Q8C4V1 · RHG24_MOUSE
- ProteinRho GTPase-activating protein 24
- GeneArhgap24
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids747 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Rho GTPase-activating protein involved in cell polarity, cell morphology and cytoskeletal organization. Acts as a GTPase activator for the Rac-type GTPase by converting it to an inactive GDP-bound state. Controls actin remodeling by inactivating Rac downstream of Rho leading to suppress leading edge protrusion and promotes cell retraction to achieve cellular polarity. Able to suppress RAC1 and CDC42 activity in vitro. Overexpression induces cell rounding with partial or complete disruption of actin stress fibers and formation of membrane ruffles, lamellipodia, and filopodia. Isoform 2 is a vascular cell-specific GAP involved in modulation of angiogenesis (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 | adherens junction | |
Cellular Component | cell projection | |
Cellular Component | cytoplasm | |
Cellular Component | cytoskeleton | |
Cellular Component | focal adhesion | |
Molecular Function | GTPase activator activity | |
Biological Process | angiogenesis | |
Biological Process | cell differentiation | |
Biological Process | negative regulation of Rac protein signal transduction | |
Biological Process | negative regulation of ruffle assembly | |
Biological Process | Rac protein signal transduction | |
Biological Process | wound healing, spreading of epidermal cells |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRho GTPase-activating protein 24
- 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 accessionQ8C4V1
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localizes to actin stress fibers. In migrating cells, localizes to membrane lamellae and protusions (By similarity).
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000280474 | 1-747 | Rho GTPase-activating protein 24 | |||
Sequence: MEERCESTESPQGQGRKNTKCGWLRKQGGFVKTWHTRWFVLKGDQLYYFKDEDETKPLGTIFLHGNKVIEHPCNEENPGKFLFDVVPGGERDRMTANHESYLLMASTQNDMEDWVKSIRRVIWGPFGGGIFGQKLEDTVRYEKRYGNRLAPMLVEQCVDFIRQRGLKEEGLFRLPGQANLVKELQDAFDCGEKPSFDSNTDVHTVASLLKLYLRELPEPVVPYAKYEDFLSCATLLSKEEEAGVKELMKQVKSLPVVNYNLLKYICRFLDEVQSYSGVNKMSAQNLATVFGPNILRPKVEDPLTIMEGTVVVQQLMSVMISKHDRLFPKDTEPQSKPQDGPNSNNNDGHKKATMGQLQNKENNNTKESPVRRCSWDKPESPQRSSVDNGSPTALSGSKTNSPRNSIHKLDISRSPPLMVKKNPAFNKGSGIVTNGSFSSSNAEGVEKPQTTPNGSLQARRTSSLKSSGTKMGTHSVQNGTVRMGILNTDTLGNSLNGRSMSWLPNGYVTLRDNKQKEPAGESGQHNRLSTYDNVHQQFSSMSLDDKHSVDSATWSTSSCEISLPENSNSCRSSTTTCPEQDFYVGNFEDPVLDGPPQDDLSHPGDYENKSDRRSVGGRSSRATSSSDNSETFVGNTSSNHSALHSLVSSLKQEMTKQKIEYESRIKSLEQRNLTLETEMLSLHDELDQERKKFTMIEIKMRNAERAKEDAEKRNDMLQKEMEQFFSTFGDLTVEPRRSERGNTIWIQ | ||||||
Modified residue | 368 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 390 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 395 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 397 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 401 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 412 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 414 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 436 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 451 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 494 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated by ROCK, leading to activate the RacGAP activity.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-20 | Disordered | ||||
Sequence: MEERCESTESPQGQGRKNTK | ||||||
Domain | 17-123 | PH | ||||
Sequence: KNTKCGWLRKQGGFVKTWHTRWFVLKGDQLYYFKDEDETKPLGTIFLHGNKVIEHPCNEENPGKFLFDVVPGGERDRMTANHESYLLMASTQNDMEDWVKSIRRVIW | ||||||
Domain | 133-327 | Rho-GAP | ||||
Sequence: QKLEDTVRYEKRYGNRLAPMLVEQCVDFIRQRGLKEEGLFRLPGQANLVKELQDAFDCGEKPSFDSNTDVHTVASLLKLYLRELPEPVVPYAKYEDFLSCATLLSKEEEAGVKELMKQVKSLPVVNYNLLKYICRFLDEVQSYSGVNKMSAQNLATVFGPNILRPKVEDPLTIMEGTVVVQQLMSVMISKHDRLF | ||||||
Region | 327-475 | Disordered | ||||
Sequence: FPKDTEPQSKPQDGPNSNNNDGHKKATMGQLQNKENNNTKESPVRRCSWDKPESPQRSSVDNGSPTALSGSKTNSPRNSIHKLDISRSPPLMVKKNPAFNKGSGIVTNGSFSSSNAEGVEKPQTTPNGSLQARRTSSLKSSGTKMGTHS | ||||||
Compositional bias | 335-364 | Polar residues | ||||
Sequence: SKPQDGPNSNNNDGHKKATMGQLQNKENNN | ||||||
Compositional bias | 379-408 | Polar residues | ||||
Sequence: ESPQRSSVDNGSPTALSGSKTNSPRNSIHK | ||||||
Compositional bias | 427-475 | Polar residues | ||||
Sequence: KGSGIVTNGSFSSSNAEGVEKPQTTPNGSLQARRTSSLKSSGTKMGTHS | ||||||
Region | 581-639 | Disordered | ||||
Sequence: DFYVGNFEDPVLDGPPQDDLSHPGDYENKSDRRSVGGRSSRATSSSDNSETFVGNTSSN | ||||||
Compositional bias | 600-616 | Basic and acidic residues | ||||
Sequence: LSHPGDYENKSDRRSVG | ||||||
Compositional bias | 617-639 | Polar residues | ||||
Sequence: GRSSRATSSSDNSETFVGNTSSN | ||||||
Coiled coil | 648-728 | |||||
Sequence: SSLKQEMTKQKIEYESRIKSLEQRNLTLETEMLSLHDELDQERKKFTMIEIKMRNAERAKEDAEKRNDMLQKEMEQFFSTF |
Domain
The coiled coil domain mediates the interaction with FLNA leading to its recruitment to lamellae.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q8C4V1-1
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
- Length747
- Mass (Da)84,100
- Last updated2007-03-20 v2
- Checksum769982BA6B90D425
Q8C4V1-2
- Name2
Q8C4V1-3
- Name3
- Differences from canonical
- 1-93: Missing
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_023720 | 1-91 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_023719 | 1-93 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_023721 | 92-128 | in isoform 2 | |||
Sequence: DRMTANHESYLLMASTQNDMEDWVKSIRRVIWGPFGG → MPEDRNSGGRPSGALASTPFIPKTTYRRIKRCFSFRK | ||||||
Sequence conflict | 183 | in Ref. 1; BAC38105 | ||||
Sequence: E → K | ||||||
Compositional bias | 335-364 | Polar residues | ||||
Sequence: SKPQDGPNSNNNDGHKKATMGQLQNKENNN | ||||||
Compositional bias | 379-408 | Polar residues | ||||
Sequence: ESPQRSSVDNGSPTALSGSKTNSPRNSIHK | ||||||
Compositional bias | 427-475 | Polar residues | ||||
Sequence: KGSGIVTNGSFSSSNAEGVEKPQTTPNGSLQARRTSSLKSSGTKMGTHS | ||||||
Compositional bias | 600-616 | Basic and acidic residues | ||||
Sequence: LSHPGDYENKSDRRSVG | ||||||
Compositional bias | 617-639 | Polar residues | ||||
Sequence: GRSSRATSSSDNSETFVGNTSSN |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK039617 EMBL· GenBank· DDBJ | BAC30402.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK080986 EMBL· GenBank· DDBJ | BAC38105.1 EMBL· GenBank· DDBJ | mRNA | ||
BC023344 EMBL· GenBank· DDBJ | AAH23344.1 EMBL· GenBank· DDBJ | mRNA | ||
BC025502 EMBL· GenBank· DDBJ | AAH25502.1 EMBL· GenBank· DDBJ | mRNA | ||
BC027070 EMBL· GenBank· DDBJ | AAH27070.1 EMBL· GenBank· DDBJ | mRNA |