEPSDCDEDDTVTDPAQHGLEMVEPWEEPQWVTSPLHSPTLKEVQESQTQGSQGHRLERRLCHRPSLRQSHSLDSKTTGNSHWTLEAPFSSSCANLETERNYEPLQPPAARTKIAGLEEKALKAFREFSGLKGLEVLPSQKGPSGIQPKPVETNFMGLAEGKEQEPQLELSNRQMKHSDVPGPDSSKESSPRAQDSTLPGEHPLQLQLKNTECGPSKGKHRPSSLNLDSATPIADLFRLENGAPFSSPGIELSELGDTKVTWMSSSHCKAAPWNSQDTQDLDIVAHTLTGRRNSAPVSVSAVRTSFMVKMCQAKAVPVIPPKIQYTQIPQPLPSQSTGEGGAQPLERSQEEPGSTPEIPQKSTKDDSPSSLGSPEEEQPKQETGASASRRQASITSCMYEGSSCSPEPSASTLASTQDAVVQCRKRTSETEPSGDNLLSSKLERASGGPKAFHRSRPGRPQSLILFPIMDHLPSSPTVIDSKVLLSPIRSPTQTVSPGLLCGELAENTWITPEGVTLRNKMTIPKNGQRLETSTSCFYQPQRRSVILDGRSGRQIE | ||||||
Modified residue | 272 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 283 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 343 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 346 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 384 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 464 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 666 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 685 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 690 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 765 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 769 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 776 | Phosphothreonine; by GSK3 | ||||
Sequence: T | ||||||
Modified residue | 961 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1092 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1093 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1163 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated on Thr-776 by GSK3; which reduces GAP activity.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed at highest levels in heart and lung.
Induction
By serum (at protein level).
Gene expression databases
Interaction
Subunit
Interacts with ITSN1, which inhibits GAP activity. Interacts with PARVA. Interacts with GTP-loaded RHOU (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | A6X8Z5 | Itsn1 Q9Z0R4 | 3 | EBI-4325995, EBI-645386 | |
XENO | A6X8Z5 | RHOU Q7L0Q8 | 2 | EBI-4325995, EBI-1638043 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 21-216 | Rho-GAP | ||||
Sequence: CDLTEYLESSGQDVPYVLKSCAEFIETHGIVDGIYRLSGITSNIQRLRQEFGSDQCPDLTREVYLQDIHCVGSLCKLYFRELPNPLLTYELYEKFTEAVSHRPEEGQLARIQNVILELPPPHYRTLEYLIRHLAHIASFSSKTNMHARNLALVWAPNLLRSKKIEATICNGDAAFLAVRVQQVVIEFILNHADQIF | ||||||
Region | 258-277 | Disordered | ||||
Sequence: LATNHPARKERRENSLPEIV | ||||||
Region | 511-621 | Disordered | ||||
Sequence: EEFSFQGSESGGWPEEEKPLGAESFPGSVTKKAATEDTKPEPEVPGRAECSQSPPLDPGTQVEKKTLHVSLGSQVSKEAEKRPKAEKVMEESQGASQPKPSTPQESLGAGT | ||||||
Compositional bias | 585-599 | Basic and acidic residues | ||||
Sequence: VSKEAEKRPKAEKVM | ||||||
Compositional bias | 604-618 | Polar residues | ||||
Sequence: GASQPKPSTPQESLG | ||||||
Region | 652-700 | Disordered | ||||
Sequence: SEEEFSSLPPAAQKTSPIPESSPAPFPFPEAPGSLPSSSAPREVWTRDA | ||||||
Compositional bias | 671-685 | Pro residues | ||||
Sequence: ESSPAPFPFPEAPGS | ||||||
Region | 756-951 | Disordered | ||||
Sequence: IEIGGPRNLSPPLTPAPPPPTPLEEEPEVLLSKEGPDREDAARDSRTDVYTEQPTPKESPGIPTPCQREEAIASPNEKQNARHAVPENKGPGLPSPTKEVDIIPQEEGGAPHSAQEPSDCDEDDTVTDPAQHGLEMVEPWEEPQWVTSPLHSPTLKEVQESQTQGSQGHRLERRLCHRPSLRQSHSLDSKTTGNSH | ||||||
Compositional bias | 765-780 | Pro residues | ||||
Sequence: SPPLTPAPPPPTPLEE | ||||||
Compositional bias | 782-806 | Basic and acidic residues | ||||
Sequence: PEVLLSKEGPDREDAARDSRTDVYT | ||||||
Compositional bias | 902-924 | Polar residues | ||||
Sequence: TSPLHSPTLKEVQESQTQGSQGH | ||||||
Compositional bias | 925-939 | Basic and acidic residues | ||||
Sequence: RLERRLCHRPSLRQS | ||||||
Region | 1031-1095 | Disordered | ||||
Sequence: KEQEPQLELSNRQMKHSDVPGPDSSKESSPRAQDSTLPGEHPLQLQLKNTECGPSKGKHRPSSLN | ||||||
Compositional bias | 1053-1081 | Polar residues | ||||
Sequence: DSSKESSPRAQDSTLPGEHPLQLQLKNTE | ||||||
Region | 1196-1260 | Disordered | ||||
Sequence: QIPQPLPSQSTGEGGAQPLERSQEEPGSTPEIPQKSTKDDSPSSLGSPEEEQPKQETGASASRRQ | ||||||
Compositional bias | 1197-1260 | Polar residues | ||||
Sequence: IPQPLPSQSTGEGGAQPLERSQEEPGSTPEIPQKSTKDDSPSSLGSPEEEQPKQETGASASRRQ | ||||||
Region | 1291-1327 | Disordered | ||||
Sequence: QCRKRTSETEPSGDNLLSSKLERASGGPKAFHRSRPG |
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,425
- Mass (Da)155,276
- Last updated2007-08-21 v1
- Checksum00A39A0664D1A558
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 292 | in Ref. 2; BAE33406 | ||||
Sequence: R → K | ||||||
Compositional bias | 585-599 | Basic and acidic residues | ||||
Sequence: VSKEAEKRPKAEKVM | ||||||
Compositional bias | 604-618 | Polar residues | ||||
Sequence: GASQPKPSTPQESLG | ||||||
Compositional bias | 671-685 | Pro residues | ||||
Sequence: ESSPAPFPFPEAPGS | ||||||
Compositional bias | 765-780 | Pro residues | ||||
Sequence: SPPLTPAPPPPTPLEE | ||||||
Compositional bias | 782-806 | Basic and acidic residues | ||||
Sequence: PEVLLSKEGPDREDAARDSRTDVYT | ||||||
Compositional bias | 902-924 | Polar residues | ||||
Sequence: TSPLHSPTLKEVQESQTQGSQGH | ||||||
Compositional bias | 925-939 | Basic and acidic residues | ||||
Sequence: RLERRLCHRPSLRQS | ||||||
Compositional bias | 1053-1081 | Polar residues | ||||
Sequence: DSSKESSPRAQDSTLPGEHPLQLQLKNTE | ||||||
Sequence conflict | 1153 | in Ref. 2; BAE38872/BAE38901 | ||||
Sequence: V → F | ||||||
Compositional bias | 1197-1260 | Polar residues | ||||
Sequence: IPQPLPSQSTGEGGAQPLERSQEEPGSTPEIPQKSTKDDSPSSLGSPEEEQPKQETGASASRRQ | ||||||
Sequence conflict | 1365 | in Ref. 2; BAE38872/BAE38901 | ||||
Sequence: S → C |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK138417 EMBL· GenBank· DDBJ | BAE23651.1 EMBL· GenBank· DDBJ | mRNA | ||
AK149975 EMBL· GenBank· DDBJ | BAE29205.1 EMBL· GenBank· DDBJ | mRNA | ||
AK150109 EMBL· GenBank· DDBJ | BAE29314.1 EMBL· GenBank· DDBJ | mRNA | ||
AK155729 EMBL· GenBank· DDBJ | BAE33406.1 EMBL· GenBank· DDBJ | mRNA | ||
AK166583 EMBL· GenBank· DDBJ | BAE38872.1 EMBL· GenBank· DDBJ | mRNA | ||
AK166622 EMBL· GenBank· DDBJ | BAE38901.1 EMBL· GenBank· DDBJ | mRNA | ||
AC154425 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CT009576 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AF151363 EMBL· GenBank· DDBJ | AAD38043.1 EMBL· GenBank· DDBJ | mRNA | ||
AK129309 EMBL· GenBank· DDBJ | BAC98119.1 EMBL· GenBank· DDBJ | mRNA |