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Protein

Multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3

Gene

PLOD3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Multifunctional enzyme that catalyzes a series of essential post-translational modifications on Lys residues in procollagen (PubMed:11956192, PubMed:12475640, PubMed:18298658, PubMed:30089812, PubMed:18834968). Plays a redundant role in catalyzing the formation of hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens (PubMed:9582318, PubMed:9724729, PubMed:11956192, PubMed:12475640, PubMed:18298658, PubMed:30089812, PubMed:18834968). Plays a redundant role in catalyzing the transfer of galactose onto hydroxylysine groups, giving rise to galactosyl 5-hydroxylysine (PubMed:12475640, PubMed:18298658, PubMed:30089812, PubMed:18834968). Has an essential role by catalyzing the subsequent transfer of glucose moieties, giving rise to 1,2-glucosylgalactosyl-5-hydroxylysine residues (PubMed:10934207, PubMed:11896059, PubMed:11956192, PubMed:12475640, PubMed:18298658, PubMed:30089812, PubMed:18834968). Catalyzes hydroxylation and glycosylation of Lys residues in the MBL1 collagen-like domain, giving rise to hydroxylysine and 1,2-glucosylgalactosyl-5-hydroxylysine residues (PubMed:25419660). Essential for normal biosynthesis and secretion of type IV collagens (PubMed:18834968) (Probable). Essential for normal formation of basement membranes (By similarity).By similarityCurated10 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Lysyl hydroxylase activity is strongly inhibited by imidazole.1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=35 µM for UDP-galactose1 Publication
  2. KM=17 µM for UDP-glucose1 Publication
  3. KM=100 µM for 2-oxoglutarate2 Publications
  4. KM=300 µM for ascorbate1 Publication
  5. KM=350 µM for ascorbate1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi112ManganeseCombined sources1 Publication1
    Metal bindingi115ManganeseCombined sources1 Publication1
    Metal bindingi253ManganeseCombined sources1 Publication1
    <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei5992-oxoglutarateCombined sources1 Publication1
    Binding sitei6562-oxoglutarateCombined sources1 Publication1
    Metal bindingi667IronPROSITE-ProRule annotationCombined sources1 Publication1
    Metal bindingi669IronPROSITE-ProRule annotationCombined sources1 Publication1
    Binding sitei6762-oxoglutarateCombined sources1 Publication1
    Metal bindingi719IronPROSITE-ProRule annotationCombined sources1 Publication1
    Binding sitei7292-oxoglutarateCombined sources1 Publication1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    • iron ion binding Source: InterPro
    • L-ascorbic acid binding Source: UniProtKB-KW
    • procollagen galactosyltransferase activity Source: UniProtKB
    • procollagen glucosyltransferase activity Source: UniProtKB
    • procollagen-lysine 5-dioxygenase activity Source: CAFA

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionDioxygenase, Glycosyltransferase, Multifunctional enzyme, Oxidoreductase, Transferase
    LigandIron, Manganese, Metal-binding, Vitamin C

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    1.14.11.4 2681
    2.4.1.50 2681
    2.4.1.66 2681

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-HSA-1650814 Collagen biosynthesis and modifying enzymes

    Protein family/group databases

    MoonDB Database of extreme multifunctional and moonlighting proteins

    More...
    MoonDBi
    O60568 Curated

    MoonProt database of moonlighting proteins

    More...
    MoonProti
    O60568

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3
    Including the following 2 domains:
    Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3 (EC:1.14.11.46 Publications)
    Alternative name(s):
    Lysyl hydroxylase 32 Publications
    Short name:
    LH31 Publication
    Procollagen glycosyltransferase (EC:2.4.1.504 Publications, EC:2.4.1.667 Publications)
    Alternative name(s):
    Galactosylhydroxylysine-glucosyltransferase
    Procollagen galactosyltransferase
    Procollagen glucosyltransferase
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:PLOD3
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 7

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    HostDB:ENSG00000106397.11

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:9083 PLOD3

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    603066 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_O60568

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Secreted

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    <p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

    Lysyl hydroxylase 3 deficiency (LH3 deficiency)2 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionConnective tissue disorder. The syndrome is characterized by congenital malformations severely affecting many tissues and organs and revealing features of several collagen disorders, most of them involving COL2A1 (type II collagen). The findings suggest that the failure of lysyl hydroxylation and hydroxylysyl carbohydrate addition, which affects many collagens, is the molecular basis of this syndrome.
    See also OMIM:612394
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_054913223N → S in LH3 deficiency; generates a new glycosylation site; decreases protein stability; strongly decreases lysyl hydroxylase activity and nearly abolishes glycosyltransferase activity. 2 PublicationsCorresponds to variant dbSNP:rs121434414EnsemblClinVar.1

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi75W → A: Decreased lysyl hydroxylase activity and loss of glycosyltransferase activity. 1 Publication1
    Mutagenesisi114Y → A: Decreased lysyl hydroxylase and glycosyltransferase activity. 1 Publication1
    Mutagenesisi144C → I: Strongly reduced glucosyltransferase activity. Strongly reduced galactosyltransferase activity. 2 Publications1
    Mutagenesisi187 – 191DDDDD → ADAAA: Loss of glucosyltransferase activity. Loss of galactosyltransferase activity. 3 Publications5
    Mutagenesisi187 – 189DDD → ADA: Nearly abolishes glucosyltransferase activity. Nearly abolishes galactosyltransferase activity. 2 Publications3
    Mutagenesisi208L → I: Reduced glucosyltransferase activity. 1 Publication1
    Mutagenesisi669D → A: Strongly decreased lysyl hydroxylase activity. No effect on glycosyltransferase activity. 2 Publications1
    Mutagenesisi672T → N: Loss of dimerization. Loss of lysyl hydroxylase activity and decreased glycosyltransferase activity. 1 Publication1
    Mutagenesisi714R → N: Loss of dimerization. Loss of lysyl hydroxylase activity and no effect on glycosyltransferase activity. 1 Publication1
    Mutagenesisi715L → D: No effect on dimerization, lysyl hydroxylase and glycosyltransferase activity. 1 Publication1
    Mutagenesisi715L → R: Loss of lysyl hydroxylase activity and decreased glycosyltransferase activity. 1 Publication1

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    8985

    MalaCards human disease database

    More...
    MalaCardsi
    PLOD3
    MIMi612394 phenotype

    Open Targets

    More...
    OpenTargetsi
    ENSG00000106397

    Orphanet; a database dedicated to information on rare diseases and orphan drugs

    More...
    Orphaneti
    300284 Connective tissue disorder due to lysyl hydroxylase-3 deficiency

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA33413

    Chemistry databases

    Drug and drug target database

    More...
    DrugBanki
    DB00139 Succinic acid
    DB00126 Vitamin C

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    PLOD3

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 24Sequence analysisAdd BLAST24
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000002468625 – 738Multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3Add BLAST714

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi63N-linked (GlcNAc...) asparagineCombined sources1 Publication1
    <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi279 ↔ 282Combined sources1 Publication
    Disulfide bondi379 ↔ 385Combined sources1 Publication
    Glycosylationi548N-linked (GlcNAc...) asparagineCombined sources1 Publication1
    Disulfide bondi563 ↔ 698Combined sources1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    O60568

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    O60568

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    O60568

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    O60568

    PeptideAtlas

    More...
    PeptideAtlasi
    O60568

    PRoteomics IDEntifications database

    More...
    PRIDEi
    O60568

    ProteomicsDB human proteome resource

    More...
    ProteomicsDBi
    49474

    PTM databases

    GlyConnect protein glycosylation platform

    More...
    GlyConnecti
    1635

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    O60568

    Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

    More...
    PhosphoSitePlusi
    O60568

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

    Ubiquitous (PubMed:9724729). Detected in heart, placenta and pancreas, and at lower levels in lung, liver and skeletal muscle (PubMed:9582318, PubMed:9724729).2 Publications

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000106397 Expressed in 220 organ(s), highest expression level in placenta

    CleanEx database of gene expression profiles

    More...
    CleanExi
    HS_PLOD3

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    O60568 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    O60568 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    HPA001236

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homodimer.1 Publication

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    114467, 60 interactors

    CORUM comprehensive resource of mammalian protein complexes

    More...
    CORUMi
    O60568

    Protein interaction database and analysis system

    More...
    IntActi
    O60568, 35 interactors

    Molecular INTeraction database

    More...
    MINTi
    O60568

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000223127

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1738
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    6FXKX-ray2.70A25-738[»]
    6FXMX-ray2.10A25-738[»]
    6FXRX-ray2.10A25-738[»]
    6FXTX-ray2.50A25-738[»]
    6FXXX-ray3.00A25-738[»]
    6FXYX-ray2.14A25-738[»]

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    O60568

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    O60568

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini647 – 738Fe2OG dioxygenasePROSITE-ProRule annotationAdd BLAST92

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni25 – 290Required for glycosyltransferase activity2 PublicationsAdd BLAST266
    Regioni44 – 46UDP-sugar bindingCombined sources1 Publication3
    Regioni112 – 114UDP-sugar bindingCombined sources1 Publication3
    Regioni256 – 259UDP-sugar bindingCombined sources1 Publication4
    Regioni295 – 520Accessory region1 PublicationAdd BLAST226
    Regioni672 – 715Important for dimerization1 PublicationAdd BLAST44

    <p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    The N-terminal domain mediates glycosyltransferase activity.1 Publication
    The C-terminal domain that mediates lysyl hydroxylase activity is also important for homodimerization.1 Publication

    Keywords - Domaini

    Signal

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG1971 Eukaryota
    ENOG410Y4QU LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000153705

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000231099

    The HOVERGEN Database of Homologous Vertebrate Genes

    More...
    HOVERGENi
    HBG053618

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    O60568

    KEGG Orthology (KO)

    More...
    KOi
    K13646

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    CIVSSPR

    Database of Orthologous Groups

    More...
    OrthoDBi
    194164at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    O60568

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF313826

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR029044 Nucleotide-diphossugar_trans
    IPR005123 Oxoglu/Fe-dep_dioxygenase
    IPR006620 Pro_4_hyd_alph
    IPR001006 Procol_lys_dOase

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF03171 2OG-FeII_Oxy, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00702 P4Hc, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF53448 SSF53448, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51471 FE2OG_OXY, 1 hit
    PS01325 LYS_HYDROXYLASE, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry has 1 described isoform and 6 potential isoforms that are computationally mapped.Show allAlign All

    O60568-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MTSSGPGPRF LLLLPLLLPP AASASDRPRG RDPVNPEKLL VITVATAETE
    60 70 80 90 100
    GYLRFLRSAE FFNYTVRTLG LGEEWRGGDV ARTVGGGQKV RWLKKEMEKY
    110 120 130 140 150
    ADREDMIIMF VDSYDVILAG SPTELLKKFV QSGSRLLFSA ESFCWPEWGL
    160 170 180 190 200
    AEQYPEVGTG KRFLNSGGFI GFATTIHQIV RQWKYKDDDD DQLFYTRLYL
    210 220 230 240 250
    DPGLREKLSL NLDHKSRIFQ NLNGALDEVV LKFDRNRVRI RNVAYDTLPI
    260 270 280 290 300
    VVHGNGPTKL QLNYLGNYVP NGWTPEGGCG FCNQDRRTLP GGQPPPRVFL
    310 320 330 340 350
    AVFVEQPTPF LPRFLQRLLL LDYPPDRVTL FLHNNEVFHE PHIADSWPQL
    360 370 380 390 400
    QDHFSAVKLV GPEEALSPGE ARDMAMDLCR QDPECEFYFS LDADAVLTNL
    410 420 430 440 450
    QTLRILIEEN RKVIAPMLSR HGKLWSNFWG ALSPDEYYAR SEDYVELVQR
    460 470 480 490 500
    KRVGVWNVPY ISQAYVIRGD TLRMELPQRD VFSGSDTDPD MAFCKSFRDK
    510 520 530 540 550
    GIFLHLSNQH EFGRLLATSR YDTEHLHPDL WQIFDNPVDW KEQYIHENYS
    560 570 580 590 600
    RALEGEGIVE QPCPDVYWFP LLSEQMCDEL VAEMEHYGQW SGGRHEDSRL
    610 620 630 640 650
    AGGYENVPTV DIHMKQVGYE DQWLQLLRTY VGPMTESLFP GYHTKARAVM
    660 670 680 690 700
    NFVVRYRPDE QPSLRPHHDS STFTLNVALN HKGLDYEGGG CRFLRYDCVI
    710 720 730
    SSPRKGWALL HPGRLTHYHE GLPTTWGTRY IMVSFVDP
    Length:738
    Mass (Da):84,785
    Last modified:August 1, 1998 - v1
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i08424B46985941F9
    GO

    <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

    There are 6 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    H7C2S8H7C2S8_HUMAN
    Multifunctional procollagen lysine ...
    PLOD3
    264Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    C9JIX5C9JIX5_HUMAN
    Multifunctional procollagen lysine ...
    PLOD3
    75Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    C9JU11C9JU11_HUMAN
    Multifunctional procollagen lysine ...
    PLOD3
    171Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    H7C2A8H7C2A8_HUMAN
    Multifunctional procollagen lysine ...
    PLOD3
    125Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    H7C0B8H7C0B8_HUMAN
    Multifunctional procollagen lysine ...
    PLOD3
    66Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    H7C2V1H7C2V1_HUMAN
    Multifunctional procollagen lysine ...
    PLOD3
    270Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_051708151A → V. Corresponds to variant dbSNP:rs35627324Ensembl.1
    Natural variantiVAR_054913223N → S in LH3 deficiency; generates a new glycosylation site; decreases protein stability; strongly decreases lysyl hydroxylase activity and nearly abolishes glycosyltransferase activity. 2 PublicationsCorresponds to variant dbSNP:rs121434414EnsemblClinVar.1
    Natural variantiVAR_012075286R → W. Corresponds to variant dbSNP:rs1134907Ensembl.1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    AF046889 mRNA Translation: AAC39753.1
    AF068229 mRNA Translation: AAC34808.1
    AF207069 Genomic DNA Translation: AAF63701.1
    AY220458 mRNA Translation: AAO61775.1
    AK312743 mRNA Translation: BAG35613.1
    AC004876 Genomic DNA Translation: AAD45831.1
    CH471197 Genomic DNA Translation: EAW50205.1
    BC011674 mRNA Translation: AAH11674.1

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS5715.1

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_001075.1, NM_001084.4

    UniGene gene-oriented nucleotide sequence clusters

    More...
    UniGenei
    Hs.153357

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000223127; ENSP00000223127; ENSG00000106397

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    8985

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:8985

    UCSC genome browser

    More...
    UCSCi
    uc003uyd.4 human

    Keywords - Coding sequence diversityi

    Polymorphism

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF046889 mRNA Translation: AAC39753.1
    AF068229 mRNA Translation: AAC34808.1
    AF207069 Genomic DNA Translation: AAF63701.1
    AY220458 mRNA Translation: AAO61775.1
    AK312743 mRNA Translation: BAG35613.1
    AC004876 Genomic DNA Translation: AAD45831.1
    CH471197 Genomic DNA Translation: EAW50205.1
    BC011674 mRNA Translation: AAH11674.1
    CCDSiCCDS5715.1
    RefSeqiNP_001075.1, NM_001084.4
    UniGeneiHs.153357

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    6FXKX-ray2.70A25-738[»]
    6FXMX-ray2.10A25-738[»]
    6FXRX-ray2.10A25-738[»]
    6FXTX-ray2.50A25-738[»]
    6FXXX-ray3.00A25-738[»]
    6FXYX-ray2.14A25-738[»]
    ProteinModelPortaliO60568
    SMRiO60568
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi114467, 60 interactors
    CORUMiO60568
    IntActiO60568, 35 interactors
    MINTiO60568
    STRINGi9606.ENSP00000223127

    Chemistry databases

    DrugBankiDB00139 Succinic acid
    DB00126 Vitamin C

    Protein family/group databases

    MoonDBiO60568 Curated
    MoonProtiO60568

    PTM databases

    GlyConnecti1635
    iPTMnetiO60568
    PhosphoSitePlusiO60568

    Polymorphism and mutation databases

    BioMutaiPLOD3

    Proteomic databases

    EPDiO60568
    jPOSTiO60568
    MaxQBiO60568
    PaxDbiO60568
    PeptideAtlasiO60568
    PRIDEiO60568
    ProteomicsDBi49474

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000223127; ENSP00000223127; ENSG00000106397
    GeneIDi8985
    KEGGihsa:8985
    UCSCiuc003uyd.4 human

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    8985
    DisGeNETi8985
    EuPathDBiHostDB:ENSG00000106397.11

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    PLOD3
    HGNCiHGNC:9083 PLOD3
    HPAiHPA001236
    MalaCardsiPLOD3
    MIMi603066 gene
    612394 phenotype
    neXtProtiNX_O60568
    OpenTargetsiENSG00000106397
    Orphaneti300284 Connective tissue disorder due to lysyl hydroxylase-3 deficiency
    PharmGKBiPA33413

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG1971 Eukaryota
    ENOG410Y4QU LUCA
    GeneTreeiENSGT00940000153705
    HOGENOMiHOG000231099
    HOVERGENiHBG053618
    InParanoidiO60568
    KOiK13646
    OMAiCIVSSPR
    OrthoDBi194164at2759
    PhylomeDBiO60568
    TreeFamiTF313826

    Enzyme and pathway databases

    BRENDAi1.14.11.4 2681
    2.4.1.50 2681
    2.4.1.66 2681
    ReactomeiR-HSA-1650814 Collagen biosynthesis and modifying enzymes

    Miscellaneous databases

    ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

    More...
    ChiTaRSi
    PLOD3 human

    The Gene Wiki collection of pages on human genes and proteins

    More...
    GeneWikii
    PLOD3

    Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

    More...
    GenomeRNAii
    8985

    Protein Ontology

    More...
    PROi
    PR:O60568

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000106397 Expressed in 220 organ(s), highest expression level in placenta
    CleanExiHS_PLOD3
    ExpressionAtlasiO60568 baseline and differential
    GenevisibleiO60568 HS

    Family and domain databases

    InterProiView protein in InterPro
    IPR029044 Nucleotide-diphossugar_trans
    IPR005123 Oxoglu/Fe-dep_dioxygenase
    IPR006620 Pro_4_hyd_alph
    IPR001006 Procol_lys_dOase
    PfamiView protein in Pfam
    PF03171 2OG-FeII_Oxy, 1 hit
    SMARTiView protein in SMART
    SM00702 P4Hc, 1 hit
    SUPFAMiSSF53448 SSF53448, 1 hit
    PROSITEiView protein in PROSITE
    PS51471 FE2OG_OXY, 1 hit
    PS01325 LYS_HYDROXYLASE, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPLOD3_HUMAN
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O60568
    Secondary accession number(s): B2R6W6, Q540C3
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: August 1, 1998
    Last modified: January 16, 2019
    This is version 174 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
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