| UniProt ID | RIFK_YEAST | |
|---|---|---|
| UniProt AC | Q03778 | |
| Protein Name | Riboflavin kinase | |
| Gene Name | FMN1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 218 | |
| Subcellular Localization | Microsome . Mitochondrion inner membrane . Endoplasmic reticulum . 90% microsomal. 10% mitochondrial. Found to be present in the inner membrane of mitochondria. The C-terminus is located in the matrix. | |
| Protein Description | Catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN) coenzyme.. | |
| Protein Sequence | MFTWTIYVSLLLVLAGTFLMNRNTNTDIIDTFKREVDLPIPAQPGPPFPLVTDYCDIVCGFGRGSAELGIPTANVPINQLPKGINDLDLGVYFGFAHIKTVDGQELSVETRRDGRTVVYNYGQYLSEANDDLSVLPMVLSVGKNPFYGNDFKTMELHIIHDFKNDFYGARVKFNILGHIRPELNYTTKEALIEDINIDIRTAQTVLATPPYQVFKQQL | |
| 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 |
|---|---|---|---|---|---|
| 3 | Phosphorylation | -----MFTWTIYVSL -----CCHHHHHHHH | 22.02 | 28132839 | |
| 5 | Phosphorylation | ---MFTWTIYVSLLL ---CCHHHHHHHHHH | 10.20 | 28132839 | |
| 7 | Phosphorylation | -MFTWTIYVSLLLVL -CCHHHHHHHHHHHH | 4.07 | 28889911 | |
| 17 | Phosphorylation | LLLVLAGTFLMNRNT HHHHHHHHHHHCCCC | 14.16 | 28132839 | |
| 147 | Phosphorylation | SVGKNPFYGNDFKTM EECCCCCCCCCCCCE | 19.10 | 28152593 |
| 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 RIFK_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RIFK_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 RIFK_YEAST !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| UTP5_YEAST | UTP5 | physical | 10688190 | |
| PIG2_YEAST | PIG2 | genetic | 19269370 | |
| 6PGD1_YEAST | GND1 | genetic | 21623372 | |
| TGL2_YEAST | TGL2 | genetic | 21623372 | |
| ELO2_YEAST | ELO2 | genetic | 21623372 | |
| FOLE_YEAST | MET7 | genetic | 21623372 | |
| DCOR_YEAST | SPE1 | genetic | 21623372 | |
| PFKA1_YEAST | PFK1 | genetic | 21623372 | |
| ADH3_YEAST | ADH3 | genetic | 21623372 | |
| APC11_YEAST | APC11 | genetic | 27708008 | |
| RPN5_YEAST | RPN5 | genetic | 27708008 | |
| GLE1_YEAST | GLE1 | genetic | 27708008 | |
| TIM22_YEAST | TIM22 | genetic | 27708008 | |
| FAL1_YEAST | FAL1 | genetic | 27708008 | |
| MOB2_YEAST | MOB2 | genetic | 27708008 | |
| MED6_YEAST | MED6 | genetic | 27708008 | |
| PRP19_YEAST | PRP19 | genetic | 27708008 | |
| TAD3_YEAST | TAD3 | genetic | 27708008 | |
| RSC9_YEAST | RSC9 | genetic | 27708008 | |
| ERO1_YEAST | ERO1 | genetic | 27708008 | |
| MCM1_YEAST | MCM1 | genetic | 27708008 | |
| DYR_YEAST | DFR1 | genetic | 27708008 | |
| TIM50_YEAST | TIM50 | genetic | 27708008 | |
| DCOR_YEAST | SPE1 | genetic | 27708008 | |
| EIF3J_YEAST | HCR1 | genetic | 27708008 | |
| SIW14_YEAST | SIW14 | genetic | 27708008 | |
| PHO80_YEAST | PHO80 | genetic | 27708008 | |
| YME1_YEAST | YME1 | genetic | 27708008 |
| 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 TYR-147, AND MASSSPECTROMETRY. | |