Overview
| Uniprot ID | Q9H479 |
| Protein Name | Fructosamine-3-kinase |
| Gene Name | FN3K |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 122 |
QKLREKLKEEENTVG |
| 41 |
DAGPVFVKVNRRTQA |
| 94 |
VMEHLKMKSLSSQAS |
Function
Fructosamine-3-kinase involved in protein deglycation by mediating phosphorylation of fructoselysine residues on glycated proteins, to generate fructoselysine-3 phosphate (PubMed:11016445, PubMed:11522682, PubMed:11975663). Fructoselysine-3 phosphate adducts are unstable and decompose under physiological conditions (PubMed:11522682, PubMed:11975663). Involved in intracellular deglycation in erythrocytes (PubMed:11975663). Involved in the response to oxidative stress by mediating deglycation of NFE2L2/NRF2, glycation impairing NFE2L2/NRF2 function (By similarity). Also able to phosphorylate psicosamines and ribulosamines (PubMed:14633848)
Protein Sequence
10
MEQLLRAELR
20
TATLRAFGGP
30
GAGCISEGRA
40
YDTDAGPVFV
50
KVNRRTQARQ
60
MFEGEVASLE
70
ALRSTGLVRV
80
PRPMKVIDLP
90
GGGAAFVMEH
100
LKMKSLSSQA
110
SKLGEQMADL
120
HLYNQKLREK
130
LKEEENTVGR
140
RGEGAEPQYV
150
DKFGFHTVTC
160
CGFIPQVNEW
170
QDDWPTFFAR
180
HRLQAQLDLI
190
EKDYADREAR
200
ELWSRLQVKI
210
PDLFCGLEIV
220
PALLHGDLWS
230
GNVAEDDVGP
240
IIYDPASFYG
250
HSEFELAIAL
260
MFGGFPRSFF
270
TAYHRKIPKA
280
PGFDQRLLLY
290
QLFNYLNHWN
300
HFGREYRSPS
LGTMRRLLK
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005829 |
cytosol |
| Cellular Component |
GO:0005739 |
mitochondrion |
| Molecular Function |
GO:0005524 |
ATP binding |
| Molecular Function |
GO:0016301 |
kinase activity |
| Molecular Function |
GO:0102194 |
protein-fructosamine 3-kinase activity |
| Molecular Function |
GO:0102193 |
protein-ribulosamine 3-kinase activity |
| Biological Process |
GO:0030855 |
epithelial cell differentiation |
| Biological Process |
GO:0030389 |
fructosamine metabolic process |
| Biological Process |
GO:0030393 |
fructoselysine metabolic process |
| Biological Process |
GO:0043687 |
post-translational protein modification |
| Biological Process |
GO:0036525 |
protein deglycation |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.