DAB2_MOUSE - dbPTM
DAB2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DAB2_MOUSE
UniProt AC P98078
Protein Name Disabled homolog 2
Gene Name Dab2
Organism Mus musculus (Mouse).
Sequence Length 766
Subcellular Localization Cytoplasmic vesicle, clathrin-coated vesicle membrane. Membrane, clathrin-coated pit. Colocalizes with large insert-containing isoforms of MYO6 at clathrin-coated pits/vesicles. During mitosis is progressively displaced from the membrane and transloc
Protein Description Adapter protein that functions as clathrin-associated sorting protein (CLASP) required for clathrin-mediated endocytosis of selected cargo proteins. Can bind and assemble clathrin, and binds simultaneously to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and cargos containing non-phosphorylated NPXY internalization motifs, such as the LDL receptor, to recruit them to clathrin-coated pits. Can function in clathrin-mediated endocytosis independently of the AP-2 complex. Involved in endocytosis of integrin beta-1; this function seems to redundant with the AP-2 complex and seems to require DAB2 binding to endocytosis accessory EH domain-containing proteins such as EPS15, EPS15L1 and ITSN1. Involved in endocytosis of cystic fibrosis transmembrane conductance regulator/CFTR. Isoform p96 is involved in endocytosis of megalin/LRP2 lipoprotein receptor during embryonal development. Required for recycling of the TGF-beta receptor. Isoform p67 is not involved in LDL receptor endocytosis. Involved in CFTR trafficking to the late endosome. Involved in several receptor-mediated signaling pathways. Involved in TGF-beta receptor signaling and facilitates phosphorylation of the signal transducer SMAD2. Mediates TFG-beta-stimulated JNK activation. May inhibit the canoniocal Wnt/beta-catenin signaling pathway by stabilizing the beta-catenin destruction complex through a competing association with axin preventing its dephosphorylation through protein phosphatase 1 (PP1). Sequesters LRP6 towards clathrin-mediated endocytosis, leading to inhibition of Wnt/beta-catenin signaling. May activate non-canonical Wnt signaling. In cell surface growth factor/Ras signaling pathways proposed to inhibit ERK activation by interrupting the binding of GRB2 to SOS1 and to inhibit SRC by preventing its activating phosphorylation at 'Tyr-419'. Proposed to be involved in modulation of androgen receptor (AR) signaling mediated by SRC activation; seems to compete with AR for interaction with SRC. Plays a role in the CSF-1 signal transduction pathway. Plays a role in cellular differentiation. Involved in cell positioning and formation of visceral endoderm (VE) during embryogenesis and proposed to be required in the VE to respond to Nodal signaling coming from the epiblast. Required for the epithelial to mesenchymal transition, a process necessary for proper embryonic development. May be involved in myeloid cell differentiation and can induce macrophage adhesion and spreading. Isoform p67 may be involved in transcriptional regulation. May act as a tumor suppressor..
Protein Sequence MSNEVETSTTNGQPDQQAAPKAPSKKEKKKGSEKTDEYLLARFKGDGVKYKAKLIGIDDVPDARGDKMSQDSMMKLKGMAAAGRSQGQHKQRIWVNISLSGIKIIDEKTGVIEHEHPVNKISFIARDVTDNRAFGYVCGGEGQHQFFAIKTGQQAEPLVVDLKDLFQVIYNVKKKEEDKKKVEEANKAEENGSEALMTLDDQANKLKLGVDQMDLFGDMSTPPDLNSPTESKDILLVDLNSEIDTNQNSLRENPFLTNGVTSCSLPRPKPQASFLPENAFSANLNFFPTPNPDPFRDDPFAQPDQSAPSSFDSLTSPDQKKASLSSSSTPQSKGPLNGDTDYFGQQFDQLSNRTGKPEAQGGPWPYPSSQTQQAVRTQNGVSEREQNGFHIKSSPNPFVGSPPKGLSVPNGVKQDLESSVQSSAHDSIAIIPPPQSTKPGRGRRTAKSSANDLLASDIFASEPPGQMSPTGQPAVPQSNFLDLFKGNAPAPVGPLVGLGTVPVTPPQAGPWTPVVYSPSTTVVPGAIISGQPPSFRQPLVFGTTPAVQVWNQSPSFATPASPPPPTVWCPTTSVAPNAWSSTSPLGNPFQSNNIFPPPTMSTQSSPQPMMSSVLATPPQPPPRNGPLKDIPSDAFTGLDPLGDKEVKEVKEMFKDFQLRQPPLVPSRKGETPPSGTSSAFSSYFNNKVGIPQEHVDHDDFDANQLLNKINEPPKPAPRQGVLLGTKSADNSLENPFSKGFSSSNPSVVSQPASSDPHRSPFGNPFA
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MSNEVETST
------CCCCCCCCC		41.52-
2Phosphorylation------MSNEVETST
------CCCCCCCCC		41.5230635358
7Phosphorylation-MSNEVETSTTNGQP
-CCCCCCCCCCCCCC		36.2330635358
8PhosphorylationMSNEVETSTTNGQPD
CCCCCCCCCCCCCCC		21.5230635358
9PhosphorylationSNEVETSTTNGQPDQ
CCCCCCCCCCCCCCC		31.5330635358
10PhosphorylationNEVETSTTNGQPDQQ
CCCCCCCCCCCCCCC		36.8030635358
24PhosphorylationQAAPKAPSKKEKKKG
CCCCCCCCHHHHCCC		62.3123984901
32PhosphorylationKKEKKKGSEKTDEYL
HHHHCCCCCCCCHHH		44.8122942356
35PhosphorylationKKKGSEKTDEYLLAR
HCCCCCCCCHHHHHH		29.9722942356
53UbiquitinationDGVKYKAKLIGIDDV
CCCEEEEEEECCCCC		36.1622790023
67UbiquitinationVPDARGDKMSQDSMM
CCCCCCCCCCHHHHH		43.1922790023
69PhosphorylationDARGDKMSQDSMMKL
CCCCCCCCHHHHHHH		36.25-
72PhosphorylationGDKMSQDSMMKLKGM
CCCCCHHHHHHHHHH		17.09-
138S-nitrosylationNRAFGYVCGGEGQHQ
CCEEEEEECCCCCEE		4.3420925432
138S-nitrosocysteineNRAFGYVCGGEGQHQ
CCEEEEEECCCCCEE		4.34-
163UbiquitinationEPLVVDLKDLFQVIY
CCEEEEHHHHHHHHH		48.17-
170PhosphorylationKDLFQVIYNVKKKEE
HHHHHHHHHHHCHHH		18.2919060867
173UbiquitinationFQVIYNVKKKEEDKK
HHHHHHHHCHHHHHH		55.2622790023
193PhosphorylationNKAEENGSEALMTLD
HHHHHHCCCCCCCHH		31.1427180971
205UbiquitinationTLDDQANKLKLGVDQ
CHHHHHHHHCCCCCH		50.4422790023
207UbiquitinationDDQANKLKLGVDQMD
HHHHHHHCCCCCHHH		44.82-
220PhosphorylationMDLFGDMSTPPDLNS
HHHCCCCCCCCCCCC		42.3725619855
221PhosphorylationDLFGDMSTPPDLNSP
HHCCCCCCCCCCCCC		32.0025619855
227PhosphorylationSTPPDLNSPTESKDI
CCCCCCCCCCCCCCE		40.2625619855
229PhosphorylationPPDLNSPTESKDILL
CCCCCCCCCCCCEEE		53.3525619855
231PhosphorylationDLNSPTESKDILLVD
CCCCCCCCCCEEEEE		37.8025619855
241PhosphorylationILLVDLNSEIDTNQN
EEEEECCCCCCCCCC		43.1323649490
257PhosphorylationLRENPFLTNGVTSCS
CCCCCCCCCCCEECC		30.2429233185
261PhosphorylationPFLTNGVTSCSLPRP
CCCCCCCEECCCCCC		25.9729233185
262PhosphorylationFLTNGVTSCSLPRPK
CCCCCCEECCCCCCC		10.1729233185
263GlutathionylationLTNGVTSCSLPRPKP
CCCCCEECCCCCCCC		3.3724333276
264PhosphorylationTNGVTSCSLPRPKPQ
CCCCEECCCCCCCCC		40.9726824392
306PhosphorylationPFAQPDQSAPSSFDS
CCCCCCCCCCCCHHC		49.9125619855
309PhosphorylationQPDQSAPSSFDSLTS
CCCCCCCCCHHCCCC		43.2725619855
310PhosphorylationPDQSAPSSFDSLTSP
CCCCCCCCHHCCCCC		31.8225619855
313PhosphorylationSAPSSFDSLTSPDQK
CCCCCHHCCCCCCHH		31.3825619855
315PhosphorylationPSSFDSLTSPDQKKA
CCCHHCCCCCCHHHC		42.0125619855
316PhosphorylationSSFDSLTSPDQKKAS
CCHHCCCCCCHHHCC		31.6025619855
323PhosphorylationSPDQKKASLSSSSTP
CCCHHHCCCCCCCCC		37.3525521595
325PhosphorylationDQKKASLSSSSTPQS
CHHHCCCCCCCCCCC		26.1930352176
326PhosphorylationQKKASLSSSSTPQSK
HHHCCCCCCCCCCCC		33.3326026062
327PhosphorylationKKASLSSSSTPQSKG
HHCCCCCCCCCCCCC		34.5526026062
328PhosphorylationKASLSSSSTPQSKGP
HCCCCCCCCCCCCCC		46.1626026062
329PhosphorylationASLSSSSTPQSKGPL
CCCCCCCCCCCCCCC		27.5630352176
332PhosphorylationSSSSTPQSKGPLNGD
CCCCCCCCCCCCCCC		40.5630635358
340PhosphorylationKGPLNGDTDYFGQQF
CCCCCCCCCHHHHHH		33.7222817900
342PhosphorylationPLNGDTDYFGQQFDQ
CCCCCCCHHHHHHHH		16.2322817900
356UbiquitinationQLSNRTGKPEAQGGP
HHHCCCCCCCCCCCC		38.79-
393PhosphorylationQNGFHIKSSPNPFVG
HCCEECCCCCCCCCC		50.8827818261
394PhosphorylationNGFHIKSSPNPFVGS
CCEECCCCCCCCCCC		24.5622942356
401PhosphorylationSPNPFVGSPPKGLSV
CCCCCCCCCCCCCCC		32.5025521595
407PhosphorylationGSPPKGLSVPNGVKQ
CCCCCCCCCCCCHHH		44.1726026062
441MethylationPQSTKPGRGRRTAKS
CCCCCCCCCCCCCCC		43.93-
449PhosphorylationGRRTAKSSANDLLAS
CCCCCCCHHHHHHHH		30.3123649490
456PhosphorylationSANDLLASDIFASEP
HHHHHHHHHHCCCCC		31.0723649490
461PhosphorylationLASDIFASEPPGQMS
HHHHHCCCCCCCCCC		39.6323649490
468PhosphorylationSEPPGQMSPTGQPAV
CCCCCCCCCCCCCCC		16.0630352176
470PhosphorylationPPGQMSPTGQPAVPQ
CCCCCCCCCCCCCCC		40.9422942356
628UbiquitinationPPRNGPLKDIPSDAF
CCCCCCCCCCCCCCC		57.66-
632PhosphorylationGPLKDIPSDAFTGLD
CCCCCCCCCCCCCCC		41.7425338131
647UbiquitinationPLGDKEVKEVKEMFK
CCCCHHHHHHHHHHH		58.8622790023
650UbiquitinationDKEVKEVKEMFKDFQ
CHHHHHHHHHHHHCC		44.5522790023
654UbiquitinationKEVKEMFKDFQLRQP
HHHHHHHHHCCCCCC		57.2122790023
668UbiquitinationPPLVPSRKGETPPSG
CCCCCCCCCCCCCCC		66.49-
671PhosphorylationVPSRKGETPPSGTSS
CCCCCCCCCCCCCHH		49.5225521595
674PhosphorylationRKGETPPSGTSSAFS
CCCCCCCCCCHHHHH		56.7727742792
676PhosphorylationGETPPSGTSSAFSSY
CCCCCCCCHHHHHHH		24.6827742792
677PhosphorylationETPPSGTSSAFSSYF
CCCCCCCHHHHHHHH		24.1627742792
678PhosphorylationTPPSGTSSAFSSYFN
CCCCCCHHHHHHHHC		32.9227742792
681PhosphorylationSGTSSAFSSYFNNKV
CCCHHHHHHHHCCCC		24.6825777480
682PhosphorylationGTSSAFSSYFNNKVG
CCHHHHHHHHCCCCC		27.5625777480
683PhosphorylationTSSAFSSYFNNKVGI
CHHHHHHHHCCCCCC		14.7725777480
725PhosphorylationRQGVLLGTKSADNSL
CCCEEECCCCCCCCC		23.0729514104
727PhosphorylationGVLLGTKSADNSLEN
CEEECCCCCCCCCCC		40.4725521595
731PhosphorylationGTKSADNSLENPFSK
CCCCCCCCCCCCCCC		37.2925619855
738UbiquitinationSLENPFSKGFSSSNP
CCCCCCCCCCCCCCC		65.44-
741PhosphorylationNPFSKGFSSSNPSVV
CCCCCCCCCCCCCCC		41.3425619855
742PhosphorylationPFSKGFSSSNPSVVS
CCCCCCCCCCCCCCC		31.6925619855
743PhosphorylationFSKGFSSSNPSVVSQ
CCCCCCCCCCCCCCC		52.1125619855
746PhosphorylationGFSSSNPSVVSQPAS
CCCCCCCCCCCCCCC		39.1325619855
749PhosphorylationSSNPSVVSQPASSDP
CCCCCCCCCCCCCCC		28.4325619855
753PhosphorylationSVVSQPASSDPHRSP
CCCCCCCCCCCCCCC		41.7925619855
754PhosphorylationVVSQPASSDPHRSPF
CCCCCCCCCCCCCCC		58.2125619855
759PhosphorylationASSDPHRSPFGNPFA
CCCCCCCCCCCCCCC		22.8812826668
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
24SPhosphorylationKinasePKCZQ02956
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DAB2_MOUSE !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of DAB2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AP2B1_RATAp2b1physical
12234931
CLH1_RATCltcphysical
12234931
CLCA_RATCltaphysical
12234931
AP2M1_RATAp2m1physical
12234931
T22D3_MOUSETsc22d3physical
11104669
ITSN1_HUMANITSN1physical
22648170
EPS15_HUMANEPS15physical
22648170
LRP2_MOUSELrp2physical
12413896
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DAB2_MOUSE

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401 AND SER-727, ANDMASS SPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-342, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory