S10A6_HUMAN - dbPTM
S10A6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID S10A6_HUMAN
UniProt AC P06703
Protein Name Protein S100-A6
Gene Name S100A6
Organism Homo sapiens (Human).
Sequence Length 90
Subcellular Localization Nucleus envelope. Cytoplasm. Cell membrane
Peripheral membrane protein
Cytoplasmic side.
Protein Description May function as calcium sensor and modulator, contributing to cellular calcium signaling. May function by interacting with other proteins, such as TPR-containing proteins, and indirectly play a role in many physiological processes such as the reorganization of the actin cytoskeleton and in cell motility. Binds 2 calcium ions. Calcium binding is cooperative..
Protein Sequence MACPLDQAIGLLVAIFHKYSGREGDKHTLSKKELKELIQKELTIGSKLQDAEIARLMEDLDRNKDQEVNFQEYVTFLGALALIYNEALKG
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
18UbiquitinationLLVAIFHKYSGREGD
HHHHHHHHHCCCCCC
30.2933845483
19PhosphorylationLVAIFHKYSGREGDK
HHHHHHHHCCCCCCC
14.05-
20PhosphorylationVAIFHKYSGREGDKH
HHHHHHHCCCCCCCC
35.86-
26AcetylationYSGREGDKHTLSKKE
HCCCCCCCCCCCHHH
49.7125825284
26UbiquitinationYSGREGDKHTLSKKE
HCCCCCCCCCCCHHH
49.7127667366
31UbiquitinationGDKHTLSKKELKELI
CCCCCCCHHHHHHHH
54.0721906983
32UbiquitinationDKHTLSKKELKELIQ
CCCCCCHHHHHHHHH
65.9722817900
35AcetylationTLSKKELKELIQKEL
CCCHHHHHHHHHHHC
52.1223954790
35UbiquitinationTLSKKELKELIQKEL
CCCHHHHHHHHHHHC
52.1221906983
40AcetylationELKELIQKELTIGSK
HHHHHHHHHCCCCHH
47.9319608861
40UbiquitinationELKELIQKELTIGSK
HHHHHHHHHCCCCHH
47.9327667366
40MalonylationELKELIQKELTIGSK
HHHHHHHHHCCCCHH
47.9326320211
43PhosphorylationELIQKELTIGSKLQD
HHHHHHCCCCHHHCH
25.1223927012
46PhosphorylationQKELTIGSKLQDAEI
HHHCCCCHHHCHHHH
26.7528355574
47UbiquitinationKELTIGSKLQDAEIA
HHCCCCHHHCHHHHH
44.9823000965
47SuccinylationKELTIGSKLQDAEIA
HHCCCCHHHCHHHHH
44.98-
47AcetylationKELTIGSKLQDAEIA
HHCCCCHHHCHHHHH
44.9823954790
47MalonylationKELTIGSKLQDAEIA
HHCCCCHHHCHHHHH
44.9826320211
47SuccinylationKELTIGSKLQDAEIA
HHCCCCHHHCHHHHH
44.98-
57SulfoxidationDAEIARLMEDLDRNK
HHHHHHHHHHHHCCC
2.9130846556
89UbiquitinationLIYNEALKG------
HHHHHHHCC------
70.40-

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 S10A6_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of S10A6_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 S10A6_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SGT1_HUMANSUGT1physical
12746458
S10A6_HUMANS100A6physical
11937060
CYBP_HUMANCACYBPphysical
18803400
SC24A_HUMANSEC24Aphysical
22939629
TM1L2_HUMANTOM1L2physical
22939629
SC23A_HUMANSEC23Aphysical
22939629
CHIP_HUMANSTUB1physical
23344957
P53_HUMANTP53physical
23796514

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 S10A6_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-40, AND MASS SPECTROMETRY.

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