CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012889
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Prolyl 3-hydroxylase 1 
Protein Synonyms/Alias
 Growth suppressor 1; Leucine- and proline-enriched proteoglycan 1; Leprecan-1 
Gene Name
 LEPRE1 
Gene Synonyms/Alias
 GROS1; P3H1; PSEC0109 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
512SPHTPNEKFYGVTVFubiquitination[1]
662TENPHGVKAVTRGQRubiquitination[2]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] 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
 Basement membrane-associated chondroitin sulfate proteoglycan (CSPG). 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. May be involved in the secretory pathway of cells. Has growth suppressive activity in fibroblasts. 
Sequence Annotation
 REPEAT 35 68 TPR 1.
 REPEAT 143 176 TPR 2.
 REPEAT 205 238 TPR 3.
 REPEAT 301 334 TPR 4.
 DOMAIN 564 678 Fe2OG dioxygenase.
 MOTIF 733 736 Prevents secretion from ER (Potential).
 ACT_SITE 669 669 By similarity.
 METAL 587 587 Iron.
 METAL 589 589 Iron.
 METAL 659 659 Iron.
 CARBOHYD 316 316 N-linked (GlcNAc...) (Potential).
 CARBOHYD 467 467 N-linked (GlcNAc...) (Potential).
 CARBOHYD 540 540 N-linked (GlcNAc...).  
Keyword
 Alternative splicing; Coiled coil; Complete proteome; Dioxygenase; Dwarfism; Endoplasmic reticulum; Extracellular matrix; Glycoprotein; Iron; Metal-binding; Osteogenesis imperfecta; Oxidoreductase; Polymorphism; Reference proteome; Repeat; Secreted; Signal; TPR repeat; Vitamin C. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 736 AA 
Protein Sequence
MAVRALKLLT TLLAVVAAAS QAEVESEAGW GMVTPDLLFA EGTAAYARGD WPGVVLSMER 60
ALRSRAALRA LRLRCRTQCA ADFPWELDPD WSPSPAQASG AAALRDLSFF GGLLRRAACL 120
RRCLGPPAAH SLSEEMELEF RKRSPYNYLQ VAYFKINKLE KAVAAAHTFF VGNPEHMEMQ 180
QNLDYYQTMS GVKEADFKDL ETQPHMQEFR LGVRLYSEEQ PQEAVPHLEA ALQEYFVAYE 240
ECRALCEGPY DYDGYNYLEY NADLFQAITD HYIQVLNCKQ NCVTELASHP SREKPFEDFL 300
PSHYNYLQFA YYNIGNYTQA VECAKTYLLF FPNDEVMNQN LAYYAAMLGE EHTRSIGPRE 360
SAKEYRQRSL LEKELLFFAY DVFGIPFVDP DSWTPEEVIP KRLQEKQKSE RETAVRISQE 420
IGNLMKEIET LVEEKTKESL DVSRLTREGG PLLYEGISLT MNSKLLNGSQ RVVMDGVISD 480
HECQELQRLT NVAATSGDGY RGQTSPHTPN EKFYGVTVFK ALKLGQEGKV PLQSAHLYYN 540
VTEKVRRIME SYFRLDTPLY FSYSHLVCRT AIEEVQAERK DDSHPVHVDN CILNAETLVC 600
VKEPPAYTFR DYSAILYLNG DFDGGNFYFT ELDAKTVTAE VQPQCGRAVG FSSGTENPHG 660
VKAVTRGQRC AIALWFTLDP RHSERDRVQA DDLVKMLFSP EEMDLSQEQP LDAQQGPPEP 720
AQESLSGSES KPKDEL 736 
Gene Ontology
 GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0005578; C:proteinaceous extracellular matrix; 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:0019797; F:procollagen-proline 3-dioxygenase activity; IEA:EC.
 GO:0016049; P:cell growth; IEA:Compara.
 GO:0030199; P:collagen fibril organization; IEA:Compara.
 GO:0030198; P:extracellular matrix organization; TAS:Reactome.
 GO:0008285; P:negative regulation of cell proliferation; NAS:UniProtKB.
 GO:0030278; P:regulation of ossification; IEA:Compara. 
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