CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016990
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Prolyl 3-hydroxylase 3 
Protein Synonyms/Alias
 Leprecan-like protein 2; Protein B 
Gene Name
 LEPREL2 
Gene Synonyms/Alias
 P3H3 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
517FEGLTVLKAAQLARAubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961
Functional Description
 Has prolyl 3-hydroxylase activity catalyzing the post- translational formation of 3-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens, especially types IV and V (By similarity). 
Sequence Annotation
 REPEAT 37 70 TPR 1.
 REPEAT 154 187 TPR 2.
 REPEAT 216 249 TPR 3.
 REPEAT 316 349 TPR 4.
 DOMAIN 561 675 Fe2OG dioxygenase.
 MOTIF 733 736 Prevents secretion from ER (Potential).
 ACT_SITE 666 666 By similarity.
 METAL 584 584 Iron.
 METAL 586 586 Iron.
 METAL 656 656 Iron.
 CARBOHYD 331 331 N-linked (GlcNAc...) (Potential).
 CARBOHYD 462 462 N-linked (GlcNAc...) (Potential).  
Keyword
 Alternative splicing; Coiled coil; Complete proteome; Dioxygenase; Endoplasmic reticulum; Glycoprotein; Iron; Metal-binding; Oxidoreductase; Polymorphism; Reference proteome; Repeat; Signal; TPR repeat; Vitamin C. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 736 AA 
Protein Sequence
MLRLLRPLLL LLLLPPPGSP EPPGLTQLSP GAPPQAPDLL YADGLRAYAA GAWAPAVALL 60
REALRSQAAL GRVRLDCGAS CAADPGAALP AVLLGAPEPD SGPGPTQGSW ERQLLRAALR 120
RADCLTQCAA RRLGPGGAAR LRVGSALRDA FRRREPYNYL QRAYYQLKKL DLAAAAAHTF 180
FVANPMHLQM REDMAKYRRM SGVRPQSFRD LETPPHWAAY DTGLELLGRQ EAGLALPRLE 240
EALQGSLAQM ESCRADCEGP EEQQGAEEEE DGAASQGGLY EAIAGHWIQV LQCRQRCVGE 300
TATRPGRSFP VPDFLPNQLR RLHEAHAQVG NLSQAIENVL SVLLFYPEDE AAKRALNQYQ 360
AQLGEPRPGL GPREDIQRFI LRSLGEKRQL YYAMEHLGTS FKDPDPWTPA ALIPEALREK 420
LREDQEKRPW DHEPVKPKPL TYWKDVLLLE GVTLTQDSRQ LNGSERAVLD GLLTPAECGV 480
LLQLAKDAAG AGARSGYRGR RSPHTPHERF EGLTVLKAAQ LARAGTVGSQ GAKLLLEVSE 540
RVRTLTQAYF SPERPLHLSF THLVCRSAIE GEQEQRMDLS HPVHADNCVL DPDTGECWRE 600
PPAYTYRDYS GLLYLNDDFQ GGDLFFTEPN ALTVTARVRP RCGRLVAFSS GVENPHGVWA 660
VTRGRRCALA LWHTWAPEHR EQEWIEAKEL LQESQEEEEE EEEEMPSKDP SPEPPSRRHQ 720
RVQDKTGRAP RVREEL 736 
Gene Ontology
 GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
 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:0019797; F:procollagen-proline 3-dioxygenase activity; IEA:EC.
 GO:0030198; P:extracellular matrix organization; TAS:Reactome.
 GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB. 
Interpro
 IPR005123; Oxoglu/Fe-dep_dioxygenase.
 IPR006620; Pro_4_hyd_alph.
 IPR011990; TPR-like_helical. 
Pfam
 PF13640; 2OG-FeII_Oxy_3 
SMART
 SM00702; P4Hc 
PROSITE
 PS00014; ER_TARGET
 PS51471; FE2OG_OXY
 PS50005; TPR
 PS50293; TPR_REGION 
PRINTS