UniProt ID | OSH6_YEAST | |
---|---|---|
UniProt AC | Q02201 | |
Protein Name | Oxysterol-binding protein homolog 6 | |
Gene Name | OSH6 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 448 | |
Subcellular Localization | Endoplasmic reticulum membrane . Localizes to the cortical endoplasmic reticulum at the endoplasmic reticulum-plasma membrane contact sites. | |
Protein Description | Lipid transporter involved in lipid countertransport between the endoplasmic reticulum and the plasma membrane: specifically exchanges phosphatidylserine with phosphatidylinositol 4-phosphate (PI4P), delivering phosphatidylserine to the plasma membrane in exchange for PI4P, which is degraded by the SAC1 phosphatase in the endoplasmic reticulum. [PubMed: 23934110] | |
Protein Sequence | MGSKKLTVGSDSHRLSKSSFSSNKSSHSATKDQPIDTDDIDEDDESGHNIILNIISQLRPGCDLTRITLPTFILEKKSMLERVTNQLQFPEFLLQAHSEKDPLKRFLYVMKWYLAGWHIAPKAVKKPLNPVLGEYFTAYWDLPNKQQAYYISEQTSHHPPECAYFYMIPESSIRVDGVVIPKSRFLGNSSAAMMDGSTVLQFLDIKDGNGKPEKYVLTQPNVYVRGILFGKMRIELGDHMIIKSPNFQADIEFKTKGYVFGTYDAIEGTVKDYDGNAYYEISGKWNDVMYLKDLKQPRSSPKVFLDTHKESPLRPKVRPLSEQGEYESRKLWKKVTDALAVRNHPVATEEKFQIEDHQRQLAKKRIEDGVEFHPKLFRRSKPGEDLDYCIYKNIPVDEDPEKQIRSILQIAPILPGQQFTDKFFIPAFEKIKSQKKMIENEKQNPAKQ | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
7 | Phosphorylation | -MGSKKLTVGSDSHR -CCCCEECCCCCCCC | 31.53 | 19823750 | |
10 | Phosphorylation | SKKLTVGSDSHRLSK CCEECCCCCCCCCCH | 31.44 | 29136822 | |
12 | Phosphorylation | KLTVGSDSHRLSKSS EECCCCCCCCCCHHH | 16.53 | 19823750 | |
16 | Phosphorylation | GSDSHRLSKSSFSSN CCCCCCCCHHHCCCC | 30.37 | 19823750 | |
18 | Phosphorylation | DSHRLSKSSFSSNKS CCCCCCHHHCCCCCC | 32.99 | 22369663 | |
19 | Phosphorylation | SHRLSKSSFSSNKSS CCCCCHHHCCCCCCC | 32.65 | 22369663 | |
21 | Phosphorylation | RLSKSSFSSNKSSHS CCCHHHCCCCCCCCC | 34.64 | 22369663 | |
22 | Phosphorylation | LSKSSFSSNKSSHSA CCHHHCCCCCCCCCC | 46.39 | 22369663 | |
28 | Phosphorylation | SSNKSSHSATKDQPI CCCCCCCCCCCCCCC | 39.31 | 30377154 | |
273 | Phosphorylation | IEGTVKDYDGNAYYE EEEEEECCCCCEEEE | 21.74 | 19779198 | |
278 | Phosphorylation | KDYDGNAYYEISGKW ECCCCCEEEEEEEEE | 12.96 | 19779198 | |
279 | Phosphorylation | DYDGNAYYEISGKWN CCCCCEEEEEEEEEC | 12.36 | 19779198 | |
300 | Phosphorylation | DLKQPRSSPKVFLDT CCCCCCCCCCEEECC | 29.98 | 27214570 | |
307 | Phosphorylation | SPKVFLDTHKESPLR CCCEEECCCCCCCCC | 36.67 | 21440633 | |
309 | Acetylation | KVFLDTHKESPLRPK CEEECCCCCCCCCCC | 63.08 | 24489116 | |
321 | Phosphorylation | RPKVRPLSEQGEYES CCCCCCCHHCCCHHH | 30.47 | 21440633 | |
328 | Phosphorylation | SEQGEYESRKLWKKV HHCCCHHHHHHHHHH | 33.54 | 29734811 | |
351 | Ubiquitination | HPVATEEKFQIEDHQ CCCCCHHHCCCHHHH | 36.02 | 23749301 | |
392 | Acetylation | DLDYCIYKNIPVDED CCCEEEEECCCCCCC | 28.61 | 24489116 | |
402 | Acetylation | PVDEDPEKQIRSILQ CCCCCHHHHHHHHHH | 57.31 | 24489116 | |
430 | Acetylation | FFIPAFEKIKSQKKM CCHHHHHHHHHHHHH | 49.32 | 24489116 | |
442 | Ubiquitination | KKMIENEKQNPAKQ- HHHHHHHCCCCCCC- | 67.94 | 23749301 |
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 OSH6_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of OSH6_YEAST !! |
* 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 OSH6_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND MASSSPECTROMETRY. |