DOK1_MOUSE - dbPTM
DOK1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DOK1_MOUSE
UniProt AC P97465
Protein Name Docking protein 1
Gene Name Dok1
Organism Mus musculus (Mouse).
Sequence Length 482
Subcellular Localization Cytoplasm. Nucleus.
Protein Description DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK1 appears to be a negative regulator of the insulin signaling pathway. Modulates integrin activation by competing with talin for the same binding site on ITGB3 (By similarity)..
Protein Sequence MDGAVMEGPLFLQSQRFGTKRWRKTWAVLYPASPHGVARLEFFDHKGSSSRGGRGGSRRLDCKMIRLAECVSVVPVTVESPPEPGAVAFRLDTAQRSHLLAADAVSSTAWVQTLCRTAFPKGGWALAQTENQPKFSALEMLENSLYSPTWEGSQFWVTSQKTEASERCGLQGSYILRVEAEKLTLLTLGAQSQILEPLLFWPYTLLRRYGRDKVMFSFEAGRRCPSGPGTFTFQTSQGNDIFQAVEAAIQQQKAQGKVGQAQDILRTDSHDGETEGKTVPPPVPQDPLGSPPALYAEPLDSLRIPPGPSQDSVYSDPLGSTPAGAGEGVHSKKPLYWDLYGHVQQQLLKTKLTDSKEDPIYDEPEGLAPAPPRGLYDLPQEPRDAWWCQARLKEEGYELPYNPATDDYAVPPPRSPKPAPAPKPQGLILPESGTTRGSGSKGFSSDTALYSQVQKSGTSGAWDCGLSKVGNDRAGVKSEGST
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
1Acetylation-------MDGAVMEG
-------CCCCCCCC		10.94-
33PhosphorylationWAVLYPASPHGVARL
EEEEEECCCCCEEEE		16.9629514104
48PhosphorylationEFFDHKGSSSRGGRG
EEECCCCCCCCCCCC		29.9126824392
49PhosphorylationFFDHKGSSSRGGRGG
EECCCCCCCCCCCCC		32.4923737553
50PhosphorylationFDHKGSSSRGGRGGS
ECCCCCCCCCCCCCC		36.3223737553
63AcetylationGSRRLDCKMIRLAEC
CCHHHCCEEEEECCC		36.717718933
80PhosphorylationVVPVTVESPPEPGAV
EEEEEECCCCCCCCE		41.2226824392
97PhosphorylationRLDTAQRSHLLAADA
EECHHHHHHHHHHHH		13.3522871156
106PhosphorylationLLAADAVSSTAWVQT
HHHHHHHCCHHHHHH		24.5622871156
117PhosphorylationWVQTLCRTAFPKGGW
HHHHHHHHHCCCCCC		31.4922871156
136PhosphorylationTENQPKFSALEMLEN
CCCCCCCCHHHHHHH		37.7622817900
146PhosphorylationEMLENSLYSPTWEGS
HHHHHCCCCCCCCCC		16.6611042170
267PhosphorylationQAQDILRTDSHDGET
CHHHHHHCCCCCCCC		38.1127087446
269PhosphorylationQDILRTDSHDGETEG
HHHHHCCCCCCCCCC		23.9027087446
274PhosphorylationTDSHDGETEGKTVPP
CCCCCCCCCCCCCCC		56.4125266776
278PhosphorylationDGETEGKTVPPPVPQ
CCCCCCCCCCCCCCC		49.4525619855
290PhosphorylationVPQDPLGSPPALYAE
CCCCCCCCCCCEEEC		35.0826824392
295PhosphorylationLGSPPALYAEPLDSL
CCCCCCEEECCCCCC		15.8325619855
301PhosphorylationLYAEPLDSLRIPPGP
EEECCCCCCCCCCCC		27.5125619855
309PhosphorylationLRIPPGPSQDSVYSD
CCCCCCCCCCCCCCC		53.1625619855
312PhosphorylationPPGPSQDSVYSDPLG
CCCCCCCCCCCCCCC		18.4725619855
314PhosphorylationGPSQDSVYSDPLGST
CCCCCCCCCCCCCCC		16.0025619855
315PhosphorylationPSQDSVYSDPLGSTP
CCCCCCCCCCCCCCC		30.5125619855
336PhosphorylationVHSKKPLYWDLYGHV
CCCCCCCHHHHHHHH		12.8520116462
340PhosphorylationKPLYWDLYGHVQQQL
CCCHHHHHHHHHHHH		11.6020116462
353PhosphorylationQLLKTKLTDSKEDPI
HHHHCCCCCCCCCCC		39.5225619855
355PhosphorylationLKTKLTDSKEDPIYD
HHCCCCCCCCCCCCC		32.4825619855
361PhosphorylationDSKEDPIYDEPEGLA
CCCCCCCCCCCCCCC		21.4612087092
376PhosphorylationPAPPRGLYDLPQEPR
CCCCCCCCCCCCCCC		20.4718515860
397PhosphorylationARLKEEGYELPYNPA
HHHHHCCCCCCCCCC		19.9922499769
401PhosphorylationEEGYELPYNPATDDY
HCCCCCCCCCCCCCC		46.5322817900
405PhosphorylationELPYNPATDDYAVPP
CCCCCCCCCCCCCCC		30.5722499769
408PhosphorylationYNPATDDYAVPPPRS
CCCCCCCCCCCCCCC		16.5918515860
415PhosphorylationYAVPPPRSPKPAPAP
CCCCCCCCCCCCCCC		42.9518515860
432PhosphorylationQGLILPESGTTRGSG
CCEEECCCCCCCCCC		39.2325777480
434PhosphorylationLILPESGTTRGSGSK
EEECCCCCCCCCCCC		23.6925777480
435PhosphorylationILPESGTTRGSGSKG
EECCCCCCCCCCCCC		36.2425777480
438PhosphorylationESGTTRGSGSKGFSS
CCCCCCCCCCCCCCC		36.2822802335
444PhosphorylationGSGSKGFSSDTALYS
CCCCCCCCCCHHHHH		35.6525619855
445PhosphorylationSGSKGFSSDTALYSQ
CCCCCCCCCHHHHHH		36.4025619855
447PhosphorylationSKGFSSDTALYSQVQ
CCCCCCCHHHHHHHH		22.1025619855
450PhosphorylationFSSDTALYSQVQKSG
CCCCHHHHHHHHHHC		8.4518515860
451PhosphorylationSSDTALYSQVQKSGT
CCCHHHHHHHHHHCC		25.4025619855
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
146YPhosphorylationKinaseSRCP12931
PSP
361YPhosphorylationKinaseABL1P00520
PhosphoELM
361YPhosphorylationKinaseABL-FAMILY-GPS
397YPhosphorylationKinaseINSRP15208
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DOK1_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 DOK1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SHIP1_MOUSEInpp5dphysical
20697350
NCK1_MOUSENck1physical
20697350
GRB2_MOUSEGrb2physical
20697350
ABL1_MOUSEAbl1physical
20697350
TEC_MOUSETecphysical
20697350
SERA_MOUSEPhgdhphysical
20697350
NCK2_MOUSENck2physical
20697350
BCR_MOUSEBcrphysical
20697350
CSK_MOUSECskphysical
20697350
INSR_MOUSEInsrphysical
10567556
SHIP1_MOUSEInpp5dphysical
11031258
P85A_MOUSEPik3r1physical
11031258
TEC_MOUSETecphysical
10823839
SHIP1_RATInpp5dphysical
11970986
AVR2A_HUMANACVR2Aphysical
11927552
AVR2B_HUMANACVR2Bphysical
11927552
PTN6_MOUSEPtpn6physical
10585470
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DOK1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269 AND TYR-450, ANDMASS SPECTROMETRY.
"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 TYR-376, AND MASSSPECTROMETRY.
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-361, AND MASSSPECTROMETRY.
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling.";
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.;
J. Immunol. 179:5864-5876(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-361; TYR-408 ANDTYR-450, AND MASS SPECTROMETRY.
"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-295; TYR-314; TYR-336;TYR-340; TYR-361 AND TYR-376, AND MASS SPECTROMETRY.

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