S10AA_HUMAN - dbPTM
S10AA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
3Phosphorylation-----MPSQMEHAME
-----CCHHHHHHHH
40.6420068231
5Sulfoxidation---MPSQMEHAMETM
---CCHHHHHHHHHH
4.8430846556
9SulfoxidationPSQMEHAMETMMFTF
CHHHHHHHHHHHHHH
4.8030846556
11PhosphorylationQMEHAMETMMFTFHK
HHHHHHHHHHHHHHH
10.8020068231
12SulfoxidationMEHAMETMMFTFHKF
HHHHHHHHHHHHHHH
1.0128465586
13SulfoxidationEHAMETMMFTFHKFA
HHHHHHHHHHHHHHH
3.6030846556
15PhosphorylationAMETMMFTFHKFAGD
HHHHHHHHHHHHHCC
13.6124043423
18UbiquitinationTMMFTFHKFAGDKGY
HHHHHHHHHHCCCCC
32.4923000965
23UbiquitinationFHKFAGDKGYLTKED
HHHHHCCCCCCCHHH
48.8423000965
232-HydroxyisobutyrylationFHKFAGDKGYLTKED
HHHHHCCCCCCCHHH
48.84-
23AcetylationFHKFAGDKGYLTKED
HHHHHCCCCCCCHHH
48.8419608861
25PhosphorylationKFAGDKGYLTKEDLR
HHHCCCCCCCHHHHH
19.5521082442
27PhosphorylationAGDKGYLTKEDLRVL
HCCCCCCCHHHHHHH
24.7328152594
28MalonylationGDKGYLTKEDLRVLM
CCCCCCCHHHHHHHH
46.7826320211
28UbiquitinationGDKGYLTKEDLRVLM
CCCCCCCHHHHHHHH
46.7823000965
28AcetylationGDKGYLTKEDLRVLM
CCCCCCCHHHHHHHH
46.7819608861
282-HydroxyisobutyrylationGDKGYLTKEDLRVLM
CCCCCCCHHHHHHHH
46.78-
37SumoylationDLRVLMEKEFPGFLE
HHHHHHHCCCCCHHH
51.1728112733
37MalonylationDLRVLMEKEFPGFLE
HHHHHHHCCCCCHHH
51.1726320211
37UbiquitinationDLRVLMEKEFPGFLE
HHHHHHHCCCCCHHH
51.1723000965
37AcetylationDLRVLMEKEFPGFLE
HHHHHHHCCCCCHHH
51.1719608861
372-HydroxyisobutyrylationDLRVLMEKEFPGFLE
HHHHHHHCCCCCHHH
51.17-
47AcetylationPGFLENQKDPLAVDK
CCHHHCCCCHHHHHH
73.2726051181
47UbiquitinationPGFLENQKDPLAVDK
CCHHHCCCCHHHHHH
73.2723000965
472-HydroxyisobutyrylationPGFLENQKDPLAVDK
CCHHHCCCCHHHHHH
73.27-
542-HydroxyisobutyrylationKDPLAVDKIMKDLDQ
CCHHHHHHHHHHHHH
37.79-
54UbiquitinationKDPLAVDKIMKDLDQ
CCHHHHHHHHHHHHH
37.7923000965
54AcetylationKDPLAVDKIMKDLDQ
CCHHHHHHHHHHHHH
37.7919608861
572-HydroxyisobutyrylationLAVDKIMKDLDQCRD
HHHHHHHHHHHHHCC
59.62-
57UbiquitinationLAVDKIMKDLDQCRD
HHHHHHHHHHHHHCC
59.6223000965
57AcetylationLAVDKIMKDLDQCRD
HHHHHHHHHHHHHCC
59.6219608861
57MalonylationLAVDKIMKDLDQCRD
HHHHHHHHHHHHHCC
59.6226320211
86PhosphorylationLTIACNDYFVVHMKQ
HHHHCCCEEEEECCC
5.58-

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 S10AA_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of S10AA_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 S10AA_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRPV5_HUMANTRPV5physical
12660155
TRPV6_HUMANTRPV6physical
12660155
CSN6_HUMANCOPS6physical
16169070
SETB1_HUMANSETDB1physical
16169070
CATB_HUMANCTSBphysical
10777578
KCNK3_HUMANKCNK3physical
12198146
S10AA_HUMANS100A10physical
9886297
ANXA2_HUMANANXA2physical
9886297
ANXA2_HUMANANXA2physical
18434302
RHG07_HUMANDLC1physical
21372205
ANXA2_HUMANANXA2physical
21372205
SIN3A_HUMANSIN3Aphysical
22939629
ZFR_HUMANZFRphysical
22939629
TMM65_HUMANTMEM65physical
22939629
SRPRB_HUMANSRPRBphysical
22939629
VATE1_HUMANATP6V1E1physical
22939629
VIGLN_HUMANHDLBPphysical
22939629
SRP09_HUMANSRP9physical
22939629
WDR92_HUMANWDR92physical
22939629
UBAP2_HUMANUBAP2physical
22939629
PA24A_HUMANPLA2G4Aphysical
14599294
ANXA2_HUMANANXA2physical
14599294
ANXA2_HUMANANXA2physical
23415230
HLTF_HUMANHLTFphysical
23415230
SPT6H_HUMANSUPT6Hphysical
23415230
AHNK_HUMANAHNAKphysical
23415230
S10AA_HUMANS100A10physical
23415230
PA24A_HUMANPLA2G4Aphysical
18065419
ANXA2_HUMANANXA2physical
18065419

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 S10AA_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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
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-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.

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