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    P4HB prolyl 4-hydroxylase, beta polypeptide [ Homo sapiens (human) ]

    Gene ID: 5034, updated on 24-Aug-2015
    Official Symbol
    P4HBprovided by HGNC
    Official Full Name
    prolyl 4-hydroxylase, beta polypeptideprovided by HGNC
    Primary source
    HGNC:HGNC:8548
    See related
    Ensembl:ENSG00000185624; HPRD:07181; MIM:176790; Vega:OTTHUMG00000150269
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Homo sapiens
    Lineage
    Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
    Also known as
    DSI; GIT; PDI; PHDB; PDIA1; PO4DB; PO4HB; PROHB; CLCRP1; ERBA2L; P4Hbeta
    Summary
    This gene encodes the beta subunit of prolyl 4-hydroxylase, a highly abundant multifunctional enzyme that belongs to the protein disulfide isomerase family. When present as a tetramer consisting of two alpha and two beta subunits, this enzyme is involved in hydroxylation of prolyl residues in preprocollagen. This enzyme is also a disulfide isomerase containing two thioredoxin domains that catalyze the formation, breakage and rearrangement of disulfide bonds. Other known functions include its ability to act as a chaperone that inhibits aggregation of misfolded proteins in a concentration-dependent manner, its ability to bind thyroid hormone, its role in both the influx and efflux of S-nitrosothiol-bound nitric oxide, and its function as a subunit of the microsomal triglyceride transfer protein complex. [provided by RefSeq, Jul 2008]
    Orthologs
    See P4HB in Epigenomics, MapViewer
    Location:
    17q25
    Exon count:
    11
    Annotation release Status Assembly Chr Location
    107 current GRCh38.p2 (GCF_000001405.28) 17 NC_000017.11 (81843158..81860668, complement)
    105 previous assembly GRCh37.p13 (GCF_000001405.25) 17 NC_000017.10 (79801034..79818566, complement)

    Chromosome 17 - NC_000017.11Genomic Context describing neighboring genes Neighboring gene family with sequence similarity 195, member B Neighboring gene protein phosphatase 1, regulatory subunit 27 Neighboring gene Rho GDP dissociation inhibitor (GDI) alpha Neighboring gene Aly/REF export factor Neighboring gene anaphase promoting complex subunit 11

    GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

    Protein interactions

    Protein Gene Interaction Pubs
    Envelope surface glycoprotein gp120 env The disulfide cross-linking interaction between gp120 and PDI is enhanced by CD4 protein PubMed
    env PDI is predominantly involved in HIV-1 entry and infection of the T cell line PM-1 and PHA-stimulated primary T lymphocytes, suggesting the preferential use of PDI relevant to the HIV-1 entry and establishment of virus reservoirs in resting CD4+ cells PubMed
    env Protein-disulfide isomerase (PDI) cleaves disulfide bonds in recombinant HIV-1 envelope glycoprotein gp120, and gp120 bound to the surface receptor CD4 undergoes a disulfide reduction that is prevented by PDI inhibitors PubMed
    Envelope surface glycoprotein gp160, precursor env HIV-1 gp160 is identified to have a physical interaction with prolyl 4-hydroxylase, beta polypeptide (P4HB) in human HEK293 and/or Jurkat cell lines by using affinity tagging and purification mass spectrometry analyses PubMed
    env Treatment of trimeric HIV-1 rgp140 with protein disulfide isomerase yields monomers by disruption of the intermolecular disulfide bonds PubMed
    Rev rev HIV-1 Rev interacting protein, prolyl 4-hydroxylase, beta polypeptide (P4HB), is identified by the in-vitro binding experiments involving cytosolic or nuclear extracts from HeLa cells. The interaction of Rev with P4HB is increased by RRE PubMed
    Vpr vpr A stable-isotope labeling by amino acids in cell culture coupled with mass spectrometry-based proteomics identifies upregulation of prolyl 4-hydroxylase, beta polypeptide (P4HB, PDIA1) expression by HIV-1 Vpr in Vpr transduced macrophages PubMed

    Go to the HIV-1, Human Interaction Database

    • Cellular responses to stress, organism-specific biosystem (from REACTOME)
      Cellular responses to stress, organism-specific biosystemCells are subject to external molecular and physical stresses such as foreign molecules that perturb metabolic or signaling processes, and changes in temperature or pH. The ability of cells and tissu...
    • Chylomicron-mediated lipid transport, organism-specific biosystem (from REACTOME)
      Chylomicron-mediated lipid transport, organism-specific biosystemChylomicrons transport triacylglycerol, phospholipid, and cholesterol derived from dietary lipid from the small intestine to other tissues of the body. Each chylomicron assembles around a single mole...
    • Collagen biosynthesis and modifying enzymes, organism-specific biosystem (from REACTOME)
      Collagen biosynthesis and modifying enzymes, organism-specific biosystemThe biosynthesis of collagen is a multistep process. Collagen propeptides are cotranslationally translocated into the ER lumen. Propeptides undergo a number of post-translational modifications. Proli...
    • Collagen formation, organism-specific biosystem (from REACTOME)
      Collagen formation, organism-specific biosystemCollagen is a family of at least 29 structural proteins derived from over 40 human genes (Myllyharju & Kivirikko 2004). It is the main component of connective tissue, and the most abundant protein in...
    • Detoxification of Reactive Oxygen Species, organism-specific biosystem (from REACTOME)
      Detoxification of Reactive Oxygen Species, organism-specific biosystemReactive oxygen species such as superoxide (O2.-), peroxides (ROOR), singlet oxygen, peroxynitrite (ONOO-), and hydroxyl radical (OH.) are generated by cellular processes such as respiration (reviewe...
    • Extracellular matrix organization, organism-specific biosystem (from REACTOME)
      Extracellular matrix organization, organism-specific biosystemThe extracellular matrix is a component of all mammalian tissues, a network consisting largely of the fibrous proteins collagen, elastin and associated-microfibrils, fibronectin and laminins embedded...
    • Hedgehog ligand biogenesis, organism-specific biosystem (from REACTOME)
      Hedgehog ligand biogenesis, organism-specific biosystemMammalian genomes encode three Hedgehog ligands, Sonic Hedgehog (SHH), Indian Hedgehog (IHH) and Desert Hedgehog (DHH). These secreted morphogens can remain associated with lipid rafts on the surfac...
    • Lipid digestion, mobilization, and transport, organism-specific biosystem (from REACTOME)
      Lipid digestion, mobilization, and transport, organism-specific biosystemProcesses annotated here include the digestion of dietary lipids, sterol uptake, the formation and turnover of lipoproteins (chylomicrons, VLDL, LDL, and HDL), and the mobilization of fatty acids thr...
    • Lipoprotein metabolism, organism-specific biosystem (from REACTOME)
      Lipoprotein metabolism, organism-specific biosystemBecause of their hydrophobicity, lipids are found in the extracellular spaces of the human body primarily in the form of lipoprotein complexes. Chylomicrons form in the small intestine and transport ...
    • Metabolism, organism-specific biosystem (from REACTOME)
      Metabolism, organism-specific biosystemMetabolic processes in human cells generate energy through the oxidation of molecules consumed in the diet and mediate the synthesis of diverse essential molecules not taken in the diet as well as th...
    • Metabolism of lipids and lipoproteins, organism-specific biosystem (from REACTOME)
      Metabolism of lipids and lipoproteins, organism-specific biosystemLipids are hydrophobic but otherwise chemically diverse molecules that play a wide variety of roles in human biology. They include ketone bodies, fatty acids, triacylglycerols, phospholipids and sphi...
    • Protein processing in endoplasmic reticulum, organism-specific biosystem (from KEGG)
      Protein processing in endoplasmic reticulum, organism-specific biosystemThe endoplasmic reticulum (ER) is a subcellular organelle where proteins are folded with the help of lumenal chaperones. Newly synthesized peptides enter the ER via the sec61 pore and are glycosylate...
    • Protein processing in endoplasmic reticulum, conserved biosystem (from KEGG)
      Protein processing in endoplasmic reticulum, conserved biosystemThe endoplasmic reticulum (ER) is a subcellular organelle where proteins are folded with the help of lumenal chaperones. Newly synthesized peptides enter the ER via the sec61 pore and are glycosylate...
    • Signal Transduction, organism-specific biosystem (from REACTOME)
      Signal Transduction, organism-specific biosystemSignal transduction is a process in which extracellular signals elicit changes in cell state and activity. Transmembrane receptors sense changes in the cellular environment by binding ligands, such a...
    • Signaling by Hedgehog, organism-specific biosystem (from REACTOME)
      Signaling by Hedgehog, organism-specific biosystemHedgehog (Hh) is a secreted morphogen that regulates developmental processes in vertebrates including limb bud formation, neural tube patterning, cell growth and differentiation (reviewed in Hui and ...
    Products Interactant Other Gene Complex Source Pubs Description

    Markers

    Homology

    Gene Ontology Provided by GOA

    Function Evidence Code Pubs
    endopeptidase activity TAS
    Traceable Author Statement
    more info
     
    enzyme binding IEA
    Inferred from Electronic Annotation
    more info
     
    poly(A) RNA binding IDA
    Inferred from Direct Assay
    more info
    PubMed 
    contributes_to procollagen-proline 4-dioxygenase activity IDA
    Inferred from Direct Assay
    more info
    PubMed 
    protein binding IPI
    Inferred from Physical Interaction
    more info
    PubMed 
    protein disulfide isomerase activity IDA
    Inferred from Direct Assay
    more info
    PubMed 
    protein heterodimerization activity IEA
    Inferred from Electronic Annotation
    more info
     
    Process Evidence Code Pubs
    cell redox homeostasis IEA
    Inferred from Electronic Annotation
    more info
     
    cellular response to hypoxia IMP
    Inferred from Mutant Phenotype
    more info
    PubMed 
    extracellular matrix organization TAS
    Traceable Author Statement
    more info
     
    lipoprotein metabolic process TAS
    Traceable Author Statement
    more info
     
    peptidyl-proline hydroxylation to 4-hydroxy-L-proline IDA
    Inferred from Direct Assay
    more info
    PubMed 
    positive regulation of viral entry into host cell IMP
    Inferred from Mutant Phenotype
    more info
    PubMed 
    protein folding IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    proteolysis TAS
    Traceable Author Statement
    more info
     
    regulation of oxidative stress-induced intrinsic apoptotic signaling pathway IMP
    Inferred from Mutant Phenotype
    more info
    PubMed 
    response to endoplasmic reticulum stress IMP
    Inferred from Mutant Phenotype
    more info
    PubMed 
    response to reactive oxygen species TAS
    Traceable Author Statement
    more info
     
    small molecule metabolic process TAS
    Traceable Author Statement
    more info
     
    Component Evidence Code Pubs
    endoplasmic reticulum IDA
    Inferred from Direct Assay
    more info
    PubMed 
    endoplasmic reticulum chaperone complex IEA
    Inferred from Electronic Annotation
    more info
     
    endoplasmic reticulum lumen TAS
    Traceable Author Statement
    more info
     
    endoplasmic reticulum-Golgi intermediate compartment IDA
    Inferred from Direct Assay
    more info
    PubMed 
    external side of plasma membrane IDA
    Inferred from Direct Assay
    more info
    PubMed 
    extracellular exosome IDA
    Inferred from Direct Assay
    more info
    PubMed 
    extracellular region NAS
    Non-traceable Author Statement
    more info
    PubMed 
    focal adhesion IDA
    Inferred from Direct Assay
    more info
    PubMed 
    melanosome IEA
    Inferred from Electronic Annotation
    more info
     
    procollagen-proline 4-dioxygenase complex IDA
    Inferred from Direct Assay
    more info
    PubMed 
    Preferred Names
    protein disulfide-isomerase
    Names
    cellular thyroid hormone-binding protein
    collagen prolyl 4-hydroxylase beta
    glutathione-insulin transhydrogenase
    p55
    procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), beta polypeptide
    prolyl 4-hydroxylase subunit beta
    protein disulfide isomerase family A, member 1
    protein disulfide isomerase-associated 1
    protein disulfide isomerase/oxidoreductase
    protocollagen hydroxylase
    thyroid hormone-binding protein p55
    NP_000909.2

    RefSeqs maintained independently of Annotated Genomes

    These reference sequences exist independently of genome builds. Explain

    These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

    Genomic

    1. NG_042033.1 RefSeqGene

      Range
      5001..22511
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_000918.3NP_000909.2  protein disulfide-isomerase precursor

      See identical proteins and their annotated locations for NP_000909.2

      Status: REVIEWED

      Source sequence(s)
      AU131354, BC010859, CA412209, DB466371
      Consensus CDS
      CCDS11787.1
      UniProtKB/TrEMBL
      A0A024R8S5
      UniProtKB/Swiss-Prot
      P07237
      Related
      ENSP00000327801, OTTHUMP00000196834, ENST00000331483, OTTHUMT00000317250
      Conserved Domains (5) summary
      cd02961
      Location:27129
      PDI_a_family; Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic proteins involved in oxidative protein folding in the endoplasmic reticulum (ER) by acting as catalysts and folding assistants. Members of this family include PDI ...
      cd02981
      Location:137232
      PDI_b_family; Protein Disulfide Isomerase (PDIb) family, redox inactive TRX-like domain b; composed of eukaryotic proteins involved in oxidative protein folding in the endoplasmic reticulum (ER) by acting as catalysts and folding assistants. Members of this family ...
      cd02982
      Location:244347
      PDI_b'_family; Protein Disulfide Isomerase (PDIb') family, redox inactive TRX-like domain b'; composed of eukaryotic proteins involved in oxidative protein folding in the endoplasmic reticulum (ER) by acting as catalysts and folding assistants. Members of this family ...
      cd02995
      Location:368470
      PDI_a_PDI_a'_C; PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' domains of PDI, ERp72, ERp57 (or ERp60) and EFP1. PDI, ERp72 and ERp57 are endoplasmic reticulum (ER)-resident eukaryotic proteins involved in oxidative protein ...
      TIGR01130
      Location:24474
      ER_PDI_fam; protein disulfide isomerase, eukaryotic

    RefSeqs of Annotated Genomes: Homo sapiens Annotation Release 107

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference GRCh38.p2 Primary Assembly

    Genomic

    1. NC_000017.11 Reference GRCh38.p2 Primary Assembly

      Range
      81843158..81860668
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    Alternate CHM1_1.1

    Genomic

    1. NC_018928.2 Alternate CHM1_1.1

      Range
      79887239..79904780
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)