UniProt ID | PHO88_YEAST | |
---|---|---|
UniProt AC | P38264 | |
Protein Name | SRP-independent targeting protein 3 {ECO:0000303|PubMed:27905431} | |
Gene Name | PHO88 {ECO:0000303|PubMed:8709965} | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 188 | |
Subcellular Localization |
Endoplasmic reticulum membrane Single-pass membrane protein . Mitochondrion . |
|
Protein Description | Functions in the SND pathway, a SRP (signal recognition particle) and GET (guided entry of tail-anchored proteins) independent pathway for targeting a broad range of substrate proteins to the endoplasmic reticulum. SND functions in parallel to GET in targeting proteins with downstream hydrophobic motifs. [PubMed: 27905431 Involved in inorganic phosphate uptake] | |
Protein Sequence | MNPQVSNIIIMLVMMQLSRRIDMEDPTIIMYIRILYCSSIGISWIIYQMARKRIVAKNDMTTMKYVEPGNAMSGEGEKLQVTTVRDYDLKEIDSAIKSIYTGMAMMGFMHLYLKYTNPLFMQSISPVKSALEHNEVKIHLFGKPATGDLKRPFKAPSLFGGMGQTGPKTDKKSIEEAERAGNAGVKAE | |
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 |
---|---|---|---|---|---|
6 | Phosphorylation | --MNPQVSNIIIMLV --CCHHHHHHHHHHH | 19.64 | 28889911 | |
18 | Phosphorylation | MLVMMQLSRRIDMED HHHHHHHHHCCCCCC | 11.56 | 28889911 | |
57 | Ubiquitination | ARKRIVAKNDMTTMK HHHCCEECCCCCCCE | 42.45 | 23749301 | |
61 | Phosphorylation | IVAKNDMTTMKYVEP CEECCCCCCCEEECC | 26.97 | 27017623 | |
64 | Acetylation | KNDMTTMKYVEPGNA CCCCCCCEEECCCCC | 44.01 | 24489116 | |
64 | Ubiquitination | KNDMTTMKYVEPGNA CCCCCCCEEECCCCC | 44.01 | 23749301 | |
73 | Phosphorylation | VEPGNAMSGEGEKLQ ECCCCCCCCCCCEEE | 31.14 | 23749301 | |
78 | Acetylation | AMSGEGEKLQVTTVR CCCCCCCEEEEEEEE | 55.89 | 24489116 | |
78 | Ubiquitination | AMSGEGEKLQVTTVR CCCCCCCEEEEEEEE | 55.89 | 23749301 | |
90 | 2-Hydroxyisobutyrylation | TVRDYDLKEIDSAIK EEECCCHHHHHHHHH | 50.12 | - | |
90 | Succinylation | TVRDYDLKEIDSAIK EEECCCHHHHHHHHH | 50.12 | 23954790 | |
90 | Acetylation | TVRDYDLKEIDSAIK EEECCCHHHHHHHHH | 50.12 | 24489116 | |
90 | Ubiquitination | TVRDYDLKEIDSAIK EEECCCHHHHHHHHH | 50.12 | 23749301 | |
114 | Ubiquitination | GFMHLYLKYTNPLFM HHHHHHHHCCCHHHH | 36.15 | 17644757 | |
123 | Phosphorylation | TNPLFMQSISPVKSA CCHHHHHCCCCHHHH | 17.16 | 24961812 | |
125 | Phosphorylation | PLFMQSISPVKSALE HHHHHCCCCHHHHHH | 28.96 | 28152593 | |
128 | Acetylation | MQSISPVKSALEHNE HHCCCCHHHHHHCCC | 33.14 | 24489116 | |
128 | Ubiquitination | MQSISPVKSALEHNE HHCCCCHHHHHHCCC | 33.14 | 24961812 | |
137 | Ubiquitination | ALEHNEVKIHLFGKP HHHCCCEEEEECCCC | 20.45 | 17644757 | |
137 | Acetylation | ALEHNEVKIHLFGKP HHHCCCEEEEECCCC | 20.45 | 24489116 | |
143 | Ubiquitination | VKIHLFGKPATGDLK EEEEECCCCCCCCCC | 24.93 | 23749301 | |
143 | Acetylation | VKIHLFGKPATGDLK EEEEECCCCCCCCCC | 24.93 | 24489116 | |
150 | Ubiquitination | KPATGDLKRPFKAPS CCCCCCCCCCCCCCH | 63.87 | 17644757 | |
154 | Ubiquitination | GDLKRPFKAPSLFGG CCCCCCCCCCHHCCC | 63.17 | 17644757 | |
154 | Acetylation | GDLKRPFKAPSLFGG CCCCCCCCCCHHCCC | 63.17 | 24489116 | |
157 | Phosphorylation | KRPFKAPSLFGGMGQ CCCCCCCHHCCCCCC | 40.99 | 22369663 | |
165 | Phosphorylation | LFGGMGQTGPKTDKK HCCCCCCCCCCCCHH | 50.12 | 22369663 | |
168 | Succinylation | GMGQTGPKTDKKSIE CCCCCCCCCCHHHHH | 71.36 | 23954790 | |
168 | Ubiquitination | GMGQTGPKTDKKSIE CCCCCCCCCCHHHHH | 71.36 | 17644757 | |
168 | Acetylation | GMGQTGPKTDKKSIE CCCCCCCCCCHHHHH | 71.36 | 24489116 | |
172 | Ubiquitination | TGPKTDKKSIEEAER CCCCCCHHHHHHHHH | 60.52 | 17644757 | |
172 | Acetylation | TGPKTDKKSIEEAER CCCCCCHHHHHHHHH | 60.52 | 24489116 | |
173 | Phosphorylation | GPKTDKKSIEEAERA CCCCCHHHHHHHHHH | 40.76 | 27717283 | |
186 | Ubiquitination | RAGNAGVKAE----- HHHHCCCCCC----- | 45.97 | 17644757 |
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 PHO88_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PHO88_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 PHO88_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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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 SER-157, AND MASSSPECTROMETRY. |