| UniProt ID | MMF1_YEAST | |
|---|---|---|
| UniProt AC | P40185 | |
| Protein Name | Protein MMF1, mitochondrial | |
| Gene Name | MMF1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 145 | |
| Subcellular Localization | Mitochondrion matrix . | |
| Protein Description | Plays a role in the maintenance of mitochondrial DNA.. | |
| Protein Sequence | MFLRNSVLRTAPVLRRGITTLTPVSTKLAPPAAASYSQAMKANNFVYVSGQIPYTPDNKPVQGSISEKAEQVFQNVKNILAESNSSLDNIVKVNVFLADMKNFAEFNSVYAKHFHTHKPARSCVGVASLPLNVDLEMEVIAVEKN | |
| 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 |
|---|---|---|---|---|---|
| 19 | Phosphorylation | PVLRRGITTLTPVST HHHHCCCCCCCCCCC | 20.69 | 28889911 | |
| 35 | Phosphorylation | LAPPAAASYSQAMKA CCCCCCCCHHHHHHH | 22.16 | 28152593 | |
| 36 | Phosphorylation | APPAAASYSQAMKAN CCCCCCCHHHHHHHC | 10.48 | 27017623 | |
| 37 | Phosphorylation | PPAAASYSQAMKANN CCCCCCHHHHHHHCC | 14.68 | 27017623 | |
| 47 | Phosphorylation | MKANNFVYVSGQIPY HHHCCEEEEECCCCC | 5.69 | 24961812 | |
| 49 | Phosphorylation | ANNFVYVSGQIPYTP HCCEEEEECCCCCCC | 13.80 | 24961812 | |
| 54 | Phosphorylation | YVSGQIPYTPDNKPV EEECCCCCCCCCCCC | 32.31 | 24961812 | |
| 55 | Phosphorylation | VSGQIPYTPDNKPVQ EECCCCCCCCCCCCC | 20.86 | 21440633 | |
| 59 | Acetylation | IPYTPDNKPVQGSIS CCCCCCCCCCCCCHH | 54.68 | 24489116 | |
| 64 | Phosphorylation | DNKPVQGSISEKAEQ CCCCCCCCHHHHHHH | 13.07 | 21440633 | |
| 66 | Phosphorylation | KPVQGSISEKAEQVF CCCCCCHHHHHHHHH | 34.44 | 24961812 | |
| 68 | Acetylation | VQGSISEKAEQVFQN CCCCHHHHHHHHHHH | 50.89 | 24489116 | |
| 77 | Acetylation | EQVFQNVKNILAESN HHHHHHHHHHHHHCC | 45.91 | 24489116 | |
| 77 | Succinylation | EQVFQNVKNILAESN HHHHHHHHHHHHHCC | 45.91 | 23954790 | |
| 83 | Phosphorylation | VKNILAESNSSLDNI HHHHHHHCCCCHHHH | 36.08 | 29734811 | |
| 85 | Phosphorylation | NILAESNSSLDNIVK HHHHHCCCCHHHHHH | 41.37 | 22369663 | |
| 86 | Phosphorylation | ILAESNSSLDNIVKV HHHHCCCCHHHHHHH | 43.95 | 22369663 | |
| 101 | Acetylation | NVFLADMKNFAEFNS HEEEHHHHCHHHHHH | 49.84 | 24489116 | |
| 108 | Phosphorylation | KNFAEFNSVYAKHFH HCHHHHHHHCHHHHC | 23.09 | 22369663 | |
| 110 | Phosphorylation | FAEFNSVYAKHFHTH HHHHHHHCHHHHCCC | 15.11 | 28889911 | |
| 112 | Acetylation | EFNSVYAKHFHTHKP HHHHHCHHHHCCCCC | 29.17 | 22865919 | |
| 118 | Acetylation | AKHFHTHKPARSCVG HHHHCCCCCCCCEEE | 41.34 | 25381059 | |
| 122 | Phosphorylation | HTHKPARSCVGVASL CCCCCCCCEEEEEEC | 18.43 | 22369663 | |
| 128 | Phosphorylation | RSCVGVASLPLNVDL CCEEEEEECCCCEEE | 28.28 | 22369663 |
| 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 MMF1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MMF1_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 MMF1_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 THR-19; SER-35 AND SER-108,AND MASS SPECTROMETRY. | |