| UniProt ID | MDV1_YEAST | |
|---|---|---|
| UniProt AC | P47025 | |
| Protein Name | Mitochondrial division protein 1 | |
| Gene Name | MDV1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 714 | |
| Subcellular Localization |
Mitochondrion outer membrane Peripheral membrane protein Cytoplasmic side . Uniformly distributed on the cytoplasmic face of the mitochondrial outer membrane. This localization is dependent on FIS1. Reorganizes to punctate structures on mitochond |
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| Protein Description | Involved in mitochondrial fission. Has a partially redundant function to CAF4 in acting as an adapter protein, binding to FIS1 on the mitochondrial outer membrane and recruiting the dynamin-like GTPase DNM1 to form mitochondrial fission complexes. Formation of these complexes is required to promote constriction and fission of the mitochondrial compartment at a late step in mitochondrial division.. | |
| Protein Sequence | MSVNDQITHIGKTLSTTASAFLNYQKSNSNTQDVLTNNGPYKNLLSNTVNNASSTSYFYKRTEHGRFVKNASNTFEDIYSKTRRGDVFRNKFTDNKTCFRMLTYISDDLLNEIPTKEGLKSDADGKLLTEGGENENLRKNASKKETSLFQGFKSYLPIAELAIENTERLNYDTNGTSGTVGAKDVMSKTNERDEIHTELPNFQDSFLIPPGVETKKISSSYSPSALKSFSQTLVNSLEFLNIQKNSTLSEIRDIEVEVENLRQKKEKLLGKIANIEQNQLLLEDNLKQIDDRLDFLEEYGLEVIEANSDENAEDDGMSERKALKNDAIRNEGVTTESISSEASNLPPRRRQQLRDDNSLNRLGAFYSKSKKRHRKSFPTFQQLYEPGTKIGSIMSTHDDFLTCLDFDAPFGTLCTAGYLDHTVKIWDLSKQNKIGELAGHLATINCMQINRDYGTLVTGGRDAALKLWNLNLAQQLYQETQNLTSPTNHIDSPCVHTFEAHTDEVTALSLDPSFLVSGSQDRTIRQWDLRSGKCLQTIDLSFANVLTTSTNVDLSKSTLLTQRNERPSIGALQSFDAALATGTKDGVVRLWDLRSGKVIRTLKGHTDAITSLKFDSACLVTGSYDRTVRIWDLRTGLLNKFHAYSAPVLSLDLFQENAAVVVADEPSVQIYDSEKDESWSCVEQGNETSVSTVKYKENYMVEGRENGDVNIWAV | |
| 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 | ------MSVNDQITH ------CCHHHHHCH | 29.63 | 22369663 | |
| 8 | Phosphorylation | MSVNDQITHIGKTLS CCHHHHHCHHHHHHH | 11.21 | 28889911 | |
| 15 | Phosphorylation | THIGKTLSTTASAFL CHHHHHHHHHHHHHH | 29.01 | 24961812 | |
| 16 | Phosphorylation | HIGKTLSTTASAFLN HHHHHHHHHHHHHHC | 29.51 | 24961812 | |
| 17 | Phosphorylation | IGKTLSTTASAFLNY HHHHHHHHHHHHHCC | 18.42 | 24961812 | |
| 19 | Phosphorylation | KTLSTTASAFLNYQK HHHHHHHHHHHCCCC | 19.91 | 24961812 | |
| 27 | Phosphorylation | AFLNYQKSNSNTQDV HHHCCCCCCCCCCHH | 29.93 | 30377154 | |
| 46 | Phosphorylation | GPYKNLLSNTVNNAS CCHHHHHHHHCCCCC | 33.35 | 30377154 | |
| 48 | Phosphorylation | YKNLLSNTVNNASST HHHHHHHHCCCCCCC | 22.64 | 30377154 | |
| 53 | Phosphorylation | SNTVNNASSTSYFYK HHHCCCCCCCCEEEE | 35.95 | 28889911 | |
| 55 | Phosphorylation | TVNNASSTSYFYKRT HCCCCCCCCEEEEEC | 25.58 | 28889911 | |
| 56 | Phosphorylation | VNNASSTSYFYKRTE CCCCCCCCEEEEECC | 18.39 | 30377154 | |
| 57 | Phosphorylation | NNASSTSYFYKRTEH CCCCCCCEEEEECCC | 15.83 | 30377154 | |
| 121 | Phosphorylation | PTKEGLKSDADGKLL CCCCCCCCCCCCCCC | 42.97 | 28889911 | |
| 126 | Ubiquitination | LKSDADGKLLTEGGE CCCCCCCCCCCCCCC | 40.65 | 23749301 | |
| 219 | Phosphorylation | VETKKISSSYSPSAL CCCEECCCCCCHHHH | 36.45 | 28889911 | |
| 220 | Phosphorylation | ETKKISSSYSPSALK CCEECCCCCCHHHHH | 23.88 | 30377154 | |
| 222 | Phosphorylation | KKISSSYSPSALKSF EECCCCCCHHHHHHH | 17.83 | 21440633 | |
| 334 | Phosphorylation | AIRNEGVTTESISSE HHHCCCCCHHHHCHH | 35.38 | 23749301 | |
| 335 | Phosphorylation | IRNEGVTTESISSEA HHCCCCCHHHHCHHH | 25.90 | 23749301 | |
| 337 | Phosphorylation | NEGVTTESISSEASN CCCCCHHHHCHHHHC | 26.19 | 23749301 | |
| 339 | Phosphorylation | GVTTESISSEASNLP CCCHHHHCHHHHCCC | 31.25 | 23749301 | |
| 340 | Phosphorylation | VTTESISSEASNLPP CCHHHHCHHHHCCCH | 35.20 | 28889911 | |
| 343 | Phosphorylation | ESISSEASNLPPRRR HHHCHHHHCCCHHHH | 34.54 | 23749301 | |
| 376 | Phosphorylation | SKKRHRKSFPTFQQL HHHHHHHCCCCHHHH | 36.09 | 22369663 | |
| 379 | Phosphorylation | RHRKSFPTFQQLYEP HHHHCCCCHHHHCCC | 31.87 | 22890988 |
| 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 MDV1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MDV1_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 MDV1_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-53; THR-55; SER-219;SER-340 AND SER-376, AND MASS SPECTROMETRY. | |