UniProt ID | S10AA_HUMAN | |
---|---|---|
UniProt AC | P60903 | |
Protein Name | Protein S100-A10 | |
Gene Name | S100A10 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 97 | |
Subcellular Localization | ||
Protein Description | Because S100A10 induces the dimerization of ANXA2/p36, it may function as a regulator of protein phosphorylation in that the ANXA2 monomer is the preferred target (in vitro) of tyrosine-specific kinase.. | |
Protein Sequence | MPSQMEHAMETMMFTFHKFAGDKGYLTKEDLRVLMEKEFPGFLENQKDPLAVDKIMKDLDQCRDGKVGFQSFFSLIAGLTIACNDYFVVHMKQKGKK | |
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 |
---|---|---|---|---|---|
3 | Phosphorylation | -----MPSQMEHAME -----CCHHHHHHHH | 40.64 | 20068231 | |
5 | Sulfoxidation | ---MPSQMEHAMETM ---CCHHHHHHHHHH | 4.84 | 30846556 | |
9 | Sulfoxidation | PSQMEHAMETMMFTF CHHHHHHHHHHHHHH | 4.80 | 30846556 | |
11 | Phosphorylation | QMEHAMETMMFTFHK HHHHHHHHHHHHHHH | 10.80 | 20068231 | |
12 | Sulfoxidation | MEHAMETMMFTFHKF HHHHHHHHHHHHHHH | 1.01 | 28465586 | |
13 | Sulfoxidation | EHAMETMMFTFHKFA HHHHHHHHHHHHHHH | 3.60 | 30846556 | |
15 | Phosphorylation | AMETMMFTFHKFAGD HHHHHHHHHHHHHCC | 13.61 | 24043423 | |
18 | Ubiquitination | TMMFTFHKFAGDKGY HHHHHHHHHHCCCCC | 32.49 | 23000965 | |
23 | Ubiquitination | FHKFAGDKGYLTKED HHHHHCCCCCCCHHH | 48.84 | 23000965 | |
23 | 2-Hydroxyisobutyrylation | FHKFAGDKGYLTKED HHHHHCCCCCCCHHH | 48.84 | - | |
23 | Acetylation | FHKFAGDKGYLTKED HHHHHCCCCCCCHHH | 48.84 | 19608861 | |
25 | Phosphorylation | KFAGDKGYLTKEDLR HHHCCCCCCCHHHHH | 19.55 | 21082442 | |
27 | Phosphorylation | AGDKGYLTKEDLRVL HCCCCCCCHHHHHHH | 24.73 | 28152594 | |
28 | Malonylation | GDKGYLTKEDLRVLM CCCCCCCHHHHHHHH | 46.78 | 26320211 | |
28 | Ubiquitination | GDKGYLTKEDLRVLM CCCCCCCHHHHHHHH | 46.78 | 23000965 | |
28 | Acetylation | GDKGYLTKEDLRVLM CCCCCCCHHHHHHHH | 46.78 | 19608861 | |
28 | 2-Hydroxyisobutyrylation | GDKGYLTKEDLRVLM CCCCCCCHHHHHHHH | 46.78 | - | |
37 | Sumoylation | DLRVLMEKEFPGFLE HHHHHHHCCCCCHHH | 51.17 | 28112733 | |
37 | Malonylation | DLRVLMEKEFPGFLE HHHHHHHCCCCCHHH | 51.17 | 26320211 | |
37 | Ubiquitination | DLRVLMEKEFPGFLE HHHHHHHCCCCCHHH | 51.17 | 23000965 | |
37 | Acetylation | DLRVLMEKEFPGFLE HHHHHHHCCCCCHHH | 51.17 | 19608861 | |
37 | 2-Hydroxyisobutyrylation | DLRVLMEKEFPGFLE HHHHHHHCCCCCHHH | 51.17 | - | |
47 | Acetylation | PGFLENQKDPLAVDK CCHHHCCCCHHHHHH | 73.27 | 26051181 | |
47 | Ubiquitination | PGFLENQKDPLAVDK CCHHHCCCCHHHHHH | 73.27 | 23000965 | |
47 | 2-Hydroxyisobutyrylation | PGFLENQKDPLAVDK CCHHHCCCCHHHHHH | 73.27 | - | |
54 | 2-Hydroxyisobutyrylation | KDPLAVDKIMKDLDQ CCHHHHHHHHHHHHH | 37.79 | - | |
54 | Ubiquitination | KDPLAVDKIMKDLDQ CCHHHHHHHHHHHHH | 37.79 | 23000965 | |
54 | Acetylation | KDPLAVDKIMKDLDQ CCHHHHHHHHHHHHH | 37.79 | 19608861 | |
57 | 2-Hydroxyisobutyrylation | LAVDKIMKDLDQCRD HHHHHHHHHHHHHCC | 59.62 | - | |
57 | Ubiquitination | LAVDKIMKDLDQCRD HHHHHHHHHHHHHCC | 59.62 | 23000965 | |
57 | Acetylation | LAVDKIMKDLDQCRD HHHHHHHHHHHHHCC | 59.62 | 19608861 | |
57 | Malonylation | LAVDKIMKDLDQCRD HHHHHHHHHHHHHCC | 59.62 | 26320211 | |
86 | Phosphorylation | LTIACNDYFVVHMKQ HHHHCCCEEEEECCC | 5.58 | - |
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 S10AA_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of S10AA_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 S10AA_HUMAN !! |
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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Acetylation | |
Reference | PubMed |
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-23; LYS-28; LYS-37; LYS-54AND LYS-57, AND MASS SPECTROMETRY. | |
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-25, 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-25, AND MASSSPECTROMETRY. |