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 | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
18 | Ubiquitination | LLVAIFHKYSGREGD HHHHHHHHHCCCCCC | 30.29 | 33845483 | |
19 | Phosphorylation | LVAIFHKYSGREGDK HHHHHHHHCCCCCCC | 14.05 | - | |
20 | Phosphorylation | VAIFHKYSGREGDKH HHHHHHHCCCCCCCC | 35.86 | - | |
26 | Acetylation | YSGREGDKHTLSKKE HCCCCCCCCCCCHHH | 49.71 | 25825284 | |
26 | Ubiquitination | YSGREGDKHTLSKKE HCCCCCCCCCCCHHH | 49.71 | 27667366 | |
31 | Ubiquitination | GDKHTLSKKELKELI CCCCCCCHHHHHHHH | 54.07 | 21906983 | |
32 | Ubiquitination | DKHTLSKKELKELIQ CCCCCCHHHHHHHHH | 65.97 | 22817900 | |
35 | Acetylation | TLSKKELKELIQKEL CCCHHHHHHHHHHHC | 52.12 | 23954790 | |
35 | Ubiquitination | TLSKKELKELIQKEL CCCHHHHHHHHHHHC | 52.12 | 21906983 | |
40 | Acetylation | ELKELIQKELTIGSK HHHHHHHHHCCCCHH | 47.93 | 19608861 | |
40 | Ubiquitination | ELKELIQKELTIGSK HHHHHHHHHCCCCHH | 47.93 | 27667366 | |
40 | Malonylation | ELKELIQKELTIGSK HHHHHHHHHCCCCHH | 47.93 | 26320211 | |
43 | Phosphorylation | ELIQKELTIGSKLQD HHHHHHCCCCHHHCH | 25.12 | 23927012 | |
46 | Phosphorylation | QKELTIGSKLQDAEI HHHCCCCHHHCHHHH | 26.75 | 28355574 | |
47 | Ubiquitination | KELTIGSKLQDAEIA HHCCCCHHHCHHHHH | 44.98 | 23000965 | |
47 | Succinylation | KELTIGSKLQDAEIA HHCCCCHHHCHHHHH | 44.98 | - | |
47 | Acetylation | KELTIGSKLQDAEIA HHCCCCHHHCHHHHH | 44.98 | 23954790 | |
47 | Malonylation | KELTIGSKLQDAEIA HHCCCCHHHCHHHHH | 44.98 | 26320211 | |
47 | Succinylation | KELTIGSKLQDAEIA HHCCCCHHHCHHHHH | 44.98 | - | |
57 | Sulfoxidation | DAEIARLMEDLDRNK HHHHHHHHHHHHCCC | 2.91 | 30846556 | |
89 | Ubiquitination | LIYNEALKG------ HHHHHHHCC------ | 70.40 | - |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of S10A6_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 S10A6_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
SGT1_HUMAN | SUGT1 | physical | 12746458 | |
S10A6_HUMAN | S100A6 | physical | 11937060 | |
CYBP_HUMAN | CACYBP | physical | 18803400 | |
SC24A_HUMAN | SEC24A | physical | 22939629 | |
TM1L2_HUMAN | TOM1L2 | physical | 22939629 | |
SC23A_HUMAN | SEC23A | physical | 22939629 | |
CHIP_HUMAN | STUB1 | physical | 23344957 | |
P53_HUMAN | TP53 | physical | 23796514 |
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-40, AND MASS SPECTROMETRY. |