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

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Summary

Official Symbol: PPIBprovided by HGNC
Official Full Name: peptidylprolyl isomerase B (cyclophilin B)provided by HGNC
Primary source: HGNC:9255
See related: Ensembl:ENSG00000166794; HPRD:00458; MIM:123841; Vega:OTTHUMG00000133018
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; MGC2224; MGC14109
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]

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Genomic context

Location :: 15q21-q22

Sequence :: Chromosome: 15; NC_000015.9 (64448014..64455354, complement)

See PPIB in Epigenomics, MapViewer

Chromosome 15 - NC_000015.9 Genomic Context describing neighboring genes

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Genomic regions, transcripts, and products

Genomic Sequence

Go to nucleotideGraphics FASTA GenBank

Go to reference sequence details

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Bibliography

GeneRIFs: Gene References Into Functions What's a GeneRIF?

First report of a unique, multicomponent, high-capacity milk fat reservoir of prolactin as a bilayer-bound complex with cyclophilins A and B in human milk.
Title: A major prolactin-binding complex on human milk fat globule membranes contains cyclophilins A and B: the complex is not the prolactin receptor.
CypB induced by hypoxia stimulates the survival of hepatocellular carcinoma via a positive feedback loop with HIF-1alpha.
Title: Role of cyclophilin B in tumorigenesis and cisplatin resistance in hepatocellular carcinoma in humans.
CAHL is a CsA associated helicase-like protein, which would form trimer complex with cyclophilin B and NS5B of HCV
Title: Cyclosporin A associated helicase-like protein facilitates the association of hepatitis C virus RNA polymerase with its cellular cyclophilin B.
peptidylprolyl cis-trans isomerase B may be required to effectively fold the proline-rich regions of the C-terminal propeptide of procollagen
Title: Mutations in PPIB (cyclophilin B) delay type I procollagen chain association and result in perinatal lethal to moderate osteogenesis imperfecta phenotypes.
cyclophilin isoform B is likely responsible for down-regulation of carrier expression by CsA and that it does so via its chaperone activity on NaDC1 (by direct interaction) rather than its rotamase activity.
Title: Synthesis, maturation, and trafficking of human Na+-dicarboxylate cotransporter NaDC1 requires the chaperone activity of cyclophilin B.
These results suggest that CypB plays a crucial role in the replication of Japanese encephalitis virus through an interaction with NS4A.
Title: Involvement of cyclophilin B in the replication of Japanese encephalitis virus.
Data indicate that CypB through its interaction with Na/K-beta1 might regulate maturation and trafficking of the pump through the secretory pathway.
Title: Cyclophilin B interacts with sodium-potassium ATPase and is required for pump activity in proximal tubule cells of the kidney.
Results reveal the P-domain functions as a unique protein-protein interaction domain and implicate a peptidyl prolyl isomerase as a new element in the calnexin cycle.
Title: Structural basis of cyclophilin B binding by the calnexin/calreticulin P-domain.
Cyclophilin B significantly modulate prolactin-induced function in breast cancer cells, ultimately resulting in enhanced levels of prolactin-responsive gene expression, cell growth, and migration.
Title: Cyclophilin B as a co-regulator of prolactin-induced gene expression and function in breast cancer cells.
a regulatory mechanism in which cell type-specific expression of certain heparan sulfate sulfotransferases determines the specific binding of CyPB to target cells
Title: Synthesis of heparan sulfate with cyclophilin B-binding properties is determined by cell type-specific expression of sulfotransferases.

Submit: New GeneRIF Correction See all (23)

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Phenotypes

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

Review eQTL and phenotype association data in this region using PheGenI

Osteogenesis imperfecta, type IX

MIM: 259440

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HIV-1 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
capsid	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 Protein Interaction Database

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Products	Interactant	Other Gene	Source	Pubs	Description
NP_000933.1	NP_751928.1	HCVgp1	BIND	PubMed	CyPB interacts with NS5B.
NP_000933.1	NP_057850.1	gag	BIND	PubMed	CyPB interacts with Pr55gag.
NP_000933.1			BIND	PubMed	CyPB interacts with NS5B-HCV RNA complex.
P23284	P04114	APOB	HPRD	PubMed
P23284	P50570	DNM2	HPRD	PubMed
P23284	Q14653	IRF3	HPRD	PubMed
P23284	P01236	PRL	HPRD	PubMed
P23284	P42229	STAT5A	HPRD	PubMed
P23284	Q9NRR5	UBQLN4	HPRD	PubMed
BioGRID:111475	BioGRID:223223	AI837181	BioGRID	PubMed	Affinity Capture-MS
BioGRID:111475	BioGRID:106835	APOB	BioGRID	PubMed	Affinity Capture-Western; Co-fractionation
BioGRID:111475	BioGRID:107269	CAMLG	BioGRID	PubMed	Two-hybrid
BioGRID:111475	BioGRID:111139	PCM1	BioGRID	PubMed	Affinity Capture-MS
BioGRID:111475	BioGRID:111602	PRL	BioGRID	PubMed	Affinity Capture-Western; Reconstituted Complex; Two-hybrid
BioGRID:111475	BioGRID:119653	TMBIM4	BioGRID	PubMed	Affinity Capture-MS
BioGRID:111475	BioGRID:113164	UBC	BioGRID	PubMed	Affinity Capture-MS
BioGRID:111475	BioGRID:117950	USP21	BioGRID	PubMed	Affinity Capture-MS
BioGRID:111475	BioGRID:113269	VHL	BioGRID	PubMed	Affinity Capture-MS
BioGRID:111475	BioGRID:121649	WDR48	BioGRID	PubMed	Affinity Capture-MS

Function	Evidence Code	Pubs
isomerase activity	IEA Inferred from Electronic Annotation more info
peptide binding	IEA Inferred from Electronic Annotation 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
unfolded protein binding	TAS Traceable Author Statement more info	PubMed

Process	Evidence Code	Pubs
protein folding	IEA Inferred from Electronic Annotation more info
protein peptidyl-prolyl isomerization	NAS Non-traceable Author Statement more info	PubMed

Component	Evidence Code	Pubs
endoplasmic reticulum	IEA Inferred from Electronic Annotation more info
endoplasmic reticulum lumen	NAS Non-traceable Author Statement more info	PubMed
melanosome	IEA Inferred from Electronic Annotation more info

General protein information

Preferred Names: peptidyl-prolyl cis-trans isomerase B

Names: peptidyl-prolyl cis-trans isomerase B; PPIase B; rotamase B; S-cyclophilin; cyclophilin-like protein

NP_000933.1

EC 5.2.1.8

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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

NG_012979.1 RefSeqGene

Range

5001..12341

Download

GenBank, FASTA, Sequence Viewer (Graphics), LRG_10

mRNA and Protein(s)

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

Status: REVIEWED

Source sequence(s)

BC001125, BC008848, BQ931949

Consensus CDS

CCDS10191.1

UniProtKB/Swiss-Prot

P23284

Related

ENSP00000300026, OTTHUMP00000163975, ENST00000300026, OTTHUMT00000256604

Conserved Domains (2) summary

cd01926
Location:45 – 203
Blast Score: 640

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 ...

PRK10791
Location:58 – 199
Blast Score: 140

PRK10791; peptidyl-prolyl cis-trans isomerase B (rotamase B); Provisional

RefSeqs of Annotated Genomes: Build 37.3

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

Reference GRCh37.p5 Primary Assembly

Genomic

NC_000015.9 Reference GRCh37.p5 Primary Assembly

Range

64448014..64455354, complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

Alternate HuRef

Genomic

AC_000147.1 Alternate HuRef

Range

41272716..41280027, complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

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Related Sequences

Nucleotide		Protein
Heading	Accession and Version	Protein
genomic	AC100840.2 (13938..21278)	None
genomic	AY962310.1	AAX44050.1
genomic	CH471082.1	EAW77669.1
genomic	CS208051.1	CAJ44951.1
genomic	HB867236.1	CBF57604.1
mRNA	AK291149.1	BAF83838.1
mRNA	AK311074.1	None
mRNA	BC001125.2	AAH01125.1
mRNA	BC008848.2	AAH08848.1
mRNA	BC020800.1	AAH20800.1
mRNA	BC032138.2	AAH32138.1
mRNA	BQ931949.1	None
mRNA	CR456829.1	CAG33110.1
mRNA	D28465.1	BAA05831.1
mRNA	M60457.1	AAA35733.1
mRNA	M60857.1	AAA52150.1
mRNA	M63573.1	AAA36601.1
other-genetic	DQ892289.2	ABM83215.1
other-genetic	DQ895488.2	ABM86414.1