Search Results
Overview
| Uniprot ID | Q14117 |
|---|---|
| Protein Name | Dihydropyrimidinase |
| Gene Name | DPYS |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 153 | MKILVQDKGVNSFKM |
| 256 | VMSKSAAKVIADARR |
| 339 | TCQKALGKDDFTKIP |
| 362 | RMSVIWEKGVHSGKM |
| 409 | DIVIWDPKGTRTISA |
| 466 | DGKFIPRKPFAEYIY |
| 474 | PFAEYIYKRIKQRDR |
| 494 | PVERAPYKGEVATLK |
| 501 | KGEVATLKSRVTKED |
| 506 | TLKSRVTKEDATAGT |
Function
Catalyzes the second step of the reductive pyrimidine degradation, the reversible hydrolytic ring opening of dihydropyrimidines. Can catalyze the ring opening of 5,6-dihydrouracil to N-carbamyl-alanine and of 5,6-dihydrothymine to N-carbamyl-amino isobutyrate
Protein Sequence
10
MAAPSRLLIR
20
GGRVVNDDFS
30
EVADVLVEDG
40
VVRALGHDLL
50
PPGGAPAGLR
60
VLDAAGKLVL
70
PGGIDTHTHM
80
QFPFMGSRSI
90
DDFHQGTKAA
100
LSGGTTMIID
110
FAIPQKGGSL
120
IEAFETWRSW
130
ADPKVCCDYS
140
LHVAVTWWSD
150
QVKEEMKILV
160
QDKGVNSFKM
170
FMAYKDLYMV
180
TDLELYEAFS
190
RCKEIGAIAQ
200
VHAENGDLIA
210
EGAKKMLALG
220
ITGPEGHELC
230
RPEAVEAEAT
240
LRAITIASAV
250
NCPLYIVHVM
260
SKSAAKVIAD
270
ARRDGKVVYG
280
EPIAASLGTD
290
GTHYWNKEWH
300
HAAHHVMGPP
310
LRPDPSTPDF
320
LMNLLANDDL
330
TTTGTDNCTF
340
NTCQKALGKD
350
DFTKIPNGVN
360
GVEDRMSVIW
370
EKGVHSGKMD
380
ENRFVAVTST
390
NAAKIFNLYP
400
RKGRIAVGSD
410
ADIVIWDPKG
420
TRTISAKTHH
430
QAVNFNIFEG
440
MVCHGVPLVT
450
ISRGKVVYEA
460
GVFSVTAGDG
470
KFIPRKPFAE
480
YIYKRIKQRD
490
RTCTPTPVER
500
APYKGEVATL
510
KSRVTKEDAT
AGTRKQAHP
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0070062 | extracellular exosome |
| Molecular Function | GO:0004157 | dihydropyrimidinase activity |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0051219 | phosphoprotein binding |
| Molecular Function | GO:0008270 | zinc ion binding |
| Biological Process | GO:0006248 | CMP catabolic process |
| Biological Process | GO:0006249 | dCMP catabolic process |
| Biological Process | GO:0046079 | dUMP catabolic process |
| Biological Process | GO:0006208 | pyrimidine nucleobase catabolic process |
| Biological Process | GO:0006210 | thymine catabolic process |
| Biological Process | GO:0046050 | UMP catabolic process |
| Biological Process | GO:0006212 | uracil catabolic process |
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.