Search Results
Overview
| Uniprot ID | Q02809 |
|---|---|
| Protein Name | Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1 |
| Gene Name | PLOD1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 77 | TSAGGGQKVRLLKKA |
Function
Part of a complex composed of PLOD1, P3H3 and P3H4 that catalyzes hydroxylation of lysine residues in collagen alpha chains and is required for normal assembly and cross-linkling of collagen fibrils (By similarity). Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens (PubMed:10686424, PubMed:15854030, PubMed:8621606). These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links (Probable)
Protein Sequence
10
MRPLLLLALL
20
GWLLLAEAKG
30
DAKPEDNLLV
40
LTVATKETEG
50
FRRFKRSAQF
60
FNYKIQALGL
70
GEDWNVEKGT
80
SAGGGQKVRL
90
LKKALEKHAD
100
KEDLVILFAD
110
SYDVLFASGP
120
RELLKKFRQA
130
RSQVVFSAEE
140
LIYPDRRLET
150
KYPVVSDGKR
160
FLGSGGFIGY
170
APNLSKLVAE
180
WEGQDSDSDQ
190
LFYTKIFLDP
200
EKREQINITL
210
DHRCRIFQNL
220
DGALDEVVLK
230
FEMGHVRARN
240
LAYDTLPVLI
250
HGNGPTKLQL
260
NYLGNYIPRF
270
WTFETGCTVC
280
DEGLRSLKGI
290
GDEALPTVLV
300
GVFIEQPTPF
310
VSLFFQRLLR
320
LHYPQKHMRL
330
FIHNHEQHHK
340
AQVEEFLAQH
350
GSEYQSVKLV
360
GPEVRMANAD
370
ARNMGADLCR
380
QDRSCTYYFS
390
VDADVALTEP
400
NSLRLLIQQN
410
KNVIAPLMTR
420
HGRLWSNFWG
430
ALSADGYYAR
440
SEDYVDIVQG
450
RRVGVWNVPY
460
ISNIYLIKGS
470
ALRGELQSSD
480
LFHHSKLDPD
490
MAFCANIRQQ
500
DVFMFLTNRH
510
TLGHLLSLDS
520
YRTTHLHNDL
530
WEVFSNPEDW
540
KEKYIHQNYT
550
KALAGKLVET
560
PCPDVYWFPI
570
FTEVACDELV
580
EEMEHFGQWS
590
LGNNKDNRIQ
600
GGYENVPTID
610
IHMNQIGFER
620
EWHKFLLEYI
630
APMTEKLYPG
640
YYTRAQFDLA
650
FVVRYKPDEQ
660
PSLMPHHDAS
670
TFTINIALNR
680
VGVDYEGGGC
690
RFLRYNCSIR
700
APRKGWTLMH
710
PGRLTHYHEG
720
LPTTRGTRYI
AVSFVDP
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:1902494 | catalytic complex |
| Cellular Component | GO:0005783 | endoplasmic reticulum |
| Cellular Component | GO:0005789 | endoplasmic reticulum membrane |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0031012 | extracellular matrix |
| Cellular Component | GO:0005615 | extracellular space |
| Cellular Component | GO:0005794 | Golgi apparatus |
| Cellular Component | GO:0030867 | rough endoplasmic reticulum membrane |
| Molecular Function | GO:0005506 | iron ion binding |
| Molecular Function | GO:0031418 | L-ascorbic acid binding |
| Molecular Function | GO:0008475 | procollagen-lysine 5-dioxygenase activity |
| Biological Process | GO:0032964 | collagen biosynthetic process |
| Biological Process | GO:0030199 | collagen fibril organization |
| Biological Process | GO:0008544 | epidermis development |
| Biological Process | GO:0046947 | hydroxylysine biosynthetic process |
| Biological Process | GO:0001666 | response to hypoxia |
Reference
[1] 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.