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Protein

Peptidyl-prolyl cis-trans isomerase FKBP1B

Gene

Fkbp1b

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Has the potential to contribute to the immunosuppressive and toxic effects of FK506 and rapamycin. 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

Inhibited by both FK506 and rapamycin.

GO - Molecular functioni

  • calcium channel inhibitor activity Source: Ensembl
  • cyclic nucleotide binding Source: RGD
  • FK506 binding Source: RGD
  • peptidyl-prolyl cis-trans isomerase activity Source: GO_Central

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Enzyme and pathway databases

ReactomeiR-RNO-2672351. Stimuli-sensing channels.
R-RNO-5578775. Ion homeostasis.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase FKBP1B (EC:5.2.1.8)
Short name:
PPIase FKBP1B
Alternative name(s):
12.6 kDa FK506-binding protein
Short name:
12.6 kDa FKBP
Short name:
FKBP-12.6
Calstabin-2
FK506-binding protein 1B
Short name:
FKBP-1B
Immunophilin FKBP12.6
Rotamase
Gene namesi
Name:Fkbp1b
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 6

Organism-specific databases

RGDi61835. Fkbp1b.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Sarcoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000752982 – 108Peptidyl-prolyl cis-trans isomerase FKBP1BAdd BLAST107

Proteomic databases

PaxDbiP97534.
PRIDEiP97534.

PTM databases

iPTMnetiP97534.
PhosphoSitePlusiP97534.

Expressioni

Tissue specificityi

Detected in heart muscle (at protein level). Ubiquitous.1 Publication

Gene expression databases

BgeeiENSRNOG00000047143.
GenevisibleiP97534. RN.

Interactioni

Subunit structurei

Identified in a complex composed of RYR2, FKBP1B, PKA catalytic subunit, PRKAR2A, AKAP6, and the protein phosphatases PP2A and PP1 (By similarity). Interacts directly with RYR2.By similarity1 Publication

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000067023.

Structurei

3D structure databases

ProteinModelPortaliP97534.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini20 – 108PPIase FKBP-typePROSITE-ProRule annotationAdd BLAST89

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0544. Eukaryota.
COG0545. LUCA.
GeneTreeiENSGT00760000119159.
HOVERGENiHBG051623.
InParanoidiP97534.
KOiK09568.
OMAiERARLTC.
OrthoDBiEOG091G02W1.
PhylomeDBiP97534.

Family and domain databases

InterProiIPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view]
PANTHERiPTHR10516. PTHR10516. 1 hit.
PfamiPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEiPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P97534-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGVEIETISP GDGRTFPKKG QICVVHYTGM LQNGKKFDSS RDRNKPFKFR
60 70 80 90 100
IGKQEVIKGF EEGAAQMSLG QRAKLTCTPD VAYGATGHPG VIPPNATLIF

DVELLNLE
Length:108
Mass (Da):11,795
Last modified:January 23, 2007 - v3
Checksum:i36136F4588F62F0B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86642 mRNA. Translation: BAA13154.1.
RefSeqiNP_073166.1. NM_022675.1.
UniGeneiRn.46439.

Genome annotation databases

EnsembliENSRNOT00000071784; ENSRNOP00000067023; ENSRNOG00000047143.
GeneIDi58950.
KEGGirno:58950.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86642 mRNA. Translation: BAA13154.1.
RefSeqiNP_073166.1. NM_022675.1.
UniGeneiRn.46439.

3D structure databases

ProteinModelPortaliP97534.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000067023.

PTM databases

iPTMnetiP97534.
PhosphoSitePlusiP97534.

Proteomic databases

PaxDbiP97534.
PRIDEiP97534.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000071784; ENSRNOP00000067023; ENSRNOG00000047143.
GeneIDi58950.
KEGGirno:58950.

Organism-specific databases

CTDi2281.
RGDi61835. Fkbp1b.

Phylogenomic databases

eggNOGiKOG0544. Eukaryota.
COG0545. LUCA.
GeneTreeiENSGT00760000119159.
HOVERGENiHBG051623.
InParanoidiP97534.
KOiK09568.
OMAiERARLTC.
OrthoDBiEOG091G02W1.
PhylomeDBiP97534.

Enzyme and pathway databases

ReactomeiR-RNO-2672351. Stimuli-sensing channels.
R-RNO-5578775. Ion homeostasis.

Miscellaneous databases

PROiP97534.

Gene expression databases

BgeeiENSRNOG00000047143.
GenevisibleiP97534. RN.

Family and domain databases

InterProiIPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view]
PANTHERiPTHR10516. PTHR10516. 1 hit.
PfamiPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEiPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFKB1B_RAT
AccessioniPrimary (citable) accession number: P97534
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 109 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Has been suggested to play a role in the regulation of RYR2 channel activity and thereby contribute to the regulation of excitation-contraction coupling in cardiac muscle. According to PubMed:20431056, the amount of FKBP1B in rat heart is much lower than that of RYR2, suggesting that FKBP1B can play only a minor role in the regulation of RYR2 channel activity.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.