UniProt ID | KES1_YEAST | |
---|---|---|
UniProt AC | P35844 | |
Protein Name | Oxysterol-binding protein homolog 4 | |
Gene Name | KES1 {ECO:0000312|SGD:S000006066} | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 434 | |
Subcellular Localization | Golgi apparatus membrane . | |
Protein Description | Lipid transporter involved in lipid countertransport between the Golgi complex and membranes of the endoplasmic reticulum: specifically exchanges sterol with phosphatidylinositol 4-phosphate (PI4P), delivering sterol to the Golgi in exchange for PI4P, which is degraded by the SAC1 phosphatase in the endoplasmic reticulum. [PubMed: 16136145] | |
Protein Sequence | MSQYASSSSWTSFLKSIASFNGDLSSLSAPPFILSPISLTEFSQYWAEHPELFLEPSFINDDNYKEHCLIDPEVESPELARMLAVTKWFISTLKSQYCSRNESLGSEKKPLNPFLGELFVGKWENKEHPEFGETVLLSEQVSHHPPVTAFSIFNDKNKVKLQGYNQIKASFTKSLMLTVKQFGHTMLDIKDESYLVTPPPLHIEGILVASPFVELEGKSYIQSSTGLLCVIEFSGRGYFSGKKNSFKARIYKDSKDSKDKEKALYTISGQWSGSSKIIKANKKEESRLFYDAARIPAEHLNVKPLEEQHPLESRKAWYDVAGAIKLGDFNLIAKTKTELEETQRELRKEEEAKGISWQRRWFKDFDYSVTPEEGALVPEKDDTFLKLASALNLSTKNAPSGTLVGDKEDRKEDLSSIHWRFQRELWDEEKEIVL | |
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 |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSQYASSSS ------CCCCCCCHH | 31.72 | 22369663 | |
4 | Phosphorylation | ----MSQYASSSSWT ----CCCCCCCHHHH | 10.92 | 28132839 | |
6 | Phosphorylation | --MSQYASSSSWTSF --CCCCCCCHHHHHH | 26.31 | 22369663 | |
7 | Phosphorylation | -MSQYASSSSWTSFL -CCCCCCCHHHHHHH | 21.88 | 22369663 | |
8 | Phosphorylation | MSQYASSSSWTSFLK CCCCCCCHHHHHHHH | 27.65 | 22369663 | |
9 | Phosphorylation | SQYASSSSWTSFLKS CCCCCCHHHHHHHHH | 36.00 | 22369663 | |
11 | Phosphorylation | YASSSSWTSFLKSIA CCCCHHHHHHHHHHH | 16.14 | 22369663 | |
12 | Phosphorylation | ASSSSWTSFLKSIAS CCCHHHHHHHHHHHH | 23.48 | 22369663 | |
95 | Phosphorylation | WFISTLKSQYCSRNE HHHHHHHHHHHCCCC | 29.51 | 27017623 | |
97 | Phosphorylation | ISTLKSQYCSRNESL HHHHHHHHHCCCCCC | 10.24 | 27017623 | |
103 | Phosphorylation | QYCSRNESLGSEKKP HHHCCCCCCCCCCCC | 41.39 | 27017623 | |
108 | Acetylation | NESLGSEKKPLNPFL CCCCCCCCCCCCHHH | 62.48 | 24489116 | |
109 | Ubiquitination | ESLGSEKKPLNPFLG CCCCCCCCCCCHHHH | 51.16 | 23749301 | |
109 | Acetylation | ESLGSEKKPLNPFLG CCCCCCCCCCCHHHH | 51.16 | 24489116 | |
156 | Ubiquitination | AFSIFNDKNKVKLQG EEEEECCCCCEEECC | 60.83 | 22817900 | |
158 | Ubiquitination | SIFNDKNKVKLQGYN EEECCCCCEEECCCH | 46.62 | 22817900 | |
160 | Ubiquitination | FNDKNKVKLQGYNQI ECCCCCEEECCCHHH | 36.38 | 23749301 | |
168 | Acetylation | LQGYNQIKASFTKSL ECCCHHHHHHHHHHH | 28.37 | 24489116 | |
185 | Phosphorylation | TVKQFGHTMLDIKDE EHHHHCCEEEEECCC | 21.58 | 19795423 | |
240 | Phosphorylation | FSGRGYFSGKKNSFK ECCCCCCCCCCCEEE | 41.02 | 23749301 | |
247 | Acetylation | SGKKNSFKARIYKDS CCCCCEEEEEEECCC | 36.25 | 25381059 | |
260 | Acetylation | DSKDSKDKEKALYTI CCCCCCCHHHEEEEE | 65.92 | 24489116 | |
315 | Ubiquitination | QHPLESRKAWYDVAG CCCCCCCCHHHHHHH | 53.18 | 23749301 | |
334 | Ubiquitination | GDFNLIAKTKTELEE CCCEEEEECHHHHHH | 43.49 | 22817900 | |
335 | Phosphorylation | DFNLIAKTKTELEET CCEEEEECHHHHHHH | 33.89 | 22369663 | |
336 | 2-Hydroxyisobutyrylation | FNLIAKTKTELEETQ CEEEEECHHHHHHHH | 39.02 | - | |
336 | Ubiquitination | FNLIAKTKTELEETQ CEEEEECHHHHHHHH | 39.02 | 23749301 | |
337 | Phosphorylation | NLIAKTKTELEETQR EEEEECHHHHHHHHH | 51.54 | 22369663 | |
342 | Phosphorylation | TKTELEETQRELRKE CHHHHHHHHHHHHHH | 24.45 | 22369663 | |
367 | Phosphorylation | RWFKDFDYSVTPEEG HHHHCCCCEECCCCC | 12.67 | 22369663 | |
368 | Phosphorylation | WFKDFDYSVTPEEGA HHHCCCCEECCCCCC | 22.74 | 22369663 | |
370 | Phosphorylation | KDFDYSVTPEEGALV HCCCCEECCCCCCCC | 21.02 | 22369663 | |
380 | Acetylation | EGALVPEKDDTFLKL CCCCCCCCCHHHHHH | 55.63 | 24489116 | |
383 | Phosphorylation | LVPEKDDTFLKLASA CCCCCCHHHHHHHHH | 40.79 | 22369663 | |
389 | Phosphorylation | DTFLKLASALNLSTK HHHHHHHHHHCCCCC | 43.66 | 22369663 | |
394 | Phosphorylation | LASALNLSTKNAPSG HHHHHCCCCCCCCCC | 35.94 | 22369663 | |
395 | Phosphorylation | ASALNLSTKNAPSGT HHHHCCCCCCCCCCC | 31.33 | 22369663 |
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 KES1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of KES1_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 KES1_YEAST !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
loading...
Phosphorylation | |
Reference | PubMed |
"A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-337; THR-370; THR-383AND SER-389, AND MASS SPECTROMETRY. |