CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000084
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2 
Protein Synonyms/Alias
 Lysyl hydroxylase 2; LH2 
Gene Name
 PLOD2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
341NKEVYHEKDIKVFFDubiquitination[1]
344VYHEKDIKVFFDKAKubiquitination[1]
Reference
 [1] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 
Functional Description
 Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links. 
Sequence Annotation
 DOMAIN 644 737 Fe2OG dioxygenase.
 ACT_SITE 728 728 Potential.
 METAL 666 666 Iron (By similarity).
 METAL 668 668 Iron (By similarity).
 METAL 718 718 Iron (By similarity).
 MOD_RES 320 320 Phosphothreonine.
 MOD_RES 323 323 Phosphotyrosine.
 CARBOHYD 63 63 N-linked (GlcNAc...) (Potential).
 CARBOHYD 209 209 N-linked (GlcNAc...).
 CARBOHYD 297 297 N-linked (GlcNAc...) (Potential).
 CARBOHYD 365 365 N-linked (GlcNAc...) (Potential).
 CARBOHYD 522 522 N-linked (GlcNAc...).
 CARBOHYD 696 696 N-linked (GlcNAc...) (Potential).
 CARBOHYD 725 725 N-linked (GlcNAc...) (Potential).  
Keyword
 Alternative splicing; Complete proteome; Dioxygenase; Disease mutation; Endoplasmic reticulum; Glycoprotein; Iron; Membrane; Metal-binding; Osteogenesis imperfecta; Oxidoreductase; Phosphoprotein; Reference proteome; Signal; Vitamin C. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 737 AA 
Protein Sequence
MGGCTVKPQL LLLALVLHPW NPCLGADSEK PSSIPTDKLL VITVATKESD GFHRFMQSAK 60
YFNYTVKVLG QGEEWRGGDG INSIGGGQKV RLMKEVMEHY ADQDDLVVMF TECFDVIFAG 120
GPEEVLKKFQ KANHKVVFAA DGILWPDKRL ADKYPVVHIG KRYLNSGGFI GYAPYVNRIV 180
QQWNLQDNDD DQLFYTKVYI DPLKREAINI TLDHKCKIFQ TLNGAVDEVV LKFENGKARA 240
KNTFYETLPV AINGNGPTKI LLNYFGNYVP NSWTQDNGCT LCEFDTVDLS AVDVHPNVSI 300
GVFIEQPTPF LPRFLDILLT LDYPKEALKL FIHNKEVYHE KDIKVFFDKA KHEIKTIKIV 360
GPEENLSQAE ARNMGMDFCR QDEKCDYYFS VDADVVLTNP RTLKILIEQN RKIIAPLVTR 420
HGKLWSNFWG ALSPDGYYAR SEDYVDIVQG NRVGVWNVPY MANVYLIKGK TLRSEMNERN 480
YFVRDKLDPD MALCRNAREM TLQREKDSPT PETFQMLSPP KGVFMYISNR HEFGRLLSTA 540
NYNTSHYNND LWQIFENPVD WKEKYINRDY SKIFTENIVE QPCPDVFWFP IFSEKACDEL 600
VEEMEHYGKW SGGKHHDSRI SGGYENVPTD DIHMKQVDLE NVWLHFIREF IAPVTLKVFA 660
GYYTKGFALL NFVVKYSPER QRSLRPHHDA STFTINIALN NVGEDFQGGG CKFLRYNCSI 720
ESPRKGWSFM HPGRLTHLHE GLPVKNGTRY IAVSFIDP 758 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
 GO:0030867; C:rough endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0005506; F:iron ion binding; IEA:InterPro.
 GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
 GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:UniProtKB-KW.
 GO:0008475; F:procollagen-lysine 5-dioxygenase activity; TAS:ProtInc.
 GO:0006464; P:cellular protein modification process; TAS:ProtInc.
 GO:0030198; P:extracellular matrix organization; TAS:Reactome.
 GO:0001666; P:response to hypoxia; IEP:UniProtKB. 
Interpro
 IPR005123; Oxoglu/Fe-dep_dioxygenase.
 IPR006620; Pro_4_hyd_alph.
 IPR001006; Procol_lys_dOase. 
Pfam
 PF03171; 2OG-FeII_Oxy 
SMART
 SM00702; P4Hc 
PROSITE
 PS51471; FE2OG_OXY
 PS01325; LYS_HYDROXYLASE 
PRINTS