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 Q8N264	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

Protein Class

Predicted intracellular proteins

Protein Function

Predicted intracellular proteins

Ensembl

ENSG00000138639

Entrez Gene Symbol

ARHGAP24

Gene Synonym (3)

DKFZP564B1162FilGAPFLJ33877

Gene Description

Rho GTPase activating protein 24

Chromosome

Position

85475150-86002668

Supporting publications (n)

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

Protein Function

Predicted intracellular proteins

Cellular Component (5)

Molecular Function (2)

Biological Process (3)

Reactome (5)

Mediation Categories (3)

Adhesion and uptake mediationFusion and delivery mediationReceptor-signaling mediation

Relations & Evidence21

Enzyme-Mediated Modification (11)

11 records.

Substrate Gene Symbol	Enzyme Gene Symbol	Enzyme UniProt ID	Residue Type	Residue Offset	Modification	Database	References
ARHGAP24	ROCK1	Q13464	S	391	phosphorylation	PhosphoSite_MIMPMIMPHPRD_MIMPSIGNORProtMapperHPRDKEASIGNOR_ProtMapperPhosphoSitePhosphoSite_ProtMapper	ProtMapper:16862148 HPRD:16862148 SIGNOR:16862148 KEA:16862148

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Ligand-Receptor Signaling (4)

4 records.

Category	Parent	Database	Transmitter	Receiver	Secreted	Plasma Membrane (Transmembrane)	Plasma Membrane (Peripheral)
intracellular	intracellular	ComPPI	No	No	No	No	No
intracellular	intracellular	GO_Intercell	No	No	No	No	No
intracellular	intracellular	UniProt_location	No	No	No	No	No
intracellular	intracellular	OmniPath	No	No	No	No	No

Regulatory Interaction Network (1)

1 record.

Source Protein Symbol	Source UniProt ID	Target Protein Symbol	Target UniProt ID	Is Directed	Is Stimulation	Is Inhibition	Database	References
ROCK1	Q13464	RHG24	Q8N264	Yes	Yes	No	AdhesomeMIMPPhosphoSite_MIMPHPRD_MIMPPhosphoSite_norefSIGNORiPTMnetProtMapperHPRDKEAHPRD_KEASIGNOR_ProtMapperPhosphoSiteHPRD-phosPhosphoSite_ProtMapper	Adhesome:16862148 HPRD:16862148 HPRD-phos:16862148 PhosphoSite:16862148 PhosphoSite:26359494 ProtMapper:16862148 KEA:16862148 SIGNOR:16862148

Protein Complex Composition (4)

4 records.

Component Gene Symbols	Component UniProt ID	Stoichiometry	Database
ARHGAP24 DKK1 RBM45 TK2 WBP4	O00142 O75554 O94907 Q8IUH3 Q8N264	0:0:0:0:0	hu.MAP2
ARHGAP24 CTNNBIP1 DKK1 GSTK1 RBM45 TK2 WBP4	O00142 O75554 O94907 Q8IUH3 Q8N264 Q9NSA3 Q9Y2Q3	0:0:0:0:0:0:0	hu.MAP2
ARHGAP24 CTNNBIP1 DKK1 GSTK1 RBM45 TK2	O00142 O94907 Q8IUH3 Q8N264 Q9NSA3 Q9Y2Q3	0:0:0:0:0:0	hu.MAP2
ARHGAP24 CTNNBIP1 DKK1 GSTK1 TK2	O00142 O94907 Q8N264 Q9NSA3 Q9Y2Q3	0:0:0:0:0	hu.MAP2

Isolation & Detection Technology (1)

1 record.

EV Isolation Method	Detection Method	Number of References	References
Polymer Precipitation	Western blotting	1	38731868

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

HPA014288

Supporting Publications1

PMID	Title	Abstract
34265469	Proteomic 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.