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Protein

Peptidyl-prolyl cis-trans isomerase B

Gene

PPIB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

Catalytic activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).

Enzyme regulationi

Cyclosporin A (CsA) inhibits CYPB.

GO - Molecular functioni

  • peptide binding Source: UniProtKB-KW
  • peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • protein complex binding Source: UniProtKB
  • RNA polymerase binding Source: AgBase
  • unfolded protein binding Source: ProtInc

GO - Biological processi

  • bone development Source: UniProtKB
  • chaperone-mediated protein folding Source: UniProtKB
  • positive regulation by host of viral genome replication Source: AgBase
  • positive regulation by host of viral process Source: AgBase
  • positive regulation of multicellular organism growth Source: UniProtKB
  • protein peptidyl-prolyl isomerization Source: UniProtKB
  • protein stabilization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Keywords - Ligandi

Cyclosporin

Enzyme and pathway databases

BioCyciZFISH:HS09452-MONOMER.
BRENDAi5.2.1.8. 2681.
ReactomeiR-HSA-1650814. Collagen biosynthesis and modifying enzymes.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase B (EC:5.2.1.8)
Short name:
PPIase B
Alternative name(s):
CYP-S1
Cyclophilin B
Rotamase B
S-cyclophilin
Short name:
SCYLP
Gene namesi
Name:PPIB
Synonyms:CYPB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:9255. PPIB.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum chaperone complex Source: Ensembl
  • endoplasmic reticulum lumen Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • macromolecular complex Source: UniProtKB
  • melanosome Source: UniProtKB-SubCell
  • membrane Source: UniProtKB
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: AgBase
  • smooth endoplasmic reticulum Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Involvement in diseasei

Osteogenesis imperfecta 9 (OI9)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI9 is a severe autosomal recessive form of the disorder.
See also OMIM:259440
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0634369M → R in OI9; patients have white sclerae, normal dentition, no rhizomelia or severe deformity of long bones. 1 PublicationCorresponds to variant rs137853864dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi129K → A: Impairs interaction with CLGN and CANX. 1 Publication1

Keywords - Diseasei

Disease mutation, Dwarfism, Osteogenesis imperfecta

Organism-specific databases

DisGeNETi5479.
MalaCardsiPPIB.
MIMi259440. phenotype.
OpenTargetsiENSG00000166794.
Orphaneti216804. Osteogenesis imperfecta type 2.
216812. Osteogenesis imperfecta type 3.
216820. Osteogenesis imperfecta type 4.
PharmGKBiPA33580.

Chemistry databases

ChEMBLiCHEMBL2075.
DrugBankiDB00172. L-Proline.

Polymorphism and mutation databases

BioMutaiPPIB.
DMDMi215273869.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 331 PublicationAdd BLAST33
ChainiPRO_000002547934 – 216Peptidyl-prolyl cis-trans isomerase BAdd BLAST183

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi148N-linked (GlcNAc...)Sequence analysis1
Modified residuei209N6-acetyllysine; alternateBy similarity1
Modified residuei209N6-succinyllysine; alternateBy similarity1

Keywords - PTMi

Acetylation, Glycoprotein

Proteomic databases

EPDiP23284.
MaxQBiP23284.
PaxDbiP23284.
PeptideAtlasiP23284.
PRIDEiP23284.
TopDownProteomicsiP23284.

2D gel databases

OGPiP23284.
REPRODUCTION-2DPAGEIPI00646304.
SWISS-2DPAGEP23284.

PTM databases

iPTMnetiP23284.
PhosphoSitePlusiP23284.
SwissPalmiP23284.

Expressioni

Gene expression databases

BgeeiENSG00000166794.
CleanExiHS_PPIB.
GenevisibleiP23284. HS.

Organism-specific databases

HPAiCAB011487.
HPA012720.

Interactioni

Subunit structurei

Interacts with DYM. Interacts with CALR, CLGN and CANX.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q9WMX27EBI-359252,EBI-9005440From a different organism.
BANPQ8N9N53EBI-359252,EBI-744695
PDIA4P136673EBI-8771982,EBI-1054653
PEX19P408555EBI-359252,EBI-594747
SGTAO437655EBI-359252,EBI-347996
UBQLN1Q9UMX03EBI-359252,EBI-741480
UBQLN1Q9UMX0-23EBI-359252,EBI-10173939

GO - Molecular functioni

  • protein complex binding Source: UniProtKB
  • RNA polymerase binding Source: AgBase
  • unfolded protein binding Source: ProtInc

Protein-protein interaction databases

BioGridi111475. 90 interactors.
IntActiP23284. 32 interactors.
MINTiMINT-1142578.
STRINGi9606.ENSP00000300026.

Chemistry databases

BindingDBiP23284.

Structurei

Secondary structure

1216
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi41 – 52Combined sources12
Beta strandi55 – 64Combined sources10
Turni66 – 68Combined sources3
Helixi70 – 81Combined sources12
Turni82 – 84Combined sources3
Beta strandi95 – 97Combined sources3
Turni98 – 100Combined sources3
Beta strandi101 – 104Combined sources4
Turni107 – 109Combined sources3
Beta strandi110 – 113Combined sources4
Beta strandi137 – 140Combined sources4
Beta strandi142 – 144Combined sources3
Beta strandi152 – 157Combined sources6
Helixi160 – 162Combined sources3
Turni163 – 165Combined sources3
Beta strandi168 – 174Combined sources7
Helixi176 – 183Combined sources8
Beta strandi193 – 195Combined sources3
Beta strandi197 – 212Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CYNX-ray1.85A39-216[»]
3ICHX-ray1.20A34-216[»]
3ICIX-ray1.70A/B34-216[»]
ProteinModelPortaliP23284.
SMRiP23284.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23284.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini47 – 204PPIase cyclophilin-typePROSITE-ProRule annotationAdd BLAST158

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi213 – 216Prevents secretion from ER4

Sequence similaritiesi

Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG0880. Eukaryota.
ENOG410Z0G4. LUCA.
GeneTreeiENSGT00760000119072.
HOGENOMiHOG000065981.
HOVERGENiHBG001065.
InParanoidiP23284.
KOiK03768.
OMAiSPAYANE.
OrthoDBiEOG091G0BGL.
PhylomeDBiP23284.
TreeFamiTF354259.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P23284-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRLSERNMK VLLAAALIAG SVFFLLLPGP SAADEKKKGP KVTVKVYFDL
60 70 80 90 100
RIGDEDVGRV IFGLFGKTVP KTVDNFVALA TGEKGFGYKN SKFHRVIKDF
110 120 130 140 150
MIQGGDFTRG DGTGGKSIYG ERFPDENFKL KHYGPGWVSM ANAGKDTNGS
160 170 180 190 200
QFFITTVKTA WLDGKHVVFG KVLEGMEVVR KVESTKTDSR DKPLKDVIIA
210
DCGKIEVEKP FAIAKE
Length:216
Mass (Da):23,743
Last modified:November 25, 2008 - v2
Checksum:i2D0410A07AA9E420
GO

Sequence cautioni

The sequence AAA52150 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti5S → R in AAA52150 (PubMed:2000394).Curated1
Sequence conflicti216E → D in CAG33110 (Ref. 3) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0634369M → R in OI9; patients have white sclerae, normal dentition, no rhizomelia or severe deformity of long bones. 1 PublicationCorresponds to variant rs137853864dbSNPEnsembl.1
Natural variantiVAR_04771160V → L.Corresponds to variant rs11558595dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63573 mRNA. Translation: AAA36601.1.
AK291149 mRNA. Translation: BAF83838.1.
CR456829 mRNA. Translation: CAG33110.1.
AY962310 Genomic DNA. Translation: AAX44050.1.
AC100840 Genomic DNA. No translation available.
CH471082 Genomic DNA. Translation: EAW77669.1.
BC001125 mRNA. Translation: AAH01125.1.
BC008848 mRNA. Translation: AAH08848.1.
BC020800 mRNA. Translation: AAH20800.1.
BC032138 mRNA. Translation: AAH32138.1.
M60857 mRNA. Translation: AAA52150.1. Different initiation.
M60457 mRNA. Translation: AAA35733.1.
CCDSiCCDS10191.1.
PIRiA39118. CSHUB.
RefSeqiNP_000933.1. NM_000942.4.
UniGeneiHs.434937.

Genome annotation databases

EnsembliENST00000300026; ENSP00000300026; ENSG00000166794.
GeneIDi5479.
KEGGihsa:5479.
UCSCiuc002and.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Osteogenesis imperfecta variant database

Peptidyl-prolyl cis-trans isomerase B (PPIB)

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63573 mRNA. Translation: AAA36601.1.
AK291149 mRNA. Translation: BAF83838.1.
CR456829 mRNA. Translation: CAG33110.1.
AY962310 Genomic DNA. Translation: AAX44050.1.
AC100840 Genomic DNA. No translation available.
CH471082 Genomic DNA. Translation: EAW77669.1.
BC001125 mRNA. Translation: AAH01125.1.
BC008848 mRNA. Translation: AAH08848.1.
BC020800 mRNA. Translation: AAH20800.1.
BC032138 mRNA. Translation: AAH32138.1.
M60857 mRNA. Translation: AAA52150.1. Different initiation.
M60457 mRNA. Translation: AAA35733.1.
CCDSiCCDS10191.1.
PIRiA39118. CSHUB.
RefSeqiNP_000933.1. NM_000942.4.
UniGeneiHs.434937.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CYNX-ray1.85A39-216[»]
3ICHX-ray1.20A34-216[»]
3ICIX-ray1.70A/B34-216[»]
ProteinModelPortaliP23284.
SMRiP23284.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111475. 90 interactors.
IntActiP23284. 32 interactors.
MINTiMINT-1142578.
STRINGi9606.ENSP00000300026.

Chemistry databases

BindingDBiP23284.
ChEMBLiCHEMBL2075.
DrugBankiDB00172. L-Proline.

PTM databases

iPTMnetiP23284.
PhosphoSitePlusiP23284.
SwissPalmiP23284.

Polymorphism and mutation databases

BioMutaiPPIB.
DMDMi215273869.

2D gel databases

OGPiP23284.
REPRODUCTION-2DPAGEIPI00646304.
SWISS-2DPAGEP23284.

Proteomic databases

EPDiP23284.
MaxQBiP23284.
PaxDbiP23284.
PeptideAtlasiP23284.
PRIDEiP23284.
TopDownProteomicsiP23284.

Protocols and materials databases

DNASUi5479.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000300026; ENSP00000300026; ENSG00000166794.
GeneIDi5479.
KEGGihsa:5479.
UCSCiuc002and.4. human.

Organism-specific databases

CTDi5479.
DisGeNETi5479.
GeneCardsiPPIB.
HGNCiHGNC:9255. PPIB.
HPAiCAB011487.
HPA012720.
MalaCardsiPPIB.
MIMi123841. gene.
259440. phenotype.
neXtProtiNX_P23284.
OpenTargetsiENSG00000166794.
Orphaneti216804. Osteogenesis imperfecta type 2.
216812. Osteogenesis imperfecta type 3.
216820. Osteogenesis imperfecta type 4.
PharmGKBiPA33580.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0880. Eukaryota.
ENOG410Z0G4. LUCA.
GeneTreeiENSGT00760000119072.
HOGENOMiHOG000065981.
HOVERGENiHBG001065.
InParanoidiP23284.
KOiK03768.
OMAiSPAYANE.
OrthoDBiEOG091G0BGL.
PhylomeDBiP23284.
TreeFamiTF354259.

Enzyme and pathway databases

BioCyciZFISH:HS09452-MONOMER.
BRENDAi5.2.1.8. 2681.
ReactomeiR-HSA-1650814. Collagen biosynthesis and modifying enzymes.

Miscellaneous databases

ChiTaRSiPPIB. human.
EvolutionaryTraceiP23284.
GeneWikiiPPIB.
GenomeRNAii5479.
PROiP23284.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000166794.
CleanExiHS_PPIB.
GenevisibleiP23284. HS.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPPIB_HUMAN
AccessioniPrimary (citable) accession number: P23284
Secondary accession number(s): A8K534, Q6IBH5, Q9BVK5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 25, 2008
Last modified: November 30, 2016
This is version 180 of the entry and version 2 of the sequence. [Complete history]
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.

Miscellaneousi

Caution

It is uncertain whether Met-1 or Met-9 is the initiator.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: 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
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.