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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
1 | Acetylation | -------MDPQNQHG -------CCCCCCCC | 17.89 | 22223895 | |
9 | Phosphorylation | DPQNQHGSGSSLVVI CCCCCCCCCCCEEEE | 33.12 | 25850435 | |
11 | Phosphorylation | QNQHGSGSSLVVIQQ CCCCCCCCCEEEEEC | 23.38 | 27251275 | |
12 | Phosphorylation | NQHGSGSSLVVIQQP CCCCCCCCEEEEECC | 28.80 | 27251275 | |
36 | Phosphorylation | YEREIQPTAILSLDQ CCCCCCCCEEEEHHH | 15.23 | 25693802 | |
40 | Phosphorylation | IQPTAILSLDQIKAI CCCCEEEEHHHHHHH | 24.64 | 25693802 | |
45 | Ubiquitination | ILSLDQIKAIRGSNE EEEHHHHHHHCCCCC | 31.93 | 32015554 | |
50 | Phosphorylation | QIKAIRGSNEYTEGP HHHHHCCCCCCCCCC | 19.35 | 25850435 | |
53 | Phosphorylation | AIRGSNEYTEGPSVV HHCCCCCCCCCCCCC | 17.84 | 25159151 | |
54 | Phosphorylation | IRGSNEYTEGPSVVK HCCCCCCCCCCCCCC | 28.43 | 26356563 | |
89 | Phosphorylation | PINVNNNYEHRHTSH EECCCCCCCCCCCCC | 18.42 | 29978859 | |
95 | Phosphorylation | NYEHRHTSHLGHAVL CCCCCCCCCCCEEEC | 15.58 | 26670566 | |
112 | Phosphorylation | NARGPILSRSTSTGS CCCCCCEECCCCCCC | 25.55 | 24719451 | |
114 | Phosphorylation | RGPILSRSTSTGSAA CCCCEECCCCCCCCC | 24.27 | 28348404 | |
115 | Phosphorylation | GPILSRSTSTGSAAS CCCEECCCCCCCCCC | 29.24 | 28348404 | |
116 | Phosphorylation | PILSRSTSTGSAASS CCEECCCCCCCCCCC | 31.83 | 28348404 | |
117 | Phosphorylation | ILSRSTSTGSAASSG CEECCCCCCCCCCCC | 34.93 | 28348404 | |
119 | Phosphorylation | SRSTSTGSAASSGSN ECCCCCCCCCCCCCC | 22.28 | 28348404 | |
122 | Phosphorylation | TSTGSAASSGSNSSA CCCCCCCCCCCCCCC | 34.64 | 22964224 | |
123 | Phosphorylation | STGSAASSGSNSSAS CCCCCCCCCCCCCCC | 41.33 | 22964224 | |
125 | Phosphorylation | GSAASSGSNSSASSE CCCCCCCCCCCCCCC | 35.17 | 22964224 | |
127 | Phosphorylation | AASSGSNSSASSEQG CCCCCCCCCCCCCCC | 29.04 | 30377224 | |
128 | Phosphorylation | ASSGSNSSASSEQGL CCCCCCCCCCCCCCC | 36.10 | 30377224 | |
131 | Phosphorylation | GSNSSASSEQGLLGR CCCCCCCCCCCCCCC | 33.39 | - | |
139 | Phosphorylation | EQGLLGRSPPTRPVP CCCCCCCCCCCCCCC | 33.17 | 29255136 | |
167 | Ubiquitination | QLIVDDLKGSLKEDL EEEHHCCCCCCCHHH | 54.14 | 32015554 | |
169 | Phosphorylation | IVDDLKGSLKEDLTQ EHHCCCCCCCHHHHH | 34.38 | 24501219 | |
171 | Ubiquitination | DDLKGSLKEDLTQHK HCCCCCCCHHHHHCC | 51.37 | 29967540 | |
304 | Phosphorylation | CKNSNTVYCKLESCP CCCCCCEEEEEECCC | 5.05 | - | |
306 | Ubiquitination | NSNTVYCKLESCPSR CCCCEEEEEECCCCC | 37.29 | 32015554 |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SPY1_HUMAN !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
TESK1_HUMAN | TESK1 | physical | 17974561 | |
CBL_HUMAN | CBL | physical | 15004239 | |
CBLB_HUMAN | CBLB | physical | 19915061 | |
CBL_HUMAN | CBL | physical | 19915061 | |
LAT_HUMAN | LAT | physical | 19915061 | |
GRB2_HUMAN | GRB2 | physical | 16893902 | |
CBL_HUMAN | CBL | physical | 16893902 | |
STAT3_HUMAN | STAT3 | physical | 21988832 | |
TYY1_HUMAN | YY1 | physical | 21988832 | |
SPY2_HUMAN | SPRY2 | physical | 25416956 | |
R3HD2_HUMAN | R3HDM2 | physical | 25416956 | |
KRA42_HUMAN | KRTAP4-2 | physical | 25416956 | |
HEXI2_HUMAN | HEXIM2 | physical | 25416956 | |
LCE1B_HUMAN | LCE1B | physical | 25416956 | |
LCE2D_HUMAN | LCE2D | physical | 25416956 | |
KR107_HUMAN | KRTAP10-7 | physical | 25416956 | |
KR109_HUMAN | KRTAP10-9 | physical | 25416956 | |
KR101_HUMAN | KRTAP10-1 | physical | 25416956 | |
KR108_HUMAN | KRTAP10-8 | physical | 25416956 | |
KR103_HUMAN | KRTAP10-3 | physical | 25416956 | |
NT2NL_HUMAN | NOTCH2NL | physical | 25416956 | |
HXA1_HUMAN | HOXA1 | physical | 21516116 |
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. |
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Phosphorylation | |
Reference | PubMed |
"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. |