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Protein

Peptidyl-prolyl cis-trans isomerase FKBP1B

Gene

FKBP1B

Organism
Homo sapiens (Human)
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: BHF-UCL
  • cyclic nucleotide binding Source: Ensembl
  • FK506 binding Source: BHF-UCL
  • ion channel binding Source: BHF-UCL
  • peptidyl-prolyl cis-trans isomerase activity Source: BHF-UCL
  • receptor binding Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Enzyme and pathway databases

BioCyciZFISH:HS04340-MONOMER.
ReactomeiR-HSA-2672351. Stimuli-sensing channels.
R-HSA-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
FK506-binding protein 1B
Short name:
FKBP-1B
Immunophilin FKBP12.6
Rotamase
h-FKBP-12
Gene namesi
Name:FKBP1B
Synonyms:FKBP12.6, FKBP1L, FKBP9, OTK4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:3712. FKBP1B.

Subcellular locationi

GO - Cellular componenti

  • calcium channel complex Source: BHF-UCL
  • cytoplasm Source: BHF-UCL
  • cytosol Source: BHF-UCL
  • membrane Source: BHF-UCL
  • sarcoplasmic reticulum membrane Source: GO_Central
  • Z disc Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Sarcoplasmic reticulum

Pathology & Biotechi

Organism-specific databases

DisGeNETi2281.
OpenTargetsiENSG00000119782.
PharmGKBiPA28154.

Chemistry databases

ChEMBLiCHEMBL2430.

Polymorphism and mutation databases

BioMutaiFKBP1B.
DMDMi61224185.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000752952 – 108Peptidyl-prolyl cis-trans isomerase FKBP1BAdd BLAST107

Proteomic databases

EPDiP68106.
MaxQBiP68106.
PaxDbiP68106.
PeptideAtlasiP68106.
PRIDEiP68106.

PTM databases

PhosphoSitePlusiP68106.

Expressioni

Tissue specificityi

Detected in heart muscle (at protein level). Isoform 1 and isoform 2 are ubiquitous with highest levels in brain and thymus.1 Publication

Gene expression databases

BgeeiENSG00000119782.
CleanExiHS_FKBP1B.
HS_FKBP9.
ExpressionAtlasiP68106. baseline and differential.
GenevisibleiP68106. HS.

Organism-specific databases

HPAiHPA051798.

Interactioni

Subunit structurei

Identified in a complex composed of RYR2, FKBP1B, PKA catalytic subunit, PRKAR2A, AKAP6, and the protein phosphatases PP2A and PP1. Interacts directly with RYR2.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ADAMTSL4Q6UY14-33EBI-6693977,EBI-10173507
Calm3P621612EBI-6693977,EBI-397530From a different organism.
CAMK2DQ135573EBI-6693977,EBI-351018
FLJ13057Q53SE73EBI-6693977,EBI-10172181
KRT31Q153233EBI-6693977,EBI-948001
KRT40Q6A1623EBI-6693977,EBI-10171697
RELQ048643EBI-6693977,EBI-307352
RYR2Q927365EBI-6693977,EBI-1170425
TRIM69Q86WT63EBI-6693977,EBI-749955

GO - Molecular functioni

  • ion channel binding Source: BHF-UCL
  • receptor binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi108571. 28 interactors.
DIPiDIP-48796N.
IntActiP68106. 14 interactors.
STRINGi9606.ENSP00000370373.

Chemistry databases

BindingDBiP68106.

Structurei

Secondary structure

1108
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 9Combined sources7
Beta strandi22 – 31Combined sources10
Beta strandi36 – 40Combined sources5
Turni41 – 44Combined sources4
Beta strandi47 – 50Combined sources4
Turni51 – 54Combined sources4
Helixi58 – 64Combined sources7
Beta strandi72 – 77Combined sources6
Helixi79 – 81Combined sources3
Turni82 – 86Combined sources5
Beta strandi89 – 91Combined sources3
Beta strandi98 – 108Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1C9HX-ray2.00A2-108[»]
4C02X-ray2.17B1-108[»]
4IQ2X-ray1.70A/B2-108[»]
4IQCX-ray1.90A/B2-108[»]
5HKGX-ray1.50A2-108[»]
5T15electron microscopy3.80A/F/H/J1-108[»]
5T9Melectron microscopy3.80A/F/H/J1-108[»]
5T9Nelectron microscopy3.80A/F/H/J1-108[»]
5T9Relectron microscopy3.80A/F/H/J1-108[»]
5T9Selectron microscopy3.80A/F/H/J1-108[»]
5T9Velectron microscopy3.80A/F/H/J1-108[»]
5TA3electron microscopy3.80A/F/H/J1-108[»]
5TALelectron microscopy3.80A/F/H/J1-108[»]
5TAMelectron microscopy3.80A/F/H/J1-108[»]
5TANelectron microscopy3.80A/F/H/J1-108[»]
5TAPelectron microscopy3.80A/F/H/J1-108[»]
5TAQelectron microscopy3.80A/F/H/J1-108[»]
5TASelectron microscopy3.80A/F/H/J1-108[»]
5TATelectron microscopy3.80A/F/H/J1-108[»]
5TAUelectron microscopy3.80A/F/H/J1-108[»]
5TAVelectron microscopy3.80A/F/H/J1-108[»]
5TAWelectron microscopy3.80A/F/H/J1-108[»]
5TAXelectron microscopy3.80A/F/H/J1-108[»]
5TAYelectron microscopy3.80A/F/H/J1-108[»]
5TAZelectron microscopy3.80A/F/H/J1-108[»]
5TB0electron microscopy3.80A/B/D/F1-108[»]
5TB1electron microscopy3.80A/F/H/J1-108[»]
5TB2electron microscopy3.80A/F/H/J1-108[»]
5TB3electron microscopy3.80A/F/H/J1-108[»]
5TB4electron microscopy3.80A/F/H/J1-108[»]
ProteinModelPortaliP68106.
SMRiP68106.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP68106.

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.
HOGENOMiHOG000154887.
HOVERGENiHBG051623.
InParanoidiP68106.
KOiK09568.
OMAiERARLTC.
OrthoDBiEOG091G02W1.
PhylomeDBiP68106.
TreeFamiTF105291.

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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P68106-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

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

DVELLNLE
Length:108
Mass (Da):11,783
Last modified:January 23, 2007 - v2
Checksum:iBAC2A25945F63AC4
GO
Isoform 2 (identifier: P68106-2) [UniParc] [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     67-108: MSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE → LGPLSPLPICPHPC

Show »
Length:80
Mass (Da):8,802
Checksum:i99C0A9C743984BA2
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_00518467 – 108MSLGQ…LLNLE → LGPLSPLPICPHPC in isoform 2. 3 PublicationsAdd BLAST42

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S69815 mRNA. Translation: AAB30684.1.
D38037 mRNA. Translation: BAA07232.1.
L37086 mRNA. Translation: AAC37581.1.
S69800 mRNA. Translation: AAB30685.1.
AF322070 mRNA. Translation: AAK11191.1.
AB190793 Genomic DNA. Translation: BAE44300.1.
AC008073 Genomic DNA. Translation: AAY14663.1.
CH471053 Genomic DNA. Translation: EAX00769.1.
BC002614 mRNA. Translation: AAH02614.1.
CCDSiCCDS1706.1.
CCDS33153.1. [P68106-2]
PIRiJC2188.
RefSeqiNP_004107.1. NM_004116.4. [P68106-1]
NP_473374.1. NM_054033.3. [P68106-2]
UniGeneiHs.709461.

Genome annotation databases

EnsembliENST00000380986; ENSP00000370373; ENSG00000119782. [P68106-1]
ENST00000380991; ENSP00000370379; ENSG00000119782. [P68106-2]
GeneIDi2281.
KEGGihsa:2281.
UCSCiuc002rer.4. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S69815 mRNA. Translation: AAB30684.1.
D38037 mRNA. Translation: BAA07232.1.
L37086 mRNA. Translation: AAC37581.1.
S69800 mRNA. Translation: AAB30685.1.
AF322070 mRNA. Translation: AAK11191.1.
AB190793 Genomic DNA. Translation: BAE44300.1.
AC008073 Genomic DNA. Translation: AAY14663.1.
CH471053 Genomic DNA. Translation: EAX00769.1.
BC002614 mRNA. Translation: AAH02614.1.
CCDSiCCDS1706.1.
CCDS33153.1. [P68106-2]
PIRiJC2188.
RefSeqiNP_004107.1. NM_004116.4. [P68106-1]
NP_473374.1. NM_054033.3. [P68106-2]
UniGeneiHs.709461.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1C9HX-ray2.00A2-108[»]
4C02X-ray2.17B1-108[»]
4IQ2X-ray1.70A/B2-108[»]
4IQCX-ray1.90A/B2-108[»]
5HKGX-ray1.50A2-108[»]
5T15electron microscopy3.80A/F/H/J1-108[»]
5T9Melectron microscopy3.80A/F/H/J1-108[»]
5T9Nelectron microscopy3.80A/F/H/J1-108[»]
5T9Relectron microscopy3.80A/F/H/J1-108[»]
5T9Selectron microscopy3.80A/F/H/J1-108[»]
5T9Velectron microscopy3.80A/F/H/J1-108[»]
5TA3electron microscopy3.80A/F/H/J1-108[»]
5TALelectron microscopy3.80A/F/H/J1-108[»]
5TAMelectron microscopy3.80A/F/H/J1-108[»]
5TANelectron microscopy3.80A/F/H/J1-108[»]
5TAPelectron microscopy3.80A/F/H/J1-108[»]
5TAQelectron microscopy3.80A/F/H/J1-108[»]
5TASelectron microscopy3.80A/F/H/J1-108[»]
5TATelectron microscopy3.80A/F/H/J1-108[»]
5TAUelectron microscopy3.80A/F/H/J1-108[»]
5TAVelectron microscopy3.80A/F/H/J1-108[»]
5TAWelectron microscopy3.80A/F/H/J1-108[»]
5TAXelectron microscopy3.80A/F/H/J1-108[»]
5TAYelectron microscopy3.80A/F/H/J1-108[»]
5TAZelectron microscopy3.80A/F/H/J1-108[»]
5TB0electron microscopy3.80A/B/D/F1-108[»]
5TB1electron microscopy3.80A/F/H/J1-108[»]
5TB2electron microscopy3.80A/F/H/J1-108[»]
5TB3electron microscopy3.80A/F/H/J1-108[»]
5TB4electron microscopy3.80A/F/H/J1-108[»]
ProteinModelPortaliP68106.
SMRiP68106.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108571. 28 interactors.
DIPiDIP-48796N.
IntActiP68106. 14 interactors.
STRINGi9606.ENSP00000370373.

Chemistry databases

BindingDBiP68106.
ChEMBLiCHEMBL2430.

PTM databases

PhosphoSitePlusiP68106.

Polymorphism and mutation databases

BioMutaiFKBP1B.
DMDMi61224185.

Proteomic databases

EPDiP68106.
MaxQBiP68106.
PaxDbiP68106.
PeptideAtlasiP68106.
PRIDEiP68106.

Protocols and materials databases

DNASUi2281.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000380986; ENSP00000370373; ENSG00000119782. [P68106-1]
ENST00000380991; ENSP00000370379; ENSG00000119782. [P68106-2]
GeneIDi2281.
KEGGihsa:2281.
UCSCiuc002rer.4. human.

Organism-specific databases

CTDi2281.
DisGeNETi2281.
GeneCardsiFKBP1B.
HGNCiHGNC:3712. FKBP1B.
HPAiHPA051798.
MIMi600620. gene.
neXtProtiNX_P68106.
OpenTargetsiENSG00000119782.
PharmGKBiPA28154.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0544. Eukaryota.
COG0545. LUCA.
GeneTreeiENSGT00760000119159.
HOGENOMiHOG000154887.
HOVERGENiHBG051623.
InParanoidiP68106.
KOiK09568.
OMAiERARLTC.
OrthoDBiEOG091G02W1.
PhylomeDBiP68106.
TreeFamiTF105291.

Enzyme and pathway databases

BioCyciZFISH:HS04340-MONOMER.
ReactomeiR-HSA-2672351. Stimuli-sensing channels.
R-HSA-5578775. Ion homeostasis.

Miscellaneous databases

EvolutionaryTraceiP68106.
GeneWikiiFKBP1B.
GenomeRNAii2281.
PROiP68106.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000119782.
CleanExiHS_FKBP1B.
HS_FKBP9.
ExpressionAtlasiP68106. baseline and differential.
GenevisibleiP68106. HS.

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_HUMAN
AccessioniPrimary (citable) accession number: P68106
Secondary accession number(s): Q13664
, Q16645, Q53TM2, Q9BQ40
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2004
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 130 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.