Protein detail

DAB2

Disabled homolog 2 (Adaptor molecule disabled-2) (Differentially expressed in ovarian carcinoma 2) (DOC-2) (Differentially-expressed protein 2)

Entry name
DAB2
UniProt ID
EVMP confidence score
0.60
Supporting publications (n)
14
Transmembrane count
Protein classification
Plasma proteinsPredicted 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
Disabled homolog 2 (Adaptor molecule disabled-2) (Differentially expressed in ovarian carcinoma 2) (DOC-2) (Differentially-expressed protein 2)
Protein Class (2)
Plasma proteinsPredicted intracellular proteins
Protein Function
Predicted intracellular proteins
Entrez Gene Symbol
Gene Synonym
DOC-2
Gene Description
DAB adaptor protein 2
Chromosome
5
Position
39371675-39462300
Supporting publications (n)
14
EVMP confidence score
0.60
Fluorescence & Localization2
DAB2 fluorescence
Cell SpecificMyonuclei
Function & Pathway8
Relations & Evidence41

Enzyme-Mediated Modification (13)

13 records.

Substrate Gene SymbolEnzyme Gene SymbolEnzyme UniProt IDResidue TypeResidue OffsetModificationDatabaseReferences
DAB2PRKCDQ05655S24phosphorylationBEL-Large-Corpus_ProtMapperphosphoELM_MIMPPhosphoSite_MIMPMIMPHPRD_MIMPSIGNORProtMapperKEASIGNOR_ProtMapperPhosphoSitePhosphoSite_ProtMapperKEA:11812785SIGNOR:10542228ProtMapper:15280374KEA:10542228ProtMapper:10542228SIGNOR:15280374
DAB2PRKCGP05129S24phosphorylationphosphoELM_MIMPPhosphoSite_MIMPMIMPHPRD_MIMPSIGNORProtMapperKEASIGNOR_ProtMapperPhosphoSitePhosphoSite_ProtMapperKEA:11812785ProtMapper:10542228KEA:10542228SIGNOR:10542228
DAB2PRKCBP05771S24phosphorylationBEL-Large-Corpus_ProtMapperphosphoELM_MIMPPhosphoSite_MIMPMIMPHPRD_MIMPSIGNORProtMapperKEASIGNOR_ProtMapperPhosphoSitePhosphoSite_ProtMapperKEA:11812785ProtMapper:10542228KEA:10542228SIGNOR:10542228
DAB2ROCK2O75116S723phosphorylationPhosphoSitePhosphoSite_ProtMapperProtMapper
DAB2CAMK2GQ13555S723phosphorylationPhosphoSitePhosphoSite_ProtMapperProtMapper
DAB2PRKCAP17252S24phosphorylationBEL-Large-Corpus_ProtMapperPhosphoNetworksphosphoELM_MIMPPhosphoSite_MIMPMIMPHPRD_MIMPProtMapperKEAKEA:17570479KEA:11812785KEA:10542228ProtMapper:15212693
DAB2PRKCEQ02156S24phosphorylationMIMPHPRD_MIMPphosphoELM_MIMPPhosphoSite_MIMP
DAB2CDK2P24941S227phosphorylationKEAKEA:17570479
DAB2CDK2P24941S401phosphorylationKEAKEA:17570479
DAB2GSK3BP49841S401phosphorylationKEAKEA:17570479
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Ligand-Receptor Signaling (5)

5 records.

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

Regulatory Interaction Network (12)

12 records.

Source Protein SymbolSource UniProt IDTarget Protein SymbolTarget UniProt IDIs DirectedIs StimulationIs InhibitionDatabaseReferences
DAB2P98082SMAD2Q15796YesYesNoWangNetPathHPRDCui2007SignaLink3CancerCellMapSPIKE_LCSPIKESPIKE:11387212CancerCellMap:11387212HPRD:11387212NetPath:11387212SPIKE_LC:16713569SignaLink3:23331499SPIKE_LC:11387212SignaLink3:11387212SPIKE:16713569
DAB2P98082DVL3Q92997YesYesYesWangNetPathHPRDCui2007SignaLink3ACSNCancerCellMapSPIKE_LCSPIKESPIKE:16713569ACSN:19581931ACSN:21304492SPIKE_LC:12805222SPIKE:12805222NetPath:12805222ACSN:17318175ACSN:15518237ACSN:21498506SPIKE_LC:16713569ACSN:20460648SignaLink3:23331499SignaLink3:12805222CancerCellMap:12805222SignaLink3:21071413ACSN:19561074HPRD:12805222
DAB2P98082TGFR2P37173YesYesNoWangNetPathHPRDCui2007SignaLink3CancerCellMapSPIKE_LCSPIKESPIKE:11387212CancerCellMap:11387212HPRD:11387212NetPath:11387212SPIKE_LC:16713569SignaLink3:23331499SPIKE_LC:11387212SignaLink3:11387212SPIKE:16713569
DAB2P98082TGFR1P36897YesYesNoWangNetPathHPRDCui2007SignaLink3SPIKE_LCSPIKESPIKE:11387212HPRD:11387212NetPath:11387212SPIKE_LC:16713569SignaLink3:23331499SPIKE_LC:11387212SignaLink3:11387212SPIKE:16713569
DAB2P98082CSKP41240YesYesNoHPRDSPIKE_LCSignaLink3SignaLink3:23331499SignaLink3:12473651SPIKE_LC:16713569HPRD:12473651
KPCDQ05655DAB2P98082YesYesYesHPRD_MIMPSIGNORProtMapperPhosphoSite_KEAHPRDCui2007CancerCellMapWangPhosphoSite_ProtMapperBEL-Large-Corpus_ProtMapperphosphoELM_MIMPPhosphoSite_MIMPMIMPiPTMnetPhosphoPointKEAHPRD_KEASIGNOR_ProtMapperREACH_ProtMapperPhosphoSiteKEA:11812785SIGNOR:10542228PhosphoSite:15280374CancerCellMap:10542228PhosphoSite:10542228ProtMapper:15280374KEA:10542228PhosphoSite:11812785ProtMapper:10542228ProtMapper:30845955SIGNOR:15280374HPRD:10542228
COMPLEX:O94973_P53680_P63010_Q96CW1DAB2P98082YesYesNoSIGNORSIGNOR:11247302
DAB2P98082LRP6O75581YesNoYesSIGNORACSNACSN:19581931ACSN:21304492ACSN:17318175ACSN:15518237ACSN:21498506ACSN:20460648SIGNOR:22491013ACSN:19561074
KPCGP05129DAB2P98082YesYesNoWangphosphoELM_MIMPPhosphoSite_MIMPMIMPHPRD_MIMPiPTMnetPhosphoPointSIGNORProtMapperHPRDCui2007PhosphoSite_KEAKEAHPRD_KEACancerCellMapSIGNOR_ProtMapperREACH_ProtMapperPhosphoSite_ProtMapperKEA:11812785SIGNOR:10542228CancerCellMap:10542228KEA:10542228ProtMapper:10542228ProtMapper:30845955HPRD:10542228
DAB2P98082DAB2PQ5VWQ8YesYesNoSIGNORSIGNOR:27858941
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Isolation & Detection Technology (1)

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationSize Exclusion ChromatographyMass spectrometry127605433
Sequence, Structure & Domains14

Sequences

Length
770
Mass
82,448
Sequence
MSNEVETSATNGQPDQQAAPKAPSKKEKKKGPEKTDEYLLARFKGDGVKYKAKLIGIDDVPDARGDKMSQDSMMKLKGMAAAGRSQGQHKQRIWVNISLSGIKIIDEKTGVIEHEHPVNKISFIARDVTDNRAFGYVCGGEGQHQFFAIKTGQQAEPLVVDLKDLFQVIYNVKKKEEEKKKIEEASKAVENGSEALMILDDQTNKLKSGVDQMDLFGDMSTPPDLNSPTESKDILLVDLNSEIDTNQNSLRENPFLTNGITSCSLPRPTPQASFLPENAFSANLNFFPTPNPDPFRDDPFTQPDQSTPSSFDSLKSPDQKKENSSSSSTPLSNGPLNGDVDYFGQQFDQISNRTGKQEAQAGPWPFSSSQTQPAVRTQNGVSEREQNGFSVKSSPNPFVGSPPKGLSIQNGVKQDLESSVQSSPHDSIAIIPPPQSTKPGRGRRTAKSSANDLLASDIFAPPVSEPSGQASPTGQPTALQPNPLDLFKTSAPAPVGPLVGLGGVTVTLPQAGPWNTASLVFNQSPSMAPGAMMGGQPSGFSQPVIFGTSPAVSGWNQPSPFAASTPPPVPVVWGPSASVAPNAWSTTSPLGNPFQSNIFPAPAVSTQPPSMHSSLLVTPPQPPPRAGPPKDISSDAFTALDPLGDKEIKDVKEMFKDFQLRQPPAVPARKGEQTSSGTLSAFASYFNSKVGIPQENADHDDFDANQLLNKINEPPKPAPRQVSLPVTKSTDNAFENPFFKDSFGSSQASVASSQPVSSEMYRDPFGNPFA
Alternative Products
Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=P98082-1; Sequence=Displayed; Name=2; IsoId=P98082-2; Sequence=VSP_004181; Name=3; IsoId=P98082-3; Sequence=VSP_038401
Alternative Sequence
209..229; Missing (in isoform 3); 230..447; Missing (in isoform 2)

3D Structural Models

Turn
44..46; 107..109
Helix
36..43; 66..85; 118..120; 156..180
Beta Strand
29..31; 48..59; 61..63; 91..98; 101..106; 112..116; 121..126; 133..138; 145..153
3D Structure
NMR spectroscopy (1); X-ray crystallography (2)

Domain & Motif Annotations

Compositional Bias
1..16; Polar residues; 302..313; Polar residues; 366..396; Polar residues; 407..425; Polar residues; 466..480; Polar residues; 604..616; Polar residues; 745..758; Low complexity
Motif
293..295; DPF 1; 298..300; DPF 2
Domain (CC)
The PID domain binds to predominantly non-phosphorylated NPXY internalization motifs present in members of the LDLR and APP family; it also mediates simultaneous binding to phosphatidylinositol 4,5-bisphosphate.; DOMAIN: The Asn-Pro-Phe (NPF) motifs, which are found in proteins involved in the endocytic pathway, mediate the interaction with the EH domain of EPS15, EPS15R and ITSN1..
Domain (FT)
45..196; PID
Region
1..38; Disordered; 230..447; Required for localization to clathrin-coated pits; 284..482; Disordered; 604..732; Sufficient for interaction with GRB2; 604..629; Disordered; 619..627; Required for interaction with CSK; 649..770; Required for interaction with MYO6; 663..671; Required for interaction with GRB2 and CSK; 709..725; Sufficient for interaction with SH3KBP1 SH3 domain; 742..770; Disordered
Clinical Relevance5
Disease Involvement
Tumor suppressor
Interaction Protein (5)
ENSG00000147010ENSG00000166949ENSG00000175387ENSG00000177885ENSG00000196586
Interaction Count
5
Interaction Dataset
intact_biogrid
Supporting Publications14
PMIDTitleAbstract
26538482Insights into immune responses in oral cancer through proteomic analysis of saliva and salivary extracellular vesicles.No abstract available
30071318Changes in the urinary extracellular vesicle proteome are associated with nephronophthisis-related ciliopathies.No abstract available
31508500Proteomic profiling of extracellular vesicles allows for human breast cancer subtyping.No abstract available
32795414Extracellular Vesicle and Particle Biomarkers Define Multiple Human Cancers.Among traditional exosome markers, CD9, HSPA8, ALIX, and HSP90AB1 represent pan-EVP markers, while ACTB, MSN, and RAP1B are novel pan-EVP markers.
33114768Proteomic Profiling of Two Distinct Populations of Extracellular Vesicles Isolated from Human Seminal Plasma.No abstract available
33718342Extracellular Vesicles Derived From Adult and Fetal Bone Marrow Mesenchymal Stromal Cells Differentially Promote ex vivo Expansion of Hematopoietic Stem and Progenitor Cells.No abstract available
37033249Altered ureido protein modification profiles in seminal plasma extracellular vesicles of non-normozoospermic men.No abstract available
37686366Identification of a Non-Invasive Urinary Exosomal Biomarker for Diabetic Nephropathy Using Data-Independent Acquisition Proteomics.No abstract available
37702715One-Pot Analytical Pipeline for Efficient and Sensitive Proteomic Analysis of Extracellular Vesicles.No abstract available
37862381Surfaceome analysis of extracellular vesicles from senescent cells uncovers uptake repressor DPP4.No abstract available
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