| UniProt ID | MPCP_MOUSE | |
|---|---|---|
| UniProt AC | Q8VEM8 | |
| Protein Name | Phosphate carrier protein, mitochondrial | |
| Gene Name | Slc25a3 | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 357 | |
| Subcellular Localization |
Mitochondrion inner membrane Multi-pass membrane protein. |
|
| Protein Description | Transport of phosphate groups from the cytosol to mitochondrial matrix. Phosphate is cotransported with H(+). May play a role regulation of the mitochondrial permeability transition pore (mPTP) (By similarity).. | |
| Protein Sequence | MFSSVAHLARANPFNAPHLQLVHDGLSGPRSPPAPPRRSRHLAAAAVEEYSCEFGSMKYYALCGFGGVLSCGLTHTAVVPLDLVKCRMQVDPQKYKGIFNGFSITLKEDGVRGLAKGWAPTLIGYSMQGLCKFGFYEVFKALYSNILGEENTYLWRTSLYLASSASAEFFADIALAPMEAAKVRIQTQPGYANTLREAVPKMYKEEGLNAFYKGVAPLWMRQIPYTMMKFACFERTVEALYKFVVPKPRSECTKAEQLVVTFVAGYIAGVFCAIVSHPADSVVSVLNKEKGSTASQVLQRLGFRGVWKGLFARIIMIGTLTALQWFIYDSVKVYFRLPRPPPPEMPESLKKKLGLTE | |
| 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 |
|---|---|---|---|---|---|
| 27 | Phosphorylation | QLVHDGLSGPRSPPA EEECCCCCCCCCCCC | 52.89 | 23140645 | |
| 31 | Phosphorylation | DGLSGPRSPPAPPRR CCCCCCCCCCCCCCH | 38.07 | 22817900 | |
| 39 | Phosphorylation | PPAPPRRSRHLAAAA CCCCCCHHHHHHHHH | 25.90 | 22817900 | |
| 50 | Phosphorylation | AAAAVEEYSCEFGSM HHHHHHHHHCCCCCC | 12.71 | - | |
| 52 | S-nitrosylation | AAVEEYSCEFGSMKY HHHHHHHCCCCCCCC | 5.00 | 22178444 | |
| 86 | S-nitrosocysteine | VPLDLVKCRMQVDPQ EEHHHHCCCCCCCHH | 3.23 | - | |
| 86 | S-nitrosylation | VPLDLVKCRMQVDPQ EEHHHHCCCCCCCHH | 3.23 | 21278135 | |
| 94 | Acetylation | RMQVDPQKYKGIFNG CCCCCHHHCCEECCC | 55.08 | 23864654 | |
| 94 | Ubiquitination | RMQVDPQKYKGIFNG CCCCCHHHCCEECCC | 55.08 | - | |
| 96 | Acetylation | QVDPQKYKGIFNGFS CCCHHHCCEECCCEE | 53.19 | 23864654 | |
| 96 | Succinylation | QVDPQKYKGIFNGFS CCCHHHCCEECCCEE | 53.19 | 24315375 | |
| 107 | Methylation | NGFSITLKEDGVRGL CCEEEEEECCCCCHH | 45.14 | - | |
| 107 | Acetylation | NGFSITLKEDGVRGL CCEEEEEECCCCCHH | 45.14 | 23576753 | |
| 107 | Succinylation | NGFSITLKEDGVRGL CCEEEEEECCCCCHH | 45.14 | 26388266 | |
| 131 | S-palmitoylation | GYSMQGLCKFGFYEV CCCHHHHHHHHHHHH | 4.37 | 28526873 | |
| 131 | S-nitrosylation | GYSMQGLCKFGFYEV CCCHHHHHHHHHHHH | 4.37 | 21278135 | |
| 131 | S-nitrosocysteine | GYSMQGLCKFGFYEV CCCHHHHHHHHHHHH | 4.37 | - | |
| 132 | Acetylation | YSMQGLCKFGFYEVF CCHHHHHHHHHHHHH | 54.27 | 23576753 | |
| 132 | Malonylation | YSMQGLCKFGFYEVF CCHHHHHHHHHHHHH | 54.27 | 26073543 | |
| 136 | Phosphorylation | GLCKFGFYEVFKALY HHHHHHHHHHHHHHH | 16.15 | 25195567 | |
| 152 | Phosphorylation | NILGEENTYLWRTSL HHCCCCCCCHHHHHH | 24.22 | 29899451 | |
| 153 | Phosphorylation | ILGEENTYLWRTSLY HCCCCCCCHHHHHHH | 18.82 | 22817900 | |
| 191 | Phosphorylation | RIQTQPGYANTLREA HHCCCCCHHHHHHHH | 11.89 | 25195567 | |
| 201 | Acetylation | TLREAVPKMYKEEGL HHHHHHHHHHHHHCH | 48.54 | 23864654 | |
| 204 | Succinylation | EAVPKMYKEEGLNAF HHHHHHHHHHCHHHH | 45.87 | 23806337 | |
| 204 | Ubiquitination | EAVPKMYKEEGLNAF HHHHHHHHHHCHHHH | 45.87 | - | |
| 204 | Acetylation | EAVPKMYKEEGLNAF HHHHHHHHHHCHHHH | 45.87 | 23806337 | |
| 212 | Phosphorylation | EEGLNAFYKGVAPLW HHCHHHHHHCCHHHH | 12.38 | 25195567 | |
| 213 | Acetylation | EGLNAFYKGVAPLWM HCHHHHHHCCHHHHH | 40.22 | 23864654 | |
| 213 | Succinylation | EGLNAFYKGVAPLWM HCHHHHHHCCHHHHH | 40.22 | 23954790 | |
| 225 | Phosphorylation | LWMRQIPYTMMKFAC HHHHHCCHHHHHHHH | 14.64 | 25195567 | |
| 229 | Acetylation | QIPYTMMKFACFERT HCCHHHHHHHHHHHH | 20.98 | 23864654 | |
| 229 | Succinylation | QIPYTMMKFACFERT HCCHHHHHHHHHHHH | 20.98 | 24315375 | |
| 229 | Ubiquitination | QIPYTMMKFACFERT HCCHHHHHHHHHHHH | 20.98 | - | |
| 232 | S-nitrosylation | YTMMKFACFERTVEA HHHHHHHHHHHHHHH | 4.02 | 21278135 | |
| 232 | S-nitrosocysteine | YTMMKFACFERTVEA HHHHHHHHHHHHHHH | 4.02 | - | |
| 242 | Acetylation | RTVEALYKFVVPKPR HHHHHHHHHHCCCCH | 32.31 | 24062335 | |
| 242 | Succinylation | RTVEALYKFVVPKPR HHHHHHHHHHCCCCH | 32.31 | 23954790 | |
| 272 | S-nitrosylation | GYIAGVFCAIVSHPA HHHHHHHHHHHCCCC | 2.04 | 22178444 | |
| 290 | Acetylation | VSVLNKEKGSTASQV HHHHCCCCCCCHHHH | 60.82 | 23864654 | |
| 290 | Malonylation | VSVLNKEKGSTASQV HHHHCCCCCCCHHHH | 60.82 | 26320211 | |
| 290 | Succinylation | VSVLNKEKGSTASQV HHHHCCCCCCCHHHH | 60.82 | 24315375 | |
| 290 | Ubiquitination | VSVLNKEKGSTASQV HHHHCCCCCCCHHHH | 60.82 | - | |
| 295 | Phosphorylation | KEKGSTASQVLQRLG CCCCCCHHHHHHHHC | 22.40 | 28464351 | |
| 308 | Acetylation | LGFRGVWKGLFARII HCCCHHHHHHHHHHH | 43.24 | 23806337 | |
| 308 | Succinylation | LGFRGVWKGLFARII HCCCHHHHHHHHHHH | 43.24 | 23806337 |
| 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 MPCP_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MPCP_MOUSE !! | ||||||
* 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 MPCP_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of MPCP_MOUSE !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "Substrate and functional diversity of lysine acetylation revealed bya proteomics survey."; Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; Mol. Cell 23:607-618(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-94 AND LYS-204, AND MASSSPECTROMETRY. | |