UniProt ID | STAR_HUMAN | |
---|---|---|
UniProt AC | P49675 | |
Protein Name | Steroidogenic acute regulatory protein, mitochondrial | |
Gene Name | STAR | |
Organism | Homo sapiens (Human). | |
Sequence Length | 285 | |
Subcellular Localization | Mitochondrion. | |
Protein Description | Plays a key role in steroid hormone synthesis by enhancing the metabolism of cholesterol into pregnenolone. Mediates the transfer of cholesterol from the outer mitochondrial membrane to the inner mitochondrial membrane where it is cleaved to pregnenolone.. | |
Protein Sequence | MLLATFKLCAGSSYRHMRNMKGLRQQAVMAISQELNRRALGGPTPSTWINQVRRRSSLLGSRLEETLYSDQELAYLQQGEEAMQKALGILSNQEGWKKESQQDNGDKVMSKVVPDVGKVFRLEVVVDQPMERLYEELVERMEAMGEWNPNVKEIKVLQKIGKDTFITHELAAEAAGNLVGPRDFVSVRCAKRRGSTCVLAGMATDFGNMPEQKGVIRAEHGPTCMVLHPLAGSPSKTKLTWLLSIDLKGWLPKSIINQVLSQTQVDFANHLRKRLESHPASEARC | |
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 |
---|---|---|---|---|---|
5 | Phosphorylation | ---MLLATFKLCAGS ---CCHHHHHHHCCC | 22.67 | 26074081 | |
12 | Phosphorylation | TFKLCAGSSYRHMRN HHHHHCCCCHHHHHH | 12.98 | 26074081 | |
13 | Phosphorylation | FKLCAGSSYRHMRNM HHHHCCCCHHHHHHC | 25.85 | 26074081 | |
14 | Phosphorylation | KLCAGSSYRHMRNMK HHHCCCCHHHHHHCC | 13.26 | 26074081 | |
32 | Phosphorylation | QQAVMAISQELNRRA HHHHHHHHHHHHHHH | 14.20 | 26074081 | |
56 | Phosphorylation | INQVRRRSSLLGSRL HHHHHHHHHHHCHHH | 24.43 | - | |
57 | Phosphorylation | NQVRRRSSLLGSRLE HHHHHHHHHHCHHHH | 26.29 | 22817900 | |
61 | Phosphorylation | RRSSLLGSRLEETLY HHHHHHCHHHHHHHC | 33.39 | - | |
100 | Phosphorylation | QEGWKKESQQDNGDK CCCHHHHHHCCCCCH | 41.86 | 30619164 | |
195 | Phosphorylation | RCAKRRGSTCVLAGM EEHHHCCCEEEEEEE | 19.47 | 9097960 | |
204 | Phosphorylation | CVLAGMATDFGNMPE EEEEEEECCCCCCCH | 23.99 | - | |
244 | Phosphorylation | TKLTWLLSIDLKGWL CCEEEEEEEECCCCC | 16.34 | 24961811 | |
254 | Phosphorylation | LKGWLPKSIINQVLS CCCCCCHHHHHHHHH | 27.11 | 27174698 | |
261 | Phosphorylation | SIINQVLSQTQVDFA HHHHHHHHHHHHHHH | 32.12 | 27174698 | |
263 | Phosphorylation | INQVLSQTQVDFANH HHHHHHHHHHHHHHH | 27.47 | 27174698 | |
273 | Acetylation | DFANHLRKRLESHPA HHHHHHHHHHHHCCC | 68.63 | 7704201 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
57 | S | Phosphorylation | Kinase | PKA-FAMILY | - | GPS |
57 | S | Phosphorylation | Kinase | PKA | - | Uniprot |
195 | S | Phosphorylation | Kinase | PKA-FAMILY | - | GPS |
195 | S | Phosphorylation | Kinase | PKA | - | Uniprot |
- | K | Ubiquitination | E3 ubiquitin ligase | SIAH1 | Q8IUQ4 | PMID:22199232 |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of STAR_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 STAR_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
NUCB2_HUMAN | NUCB2 | physical | 12909641 | |
CCHCR_HUMAN | CCHCR1 | physical | 12909641 | |
FEZ1_HUMAN | FEZ1 | physical | 16169070 |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
201710 | Adrenal hyperplasia 1 (AH1) | |||||
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 |
"The steroidogenic acute regulatory protein (StAR): a window into thecomplexities of intracellular cholesterol trafficking."; Strauss J.F. III, Kallen C.B., Christenson L.K., Watari H., Devoto L.,Arakane F., Kiriakidou M., Sugawara T.; Recent Prog. Horm. Res. 54:369-394(1999). Cited for: PHOSPHORYLATION AT SER-57 AND SER-195. |