UniProt ID | FRE7_YEAST | |
---|---|---|
UniProt AC | Q12333 | |
Protein Name | Ferric/cupric reductase transmembrane component 7 | |
Gene Name | FRE7 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 620 | |
Subcellular Localization |
Cell membrane Multi-pass membrane protein . |
|
Protein Description | Cell surface metalloreductase. May be involved in copper homeostasis.. | |
Protein Sequence | MIEERDLVLSNGIHCIADIHSELYARLKKESQAATPWVYQKQYGKFVTYFVAVIIFLSLIKKLAFMYYDSSEEFLPEKKNSPTTPSVFLARIMTKLVAFNRYICYRKFPTLIFSYLGIPTSVGTFLVVMATTLYTLLYCFVPHPFYRPCAGFGSPPLSVRAGIMAISLVPFVFSLSGKINVIGWLVGLSYEKINIYHQWASILCLFFSWVHVIPFLRQARHEGGYERMHQRWKASDMWRSGVPPILFLNLLWLSSLPIARRHFYEIFLQLHWILAVGFYISLFYHVYPELNSHMYLVATIVVWFAQLFYRLAVKGYLRPGRSFMASTIANVSIVGEGCVELIVKDVEMAYSPGQHIFVRTIDKGIISNHPFSIFPSAKYPGGIKMLIRAQKGFSKRLYESNDDMKKILIDGPYGGIERDIRSFTNVYLICSGSGISTCLPFLQKYGPILHKTNLEVITLDWVVRHREDISWIRDEMCTLSNNLRQLFLDGKIVVRIYVCSDSTVPGIIKTFPQTIDTASDQSDLAKREKDTEFGQDDTESNSTFDKSNNEYKGLITIIPSKPDLNQVINDYQIGFRNCFICSGSDSLRYTVGNSVAGLQAKVFSNKNVEECYLHSESFGY | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
367 | Phosphorylation | TIDKGIISNHPFSIF EECCCHHCCCCCEEC | 27.45 | 28889911 | |
517 | Phosphorylation | TFPQTIDTASDQSDL HCCHHHCCCCCHHHH | 24.98 | 20377248 | |
519 | Phosphorylation | PQTIDTASDQSDLAK CHHHCCCCCHHHHHH | 37.97 | 20377248 | |
522 | Phosphorylation | IDTASDQSDLAKREK HCCCCCHHHHHHHHH | 39.31 | 20377248 | |
526 | Ubiquitination | SDQSDLAKREKDTEF CCHHHHHHHHHCCCC | 69.27 | 22817900 | |
529 | Ubiquitination | SDLAKREKDTEFGQD HHHHHHHHCCCCCCC | 74.18 | 22817900 | |
540 | Phosphorylation | FGQDDTESNSTFDKS CCCCCCCCCCCCCCC | 37.87 | 28889911 | |
542 | Phosphorylation | QDDTESNSTFDKSNN CCCCCCCCCCCCCCC | 39.47 | 28889911 | |
543 | Phosphorylation | DDTESNSTFDKSNNE CCCCCCCCCCCCCCE | 39.85 | 28889911 |
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 FRE7_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of FRE7_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 FRE7_YEAST !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
NRG1_YEAST | NRG1 | genetic | 20093466 | |
SWF1_YEAST | SWF1 | genetic | 20093466 | |
MNN10_YEAST | MNN10 | genetic | 20093466 | |
SCS2_YEAST | SCS2 | genetic | 20093466 | |
RS26B_YEAST | RPS26B | genetic | 20093466 | |
ATC1_YEAST | PMR1 | genetic | 20093466 | |
FIS1_YEAST | FIS1 | genetic | 20093466 | |
YM49_YEAST | YMR187C | genetic | 20093466 | |
MKS1_YEAST | MKS1 | genetic | 20093466 | |
SIN3_YEAST | SIN3 | genetic | 20093466 | |
NCBP2_YEAST | CBC2 | genetic | 20093466 | |
CSG2_YEAST | CSG2 | genetic | 27708008 | |
RV161_YEAST | RVS161 | genetic | 27708008 | |
BRE1_YEAST | BRE1 | genetic | 27708008 | |
MED20_YEAST | SRB2 | genetic | 27708008 | |
AIM34_YEAST | AIM34 | genetic | 27708008 | |
MKS1_YEAST | MKS1 | genetic | 27708008 | |
EOS1_YEAST | EOS1 | genetic | 27708008 | |
SIN3_YEAST | SIN3 | genetic | 27708008 | |
SUR1_YEAST | SUR1 | genetic | 27708008 |
Kegg Drug | ||||||
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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-367, AND MASSSPECTROMETRY. |