Protein detail

ASAP1

Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 (130 kDa phosphatidylinositol 4,5-bisphosphate-dependent ARF1 GTPase-activating protein) (ADP-ribosylation factor-directed GTPase-activating protein 1) (ARF GTPase-activating protein 1) (Development and differentiation-enhancing factor 1) (DEF-1) (Differentiation-enhancing factor 1) (PIP2-dependent ARF1 GAP)

Entry name
ASAP1
UniProt ID
EVMP confidence score
0.63
Supporting publications (n)
7
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
Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 (130 kDa phosphatidylinositol 4,5-bisphosphate-dependent ARF1 GTPase-activating protein) (ADP-ribosylation factor-directed GTPase-activating protein 1) (ARF GTPase-activating protein 1) (Development and differentiation-enhancing factor 1) (DEF-1) (Differentiation-enhancing factor 1) (PIP2-dependent ARF1 GAP)
Protein Class
Predicted intracellular proteins
Protein Function
Predicted intracellular proteins
Entrez Gene Symbol
Gene Synonym (5)
CENTB4DDEF1KIAA1249PAPZG14P
Gene Description
ArfGAP with SH3 domain, ankyrin repeat and PH domain 1
Chromosome
8
Position
130052104-130443674
Supporting publications (n)
7
EVMP confidence score
0.63
Fluorescence & Localization6
ASAP1 fluorescence
Tissue Specificadipose tissueCell SpecificB-cellsSingle-Nuclei Brain SpecificfibroblastBlood Cell SpecificbasophilBlood Lineage Specificgranulocytes
Function & Pathway8
Relations & Evidence11

Enzyme-Mediated Modification (3)

3 records.

Substrate Gene SymbolEnzyme Gene SymbolEnzyme UniProt IDResidue TypeResidue OffsetModificationDatabaseReferences
ASAP1PTK2BQ14289Y767phosphorylationSIGNORSIGNOR:12771146
ASAP1PTK2BQ14289Y323phosphorylationSIGNORSIGNOR:12771146
ASAP1SRCP12931Y767phosphorylationREACH_ProtMapperSparser_ProtMapperProtMapperProtMapper:24957964

Ligand-Receptor Signaling (5)

5 records.

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

Regulatory Interaction Network (1)

1 record.

Source Protein SymbolSource UniProt IDTarget Protein SymbolTarget UniProt IDIs DirectedIs StimulationIs InhibitionDatabaseReferences
FAK2Q14289ASAP1Q9ULH1YesYesYesWangAdhesomeiPTMnetSIGNORProtMapperHPRDKEAphosphoELM_KEASIGNOR_ProtMapperKEA:12771146ProtMapper:12771146HPRD:12771146Adhesome:12771146SIGNOR:12771146

Protein Complex Composition (1)

1 record.

Component NameComponent Gene SymbolsComponent UniProt IDStoichiometryDatabaseDatabase IDsReferences
ASAP1DOK1NCK2WIPF3A6NGB9O43639Q99704Q9ULH10:0:0:0hu.MAP

Isolation & Detection Technology (1)

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationSize Exclusion ChromatographyMass spectrometryMass spectrometry [LTQ-FT Ultra]Mass spectrometry [QTOF]R Sequencing138037300
Sequence, Structure & Domains15

Sequences

Length
1,129
Mass
125,498
Sequence
MRSSASRLSSFSSRDSLWNRMPDQISVSEFIAETTEDYNSPTTSSFTTRLHNCRNTVTLLEEALDQDRTALQKVKKSVKAIYNSGQDHVQNEENYAQVLDKFGSNFLSRDNPDLGTAFVKFSTLTKELSTLLKNLLQGLSHNVIFTLDSLLKGDLKGVKGDLKKPFDKAWKDYETKFTKIEKEKREHAKQHGMIRTEITGAEIAEEMEKERRLFQLQMCEYLIKVNEIKTKKGVDLLQNLIKYYHAQCNFFQDGLKTADKLKQYIEKLAADLYNIKQTQDEEKKQLTALRDLIKSSLQLDQKEDSQSRQGGYSMHQLQGNKEYGSEKKGYLLKKSDGIRKVWQRRKCSVKNGILTISHATSNRQPAKLNLLTCQVKPNAEDKKSFDLISHNRTYHFQAEDEQDYVAWISVLTNSKEEALTMAFRGEQSAGENSLEDLTKAIIEDVQRLPGNDICCDCGSSEPTWLSTNLGILTCIECSGIHREMGVHISRIQSLELDKLGTSELLLAKNVGNNSFNDIMEANLPSPSPKPTPSSDMTVRKEYITAKYVDHRFSRKTCSTSSAKLNELLEAIKSRDLLALIQVYAEGVELMEPLLEPGQELGETALHLAVRTADQTSLHLVDFLVQNCGNLDKQTALGNTVLHYCSMYSKPECLKLLLRSKPTVDIVNQAGETALDIAKRLKATQCEDLLSQAKSGKFNPHVHVEYEWNLRQEEIDESDDDLDDKPSPIKKERSPRPQSFCHSSSISPQDKLALPGFSTPRDKQRLSYGAFTNQIFVSTSTDSPTSPTTEAPPLPPRNAGKGPTGPPSTLPLSTQTSSGSSTLSKKRPPPPPPGHKRTLSDPPSPLPHGPPNKGAVPWGNDGGPSSSSKTTNKFEGLSQQSSTSSAKTALGPRVLPKLPQKVALRKTDHLSLDKATIPPEIFQKSSQLAELPQKPPPGDLPPKPTELAPKPQIGDLPPKPGELPPKPQLGDLPPKPQLSDLPPKPQMKDLPPKPQLGDLLAKSQTGDVSPKAQQPSEVTLKSHPLDLSPNVQSRDAIQKQASEDSNDLTPTLPETPVPLPRKINTGKNKVRRVKTIYDCQADNDDELTFIEGEVIIVTGEEDQEWWIGHIEGQPERKGVFPVSFVHILSD
Alternative Products
Event=Alternative splicing; Named isoforms=2; Name=2; IsoId=Q9ULH1-1; Sequence=Displayed; Name=1; IsoId=Q9ULH1-2; Sequence=VSP_008365
Alternative Sequence
303; E -> ESRR (in isoform 1)

3D Structural Models

Turn
370..372
Helix
401..419; 1121..1123
Beta Strand
327..334; 336..338; 342..350; 353..356; 366..369; 373..377; 379..383; 385..389; 392..397; 1070..1076; 1081..1085; 1093..1098; 1101..1109; 1116..1120; 1124..1126
3D Structure
NMR spectroscopy (4); X-ray crystallography (1)

Domain & Motif Annotations

Compositional Bias
713..722; Acidic residues; 723..734; Basic and acidic residues; 735..747; Polar residues; 777..788; Low complexity; 809..822; Low complexity; 862..872; Polar residues; 876..889; Low complexity; 932..943; Pro residues; 956..966; Pro residues; 1001..1018; Polar residues
Repeat
600..632; ANK 1; 636..665; ANK 2
Zinc Finger
454..477; C4-type
Domain (CC)
The PH domain most probably contributes to the phosphoinositide-dependent regulation of ADP ribosylation factors.
Domain (FT)
324..416; PH; 439..560; Arf-GAP; 1067..1129; SH3
Region
713..760; Disordered; 776..1062; Disordered
Clinical Relevance4
Interaction Protein (5)
ENSG00000085733ENSG00000147010ENSG00000167193ENSG00000177885ENSG00000197122
Interaction Count
5
Interaction Dataset
intact_biogrid
Supporting Publications7
PMIDTitleAbstract
36064647Systemic proteomics and miRNA profile analysis of exosomes derived from human pluripotent stem cells.No abstract available
37322475Comprehensive profiling of extracellular vesicles in uveitis and scleritis enables biomarker discovery and mechanism exploration.No abstract available
38207106Proteomic, Metabolomic, and Fatty Acid Profiling of Small Extracellular Vesicles from Glioblastoma Stem-Like Cells and Their Role in Tumor Heterogeneity.No abstract available
39207047The trajectory of vesicular proteomic signatures from HBV-HCC by chitosan-magnetic bead-based separation and DIA-proteomic analysis.No abstract available
40465195Extracellular 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
40840701Multiomics analysis to evaluate the enrichment of extracellular vesicles from human plasma.No abstract available
40985879TurboID-Mediated Profiling of Glioblastoma-Derived Extracellular Vesicle Cargo Proteins.No abstract available