Protein detail

RHG24

Rho GTPase-activating protein 24 (Filamin-A-associated RhoGAP) (FilGAP) (RAC1- and CDC42-specific GTPase-activating protein of 72 kDa) (RC-GAP72) (Rho-type GTPase-activating protein 24) (RhoGAP of 73 kDa) (Sarcoma antigen NY-SAR-88) (p73RhoGAP)

Entry name
RHG24
UniProt ID
EVMP confidence score
0.38
Supporting publications (n)
1
Transmembrane count
Protein classification
Predicted intracellular proteins
EVMP confidence score

Annotation confidence score; open for threshold definitions.

Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
Basic Information11
Protein Names
Rho GTPase-activating protein 24 (Filamin-A-associated RhoGAP) (FilGAP) (RAC1- and CDC42-specific GTPase-activating protein of 72 kDa) (RC-GAP72) (Rho-type GTPase-activating protein 24) (RhoGAP of 73 kDa) (Sarcoma antigen NY-SAR-88) (p73RhoGAP)
Protein Class
Predicted intracellular proteins
Protein Function
Predicted intracellular proteins
Entrez Gene Symbol
Gene Synonym (3)
DKFZP564B1162FilGAPFLJ33877
Gene Description
Rho GTPase activating protein 24
Chromosome
4
Position
85475150-86002668
Supporting publications (n)
1
EVMP confidence score
0.38
Fluorescence & Localization5
Tissue Specificblood vesselCell SpecificFibro-adipogenic progenitorsSingle-Nuclei Brain Specificendothelial cellSecretome LocationSecreted to extracellular matrixSecretome FunctionNo annotated function
Function & Pathway6
Relations & Evidence21

Enzyme-Mediated Modification (11)

11 records.

Substrate Gene SymbolEnzyme Gene SymbolEnzyme UniProt IDResidue TypeResidue OffsetModificationDatabaseReferences
ARHGAP24ROCK1Q13464S574phosphorylationMIMPHPRD_MIMPSIGNORProtMapperHPRDKEASIGNOR_ProtMapperProtMapper:16862148HPRD:16862148SIGNOR:16862148KEA:16862148
ARHGAP24ROCK1Q13464T576phosphorylationMIMPHPRD_MIMPSIGNORProtMapperHPRDKEASIGNOR_ProtMapperProtMapper:16862148HPRD:16862148SIGNOR:16862148KEA:16862148
ARHGAP24ROCK1Q13464S415phosphorylationPhosphoSite_MIMPMIMPHPRD_MIMPSIGNORProtMapperHPRDKEASIGNOR_ProtMapperPhosphoSitePhosphoSite_ProtMapperProtMapper:16862148HPRD:16862148SIGNOR:16862148KEA:16862148
ARHGAP24ROCK1Q13464T577phosphorylationMIMPHPRD_MIMPSIGNORProtMapperHPRDKEASIGNOR_ProtMapperProtMapper:16862148HPRD:16862148SIGNOR:16862148KEA:16862148
ARHGAP24ROCK1Q13464S437phosphorylationPhosphoSite_MIMPMIMPHPRD_MIMPSIGNORProtMapperHPRDKEASIGNOR_ProtMapperPhosphoSitePhosphoSite_ProtMapperProtMapper:16862148HPRD:16862148SIGNOR:16862148KEA:16862148
ARHGAP24ROCK1Q13464S413phosphorylationPhosphoSite_MIMPMIMPHPRD_MIMPSIGNORProtMapperHPRDKEASIGNOR_ProtMapperPhosphoSitePhosphoSite_ProtMapperProtMapper:16862148HPRD:16862148SIGNOR:16862148KEA:16862148
ARHGAP24ROCK1Q13464S402phosphorylationPhosphoSite_MIMPMIMPHPRD_MIMPSIGNORProtMapperHPRDKEASIGNOR_ProtMapperPhosphoSitePhosphoSite_ProtMapperProtMapper:16862148HPRD:16862148SIGNOR:16862148KEA:16862148
ARHGAP24ROCK1Q13464S573phosphorylationMIMPHPRD_MIMPSIGNORProtMapperHPRDKEASIGNOR_ProtMapperProtMapper:16862148HPRD:16862148SIGNOR:16862148KEA:16862148
ARHGAP24ROCK1Q13464T575phosphorylationMIMPHPRD_MIMPSIGNORProtMapperHPRDKEASIGNOR_ProtMapperProtMapper:16862148HPRD:16862148SIGNOR:16862148KEA:16862148
ARHGAP24ROCK1Q13464T452phosphorylationPhosphoSite_MIMPMIMPHPRD_MIMPSIGNORProtMapperHPRDKEASIGNOR_ProtMapperPhosphoSitePhosphoSite_ProtMapperProtMapper:16862148HPRD:16862148SIGNOR:16862148KEA:16862148
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Ligand-Receptor Signaling (4)

4 records.

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

Regulatory Interaction Network (1)

1 record.

Source Protein SymbolSource UniProt IDTarget Protein SymbolTarget UniProt IDIs DirectedIs StimulationIs InhibitionDatabaseReferences
ROCK1Q13464RHG24Q8N264YesYesNoAdhesomeMIMPPhosphoSite_MIMPHPRD_MIMPPhosphoSite_norefSIGNORiPTMnetProtMapperHPRDKEAHPRD_KEASIGNOR_ProtMapperPhosphoSiteHPRD-phosPhosphoSite_ProtMapperAdhesome:16862148HPRD:16862148HPRD-phos:16862148PhosphoSite:16862148PhosphoSite:26359494ProtMapper:16862148KEA:16862148SIGNOR:16862148

Isolation & Detection Technology (1)

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Polymer PrecipitationWestern blotting138731868
Sequence, Structure & Domains10

Sequences

Length
748
Mass
84,258
Sequence
MEENNDSTENPQQGQGRQNAIKCGWLRKQGGFVKTWHTRWFVLKGDQLYYFKDEDETKPLGTIFLPGNKVSEHPCNEENPGKFLFEVVPGGDRDRMTANHESYLLMASTQNDMEDWVKSIRRVIWGPFGGGIFGQKLEDTVRYEKRYGNRLAPMLVEQCVDFIRQRGLKEEGLFRLPGQANLVKELQDAFDCGEKPSFDSNTDVHTVASLLKLYLRELPEPVIPYAKYEDFLSCAKLLSKEEEAGVKELAKQVKSLPVVNYNLLKYICRFLDEVQSYSGVNKMSVQNLATVFGPNILRPKVEDPLTIMEGTVVVQQLMSVMISKHDCLFPKDAELQSKPQDGVSNNNEIQKKATMGQLQNKENNNTKDSPSRQCSWDKSESPQRSSMNNGSPTALSGSKTNSPKNSVHKLDVSRSPPLMVKKNPAFNKGSGIVTNGSFSSSNAEGLEKTQTTPNGSLQARRSSSLKVSGTKMGTHSVQNGTVRMGILNSDTLGNPTNVRNMSWLPNGYVTLRDNKQKEQAGELGQHNRLSTYDNVHQQFSMMNLDDKQSIDSATWSTSSCEISLPENSNSCRSSTTTCPEQDFFGGNFEDPVLDGPPQDDLSHPRDYESKSDHRSVGGRSSRATSSSDNSETFVGNSSSNHSALHSLVSSLKQEMTKQKIEYESRIKSLEQRNLTLETEMMSLHDELDQERKKFTMIEIKMRNAERAKEDAEKRNDMLQKEMEQFFSTFGELTVEPRRTERGNTIWIQ
Alternative Products
Event=Alternative splicing; Named isoforms=5; Name=1; IsoId=Q8N264-1; Sequence=Displayed; Name=2; IsoId=Q8N264-2; Sequence=VSP_023712, VSP_023715; Name=3; IsoId=Q8N264-3; Sequence=VSP_023711; Name=4; IsoId=Q8N264-4; Sequence=VSP_023717, VSP_023718; Name=5; IsoId=Q8N264-5; Sequence=VSP_023713, VSP_023714, VSP_023716
Alternative Sequence
1..95; Missing (in isoform 3); 1..93; Missing (in isoform 2); 1; M -> MWLRKKDWQIFNEQFLKKEHAVGFCFSKCVLVEFSLKCFKKIKSSYWNNDALAFLGKKFLREKNKMTKKQTRNRQNKFPPKPALRSSPVHRVQHFPLLWKVKEPHYHLFFFAFSYCWSWEPFPSEQQPCPASVLSSQQGKSISLIM (in isoform 5); 91..94; GDRD -> KIFS (in isoform 5); 94..130; DRMTANHESYLLMASTQNDMEDWVKSIRRVIWGPFGG -> MPEDRNSGGCPAGALASTPFIPKTTYRRIKRCFSFRK (in isoform 2); 95..748; Missing (in isoform 5); 245..246; GV -> VS (in isoform 4); 247..748; Missing (in isoform 4)

Domain & Motif Annotations

Compositional Bias
7..18; Polar residues; 356..374; Polar residues; 382..405; Polar residues; 432..476; Polar residues; 600..615; Basic and acidic residues; 617..641; Low complexity
Coiled Coil
649..729
Domain (CC)
The coiled coil domain mediates the interaction with FLNA leading to its recruitment to lamellae.
Domain (FT)
19..125; PH; 135..329; Rho-GAP
Region
1..20; Disordered; 354..476; Disordered; 582..641; Disordered
Clinical Relevance1
Antibody
Supporting Publications1
PMIDTitleAbstract
34265469Proteomic Landscape of Exosomes Reveals the Functional Contributions of CD151 in Triple-Negative Breast Cancer.Furthermore, utilizing quantitative proteomics approach to reveal the proteomes of CD151-deleted exosomes and cells, we found that exosomal CD151 facilitated secretion of ribosomal proteins via exosomes while inhibiting exosome secretion of complement proteins. Moreover, we proved that CD151-deleted exosomes significantly decreased the migration and invasion of TNBC cells. Most importantly, we found that the tetraspanin CD151 expression levels in TNBC-derived serum exosomes were significantly higher than those exosomes from healthy subjects, and we validated our findings with samples from 16 additional donors. This is the first comparative study of the proteomes of TNBC patient-derived and CD151-deleted exosomes.