SPY1_HUMAN - dbPTM
SPY1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPY1_HUMAN
UniProt AC O43609
Protein Name Protein sprouty homolog 1
Gene Name SPRY1
Organism Homo sapiens (Human).
Sequence Length 319
Subcellular Localization Cytoplasm. Membrane
Peripheral membrane protein. Found in the cytoplasm in unstimulated cells but is translocated to the membrane ruffles in cells stimulated with EGF (epidermal growth factor).
Protein Description May function as an antagonist of fibroblast growth factor (FGF) pathways and may negatively modulate respiratory organogenesis..
Protein Sequence MDPQNQHGSGSSLVVIQQPSLDSRQRLDYEREIQPTAILSLDQIKAIRGSNEYTEGPSVVKRPAPRTAPRQEKHERTHEIIPINVNNNYEHRHTSHLGHAVLPSNARGPILSRSTSTGSAASSGSNSSASSEQGLLGRSPPTRPVPGHRSERAIRTQPKQLIVDDLKGSLKEDLTQHKFICEQCGKCKCGECTAPRTLPSCLACNRQCLCSAESMVEYGTCMCLVKGIFYHCSNDDEGDSYSDNPCSCSQSHCCSRYLCMGAMSLFLPCLLCYPPAKGCLKLCRRCYDWIHRPGCRCKNSNTVYCKLESCPSRGQGKPS
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-------MDPQNQHG
-------CCCCCCCC
17.8922223895
9PhosphorylationDPQNQHGSGSSLVVI
CCCCCCCCCCCEEEE
33.1225850435
11PhosphorylationQNQHGSGSSLVVIQQ
CCCCCCCCCEEEEEC
23.3827251275
12PhosphorylationNQHGSGSSLVVIQQP
CCCCCCCCEEEEECC
28.8027251275
36PhosphorylationYEREIQPTAILSLDQ
CCCCCCCCEEEEHHH
15.2325693802
40PhosphorylationIQPTAILSLDQIKAI
CCCCEEEEHHHHHHH
24.6425693802
45UbiquitinationILSLDQIKAIRGSNE
EEEHHHHHHHCCCCC
31.9332015554
50PhosphorylationQIKAIRGSNEYTEGP
HHHHHCCCCCCCCCC
19.3525850435
53PhosphorylationAIRGSNEYTEGPSVV
HHCCCCCCCCCCCCC
17.8425159151
54PhosphorylationIRGSNEYTEGPSVVK
HCCCCCCCCCCCCCC
28.4326356563
89PhosphorylationPINVNNNYEHRHTSH
EECCCCCCCCCCCCC
18.4229978859
95PhosphorylationNYEHRHTSHLGHAVL
CCCCCCCCCCCEEEC
15.5826670566
112PhosphorylationNARGPILSRSTSTGS
CCCCCCEECCCCCCC
25.5524719451
114PhosphorylationRGPILSRSTSTGSAA
CCCCEECCCCCCCCC
24.2728348404
115PhosphorylationGPILSRSTSTGSAAS
CCCEECCCCCCCCCC
29.2428348404
116PhosphorylationPILSRSTSTGSAASS
CCEECCCCCCCCCCC
31.8328348404
117PhosphorylationILSRSTSTGSAASSG
CEECCCCCCCCCCCC
34.9328348404
119PhosphorylationSRSTSTGSAASSGSN
ECCCCCCCCCCCCCC
22.2828348404
122PhosphorylationTSTGSAASSGSNSSA
CCCCCCCCCCCCCCC
34.6422964224
123PhosphorylationSTGSAASSGSNSSAS
CCCCCCCCCCCCCCC
41.3322964224
125PhosphorylationGSAASSGSNSSASSE
CCCCCCCCCCCCCCC
35.1722964224
127PhosphorylationAASSGSNSSASSEQG
CCCCCCCCCCCCCCC
29.0430377224
128PhosphorylationASSGSNSSASSEQGL
CCCCCCCCCCCCCCC
36.1030377224
131PhosphorylationGSNSSASSEQGLLGR
CCCCCCCCCCCCCCC
33.39-
139PhosphorylationEQGLLGRSPPTRPVP
CCCCCCCCCCCCCCC
33.1729255136
167UbiquitinationQLIVDDLKGSLKEDL
EEEHHCCCCCCCHHH
54.1432015554
169PhosphorylationIVDDLKGSLKEDLTQ
EHHCCCCCCCHHHHH
34.3824501219
171UbiquitinationDDLKGSLKEDLTQHK
HCCCCCCCHHHHHCC
51.3729967540
304PhosphorylationCKNSNTVYCKLESCP
CCCCCCEEEEEECCC
5.05-
306UbiquitinationNSNTVYCKLESCPSR
CCCCEEEEEECCCCC
37.2932015554

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 SPY1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPY1_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 SPY1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TESK1_HUMANTESK1physical
17974561
CBL_HUMANCBLphysical
15004239
CBLB_HUMANCBLBphysical
19915061
CBL_HUMANCBLphysical
19915061
LAT_HUMANLATphysical
19915061
GRB2_HUMANGRB2physical
16893902
CBL_HUMANCBLphysical
16893902
STAT3_HUMANSTAT3physical
21988832
TYY1_HUMANYY1physical
21988832
SPY2_HUMANSPRY2physical
25416956
R3HD2_HUMANR3HDM2physical
25416956
KRA42_HUMANKRTAP4-2physical
25416956
HEXI2_HUMANHEXIM2physical
25416956
LCE1B_HUMANLCE1Bphysical
25416956
LCE2D_HUMANLCE2Dphysical
25416956
KR107_HUMANKRTAP10-7physical
25416956
KR109_HUMANKRTAP10-9physical
25416956
KR101_HUMANKRTAP10-1physical
25416956
KR108_HUMANKRTAP10-8physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956
HXA1_HUMANHOXA1physical
21516116

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 SPY1_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-53, 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-53, 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-53, AND MASSSPECTROMETRY.

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