PPIB peptidylprolyl isomerase B [Homo sapiens (human)] - Gene

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; AllianceGenome:HGNC:9255
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: 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: mouse all
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Genomic context

Location:: 15q22.31

Exon count:: 5

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	15	NC_000015.10 (64155817..64163022, complement)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	15	NC_060939.1 (61962993..61970198, complement)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	15	NC_000015.9 (64448016..64455221, complement)

Chromosome 15 - NC_000015.10 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: HPA RNA-seq normal tissues 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

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Cyclophilins A and B oppositely regulate renal tubular epithelial cell phenotype.
Title: Cyclophilins A and B oppositely regulate renal tubular epithelial cell phenotype.
Influences of cyclosporin A and non-immunosuppressive derivatives on cellular cyclophilins and viral nucleocapsid protein during human coronavirus 229E replication.
Title: Influences of cyclosporin A and non-immunosuppressive derivatives on cellular cyclophilins and viral nucleocapsid protein during human coronavirus 229E replication.
findings suggested that CypB silencing may suppress the proliferation, invasion, migration and angiogenesis of A549 cells via inhibiting STAT3 pathway.
Title: Cyclophilin B promotes cell proliferation, migration, invasion and angiogenesis via regulating the STAT3 pathway in non-small cell lung cancer.
Results provide novel structural information on how PPIB interacts with other components of the P3H1 complex and indicate that the integrity of P3H1 complex is required for proper collagen formation.
Title: Characterization of PPIB interaction in the P3H1 ternary complex and implications for its pathological mutations.
A graphene-based nanocarrier modified with death receptor 4 (DR4) antibody and AKT siRNA has been developed, which can synergistically strengthen death receptor-mediated apoptosis and enhance the cancer therapeutic effect in vivo.
Title: A DR4 capturer with AKT siRNA for the synergetic enhancement of death receptor-mediated apoptosis.
Data show that Cyclophilin B is present on the erythrocytes and binds strongly to merozoites.
Title: Human Cyclophilin B forms part of a multi-protein complex during erythrocyte invasion by Plasmodium falciparum.
cyclophilin B (CYPB) functions in protecting cells against aldosterone-induced oxidative stress, endoplasmic reticulum stress (ERS) and tubular cell injury via its peptidyl-prolyl cis-trans isomerase (PPIase) activity.
Title: Overexpressed cyclophilin B suppresses aldosterone-induced proximal tubular cell injury both in vitro and in vivo.
PPIB mutations and their associated phenotypes
Title: Two novel mutations in the PPIB gene cause a rare pedigree of osteogenesis imperfecta type IX.
observed changes in activity of six rER-resident PPIases, cyclophilin B (encoded by the PPIB gene), FKBP13 (FKBP2), FKBP19 (FKBP11), FKBP22 (FKBP14), FKBP23 (FKBP7), and FKBP65 (FKBP10), due to posttranslational modifications of proline residues in the substrate.
Title: Ziploc-ing the structure 2.0: Endoplasmic reticulum-resident peptidyl prolyl isomerases show different activities toward hydroxyproline.
The data suggest that overexpressed CypB protects neuronal cells from MPP+-induced dopaminergic neuronal cell death
Title: Cyclophilin B protects SH-SY5Y human neuroblastoma cells against MPP(+)-induced neurotoxicity via JNK pathway.

Submit: New GeneRIF Correction See all GeneRIFs (47)

Phenotypes

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Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

Associated conditions

Description	Tests
Osteogenesis imperfecta type 9 MedGen: C1850169 OMIM: 259440 GeneReviews: Not available	Compare labs

Variation

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See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

HIV-1 interactions

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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

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

D8S2279 (e-PCR)
- UniSTS:473907

RH91503 (e-PCR)
- UniSTS:85813

RH98542 (e-PCR)
- UniSTS:87888

RH103326 (e-PCR)
- UniSTS:97657

Ppib (e-PCR), detects polymorphism
- UniSTS:144252

MARC_7211-7212:992008294:1 (e-PCR)
- UniSTS:231310

MARC_7211-7212:996687645:1 (e-PCR)
- UniSTS:231310

WI-9117 (e-PCR)
- UniSTS:32161

MARC_23668-23669:1029507689:1 (e-PCR)
- UniSTS:268742

D15S1174 (e-PCR)
- UniSTS:61138

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables RNA binding	HDA more info	PubMed
enables RNA polymerase binding	IPI Inferred from Physical Interaction more info	PubMed
contributes_to collagen binding	ISS Inferred from Sequence or Structural Similarity more info
enables cyclosporin A binding	IBA Inferred from Biological aspect of Ancestor more info
enables peptidyl-prolyl cis-trans isomerase activity	IBA Inferred from Biological aspect of Ancestor more info
enables peptidyl-prolyl cis-trans isomerase activity	IDA Inferred from Direct Assay more info	PubMed
enables peptidyl-prolyl cis-trans isomerase activity	ISS Inferred from Sequence or Structural Similarity more info
enables peptidyl-prolyl cis-trans isomerase activity	NAS Non-traceable Author Statement more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein binding	ISS Inferred from Sequence or Structural Similarity more info
enables unfolded protein binding	TAS Traceable Author Statement more info	PubMed

Process	Evidence Code	Pubs
involved_in bone development	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in chaperone-mediated protein folding	IDA Inferred from Direct Assay more info	PubMed
NOT involved_in chaperone-mediated protein folding	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in neutrophil chemotaxis	IDA Inferred from Direct Assay more info	PubMed
involved_in positive regulation by host of viral genome replication	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation by host of viral process	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of multicellular organism growth	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein folding	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein peptidyl-prolyl isomerization	ISS Inferred from Sequence or Structural Similarity more info
involved_in protein stabilization	IMP Inferred from Mutant Phenotype more info	PubMed
NOT involved_in regulation of post-translational protein modification	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytosol	TAS Traceable Author Statement more info
located_in endoplasmic reticulum	IDA Inferred from Direct Assay more info	PubMed
part_of endoplasmic reticulum chaperone complex	IEA Inferred from Electronic Annotation more info
located_in endoplasmic reticulum lumen	NAS Non-traceable Author Statement more info	PubMed
located_in endoplasmic reticulum lumen	TAS Traceable Author Statement more info
located_in extracellular exosome	HDA more info	PubMed
located_in focal adhesion	HDA more info	PubMed
is_active_in intracellular membrane-bounded organelle	IBA Inferred from Biological aspect of Ancestor more info
located_in melanosome	IEA Inferred from Electronic Annotation more info
located_in membrane	HDA more info	PubMed
located_in nucleoplasm	IDA Inferred from Direct Assay more info
located_in nucleus	HDA more info	PubMed
located_in perinuclear region of cytoplasm	IDA Inferred from Direct Assay more info	PubMed
part_of protein-containing complex	ISS Inferred from Sequence or Structural Similarity more info
located_in smooth endoplasmic reticulum	IEA Inferred from Electronic Annotation more info

General protein information

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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

EC 5.2.1.8

NCBI Reference Sequences (RefSeq)

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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

NG_012979.1 RefSeqGene

Range

5001..12341

Download

GenBank, FASTA, Sequence Viewer (Graphics), LRG_10

mRNA and Protein(s)

NM_000942.5 → NP_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

Consensus CDS

CCDS10191.1

UniProtKB/Swiss-Prot

A8K534, P23284, Q6IBH5, Q9BVK5

UniProtKB/TrEMBL

A0A7P0TB45

Related

ENSP00000300026.4, ENST00000300026.4

Conserved Domains (1) summary

cd01926
Location:45 → 203

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 accelerates protein folding ...