CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022734
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1 
Protein Synonyms/Alias
 Lysyl hydroxylase 1; LH1 
Gene Name
 Plod1 
Gene Synonyms/Alias
 Plod 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
402RLLIEQNKNVIAPLMacetylation[1]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441
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 637 728 Fe2OG dioxygenase.
 ACT_SITE 719 719 Potential.
 METAL 657 657 Iron (By similarity).
 METAL 659 659 Iron (By similarity).
 METAL 709 709 Iron (By similarity).
 CARBOHYD 198 198 N-linked (GlcNAc...).
 CARBOHYD 539 539 N-linked (GlcNAc...) (Potential).
 CARBOHYD 687 687 N-linked (GlcNAc...) (Potential).  
Keyword
 Complete proteome; Dioxygenase; Endoplasmic reticulum; Glycoprotein; Iron; Membrane; Metal-binding; Oxidoreductase; Reference proteome; Signal; Vitamin C. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 728 AA 
Protein Sequence
MRSLLLLAPL AWLLLVQAKD DAKLEDNLLV LTVATKETEG FRRFKRSAQF FNYKIQSLGL 60
GEDWSVDGGP AAAGGGQKVR LLKKALEKHA DKEDLVILFV DSYDVVFASG PRELLKKFQQ 120
AKSQVVFSAE EHIYPDRRLE AKYPTVPDGK RFLGSGGFIG YAPSLSKLVA EWEGQDSDSD 180
QLFYTKIFLN PEKREQINIS LDHRCRIFQN LDGALDEVVL KFEMGHVRAR NLAYDTLPVV 240
VHGNGPTKLQ LNYLGNYIPR FWTFETGCTV CDEGLRSLKG IGDEALPTVL VGVFIEQPTP 300
FLSLFFLRLL RLRYPQKQMR LFIHNQERHH KLQVEQFLAE HGSEYQSVKL VGPEVRMANA 360
DARNMGADLC RQDQTCTYYF SVDADVALTE PNSLRLLIEQ NKNVIAPLMT RHGRLWSNFW 420
GGLSADGYYA RSEDYVDIVQ GRRVGVWNVP YISNIYLIKG SALRAELQNV DLFHYSKLDS 480
DMSFCANVRQ QEVFMFLTNR HTFGHLLSLD NYQTTHLHND LWEVFSNPED WKEKYIHENY 540
TKALAGKLVE TPCPDVYWFP IFTEAACDEL VEEMEHYGQW SLGDNKDNRI QGGYENVPTI 600
DIHMNQITFE REWHKFLVEY IAPMTEKLYP GYYTRAQFDL AFVVRYKPDE QPSLMPHHDA 660
STFTVNIALN RVGEDYEGGG CRFLRYNCSV RAPRKGWALL HPGRLTHYHE GLPTTKGTRY 720
IAVSFVDP 728 
Gene Ontology
 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; IEA:EC.
 GO:0001666; P:response to hypoxia; IEA:Compara. 
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