DOK1_HUMAN - dbPTM
DOK1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DOK1_HUMAN
UniProt AC Q99704
Protein Name Docking protein 1
Gene Name DOK1
Organism Homo sapiens (Human).
Sequence Length 481
Subcellular Localization Isoform 1: Cytoplasm. Nucleus.
Isoform 3: Cytoplasm, perinuclear region.
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..
Protein Sequence MDGAVMEGPLFLQSQRFGTKRWRKTWAVLYPASPHGVARLEFFDHKGSSSGGGRGSSRRLDCKVIRLAECVSVAPVTVETPPEPGATAFRLDTAQRSHLLAADAPSSAAWVQTLCRNAFPKGSWTLAPTDNPPKLSALEMLENSLYSPTWEGSQFWVTVQRTEAAERCGLHGSYVLRVEAERLTLLTVGAQSQILEPLLSWPYTLLRRYGRDKVMFSFEAGRRCPSGPGTFTFQTAQGNDIFQAVETAIHRQKAQGKAGQGHDVLRADSHEGEVAEGKLPSPPGPQELLDSPPALYAEPLDSLRIAPCPSQDSLYSDPLDSTSAQAGEGVQRKKPLYWDLYEHAQQQLLKAKLTDPKEDPIYDEPEGLAPVPPQGLYDLPREPKDAWWCQARVKEEGYELPYNPATDDYAVPPPRSTKPLLAPKPQGPAFPEPGTATGSGIKSHNSALYSQVQKSGASGSWDCGLSRVGTDKTGVKSEGST
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		10.9422814378
1 (in isoform 3)Acetylation-10.9419481542
14PhosphorylationEGPLFLQSQRFGTKR
CCCCEEEECCCCCCC		26.0128857561
30PhosphorylationRKTWAVLYPASPHGV
EEEEEEEEECCCCCE		7.0823917254
33PhosphorylationWAVLYPASPHGVARL
EEEEEECCCCCEEEE		16.9622199227
39MethylationASPHGVARLEFFDHK
CCCCCEEEEEEECCC		32.13-
46UbiquitinationRLEFFDHKGSSSGGG
EEEEECCCCCCCCCC		63.43-
48PhosphorylationEFFDHKGSSSGGGRG
EEECCCCCCCCCCCC		26.5723917254
56PhosphorylationSSGGGRGSSRRLDCK
CCCCCCCCCCHHCCE		21.2224275569
63MalonylationSSRRLDCKVIRLAEC
CCCHHCCEEEEEEEE		40.1226320211
80PhosphorylationVAPVTVETPPEPGAT
EECEEEECCCCCCCE		39.5527067055
93PhosphorylationATAFRLDTAQRSHLL
CEEEEECHHHHHHHH		29.31-
121UbiquitinationLCRNAFPKGSWTLAP
HHHHCCCCCCEEECC		60.15-
123PhosphorylationRNAFPKGSWTLAPTD
HHCCCCCCEEECCCC		24.0227251275
125PhosphorylationAFPKGSWTLAPTDNP
CCCCCCEEECCCCCC		18.1027251275
146PhosphorylationEMLENSLYSPTWEGS
HHHHHCCCCCCCCCC		16.6611042170
174PhosphorylationRCGLHGSYVLRVEAE
HHCCCCEEEEEEEEE		14.2210799545
184PhosphorylationRVEAERLTLLTVGAQ
EEEEEEEEEEEECCC		26.4124043423
187PhosphorylationAERLTLLTVGAQSQI
EEEEEEEEECCCHHH		21.7224043423
192PhosphorylationLLTVGAQSQILEPLL
EEEECCCHHHHHHHH		20.7524043423
200PhosphorylationQILEPLLSWPYTLLR
HHHHHHHCCHHHHHH		33.4224043423
203PhosphorylationEPLLSWPYTLLRRYG
HHHHCCHHHHHHHHC		12.0812087092
204PhosphorylationPLLSWPYTLLRRYGR
HHHCCHHHHHHHHCC		18.4224043423
217PhosphorylationGRDKVMFSFEAGRRC
CCCCEEEEEECCCCC		12.23-
257UbiquitinationHRQKAQGKAGQGHDV
HHHHHCCCCCCCCCC		36.94-
269PhosphorylationHDVLRADSHEGEVAE
CCCEECCCCCCCCCC		23.5823401153
281PhosphorylationVAEGKLPSPPGPQEL
CCCCCCCCCCCCHHH		54.919008160
291PhosphorylationGPQELLDSPPALYAE
CCHHHHCCCCCEECC		32.529008160
296PhosphorylationLDSPPALYAEPLDSL
HCCCCCEECCCCCCC		15.8312087092
302PhosphorylationLYAEPLDSLRIAPCP
EECCCCCCCEEECCC		27.5126356563
310PhosphorylationLRIAPCPSQDSLYSD
CEEECCCCCCCCCCC		54.0221945579
313PhosphorylationAPCPSQDSLYSDPLD
ECCCCCCCCCCCCCC		22.9021945579
315PhosphorylationCPSQDSLYSDPLDST
CCCCCCCCCCCCCCC		18.2521945579
316PhosphorylationPSQDSLYSDPLDSTS
CCCCCCCCCCCCCCC		37.7421945579
321PhosphorylationLYSDPLDSTSAQAGE
CCCCCCCCCCCCCCC		31.7621945579
322PhosphorylationYSDPLDSTSAQAGEG
CCCCCCCCCCCCCCC		27.9621945579
323PhosphorylationSDPLDSTSAQAGEGV
CCCCCCCCCCCCCCC		23.4921945579
337PhosphorylationVQRKKPLYWDLYEHA
CCCCCCCHHHHHHHH		12.8516497976
341PhosphorylationKPLYWDLYEHAQQQL
CCCHHHHHHHHHHHH		11.8212087092
354PhosphorylationQLLKAKLTDPKEDPI
HHHHCCCCCCCCCCC		49.9328796482
362PhosphorylationDPKEDPIYDEPEGLA
CCCCCCCCCCCCCCC		21.4622252131
377PhosphorylationPVPPQGLYDLPREPK
CCCCCCCCCCCCCCC		23.4312087092
394UbiquitinationWWCQARVKEEGYELP
CCCEEEECCCCCCCC		44.49-
398PhosphorylationARVKEEGYELPYNPA
EEECCCCCCCCCCCC		19.9912087092
402PhosphorylationEEGYELPYNPATDDY
CCCCCCCCCCCCCCC		46.539008160
406PhosphorylationELPYNPATDDYAVPP
CCCCCCCCCCCCCCC		30.5728796482
409PhosphorylationYNPATDDYAVPPPRS
CCCCCCCCCCCCCCC		16.5927273156
416PhosphorylationYAVPPPRSTKPLLAP
CCCCCCCCCCCCCCC		46.70-
418AcetylationVPPPRSTKPLLAPKP
CCCCCCCCCCCCCCC		34.6126051181
435PhosphorylationPAFPEPGTATGSGIK
CCCCCCCCCCCCCHH		31.5922199227
437PhosphorylationFPEPGTATGSGIKSH
CCCCCCCCCCCHHHC		31.5522199227
439PhosphorylationEPGTATGSGIKSHNS
CCCCCCCCCHHHCCH		32.7522199227
443PhosphorylationATGSGIKSHNSALYS
CCCCCHHHCCHHHHH		26.4421945579
446PhosphorylationSGIKSHNSALYSQVQ
CCHHHCCHHHHHHHH		17.7721945579
449PhosphorylationKSHNSALYSQVQKSG
HHCCHHHHHHHHHCC		9.2121945579
450PhosphorylationSHNSALYSQVQKSGA
HCCHHHHHHHHHCCC		25.4021945579
455PhosphorylationLYSQVQKSGASGSWD
HHHHHHHCCCCCCCC		23.6226552605
458PhosphorylationQVQKSGASGSWDCGL
HHHHCCCCCCCCCCC		36.5630108239
460PhosphorylationQKSGASGSWDCGLSR
HHCCCCCCCCCCCCC		19.7623401153
466PhosphorylationGSWDCGLSRVGTDKT
CCCCCCCCCCCCCCC		15.3729978859
470PhosphorylationCGLSRVGTDKTGVKS
CCCCCCCCCCCCCCC		31.3128857561
477PhosphorylationTDKTGVKSEGST---
CCCCCCCCCCCC---		44.7923312004
480PhosphorylationTGVKSEGST------
CCCCCCCCC------		27.2225262027
481PhosphorylationGVKSEGST-------
CCCCCCCC-------		54.1924719451
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
362YPhosphorylationKinaseINSRP06213
Uniprot
362YPhosphorylationKinaseSRCP12931
PSP
398YPhosphorylationKinaseINSRP06213
Uniprot
398YPhosphorylationKinaseRETP07949
PSP
439SPhosphorylationKinaseIKBKBO14920
GPS
443SPhosphorylationKinaseIKBKBO14920
GPS
446SPhosphorylationKinaseIKBKBO14920
GPS
450SPhosphorylationKinaseIKBKBO14920
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DOK1_HUMAN !!
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DOK2_HUMANDOK2physical
10822173
SHC1_HUMANSHC1physical
10822173
SHIP1_HUMANINPP5Dphysical
10822173
CRKL_HUMANCRKLphysical
11071635
FGR_HUMANFGRphysical
11071635
HCK_HUMANHCKphysical
11071635
LYN_HUMANLYNphysical
11071635
PLCG1_HUMANPLCG1physical
11071635
P85A_HUMANPIK3R1physical
11071635
SHIP1_HUMANINPP5Dphysical
11071635
SRC_HUMANSRCphysical
11071635
YES_HUMANYES1physical
11071635
TEC_HUMANTECphysical
11071635
ABL1_HUMANABL1physical
11071635
ABL1_HUMANABL1physical
9008161
RASA1_HUMANRASA1physical
9008161
RET_HUMANRETphysical
12087092
KIT_HUMANKITphysical
11825908
DOK1_HUMANDOK1physical
11825908
CRK_HUMANCRKphysical
22974441
RASA1_HUMANRASA1physical
22974441
NCK1_HUMANNCK1physical
22974441
ABL1_HUMANABL1physical
22974441
ABL2_HUMANABL2physical
22974441
PTK6_HUMANPTK6physical
22974441
FGR_HUMANFGRphysical
22974441
ITK_HUMANITKphysical
22974441
P85A_HUMANPIK3R1physical
22974441
SHC1_HUMANSHC1physical
22974441
SRC_HUMANSRCphysical
22974441
VAV_HUMANVAV1physical
22974441
BCR_HUMANBCRphysical
9822717
ABL1_HUMANABL1physical
9822717
CRKL_HUMANCRKLphysical
9822717
RASA1_HUMANRASA1physical
9822717
RASA1_HUMANRASA1physical
11551902
RASA1_HUMANRASA1physical
10688886
SHIP1_HUMANINPP5Dphysical
15151996
RASA1_HUMANRASA1physical
15151996
DOK3_HUMANDOK3physical
25814554
CRKL_HUMANCRKLphysical
25814554
TLN1_HUMANTLN1physical
19843520
ITB1_HUMANITGB1physical
19843520
ITB3_HUMANITGB3physical
19843520
ITB7_HUMANITGB7physical
19843520
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DOK1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269; TYR-341; TYR-362;TYR-409 AND TYR-449, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281 AND SER-291, ANDMASS SPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269, AND MASSSPECTROMETRY.
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry.";
Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.;
Nat. Methods 2:591-598(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269; TYR-362; TYR-377;TYR-398; TYR-409 AND TYR-449, AND MASS SPECTROMETRY.
"p62(dok): a constitutively tyrosine-phosphorylated, GAP-associatedprotein in chronic myelogenous leukemia progenitor cells.";
Carpino N., Wisniewski D., Strife A., Marshak D., Kobayashi R.,Stillman B., Clarkson B.;
Cell 88:197-204(1997).
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PHOSPHORYLATION ATTYROSINE RESIDUES.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-315 AND TYR-449, ANDMASS 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-398; TYR-402; TYR-409AND TYR-449, AND MASS SPECTROMETRY.
"Profiling of tyrosine phosphorylation pathways in human cells usingmass spectrometry.";
Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T.,Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C.;
Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-449, AND MASSSPECTROMETRY.
"Insulin receptor-mediated p62dok tyrosine phosphorylation at residues362 and 398 plays distinct roles for binding GTPase-activating proteinand Nck and is essential for inhibiting insulin-stimulated activationof Ras and Akt.";
Wick M.J., Dong L.Q., Hu D., Langlais P., Liu F.;
J. Biol. Chem. 276:42843-42850(2001).
Cited for: PHOSPHORYLATION AT TYR-362 AND TYR-398, AND MUTAGENESIS OF TYR-362 ANDTYR-398.

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