Search Results
Overview
| Uniprot ID | Q3LXA3 |
|---|---|
| Protein Name | Triokinase/FMN cyclase |
| Gene Name | TKFC |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 109 | VGTLLIVKNYTGDRL |
| 147 | DSAFTVLKKAGRRGL |
| 230 | EAGVRRIKMATADEI |
| 372 | AAGGSASKRMALVLE |
| 46 | RSDLDSLKGRVALLS |
| 465 | AAQPLKAKTSLPAWS |
| 487 | EAMQKYGKAAPGDRT |
| 522 | DLLQVLTKAVKSAEA |
| 525 | QVLTKAVKSAEAAAE |
| 535 | EAAAEATKNMEAGAG |
Function
Catalyzes both the phosphorylation of dihydroxyacetone and of glyceraldehyde, and the splitting of ribonucleoside diphosphate-X compounds among which FAD is the best substrate. Represses IFIH1-mediated cellular antiviral response (PubMed:17600090)
Protein Sequence
10
MTSKKLVNSV
20
AGCADDALAG
30
LVACNPNLQL
40
LQGHRVALRS
50
DLDSLKGRVA
60
LLSGGGSGHE
70
PAHAGFIGKG
80
MLTGVIAGAV
90
FTSPAVGSIL
100
AAIRAVAQAG
110
TVGTLLIVKN
120
YTGDRLNFGL
130
AREQARAEGI
140
PVEMVVIGDD
150
SAFTVLKKAG
160
RRGLCGTVLI
170
HKVAGALAEA
180
GVGLEEIAKQ
190
VNVVAKAMGT
200
LGVSLSSCSV
210
PGSKPTFELS
220
ADEVELGLGI
230
HGEAGVRRIK
240
MATADEIVKL
250
MLDHMTNTTN
260
ASHVPVQPGS
270
SVVMMVNNLG
280
GLSFLELGII
290
ADATVRSLEG
300
RGVKIARALV
310
GTFMSALEMP
320
GISLTLLLVD
330
EPLLKLIDAE
340
TTAAAWPNVA
350
AVSITGRKRS
360
RVAPAEPQEA
370
PDSTAAGGSA
380
SKRMALVLER
390
VCSTLLGLEE
400
HLNALDRAAG
410
DGDCGTTHSR
420
AARAIQEWLK
430
EGPPPASPAQ
440
LLSKLSVLLL
450
EKMGGSSGAL
460
YGLFLTAAAQ
470
PLKAKTSLPA
480
WSAAMDAGLE
490
AMQKYGKAAP
500
GDRTMLDSLW
510
AAGQELQAWK
520
SPGADLLQVL
530
TKAVKSAEAA
540
AEATKNMEAG
550
AGRASYISSA
560
RLEQPDPGAV
570
AAAAILRAIL
EVLQS
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0005634 | nucleus |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0034012 | FAD-AMP lyase (cyclizing) activity |
| Molecular Function | GO:0004371 | glycerone kinase activity |
| Molecular Function | GO:0046872 | metal ion binding |
| Molecular Function | GO:0050354 | triokinase activity |
| Biological Process | GO:0005975 | carbohydrate metabolic process |
| Biological Process | GO:0046835 | carbohydrate phosphorylation |
| Biological Process | GO:0061624 | fructose catabolic process to hydroxyacetone phosphate and glyceraldehyde-3-phosphate |
| Biological Process | GO:0019563 | glycerol catabolic process |
| Biological Process | GO:0039534 | negative regulation of MDA-5 signaling pathway |
| Biological Process | GO:0045088 | regulation of innate immune response |
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.
[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.