DAPP1_HUMAN - dbPTM
DAPP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DAPP1_HUMAN
UniProt AC Q9UN19
Protein Name Dual adapter for phosphotyrosine and 3-phosphotyrosine and 3-phosphoinositide
Gene Name DAPP1
Organism Homo sapiens (Human).
Sequence Length 280
Subcellular Localization Cytoplasm . Membrane
Peripheral membrane protein . Membrane-associated after cell stimulation leading to its translocation.
Protein Description May act as a B-cell-associated adapter that regulates B-cell antigen receptor (BCR)-signaling downstream of PI3K..
Protein Sequence MGRAELLEGKMSTQDPSDLWSRSDGEAELLQDLGWYHGNLTRHAAEALLLSNGCDGSYLLRDSNETTGLYSLSVRAKDSVKHFHVEYTGYSFKFGFNEFSSLKDFVKHFANQPLIGSETGTLMVLKHPYPRKVEEPSIYESVRVHTAMQTGRTEDDLVPTAPSLGTKEGYLTKQGGLVKTWKTRWFTLHRNELKYFKDQMSPEPIRILDLTECSAVQFDYSQERVNCFCLVFPFRTFYLCAKTGVEADEWIKILRWKLSQIRKQLNQGEGTIRSRSFIFK
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
12PhosphorylationELLEGKMSTQDPSDL
HHHCCCCCCCCHHHH
26.8025907765
13PhosphorylationLLEGKMSTQDPSDLW
HHCCCCCCCCHHHHH
33.2325907765
17PhosphorylationKMSTQDPSDLWSRSD
CCCCCCHHHHHCCCC
54.3325907765
73PhosphorylationTTGLYSLSVRAKDSV
CCCEEEEEEEECCCC
12.0124719451
100PhosphorylationKFGFNEFSSLKDFVK
EECCCCCCCHHHHHH
28.6928348404
101PhosphorylationFGFNEFSSLKDFVKH
ECCCCCCCHHHHHHH
44.7728348404
117PhosphorylationANQPLIGSETGTLMV
CCCCEECCCCCCEEE
25.6228060719
119PhosphorylationQPLIGSETGTLMVLK
CCEECCCCCCEEEEE
36.8428060719
121PhosphorylationLIGSETGTLMVLKHP
EECCCCCCEEEEECC
21.0728060719
132UbiquitinationLKHPYPRKVEEPSIY
EECCCCCCCCCCCHH
49.87-
137PhosphorylationPRKVEEPSIYESVRV
CCCCCCCCHHHHHHH
40.8728796482
138PhosphorylationRKVEEPSIYESVRVH
CCCCCCCHHHHHHHH
6.9117016520
139PhosphorylationKVEEPSIYESVRVHT
CCCCCCHHHHHHHHH
13.3928176443
141PhosphorylationEEPSIYESVRVHTAM
CCCCHHHHHHHHHHH
9.7628796482
160PhosphorylationTEDDLVPTAPSLGTK
CCCCCCCCCCCCCCC
43.6629083192
163PhosphorylationDLVPTAPSLGTKEGY
CCCCCCCCCCCCCEE
36.6529083192
166PhosphorylationPTAPSLGTKEGYLTK
CCCCCCCCCCEEEEC
31.0829083192
167UbiquitinationTAPSLGTKEGYLTKQ
CCCCCCCCCEEEECC
47.55-
173UbiquitinationTKEGYLTKQGGLVKT
CCCEEEECCCCEECE
44.33-
180PhosphorylationKQGGLVKTWKTRWFT
CCCCEECEEEEEEEE
25.3924719451
182AcetylationGGLVKTWKTRWFTLH
CCEECEEEEEEEEEE
33.1820167786
195PhosphorylationLHRNELKYFKDQMSP
EEHHHHHHHHHCCCC
28.6123663014
201PhosphorylationKYFKDQMSPEPIRIL
HHHHHCCCCCCEEEE
22.0723663014
263UbiquitinationWKLSQIRKQLNQGEG
HHHHHHHHHHHCCCC
61.85-
271PhosphorylationQLNQGEGTIRSRSFI
HHHCCCCCCCCCEEE
14.6527535140
274PhosphorylationQGEGTIRSRSFIFK-
CCCCCCCCCEEECC-
28.5528176443
276PhosphorylationEGTIRSRSFIFK---
CCCCCCCEEECC---
24.7625394399

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
139YPhosphorylationKinaseLCKP06239
PSP
139YPhosphorylationKinaseLYNP07948
PSP
139YPhosphorylationKinaseSRCP12931
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DAPP1_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 DAPP1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RL23_HUMANRPL23physical
21988832
FCSD2_HUMANFCHSD2physical
21988832
3BHS7_HUMANHSD3B7physical
21988832
GSTCD_HUMANGSTCDphysical
25814554
MYLIP_HUMANMYLIPphysical
25814554
WDR20_HUMANWDR20physical
25814554
BACD2_HUMANTNFAIP1physical
25814554
ZNHI1_HUMANZNHIT1physical
25814554
CNDP2_HUMANCNDP2physical
25814554
HUMMR_HUMANMGARPphysical
25814554
RET7_HUMANRBP7physical
25814554
T4S19_HUMANTM4SF19physical
25814554
APBB3_HUMANAPBB3physical
25814554
PLAL2_HUMANPLAGL2physical
25814554

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 DAPP1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-139, AND MASSSPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-139, 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-139, AND MASSSPECTROMETRY.

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