Protein detail

RHG15

Rho GTPase-activating protein 15 (ArhGAP15) (Rho-type GTPase-activating protein 15)

Entry name
RHG15
UniProt ID
EVMP score
0.50
Frequency
1
Transmembrane count
Protein classification
EVMP score: annotation confidence score.
Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
Basic Information
Protein Names
Rho GTPase-activating protein 15 (ArhGAP15) (Rho-type GTPase-activating protein 15)
Protein Function
Predicted intracellular proteins
Entrez Gene Symbol
Frequency
1
EVMP Score
0.50
Fluorescence & Localization
Function & Pathway
Relations & Evidence

Enzyme-Mediated Modification

4 records.

Substrate Gene SymbolEnzyme Gene SymbolEnzyme UniProt IDResidue TypeResidue OffsetModificationDatabaseReferences
ARHGAP15PAK2Q13177S292phosphorylationPhosphoSite
ARHGAP15PAK2Q13177S4phosphorylationPhosphoSite
ARHGAP15PAK2Q13177S43phosphorylationPhosphoSite
ARHGAP15PAK2Q13177S41phosphorylationPhosphoSite

Ligand-Receptor Signaling

4 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
intracellularintracellularComPPINoNoNoNoNo
intracellularintracellularGO_IntercellNoNoNoNoNo
intracellularintracellularUniProt_locationNoNoNoNoNo
intracellularintracellularOmniPathNoNoNoNoNo

Regulatory Interaction Network

2 records.

Source Protein SymbolSource UniProt IDTarget Protein SymbolTarget UniProt IDIs DirectedIs StimulationIs InhibitionDatabaseReferences
RHG15Q53QZ3RAC1P63000YesNoYesHPRDSPIKE_LCSIGNORHPRD:12650940SPIKE_LC:12650940SIGNOR:32203420
PAK2Q13177RHG15Q53QZ3YesNoNoPhosphoSite_norefPhosphoSitePhosphoSite_ProtMapperProtMapperPhosphoSite:23760270

Protein Complex Composition

1 record.

Component NameComponent Gene SymbolsComponent UniProt IDStoichiometryDatabaseDatabase IDsReferences
ARHGAP15Q53QZ34PDBPDB:3byi

Isolation & Detection Technology

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationUltrafiltration / Tangential Flow FiltrationSize Exclusion ChromatographyData-Dependent Acquisition LC-MS/MS;Gel-LC-MS/MS23279541426801919
Sequence, Structure & Domains

Sequences

Length
475
Mass
54,544
Sequence
MQKSTNSDTSVETLNSTRQGTGAVQMRIKNANSHHDRLSQSKSMILTDVGKVTEPISRHRRNHSQHILKDVIPPLEQLMVEKEGYLQKAKIADGGKKLRKNWSTSWIVLSSRRIEFYKESKQQALSNMKTGHKPESVDLCGAHIEWAKEKSSRKNVFQITTVSGNEFLLQSDIDFIILDWFHAIKNAIDRLPKDSSCPSRNLELFKIQRSSSTELLSHYDSDIKEQKPEHRKSLMFRLHHSASDTSDKNRVKSRLKKFITRRPSLKTLQEKGLIKDQIFGSHLHKVCERENSTVPWFVKQCIEAVEKRGLDVDGIYRVSGNLATIQKLRFIVNQEEKLNLDDSQWEDIHVVTGALKMFFRELPEPLFPYSFFEQFVEAIKKQDNNTRIEAVKSLVQKLPPPNRDTMKVLFGHLTKIVAKASKNLMSTQSLGIVFGPTLLRAENETGNMAIHMVYQNQIAELMLSEYSKIFGSEED

3D Structural Models

Turn
309..311; 313..317
Helix
265..270; 283..290; 296..308; 322..333; 343..345; 348..361; 369..379; 384..397; 400..418; 420..423; 427..439; 448..464; 466..470
Beta Strand
362..364; 381..383; 444..446
3D Structure
X-ray crystallography (1)

Domain & Motif Annotations

Compositional Bias
1..22; Polar residues
Domain (CC)
The PH domain is required for localization to the membrane.
Domain (FT)
79..189; PH; 281..470; Rho-GAP
Region
1..23; Disordered
Clinical Relevance