| UniProt ID | VDAC2_RAT | |
|---|---|---|
| UniProt AC | P81155 | |
| Protein Name | Voltage-dependent anion-selective channel protein 2 | |
| Gene Name | Vdac2 | |
| Organism | Rattus norvegicus (Rat). | |
| Sequence Length | 295 | |
| Subcellular Localization | Mitochondrion outer membrane. | |
| Protein Description | Forms a channel through the mitochondrial outer 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 (By similarity).. | |
| Protein Sequence | MAECCVPVCQRPICIPPPYADLGKAARDIFNKGFGFGLVKLDVKTKSCSGVEFSTSGSSNTDTGKVSGTLETKYKWCEYGLTFTEKWNTDNTLGTEIAIEDQICQGLKLTFDTTFSPNTGKKSGKIKSAYKRECINLGCDVDFDFAGPAIHGSAVFGYEGWLAGYQMTFDSAKSKLTRSNFAVGYRTGDFQLHTNVNNGTEFGGSIYQKVCEDFDTSVNLAWTSGTNCTRFGIAAKYQLDPTASISAKVNNSSLIGVGYTQTLRPGVKLTLSALVDGKSFNAGGHKLGLALELEA | |
| 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 |
|---|---|---|---|---|---|
| 32 | Succinylation | AARDIFNKGFGFGLV HHHHHHHCCCCCEEE | 44.88 | - | |
| 32 | Ubiquitination | AARDIFNKGFGFGLV HHHHHHHCCCCCEEE | 44.88 | - | |
| 32 | Acetylation | AARDIFNKGFGFGLV HHHHHHHCCCCCEEE | 44.88 | 18763707 | |
| 32 | Succinylation | AARDIFNKGFGFGLV HHHHHHHCCCCCEEE | 44.88 | - | |
| 40 | Acetylation | GFGFGLVKLDVKTKS CCCCEEEEEEECCCC | 43.97 | 22902405 | |
| 67 | Phosphorylation | NTDTGKVSGTLETKY CCCCCEEEEEEECEE | 29.55 | 30181290 | |
| 67 | O-linked_Glycosylation | NTDTGKVSGTLETKY CCCCCEEEEEEECEE | 29.55 | 27213235 | |
| 69 | Phosphorylation | DTGKVSGTLETKYKW CCCEEEEEEECEEEE | 17.57 | 30181290 | |
| 72 | Phosphorylation | KVSGTLETKYKWCEY EEEEEEECEEEEECC | 42.67 | 30181290 | |
| 73 | Acetylation | VSGTLETKYKWCEYG EEEEEECEEEEECCC | 35.14 | 165097 | |
| 75 | Acetylation | GTLETKYKWCEYGLT EEEECEEEEECCCCE | 47.10 | 25786129 | |
| 79 | Phosphorylation | TKYKWCEYGLTFTEK CEEEEECCCCEEEEC | 17.82 | - | |
| 86 | Acetylation | YGLTFTEKWNTDNTL CCCEEEECCCCCCCC | 42.56 | 26302492 | |
| 110 | Phosphorylation | ICQGLKLTFDTTFSP HHCCCEEEEEEEECC | 20.20 | 28551015 | |
| 113 | Phosphorylation | GLKLTFDTTFSPNTG CCEEEEEEEECCCCC | 26.08 | 23991683 | |
| 114 | Phosphorylation | LKLTFDTTFSPNTGK CEEEEEEEECCCCCC | 24.78 | 23991683 | |
| 116 | Phosphorylation | LTFDTTFSPNTGKKS EEEEEEECCCCCCCC | 18.36 | 29779826 | |
| 119 | Phosphorylation | DTTFSPNTGKKSGKI EEEECCCCCCCCCCC | 54.48 | 23991683 | |
| 121 | Acetylation | TFSPNTGKKSGKIKS EECCCCCCCCCCCCE | 41.55 | 22902405 | |
| 177 | Phosphorylation | DSAKSKLTRSNFAVG HHHHHHHHCCCEEEE | 35.47 | 23991683 | |
| 179 | Phosphorylation | AKSKLTRSNFAVGYR HHHHHHCCCEEEEEE | 30.94 | 23991683 | |
| 207 | Phosphorylation | TEFGGSIYQKVCEDF CCCCCHHHHHHHCCC | 12.18 | - | |
| 236 | Acetylation | TRFGIAAKYQLDPTA CEEEEEEEEECCCCC | 25.22 | 22902405 | |
| 237 | Phosphorylation | RFGIAAKYQLDPTAS EEEEEEEEECCCCCE | 15.02 | 22817900 | |
| 242 | Phosphorylation | AKYQLDPTASISAKV EEEECCCCCEEEEEE | 32.48 | 23984901 | |
| 244 | Phosphorylation | YQLDPTASISAKVNN EECCCCCEEEEEECC | 21.39 | 23984901 | |
| 246 | Phosphorylation | LDPTASISAKVNNSS CCCCCEEEEEECCCC | 21.39 | 23984901 | |
| 248 | Acetylation | PTASISAKVNNSSLI CCCEEEEEECCCCEE | 38.41 | 22902405 | |
| 252 | Phosphorylation | ISAKVNNSSLIGVGY EEEEECCCCEEEECC | 22.71 | 23984901 | |
| 253 | Phosphorylation | SAKVNNSSLIGVGYT EEEECCCCEEEECCC | 26.57 | 23984901 | |
| 259 | Phosphorylation | SSLIGVGYTQTLRPG CCEEEECCCCCCCCC | 8.02 | 23991683 | |
| 260 | Phosphorylation | SLIGVGYTQTLRPGV CEEEECCCCCCCCCC | 14.78 | 23991683 | |
| 262 | Phosphorylation | IGVGYTQTLRPGVKL EEECCCCCCCCCCEE | 19.55 | 23991683 | |
| 278 | Acetylation | LSALVDGKSFNAGGH EEEEECCCCCCCCCC | 47.62 | 22902405 | |
| 286 | Ubiquitination | SFNAGGHKLGLALEL CCCCCCCEEEEEEEE | 47.74 | - |
| 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 VDAC2_RAT !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of VDAC2_RAT !! | ||||||
* 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 VDAC2_RAT !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of VDAC2_RAT !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Post-translational modifications of rat liver mitochondrial outermembrane proteins identified by mass spectrometry."; Distler A.M., Kerner J., Hoppel C.L.; Biochim. Biophys. Acta 1774:628-636(2007). Cited for: PROTEIN SEQUENCE OF 236-243, PHOSPHORYLATION AT TYR-237, AND MASSSPECTROMETRY. | |