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PPIB peptidylprolyl isomerase B [ Homo sapiens (human) ]

Gene ID: 5479, updated on 7-Jul-2019

Summary

Official Symbol
PPIBprovided by HGNC
Official Full Name
peptidylprolyl isomerase Bprovided by HGNC
Primary source
HGNC:HGNC:9255
See related
Ensembl:ENSG00000166794 MIM:123841
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
B; OI9; CYPB; SCYLP; CYP-S1; HEL-S-39
Summary
The protein encoded by this gene is a cyclosporine-binding protein and is mainly located within the endoplasmic reticulum. It is associated with the secretory pathway and released in biological fluids. This protein can bind to cells derived from T- and B-lymphocytes, and may regulate cyclosporine A-mediated immunosuppression. Variants have been identified in this protein that give rise to recessive forms of osteogenesis imperfecta. [provided by RefSeq, Oct 2009]
Expression
Ubiquitous expression in thyroid (RPKM 295.6), placenta (RPKM 241.5) and 25 other tissues See more
Orthologs

Genomic context

See PPIB in Genome Data Viewer
Location:
15q22.31
Exon count:
5
Annotation release Status Assembly Chr Location
109.20190607 current GRCh38.p13 (GCF_000001405.39) 15 NC_000015.10 (64155815..64163155, complement)
105 previous assembly GRCh37.p13 (GCF_000001405.25) 15 NC_000015.9 (64448014..64455354, complement)

Chromosome 15 - NC_000015.10Genomic Context describing neighboring genes Neighboring gene cytosolic iron-sulfur assembly component 2A Neighboring gene sorting nexin 1 Neighboring gene sorting nexin 22 Neighboring gene casein kinase 1 gamma 1 Neighboring gene Sharpr-MPRA regulatory region 12494 Neighboring gene PCNA clamp associated factor

Genomic regions, transcripts, and products

Expression

  • Project title: HPA RNA-seq normal tissues
  • Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
  • BioProject: PRJEB4337
  • Publication: PMID 24309898
  • Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

HIV-1 interactions

Replication interactions

Interaction Pubs
HIV-1 replication, specifically nuclear import, is enhanced by over-expression of PPIB (CypB); enhancement is dependent dose and the N-terminus of PPIB PubMed
Knockdown of peptidylprolyl isomerase B (PPIB; cyclophilin B) by siRNA inhibits HIV-1 replication in HeLa-derived TZM-bl cells PubMed

Protein interactions

Protein Gene Interaction Pubs
Envelope surface glycoprotein gp120 env Macrophage- and T-cell-tropic V3 loop peptides of HIV-1 gp120 bind specifically to the active site of the immunophilins FK506-binding protein (FKBP12), and cyclophilins A and B, and inhibit their peptidyl-prolyl cis-trans isomerase (PPIase) activities PubMed
Rev rev HIV-1 Rev interacting protein, peptidylprolyl isomerase B (cyclophilin B), is identified by the in-vitro binding experiments involving cytosolic or nuclear extracts from HeLa cells. The interaction of Rev with PPIB is increased by RRE PubMed
capsid gag The interaction of HIV-1 CA with human cellular peptidylprolyl isomerase B (PPIB, cyclophilin B) is identified by yeast two-hybrid screen PubMed
gag Cyclophilin B binds to several Gly-Pro amino acid motifs in HIV-1 Capsid (amino acids 89-90, 156-157, and 223-224 PubMed

Go to the HIV-1, Human Interaction Database

Pathways from BioSystems

  • 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...
  • 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...
  • Prolactin Signaling Pathway, organism-specific biosystem (from WikiPathways)
    Prolactin Signaling Pathway, organism-specific biosystemProlactin (PRL), a pleiotropic polypeptide hormone, mostly secreted by the lactotrophic cells of anterior pituitary gland and to a lesser extent expressed in numerous extra pituitary tissues such as ...
  • Syndecan-1-mediated signaling events, organism-specific biosystem (from Pathway Interaction Database)
    Syndecan-1-mediated signaling events, organism-specific biosystem
    Syndecan-1-mediated signaling events

Interactions

Products Interactant Other Gene Complex Source Pubs Description

General gene information

Markers

Homology

Clone Names

  • MGC2224, MGC14109

Gene Ontology Provided by GOA

Function Evidence Code Pubs
RNA binding HDA PubMed 
RNA polymerase binding IPI
Inferred from Physical Interaction
more info
PubMed 
contributes_to collagen binding IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
contributes_to collagen binding ISS
Inferred from Sequence or Structural Similarity
more info
 
cyclosporin A binding IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
cyclosporin A binding IDA
Inferred from Direct Assay
more info
PubMed 
peptidyl-prolyl cis-trans isomerase activity IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
peptidyl-prolyl cis-trans isomerase activity IDA
Inferred from Direct Assay
more info
PubMed 
peptidyl-prolyl cis-trans isomerase activity ISS
Inferred from Sequence or Structural Similarity
more info
 
peptidyl-prolyl cis-trans isomerase activity NAS
Non-traceable Author Statement
more info
PubMed 
protein binding IPI
Inferred from Physical Interaction
more info
PubMed 
protein binding ISS
Inferred from Sequence or Structural Similarity
more info
 
unfolded protein binding IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
Process Evidence Code Pubs
bone development IMP
Inferred from Mutant Phenotype
more info
PubMed 
chaperone-mediated protein folding IDA
Inferred from Direct Assay
more info
PubMed 
NOT chaperone-mediated protein folding IMP
Inferred from Mutant Phenotype
more info
PubMed 
positive regulation by host of viral genome replication IMP
Inferred from Mutant Phenotype
more info
PubMed 
positive regulation by host of viral process IMP
Inferred from Mutant Phenotype
more info
PubMed 
positive regulation of multicellular organism growth IMP
Inferred from Mutant Phenotype
more info
PubMed 
protein peptidyl-prolyl isomerization IDA
Inferred from Direct Assay
more info
PubMed 
protein peptidyl-prolyl isomerization ISS
Inferred from Sequence or Structural Similarity
more info
 
protein refolding IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
protein stabilization IMP
Inferred from Mutant Phenotype
more info
PubMed 
NOT regulation of post-translational protein modification IMP
Inferred from Mutant Phenotype
more info
PubMed 
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 NAS
Non-traceable Author Statement
more info
PubMed 
endoplasmic reticulum lumen TAS
Traceable Author Statement
more info
 
extracellular exosome HDA PubMed 
focal adhesion HDA PubMed 
melanosome IEA
Inferred from Electronic Annotation
more info
 
membrane HDA PubMed 
nucleus HDA PubMed 
nucleus IDA
Inferred from Direct Assay
more info
 
perinuclear region of cytoplasm IDA
Inferred from Direct Assay
more info
PubMed 
protein-containing complex ISS
Inferred from Sequence or Structural Similarity
more info
 
smooth endoplasmic reticulum IEA
Inferred from Electronic Annotation
more info
 

General protein information

Preferred Names
peptidyl-prolyl cis-trans isomerase B
Names
PPIase B
S-cyclophilin
cyclophilin-like protein
epididymis secretory protein Li 39
peptidylprolyl isomerase B (cyclophilin B)
rotamase B
NP_000933.1

NCBI Reference Sequences (RefSeq)

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_012979.1 RefSeqGene

    Range
    5001..12341
    Download
    GenBank, FASTA, Sequence Viewer (Graphics), LRG_10

mRNA and Protein(s)

  1. NM_000942.4NP_000933.1  peptidyl-prolyl cis-trans isomerase B precursor

    See identical proteins and their annotated locations for NP_000933.1

    Status: REVIEWED

    Source sequence(s)
    BC001125, BC008848, BQ931949
    Consensus CDS
    CCDS10191.1
    UniProtKB/Swiss-Prot
    P23284
    Related
    ENSP00000300026.3, ENST00000300026.3
    Conserved Domains (1) summary
    cd01926
    Location:45203
    cyclophilin_ABH_like; cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans isomerase (PPIase) domain. This family represents the archetypal cystolic cyclophilin similar to human cyclophilins A, B and H. PPIase is an enzyme which ...

RefSeqs of Annotated Genomes: Homo sapiens Annotation Release 109

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

Reference GRCh38.p13 Primary Assembly

Genomic

  1. NC_000015.10 Reference GRCh38.p13 Primary Assembly

    Range
    64155815..64163155 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)
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