Protein detail
ARAP1
Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 1 (Centaurin-delta-2) (Cnt-d2)
Entry name ARAP1 | UniProt ID | EVMP confidence score 0.72 |
Supporting publications (n) 11 | 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 >= 0.40Basic Information11
Protein Names
Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 1 (Centaurin-delta-2) (Cnt-d2)
Protein Class
Predicted intracellular proteins
Protein Function
Predicted intracellular proteins
Ensembl
Entrez Gene Symbol
Gene Synonym
CENTD2
Gene Description
ArfGAP with RhoGAP domain, ankyrin repeat and PH domain 1
Chromosome
11
Position
72685069-72793599
Supporting publications (n)
11
EVMP confidence score
0.72
Fluorescence & Localization4
Cell SpecificChoroid plexus epithelial cellsBlood Cell SpecificbasophilBlood Lineage Specificgranulocytes
Function & Pathway7
Protein Function
Predicted intracellular proteins
Cellular Component (8)
Molecular Function (5)
Biological Process (3)
Reactome (7)
Mediation Categories (2)
Fusion and delivery mediationReceptor-signaling mediation
Relations & Evidence14
Enzyme-Mediated Modification (2)
2 records.
| Substrate Gene Symbol | Enzyme Gene Symbol | Enzyme UniProt ID | Residue Type | Residue Offset | Modification | Database | References |
|---|---|---|---|---|---|---|---|
| ARAP1 | PTK6 | Q13882 | Y | 231 | phosphorylation | phosphoELM_MIMPPhosphoSite_MIMPMIMPHPRD_MIMPSIGNORProtMapperRLIMS-P_ProtMapperPhosphoSitePhosphoSite_ProtMapper | ProtMapper:20554524SIGNOR:20554524 |
| ARAP1 | HIPK4 | Q8NE63 | S | 648 | phosphorylation | PhosphoNetworks |
Ligand-Receptor Signaling (6)
6 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 |
| plasma_membrane | plasma_membrane | UniProt_location | No | No | No | No | No |
| plasma_membrane | plasma_membrane | OmniPath | No | No | No | No | No |
Regulatory Interaction Network (3)
3 records.
| Source Protein Symbol | Source UniProt ID | Target Protein Symbol | Target UniProt ID | Is Directed | Is Stimulation | Is Inhibition | Database | References |
|---|---|---|---|---|---|---|---|---|
| ARAP1 | Q96P48 | CDC42 | P60953 | Yes | No | Yes | SIGNOR | SIGNOR:32203420 |
| PTK6 | Q13882 | ARAP1 | Q96P48 | Yes | Yes | No | phosphoELM_MIMPPhosphoSite_MIMPMIMPHPRD_MIMPiPTMnetSIGNORProtMapperRLIMS-P_ProtMapperSIGNOR_ProtMapperPhosphoSitePhosphoSite_ProtMapper | PhosphoSite:20554524ProtMapper:20554524SIGNOR:20554524 |
| ARAP1 | Q96P48 | RAC1 | P63000 | Yes | No | Yes | WangSIGNOR | SIGNOR:32203420 |
Protein Complex Composition (2)
Isolation & Detection Technology (1)
Sequence, Structure & Domains11
Sequences
Length
1,450
Mass
162,192
Sequence
MAEAGDAALSVAEWLRALHLEQYTGLFEQHGLVWATECQGLSDTRLMDMGMLLPGHRRRILAGLLRAHTSPAPAPRPTPRPVPMKRHIFRSPPVPATPPEPLPTTTEDEGLPAAPPIPPRRSCLPPTCFTTPSTAAPDPVLPPLPAKRHLAELSVPPVPPRTGPPRLLVSLPTKEEESLLPSLSSPPQPQSEEPLSTLPQGPPQPPSPPPCPPEIPPKPVRLFPEFDDSDYDEVPEEGPGAPARVMTKKEEPPPSRVPRAVRVASLLSEGEELSGDDQGDEEEDDHAYEGVPNGGWHTSSLSLSLPSTIAAPHPMDGPPGGSTPVTPVIKAGWLDKNPPQGSYIYQKRWVRLDTDHLRYFDSNKDAYSKRFISVACISHVAAIGDQKFEVITNNRTFAFRAESDVERKEWMQALQQAMAEQRARARLSSAYLLGVPGSEQPDRAGSLELRGFKNKLYVAVVGDKVQLYKNLEEYHLGIGITFIDMSVGNVKEVDRRSFDLTTPYRIFSFSADSELEKEQWLEAMQGAIAEALSTSEVAERIWAAAPNRFCADCGAPQPDWASINLCVVICKRCAGEHRGLGAGVSKVRSLKMDRKVWTETLIELFLQLGNGAGNRFWAANVPPSEALQPSSSPSTRRCHLEAKYREGKYRRYHPLFGNQEELDKALCAAVTTTDLAETQALLGCGAGINCFSGDPEAPTPLALAEQAGQTLQMEFLRNNRTTEVPRLDSMKPLEKHYSVVLPTVSHSGFLYKTASAGKLLQDRRAREEFSRRWCVLGDGVLSYFENERAVTPNGEIRASEIVCLAVPPPDTHGFEHTFEVYTEGERLYLFGLESAEQAHEWVKCIAKAFVPPLAEDLLARDFERLGRLPYKAGLSLQRAQEGWFSLSGSELRAVFPEGPCEEPLQLRKLQELSIQGDSENQVLVLVERRRTLYIQGERRLDFMGWLGAIQKAAASMGDTLSEQQLGDSDIPVIVYRCVDYITQCGLTSEGIYRKCGQTSKTQRLLESLRQDARSVHLKEGEQHVDDVSSALKRFLRDLPDGLFTRAQRLTWLEASEIEDEEEKVSRYRELLVRLPPVNRATVKALISHLYCVQCFSDTNQMNVHNLAIVFGPTLFQTDGQDYKAGRVVEDLINHYVVVFSVDEEELRKQREEITAIVKMRVAGTASGTQHAGDFICTVYLEEKKAETEQHIKVPASMTAEELTLEILDRRNVGIREKDYWTCFEVNEREEAERPLHFAEKVLPILHGLGTDSHLVVKKHQAMEAMLLYLASRVGDTKHGMMKFREDRSLLGLGLPSGGFHDRYFILNSSCLRLYKEVRSQRPWSGAPETSHRPEKEWPIKSLKVYLGVKKKLRPPTCWGFTVVHETEKHEKQQWYLCCDTQMELREWFATFLFVQHDGLVWPSEPSRVSRAVPEVRLGSVSLIPLRGSENEMRRSVAAFTADPLSLLRNV
Alternative Products
Event=Alternative splicing; Named isoforms=7; Name=6; Synonyms=ARAP1b; IsoId=Q96P48-6; Sequence=Displayed; Name=1; IsoId=Q96P48-1; Sequence=VSP_036607, VSP_036608; Name=2; IsoId=Q96P48-2; Sequence=VSP_036607, VSP_036608, VSP_000311; Name=3; IsoId=Q96P48-3; Sequence=VSP_000311; Name=4; IsoId=Q96P48-4; Sequence=VSP_015000; Name=5; IsoId=Q96P48-5; Sequence=VSP_014998, VSP_015001, VSP_000311; Name=7; IsoId=Q96P48-7; Sequence=VSP_015000, VSP_043530, VSP_000311
Alternative Sequence
1..760; Missing (in isoform 5); 1..245; Missing (in isoform 4 and isoform 7); 1..240; Missing (in isoform 1 and isoform 2); 241..249; APARVMTKK -> MTLSGSRGQ (in isoform 1 and isoform 2); 604..664; Missing (in isoform 7); 761..767; QDRRARE -> MDASGKG (in isoform 5); 1320..1330; Missing (in isoform 2, isoform 3, isoform 5 and isoform 7)
3D Structural Models
3D Structure
X-ray crystallography (1)
Domain & Motif Annotations
Compositional Bias
92..102; Pro residues; 190..199; Low complexity; 200..219; Pro residues; 225..236; Acidic residues; 269..286; Acidic residues
Zinc Finger
550..576; C4-type
Domain (CC)
The first PH domain, PH 1, interacts with PtdIns(3,4,5)P3 which stimulates ARAP1 GTPase-activating activity and is also required for ARAP1-mediated regulation of endocytic trafficking of EGFR (PubMed:18939958, PubMed:19666464). It does not mediate PtdIns(3,4,5)P3-dependent recruitment of ARAP1 to membranes although this may be mediated by other PH domains (PubMed:19666464).
Domain (FT)
6..70; SAM; 327..419; PH 1; 440..529; PH 2; 535..660; Arf-GAP; 743..850; PH 3; 954..1139; Rho-GAP; 1172..1261; Ras-associating; 1274..1396; PH 4
Region
81..90; Required for interaction with SH3KBP1; 89..144; Disordered; 173..302; Disordered
Clinical Relevance5
Supporting Publications11
| PMID | Title | Abstract |
|---|---|---|
| 32854315 | Proteomic Profiling of Extracellular Vesicles Derived from Cerebrospinal Fluid of Alzheimer's Disease Patients: A Pilot Study. | Recent studies have highlighted the importance of Aβ and tau-containing extracellular vesicles (EVs) in AD. |
| 36064647 | Systemic proteomics and miRNA profile analysis of exosomes derived from human pluripotent stem cells. | No abstract available |
| 37322475 | Comprehensive profiling of extracellular vesicles in uveitis and scleritis enables biomarker discovery and mechanism exploration. | No abstract available |
| 38113368 | In-Depth Proteome Profiling of Small Extracellular Vesicles Isolated from Cancer Cell Lines and Patient Serum. | No abstract available |
| 38207106 | Proteomic, Metabolomic, and Fatty Acid Profiling of Small Extracellular Vesicles from Glioblastoma Stem-Like Cells and Their Role in Tumor Heterogeneity. | No abstract available |
| 39207047 | The trajectory of vesicular proteomic signatures from HBV-HCC by chitosan-magnetic bead-based separation and DIA-proteomic analysis. | No abstract available |
| 40189497 | Small extracellular vesicle-based one-step high-throughput microfluidic platform for epithelial ovarian cancer diagnosis. | No abstract available |
| 40465195 | Extracellular vesicle proteomics uncovers energy metabolism, complement system, and endoplasmic reticulum stress response dysregulation postexercise in males with myalgic encephalomyelitis/chronic fatigue syndrome. | No abstract available |
| 40840701 | Multiomics analysis to evaluate the enrichment of extracellular vesicles from human plasma. | No abstract available |
| 40940449 | Extracellular vesicle-associated transcriptomic and proteomic biomarkers show in vitro potential for vandetanib treatment monitoring in anaplastic thyroid cancer. | No abstract available |
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