| UniProt ID | UIP4_YEAST | |
|---|---|---|
| UniProt AC | Q08926 | |
| Protein Name | ULP1-interacting protein 4 | |
| Gene Name | UIP4 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 304 | |
| Subcellular Localization |
Endoplasmic reticulum membrane Peripheral membrane protein . Mitochondrion outer membrane . Nucleus envelope . |
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| Protein Description | ||
| Protein Sequence | MVTIVFDHPAEDFPELKIAGEFTNWEGVPMKINTSSGKWEYKFDESSVTKHNDKDKVHFKFIDQNGNWFADDEYPKEVDEHSNENNVATLNNEEDGGSAGEEKDEGDKTAHNTNENGSELYYEGPETPTPSLKGNVTFPSPKTAISQDGSAFAKETTRKERKYEHAPLNEVPVERDPKEENKELSPNFSQEQTENKQDKGLDNLSEGNDNDNTRVNEDTDVTDTQESEHEINGSDTENTDMSEQEEIQKIDKPADQNAKSIVKEGDANTEDYESVLKKLLGALGRFFGSWFSWLTTKMSSSEAS | |
| 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 |
|---|---|---|---|---|---|
| 46 | Phosphorylation | WEYKFDESSVTKHND EEEEECHHHCCCCCC | 31.77 | 30377154 | |
| 82 | Phosphorylation | PKEVDEHSNENNVAT CCCCCCCCCCCCEEE | 43.73 | 22369663 | |
| 89 | Phosphorylation | SNENNVATLNNEEDG CCCCCEEECCCCCCC | 26.24 | 22369663 | |
| 98 | Phosphorylation | NNEEDGGSAGEEKDE CCCCCCCCCCCCCCC | 38.33 | 22369663 | |
| 109 | Phosphorylation | EKDEGDKTAHNTNEN CCCCCCCCCCCCCCC | 37.58 | 22369663 | |
| 113 | Phosphorylation | GDKTAHNTNENGSEL CCCCCCCCCCCCCEE | 33.76 | 22369663 | |
| 118 | Phosphorylation | HNTNENGSELYYEGP CCCCCCCCEEEEECC | 35.69 | 22369663 | |
| 121 | Phosphorylation | NENGSELYYEGPETP CCCCCEEEEECCCCC | 8.74 | 22369663 | |
| 122 | Phosphorylation | ENGSELYYEGPETPT CCCCEEEEECCCCCC | 27.34 | 22369663 | |
| 127 | Phosphorylation | LYYEGPETPTPSLKG EEEECCCCCCCCCCC | 35.28 | 22369663 | |
| 129 | Phosphorylation | YEGPETPTPSLKGNV EECCCCCCCCCCCCE | 32.69 | 22369663 | |
| 131 | Phosphorylation | GPETPTPSLKGNVTF CCCCCCCCCCCCEEC | 45.23 | 22369663 | |
| 137 | Phosphorylation | PSLKGNVTFPSPKTA CCCCCCEECCCCCCE | 33.55 | 22369663 | |
| 140 | Phosphorylation | KGNVTFPSPKTAISQ CCCEECCCCCCEECC | 34.53 | 22369663 | |
| 143 | Phosphorylation | VTFPSPKTAISQDGS EECCCCCCEECCCCC | 32.38 | 22369663 | |
| 146 | Phosphorylation | PSPKTAISQDGSAFA CCCCCEECCCCCHHH | 21.54 | 22369663 | |
| 150 | Phosphorylation | TAISQDGSAFAKETT CEECCCCCHHHHHHH | 28.62 | 29136822 | |
| 185 | Phosphorylation | KEENKELSPNFSQEQ HHHCCCCCCCCCHHH | 20.91 | 22369663 | |
| 189 | Phosphorylation | KELSPNFSQEQTENK CCCCCCCCHHHHHCC | 39.17 | 22369663 | |
| 193 | Phosphorylation | PNFSQEQTENKQDKG CCCCHHHHHCCCCCC | 40.55 | 22369663 | |
| 205 | Phosphorylation | DKGLDNLSEGNDNDN CCCCCCCCCCCCCCC | 50.11 | 22369663 | |
| 213 | Phosphorylation | EGNDNDNTRVNEDTD CCCCCCCCCCCCCCC | 38.57 | 22369663 | |
| 278 | Acetylation | DYESVLKKLLGALGR HHHHHHHHHHHHHHH | 44.79 | 24489116 |
| 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 UIP4_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of UIP4_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 UIP4_YEAST !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| SWA2_YEAST | SWA2 | genetic | 21987634 | |
| GABAT_YEAST | UGA1 | genetic | 21987634 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| 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-140; SER-185 ANDSER-205, AND MASS SPECTROMETRY. | |
| "Profiling phosphoproteins of yeast mitochondria reveals a role ofphosphorylation in assembly of the ATP synthase."; Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.; Mol. Cell. Proteomics 6:1896-1906(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-185 ANDSER-205, AND MASS SPECTROMETRY. | |