DOK2_HUMAN - dbPTM
DOK2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DOK2_HUMAN
UniProt AC O60496
Protein Name Docking protein 2
Gene Name DOK2
Organism Homo sapiens (Human).
Sequence Length 412
Subcellular Localization
Protein Description DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK2 may modulate the cellular proliferation induced by IL-4, as well as IL-2 and IL-3. May be involved in modulating Bcr-Abl signaling. Attenuates EGF-stimulated MAP kinase activation (By similarity)..
Protein Sequence MGDGAVKQGFLYLQQQQTFGKKWRRFGASLYGGSDCALARLELQEGPEKPRRCEAARKVIRLSDCLRVAEAGGEASSPRDTSAFFLETKERLYLLAAPAAERGDWVQAICLLAFPGQRKELSGPEGKQSRPCMEENELYSSAVTVGPHKEFAVTMRPTEASERCHLRGSYTLRAGESALELWGGPEPGTQLYDWPYRFLRRFGRDKVTFSFEAGRRCVSGEGNFEFETRQGNEIFLALEEAISAQKNAAPATPQPQPATIPASLPRPDSPYSRPHDSLPPPSPTTPVPAPRPRGQEGEYAVPFDAVARSLGKNFRGILAVPPQLLADPLYDSIEETLPPRPDHIYDEPEGVAALSLYDSPQEPRGEAWRRQATADRDPAGLQHVQPAGQDFSASGWQPGTEYDNVVLKKGPK
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
7Ubiquitination-MGDGAVKQGFLYLQ
-CCCHHHHHCEEHHH		44.1421890473
12PhosphorylationAVKQGFLYLQQQQTF
HHHHCEEHHHHHHHH		10.53-
29PhosphorylationKWRRFGASLYGGSDC
HHHHHCCHHCCCCCH		23.6227080861
31PhosphorylationRRFGASLYGGSDCAL
HHHCCHHCCCCCHHH		19.5627080861
34PhosphorylationGASLYGGSDCALARL
CCHHCCCCCHHHHHH		25.7527080861
49UbiquitinationELQEGPEKPRRCEAA
HHCCCCCCCCHHHHH		47.13-
63PhosphorylationARKVIRLSDCLRVAE
HHHHHHHHHHCHHHH		19.2127067055
76PhosphorylationAEAGGEASSPRDTSA
HHCCCCCCCCCCCCC		36.2526699800
77PhosphorylationEAGGEASSPRDTSAF
HCCCCCCCCCCCCCE		30.8825954137
122PhosphorylationPGQRKELSGPEGKQS
CCCCCCCCCCCCCCC		54.0928674151
129PhosphorylationSGPEGKQSRPCMEEN
CCCCCCCCCCCCCCC		41.4929978859
139PhosphorylationCMEENELYSSAVTVG
CCCCCCEECEEEEEC		8.3928796482
140PhosphorylationMEENELYSSAVTVGP
CCCCCEECEEEEECC		25.1729978859
141PhosphorylationEENELYSSAVTVGPH
CCCCEECEEEEECCC		17.1329978859
144PhosphorylationELYSSAVTVGPHKEF
CEECEEEEECCCCCE		21.3329978859
169PhosphorylationERCHLRGSYTLRAGE
HCCCCCCCEEECCCC		14.4427067055
170PhosphorylationRCHLRGSYTLRAGES
CCCCCCCEEECCCCC		16.77-
171PhosphorylationCHLRGSYTLRAGESA
CCCCCCEEECCCCCH		16.0924719451
189PhosphorylationWGGPEPGTQLYDWPY
HCCCCCCCEECCCCH		26.56-
192PhosphorylationPEPGTQLYDWPYRFL
CCCCCEECCCCHHHH		13.2227642862
243PhosphorylationLALEEAISAQKNAAP
EHHHHHHHHHCCCCC		31.5326074081
252PhosphorylationQKNAAPATPQPQPAT
HCCCCCCCCCCCCCC		22.7726074081
259PhosphorylationTPQPQPATIPASLPR
CCCCCCCCCCCCCCC		33.8926074081
263PhosphorylationQPATIPASLPRPDSP
CCCCCCCCCCCCCCC		33.2928796482
269PhosphorylationASLPRPDSPYSRPHD
CCCCCCCCCCCCCCC		28.5528796482
271PhosphorylationLPRPDSPYSRPHDSL
CCCCCCCCCCCCCCC		22.6728796482
272PhosphorylationPRPDSPYSRPHDSLP
CCCCCCCCCCCCCCC		42.6028796482
277PhosphorylationPYSRPHDSLPPPSPT
CCCCCCCCCCCCCCC		39.4828796482
282PhosphorylationHDSLPPPSPTTPVPA
CCCCCCCCCCCCCCC		40.4228796482
284PhosphorylationSLPPPSPTTPVPAPR
CCCCCCCCCCCCCCC		48.3328796482
285PhosphorylationLPPPSPTTPVPAPRP
CCCCCCCCCCCCCCC		26.1828796482
299PhosphorylationPRGQEGEYAVPFDAV
CCCCCCCCCCCHHHH		24.6122322096
309PhosphorylationPFDAVARSLGKNFRG
CHHHHHHHCCCCCCC		31.56-
312UbiquitinationAVARSLGKNFRGILA
HHHHHCCCCCCCEEC		59.20-
330PhosphorylationQLLADPLYDSIEETL
HHHCCCCHHCHHHHC		17.0322817900
332PhosphorylationLADPLYDSIEETLPP
HCCCCHHCHHHHCCC		20.53-
336PhosphorylationLYDSIEETLPPRPDH
CHHCHHHHCCCCCCC		31.60-
345PhosphorylationPPRPDHIYDEPEGVA
CCCCCCCCCCCCCEE		15.7222817900
357PhosphorylationGVAALSLYDSPQEPR
CEEEEECCCCCCCCC		15.8226074081
359PhosphorylationAALSLYDSPQEPRGE
EEEECCCCCCCCCHH		18.2226074081
392PhosphorylationQPAGQDFSASGWQPG
EECCCCCCCCCCCCC		29.7929978859
394PhosphorylationAGQDFSASGWQPGTE
CCCCCCCCCCCCCCC		39.0929978859
400PhosphorylationASGWQPGTEYDNVVL
CCCCCCCCCCCCEEE		37.7528796482
402PhosphorylationGWQPGTEYDNVVLKK
CCCCCCCCCCEEEEC		16.8028796482
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

Oops, there are no upstream regulatory protein records of DOK2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DOK2_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 DOK2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KBP_HUMANKIAA1279physical
16189514
HS74L_HUMANHSPA4Lphysical
17353931
RAB10_HUMANRAB10physical
17353931
DJB11_HUMANDNAJB11physical
17353931
SHIP1_HUMANINPP5Dphysical
10822173
EGFR_HUMANEGFRphysical
10508618
TIE2_HUMANTEKphysical
9764820
RET_HUMANRETphysical
11470823
NCK1_HUMANNCK1physical
11689432
TIE2_HUMANTEKphysical
11689432
DOK3_HUMANDOK3physical
25814554
CRKL_HUMANCRKLphysical
25814554
LCK_HUMANLCKphysical
25814554
PLCG1_HUMANPLCG1physical
28514442
LANC2_HUMANLANCL2physical
28514442
NCK2_HUMANNCK2physical
28514442
F120B_HUMANFAM120Bphysical
28514442
MINY3_HUMANFAM188Aphysical
28514442
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 DOK2_HUMAN

loading...

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 TYR-299, AND MASSSPECTROMETRY.
"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-299, 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 TYR-299, 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-299, AND MASSSPECTROMETRY.
"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-299, AND MASSSPECTROMETRY.

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