| UniProt ID | FN3K_HUMAN | |
|---|---|---|
| UniProt AC | Q9H479 | |
| Protein Name | Fructosamine-3-kinase | |
| Gene Name | FN3K | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 309 | |
| Subcellular Localization | ||
| Protein Description | May initiate a process leading to the deglycation of fructoselysine and of glycated proteins. May play a role in the phosphorylation of 1-deoxy-1-morpholinofructose (DMF), fructoselysine, fructoseglycine, fructose and glycated lysozyme.. | |
| Protein Sequence | MEQLLRAELRTATLRAFGGPGAGCISEGRAYDTDAGPVFVKVNRRTQARQMFEGEVASLEALRSTGLVRVPRPMKVIDLPGGGAAFVMEHLKMKSLSSQASKLGEQMADLHLYNQKLREKLKEEENTVGRRGEGAEPQYVDKFGFHTVTCCGFIPQVNEWQDDWPTFFARHRLQAQLDLIEKDYADREARELWSRLQVKIPDLFCGLEIVPALLHGDLWSGNVAEDDVGPIIYDPASFYGHSEFELAIALMFGGFPRSFFTAYHRKIPKAPGFDQRLLLYQLFNYLNHWNHFGREYRSPSLGTMRRLLK | |
| 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 |
|---|---|---|---|---|---|
| 1 | Acetylation | -------MEQLLRAE -------CHHHHHHH | 7.17 | 11016445 | |
| 97 | Phosphorylation | HLKMKSLSSQASKLG HHHHHHHHHHHHHHH | 27.74 | - | |
| 102 | Ubiquitination | SLSSQASKLGEQMAD HHHHHHHHHHHHHHH | 64.62 | 29967540 | |
| 116 | Ubiquitination | DLHLYNQKLREKLKE HHHHHHHHHHHHHHH | 45.96 | 29967540 | |
| 258 | Phosphorylation | MFGGFPRSFFTAYHR HHCCCCHHHHHHHHC | 25.58 | 17924679 | |
| 263 | Phosphorylation | PRSFFTAYHRKIPKA CHHHHHHHHCCCCCC | 10.09 | 17924679 | |
| 296 | Phosphorylation | WNHFGREYRSPSLGT HCCCCHHHCCCCHHH | 18.28 | 24719451 | |
| 298 | Phosphorylation | HFGREYRSPSLGTMR CCCHHHCCCCHHHHH | 20.24 | 28857561 |
| 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 FN3K_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of FN3K_HUMAN !! | ||||||
* 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 FN3K_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of FN3K_HUMAN !! | ||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "Identification, cloning, and heterologous expression of a mammalianfructosamine-3-kinase."; Delpierre G., Rider M.H., Collard F., Stroobant V., Vanstapel F.,Santos H., Van Schaftingen E.; Diabetes 49:1627-1634(2000). Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, ACETYLATION ATMET-1, AND CHARACTERIZATION. | |
| Phosphorylation | |
| Reference | PubMed |
| "Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND TYR-263, ANDMASS SPECTROMETRY. | |
