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Protein

Peptidyl-prolyl cis-trans isomerase B

Gene

Ppib

Organism
Mus musculus (Mouse)
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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Keywords - Ligandi

Cyclosporin

Enzyme and pathway databases

ReactomeiR-MMU-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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:97750. Ppib.

Subcellular locationi

  • Endoplasmic reticulum lumen By similarity
  • Melanosome By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3333By similarityAdd
BLAST
Chaini34 – 216183Peptidyl-prolyl cis-trans isomerase BPRO_0000025480Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei209 – 2091N6-acetyllysine; alternateCombined sources
Modified residuei209 – 2091N6-succinyllysine; alternateCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP24369.
PaxDbiP24369.
PRIDEiP24369.
TopDownProteomicsiP24369.

PTM databases

iPTMnetiP24369.
PhosphoSiteiP24369.

Expressioni

Gene expression databases

BgeeiP24369.
CleanExiMM_PPIB.
ExpressionAtlasiP24369. baseline and differential.
GenevisibleiP24369. MM.

Interactioni

Subunit structurei

Interacts with DYM. Interacts with CALR, CANX and CLGN (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi202328. 2 interactions.
IntActiP24369. 8 interactions.
MINTiMINT-1853937.
STRINGi10090.ENSMUSP00000034947.

Structurei

3D structure databases

ProteinModelPortaliP24369.
SMRiP24369. Positions 37-216.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini47 – 204158PPIase cyclophilin-typePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi213 – 2164Prevents secretion from ERBy similarity

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG0880. Eukaryota.
ENOG410Z0G4. LUCA.
HOGENOMiHOG000065981.
HOVERGENiHBG001065.
InParanoidiP24369.
KOiK03768.
OMAiPSVANDK.
OrthoDBiEOG7RFTK4.
PhylomeDBiP24369.
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.

P24369-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRLSERNMK VLFAAALIVG SVVFLLLPGP SVANDKKKGP KVTVKVYFDL
60 70 80 90 100
QIGDESVGRV VFGLFGKTVP KTVDNFVALA TGEKGFGYKN SKFHRVIKDF
110 120 130 140 150
MIQGGDFTRG DGTGGKSIYG ERFPDENFKL KHYGPGWVSM ANAGKDTNGS
160 170 180 190 200
QFFITTVKTS WLDGKHVVFG KVLEGMDVVR KVESTKTDSR DKPLKDVIIV
210
DSGKIEVEKP FAIAKE
Length:216
Mass (Da):23,713
Last modified:November 25, 2008 - v2
Checksum:iCE9DAD1544AE72FE
GO

Sequence cautioni

The sequence AAA37498.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA41736.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60456 mRNA. Translation: AAA37498.1. Different initiation.
X58990 mRNA. Translation: CAA41736.1. Different initiation.
CCDSiCCDS23301.1.
RefSeqiNP_035279.2. NM_011149.2.
UniGeneiMm.335249.

Genome annotation databases

EnsembliENSMUST00000034947; ENSMUSP00000034947; ENSMUSG00000032383.
GeneIDi19035.
KEGGimmu:19035.
UCSCiuc009qei.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60456 mRNA. Translation: AAA37498.1. Different initiation.
X58990 mRNA. Translation: CAA41736.1. Different initiation.
CCDSiCCDS23301.1.
RefSeqiNP_035279.2. NM_011149.2.
UniGeneiMm.335249.

3D structure databases

ProteinModelPortaliP24369.
SMRiP24369. Positions 37-216.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202328. 2 interactions.
IntActiP24369. 8 interactions.
MINTiMINT-1853937.
STRINGi10090.ENSMUSP00000034947.

PTM databases

iPTMnetiP24369.
PhosphoSiteiP24369.

Proteomic databases

EPDiP24369.
PaxDbiP24369.
PRIDEiP24369.
TopDownProteomicsiP24369.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034947; ENSMUSP00000034947; ENSMUSG00000032383.
GeneIDi19035.
KEGGimmu:19035.
UCSCiuc009qei.1. mouse.

Organism-specific databases

CTDi5479.
MGIiMGI:97750. Ppib.

Phylogenomic databases

eggNOGiKOG0880. Eukaryota.
ENOG410Z0G4. LUCA.
HOGENOMiHOG000065981.
HOVERGENiHBG001065.
InParanoidiP24369.
KOiK03768.
OMAiPSVANDK.
OrthoDBiEOG7RFTK4.
PhylomeDBiP24369.
TreeFamiTF354259.

Enzyme and pathway databases

ReactomeiR-MMU-1650814. Collagen biosynthesis and modifying enzymes.

Miscellaneous databases

NextBioi295477.
PROiP24369.
SOURCEiSearch...

Gene expression databases

BgeeiP24369.
CleanExiMM_PPIB.
ExpressionAtlasiP24369. baseline and differential.
GenevisibleiP24369. MM.

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...

Publicationsi

« Hide 'large scale' publications
  1. "An endoplasmic reticulum-specific cyclophilin."
    Hasel K.W., Glass J.R., Godbout M., Sutcliffe J.G.
    Mol. Cell. Biol. 11:3484-3491(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Murine cyclophilin-S1: a variant peptidyl-prolyl isomerase with a putative signal sequence expressed in differentiating F9 cells."
    Schumacher A., Schroeter H., Multhaup G., Nordheim A.
    Biochim. Biophys. Acta 1129:13-22(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-209, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast and Liver.

Entry informationi

Entry nameiPPIB_MOUSE
AccessioniPrimary (citable) accession number: P24369
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: November 25, 2008
Last modified: May 11, 2016
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.