| UniProt ID | ADT1_RAT | |
|---|---|---|
| UniProt AC | Q05962 | |
| Protein Name | ADP/ATP translocase 1 | |
| Gene Name | Slc25a4 | |
| Organism | Rattus norvegicus (Rat). | |
| Sequence Length | 298 | |
| Subcellular Localization |
Mitochondrion inner membrane Multi-pass membrane protein. |
|
| Protein Description | Involved in mitochondrial ADP/ATP transport. Catalyzes the exchange of cytoplasmic ADP with mitochondrial ATP across the mitochondrial inner membrane.. | |
| Protein Sequence | MGDQALSFLKDFLAGGIAAAVSKTAVAPIERVKLLLQVQHASKQISAEKQYKGIIDCVVRIPKEQGFLSFWRGNLANVIRYFPTQALNFAFKDKYKQIFLGGVDRHKQFWRYFAGNLASGGAAGATSLCFVYPLDFARTRLAADVGKGSSQREFNGLGDCLTKIFKSDGLKGLYQGFSVSVQGIIIYRAAYFGVYDTAKGMLPDPKNVHIIVSWMIAQSVTAVAGLVSYPFDTVRRRMMMQSGRKGADIMYTGTVDCWRKIAKDEGRKAFFKGAWSNVLRGMGGAFVLVLYDEIKKYV | |
| 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 | Acetylation | ------MGDQALSFL ------CCHHHHHHH | 35.42 | - | |
| 7 | Phosphorylation | -MGDQALSFLKDFLA -CCHHHHHHHHHHHH | 31.39 | 22673903 | |
| 10 | Acetylation | DQALSFLKDFLAGGI HHHHHHHHHHHHHHH | 44.41 | 25786129 | |
| 22 | Phosphorylation | GGIAAAVSKTAVAPI HHHHHHHCCCCCCCH | 21.40 | 23991683 | |
| 22 | O-linked_Glycosylation | GGIAAAVSKTAVAPI HHHHHHHCCCCCCCH | 21.40 | 27213235 | |
| 23 | Acetylation | GIAAAVSKTAVAPIE HHHHHHCCCCCCCHH | 33.63 | 25786129 | |
| 24 | Phosphorylation | IAAAVSKTAVAPIER HHHHHCCCCCCCHHH | 20.89 | 23991683 | |
| 33 | Acetylation | VAPIERVKLLLQVQH CCCHHHHHHHHHHHH | 39.37 | 22902405 | |
| 42 | Phosphorylation | LLQVQHASKQISAEK HHHHHHHHHHCCHHH | 23.98 | 23991683 | |
| 43 | Acetylation | LQVQHASKQISAEKQ HHHHHHHHHCCHHHH | 53.05 | 22902405 | |
| 52 | Methylation | ISAEKQYKGIIDCVV CCHHHHHCCEEEEEE | 40.93 | 31213526 | |
| 57 | Glutathionylation | QYKGIIDCVVRIPKE HHCCEEEEEEECCHH | 1.83 | 22833525 | |
| 63 | Acetylation | DCVVRIPKEQGFLSF EEEEECCHHHCCHHH | 61.37 | 22902405 | |
| 69 | O-linked_Glycosylation | PKEQGFLSFWRGNLA CHHHCCHHHHCCCHH | 22.09 | 27213235 | |
| 81 | Phosphorylation | NLANVIRYFPTQALN CHHHHHHHCHHHHHH | 11.64 | 30181290 | |
| 84 | Phosphorylation | NVIRYFPTQALNFAF HHHHHCHHHHHHHHC | 19.30 | 22108457 | |
| 92 | Acetylation | QALNFAFKDKYKQIF HHHHHHCHHHCCEEE | 50.29 | 25786129 | |
| 94 | Acetylation | LNFAFKDKYKQIFLG HHHHCHHHCCEEEEC | 55.74 | 22902405 | |
| 96 | Acetylation | FAFKDKYKQIFLGGV HHCHHHCCEEEECCC | 42.53 | 22902405 | |
| 107 | Acetylation | LGGVDRHKQFWRYFA ECCCHHHHHHHHHHH | 48.35 | 22902405 | |
| 112 | Phosphorylation | RHKQFWRYFAGNLAS HHHHHHHHHHHCCCC | 6.59 | 23991683 | |
| 119 | Phosphorylation | YFAGNLASGGAAGAT HHHHCCCCCCCCCCC | 40.71 | 23991683 | |
| 126 | Phosphorylation | SGGAAGATSLCFVYP CCCCCCCCEEEEEEE | 22.70 | 23991683 | |
| 127 | Phosphorylation | GGAAGATSLCFVYPL CCCCCCCEEEEEEEC | 23.70 | 23991683 | |
| 147 | Succinylation | RLAADVGKGSSQREF HHHHCCCCCCCCHHC | 56.31 | - | |
| 147 | Acetylation | RLAADVGKGSSQREF HHHHCCCCCCCCHHC | 56.31 | 22902405 | |
| 147 | Succinylation | RLAADVGKGSSQREF HHHHCCCCCCCCHHC | 56.31 | - | |
| 147 | Ubiquitination | RLAADVGKGSSQREF HHHHCCCCCCCCHHC | 56.31 | - | |
| 149 | Phosphorylation | AADVGKGSSQREFNG HHCCCCCCCCHHCCC | 27.12 | 27097102 | |
| 150 | O-linked_Glycosylation | ADVGKGSSQREFNGL HCCCCCCCCHHCCCH | 41.76 | 27213235 | |
| 150 | Phosphorylation | ADVGKGSSQREFNGL HCCCCCCCCHHCCCH | 41.76 | 27097102 | |
| 160 | S-nitrosylation | EFNGLGDCLTKIFKS HCCCHHHHHHHHHHH | 5.02 | 16418269 | |
| 160 | S-nitrosocysteine | EFNGLGDCLTKIFKS HCCCHHHHHHHHHHH | 5.02 | - | |
| 163 | Acetylation | GLGDCLTKIFKSDGL CHHHHHHHHHHHCCC | 32.95 | 22902405 | |
| 166 | Acetylation | DCLTKIFKSDGLKGL HHHHHHHHHCCCCHH | 51.62 | 22902405 | |
| 167 | O-linked_Glycosylation | CLTKIFKSDGLKGLY HHHHHHHHCCCCHHH | 26.60 | 27213235 | |
| 167 | Phosphorylation | CLTKIFKSDGLKGLY HHHHHHHHCCCCHHH | 26.60 | 23991683 | |
| 171 | Acetylation | IFKSDGLKGLYQGFS HHHHCCCCHHHCCCC | 53.01 | 26302492 | |
| 191 | Phosphorylation | IIIYRAAYFGVYDTA EEEEEEHHHCCHHCC | 10.40 | 23991683 | |
| 195 | Phosphorylation | RAAYFGVYDTAKGML EEHHHCCHHCCCCCC | 14.14 | 23991683 | |
| 197 | Phosphorylation | AYFGVYDTAKGMLPD HHHCCHHCCCCCCCC | 16.75 | 23991683 | |
| 199 | Acetylation | FGVYDTAKGMLPDPK HCCHHCCCCCCCCCC | 47.12 | 22902405 | |
| 219 | Phosphorylation | VSWMIAQSVTAVAGL EEHHHHHHHHHHHHH | 16.65 | 22817900 | |
| 242 | Phosphorylation | RRRMMMQSGRKGADI HHHHHHHCCCCCCCE | 23.75 | 23991683 | |
| 245 | Succinylation | MMMQSGRKGADIMYT HHHHCCCCCCCEEEE | 63.07 | - | |
| 245 | Succinylation | MMMQSGRKGADIMYT HHHHCCCCCCCEEEE | 63.07 | - | |
| 257 | S-nitrosocysteine | MYTGTVDCWRKIAKD EEEECHHHHHHHHHH | 3.09 | - | |
| 257 | S-nitrosylation | MYTGTVDCWRKIAKD EEEECHHHHHHHHHH | 3.09 | 16418269 | |
| 272 | Succinylation | EGRKAFFKGAWSNVL HHHHHHHHHHHHHHH | 41.06 | 26843850 | |
| 272 | Succinylation | EGRKAFFKGAWSNVL HHHHHHHHHHHHHHH | 41.06 | - | |
| 272 | Acetylation | EGRKAFFKGAWSNVL HHHHHHHHHHHHHHH | 41.06 | 25786129 | |
| 276 | Phosphorylation | AFFKGAWSNVLRGMG HHHHHHHHHHHHHCC | 19.27 | 23991683 |
| 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 ADT1_RAT !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ADT1_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 ADT1_RAT !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of ADT1_RAT !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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