| UniProt ID | VDAC1_YEAST | |
|---|---|---|
| UniProt AC | P04840 | |
| Protein Name | Mitochondrial outer membrane protein porin 1 | |
| Gene Name | POR1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 283 | |
| Subcellular Localization | Mitochondrion outer membrane. | |
| Protein Description | Forms a channel through the cell membrane that allows diffusion of small hydrophilic molecules. The channel adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation-selective. Is the major permeability factor of the mitochondrial outer membrane.. | |
| Protein Sequence | MSPPVYSDISRNINDLLNKDFYHATPAAFDVQTTTANGIKFSLKAKQPVKDGPLSTNVEAKLNDKQTGLGLTQGWSNTNNLQTKLEFANLTPGLKNELITSLTPGVAKSAVLNTTFTQPFFTARGAFDLCLKSPTFVGDLTMAHEGIVGGAEFGYDISAGSISRYAMALSYFAKDYSLGATLNNEQITTVDFFQNVNAFLQVGAKATMNCKLPNSNVNIEFATRYLPDASSQVKAKVSDSGIVTLAYKQLLRPGVTLGVGSSFDALKLSEPVHKLGWSLSFDA | |
| 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 |
|---|---|---|---|---|---|
| 2 | Phosphorylation | ------MSPPVYSDI ------CCCCCCCHH | 37.60 | 22369663 | |
| 6 | Phosphorylation | --MSPPVYSDISRNI --CCCCCCCHHHHHH | 13.34 | 28889911 | |
| 7 | Phosphorylation | -MSPPVYSDISRNIN -CCCCCCCHHHHHHH | 28.80 | 28889911 | |
| 10 | Phosphorylation | PPVYSDISRNINDLL CCCCCHHHHHHHHHH | 25.02 | 27214570 | |
| 19 | Acetylation | NINDLLNKDFYHATP HHHHHHCCCCCCCCC | 49.54 | 24489116 | |
| 19 | Succinylation | NINDLLNKDFYHATP HHHHHHCCCCCCCCC | 49.54 | 23954790 | |
| 25 | Phosphorylation | NKDFYHATPAAFDVQ CCCCCCCCCCEEECE | 10.51 | 27214570 | |
| 44 | Ubiquitination | NGIKFSLKAKQPVKD CCEEEEEEECCCCCC | 52.95 | 17644757 | |
| 46 | Ubiquitination | IKFSLKAKQPVKDGP EEEEEEECCCCCCCC | 54.25 | 17644757 | |
| 50 | Ubiquitination | LKAKQPVKDGPLSTN EEECCCCCCCCCCCC | 64.75 | 23749301 | |
| 50 | Succinylation | LKAKQPVKDGPLSTN EEECCCCCCCCCCCC | 64.75 | 23954790 | |
| 55 | Phosphorylation | PVKDGPLSTNVEAKL CCCCCCCCCCEEEEC | 22.52 | 27214570 | |
| 56 | Phosphorylation | VKDGPLSTNVEAKLN CCCCCCCCCEEEECC | 51.47 | 28889911 | |
| 61 | Ubiquitination | LSTNVEAKLNDKQTG CCCCEEEECCCCCCC | 34.03 | 17644757 | |
| 61 | Acetylation | LSTNVEAKLNDKQTG CCCCEEEECCCCCCC | 34.03 | 24489116 | |
| 65 | Ubiquitination | VEAKLNDKQTGLGLT EEEECCCCCCCCCCC | 49.00 | 24961812 | |
| 65 | Acetylation | VEAKLNDKQTGLGLT EEEECCCCCCCCCCC | 49.00 | 24489116 | |
| 84 | Ubiquitination | NTNNLQTKLEFANLT CCCCHHHHHHHCCCC | 32.81 | 17644757 | |
| 91 | Phosphorylation | KLEFANLTPGLKNEL HHHHCCCCHHHCHHH | 18.34 | 20377248 | |
| 95 | Ubiquitination | ANLTPGLKNELITSL CCCCHHHCHHHHHHC | 55.05 | 17644757 | |
| 95 | Acetylation | ANLTPGLKNELITSL CCCCHHHCHHHHHHC | 55.05 | 24489116 | |
| 100 | Phosphorylation | GLKNELITSLTPGVA HHCHHHHHHCCHHHH | 30.24 | 22369663 | |
| 101 | Phosphorylation | LKNELITSLTPGVAK HCHHHHHHCCHHHHH | 24.21 | 22369663 | |
| 103 | Phosphorylation | NELITSLTPGVAKSA HHHHHHCCHHHHHHH | 20.12 | 22369663 | |
| 108 | Ubiquitination | SLTPGVAKSAVLNTT HCCHHHHHHHHHCCE | 36.22 | 17644757 | |
| 109 | Phosphorylation | LTPGVAKSAVLNTTF CCHHHHHHHHHCCEE | 17.55 | 21440633 | |
| 117 | Phosphorylation | AVLNTTFTQPFFTAR HHHCCEECCCCCCCH | 32.99 | 27214570 | |
| 165 | Phosphorylation | SAGSISRYAMALSYF CHHHHHHHHHHHHHH | 8.24 | 21440633 | |
| 215 | Phosphorylation | MNCKLPNSNVNIEFA ECCCCCCCCCEEEEE | 39.97 | 29734811 | |
| 234 | 2-Hydroxyisobutyrylation | PDASSQVKAKVSDSG CCCCHHHEEEECCCC | 34.55 | - | |
| 238 | Phosphorylation | SQVKAKVSDSGIVTL HHHEEEECCCCHHHH | 25.92 | 27017623 | |
| 247 | Phosphorylation | SGIVTLAYKQLLRPG CCHHHHHHHHHHCCC | 11.46 | 27017623 | |
| 267 | Acetylation | GSSFDALKLSEPVHK CCCCHHHHCCCCHHH | 52.25 | 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 VDAC1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of VDAC1_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 VDAC1_YEAST !! | ||||||
| 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-2; THR-103 AND THR-117,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-109, AND MASSSPECTROMETRY. | |
