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P68106 (FKB1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase FKBP1B

Short name=PPIase FKBP1B
EC=5.2.1.8
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 names
Name:FKBP1B
Synonyms:FKBP12.6, FKBP1L, FKBP9, OTK4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length108 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Enzyme regulation

Inhibited by both FK506 and rapamycin.

Subunit structure

Identified in a complex composed of RYR2, FKBP1B, PKA catalytic subunit, PRKAR2A, AKAP6, and the protein phosphatases PP2A and PP1. Interacts directly with RYR2. Ref.8

Subcellular location

Cytoplasm By similarity. Sarcoplasmic reticulum By similarity.

Tissue specificity

Detected in heart muscle (at protein level). Isoform 1 and isoform 2 are ubiquitous with highest levels in brain and thymus. Ref.8

Sequence similarities

Belongs to the FKBP-type PPIase family. FKBP1 subfamily.

Contains 1 PPIase FKBP-type domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Sarcoplasmic reticulum
   Coding sequence diversityAlternative splicing
   Molecular functionIsomerase
Rotamase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process'de novo' protein folding

Traceable author statement PubMed 11322937. Source: BHF-UCL

T cell proliferation

Inferred from electronic annotation. Source: Ensembl

calcium ion transmembrane transport

Traceable author statement PubMed 11322937. Source: GOC

calcium-mediated signaling using intracellular calcium source

Traceable author statement PubMed 22087651. Source: BHF-UCL

cell communication by electrical coupling involved in cardiac conduction

Traceable author statement PubMed 22087651. Source: BHF-UCL

cytosolic calcium ion homeostasis

Inferred from direct assay PubMed 20431056. Source: BHF-UCL

insulin secretion

Inferred from electronic annotation. Source: Ensembl

negative regulation of heart rate

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of insulin secretion involved in cellular response to glucose stimulus

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein phosphatase type 2B activity

Inferred from direct assay Ref.2. Source: BHF-UCL

negative regulation of release of sequestered calcium ion into cytosol

Inferred from direct assay PubMed 12443530. Source: BHF-UCL

negative regulation of ryanodine-sensitive calcium-release channel activity

Inferred from direct assay PubMed 12443530. Source: BHF-UCL

neuronal action potential propagation

Inferred from electronic annotation. Source: Ensembl

peptidyl-proline modification

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of axon regeneration

Inferred from electronic annotation. Source: Ensembl

positive regulation of sequestering of calcium ion

Inferred from direct assay PubMed 12443530. Source: BHF-UCL

protein maturation by protein folding

Traceable author statement PubMed 11322937. Source: BHF-UCL

protein peptidyl-prolyl isomerization

Inferred from direct assay Ref.2. Source: BHF-UCL

protein refolding

Traceable author statement PubMed 11322937. Source: BHF-UCL

regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum

Inferred from direct assay PubMed 20431056. Source: BHF-UCL

regulation of ryanodine-sensitive calcium-release channel activity

Inferred from direct assay PubMed 20431056. Source: BHF-UCL

release of sequestered calcium ion into cytosol by sarcoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

response to glucose

Inferred from electronic annotation. Source: Ensembl

response to hydrogen peroxide

Inferred from electronic annotation. Source: Ensembl

response to redox state

Inferred from direct assay PubMed 19226252. Source: BHF-UCL

response to vitamin E

Inferred from electronic annotation. Source: Ensembl

smooth muscle contraction

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentZ disc

Inferred from direct assay PubMed 20431056. Source: BHF-UCL

calcium channel complex

Inferred from direct assay Ref.8. Source: BHF-UCL

cytoplasm

Inferred from direct assay PubMed 12443530. Source: BHF-UCL

cytosol

Inferred by curator Ref.2. Source: BHF-UCL

membrane

Inferred from direct assay PubMed 12443530. Source: BHF-UCL

sarcoplasmic reticulum membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionFK506 binding

Inferred from direct assay Ref.2. Source: BHF-UCL

calcium channel inhibitor activity

Inferred from direct assay PubMed 12443530PubMed 20431056. Source: BHF-UCL

cyclic nucleotide binding

Inferred from electronic annotation. Source: Ensembl

ion channel binding

Inferred from sequence or structural similarity. Source: BHF-UCL

peptidyl-prolyl cis-trans isomerase activity

Inferred from direct assay Ref.2Ref.1. Source: BHF-UCL

receptor binding

Inferred from physical interaction Ref.8PubMed 17921453. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RYR2Q927362EBI-6693977,EBI-1170425

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P68106-1)

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.
Isoform 2 (identifier: P68106-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 108107Peptidyl-prolyl cis-trans isomerase FKBP1B
PRO_0000075295

Regions

Domain20 – 10889PPIase FKBP-type

Natural variations

Alternative sequence67 – 10842MSLGQ…LLNLE → LGPLSPLPICPHPC in isoform 2.
VSP_005184

Secondary structure

..................... 108
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: BAC2A25945F63AC4

FASTA10811,783
        10         20         30         40         50         60 
MGVEIETISP GDGRTFPKKG QTCVVHYTGM LQNGKKFDSS RDRNKPFKFR IGKQEVIKGF 

        70         80         90        100 
EEGAAQMSLG QRAKLTCTPD VAYGATGHPG VIPPNATLIF DVELLNLE 

« Hide

Isoform 2 [UniParc] [UniParc].

Checksum: 99C0A9C743984BA2
Show »

FASTA808,802

References

« Hide 'large scale' references
[1]"Molecular cloning and expression of a novel human gene that is highly homologous to human FK506-binding protein 12kDa (hFKBP-12) and characterization of two alternatively spliced transcripts."
Arakawa H., Nagase H., Hayashi N., Fujiwara T., Ogawa M., Shin S., Nakamura Y.
Biochem. Biophys. Res. Commun. 200:836-843(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Tissue: Fetal brain.
[2]"A novel FK506 binding protein can mediate the immunosuppressive effects of FK506 and is associated with the cardiac ryanodine receptor."
Lam E., Martin M.M., Timerman A.P., Sabers C., Fleischer S., Lukas T., Abraham R.T., O'Keefe S.J., O'Neill E.A., Wiederrecht G.J.
J. Biol. Chem. 270:26511-26522(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain and Heart muscle.
[3]"FKBP9: an alternative splice variant of the FK506-binding protein FKBP12.6 expressed in the human heart."
Seidler T., Kussebi N., Prestle J.
Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[4]"Genomic organization, chromosomal localization, and promoter of human gene for FK506-binding protein 12.6."
Nakazawa T., Takasawa S., Noguchi N., Nata K., Tohgo A., Mori M., Nakagawara K., Akiyama T., Ikeda T., Yamauchi A., Takahashi I., Yoshikawa T., Okamoto H.
Gene 360:55-64(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[8]"PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): defective regulation in failing hearts."
Marx S.O., Reiken S., Hisamatsu Y., Jayaraman T., Burkhoff D., Rosemblit N., Marks A.R.
Cell 101:365-376(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH RYR2; PP1; PP2A AKAP6 AND PKA, INTERACTION WITH RYR2, TISSUE SPECIFICITY.
[9]"Structure of FKBP12.6 in complex with rapamycin."
Deivanayagam C.C., Carson M., Thotakura A., Narayana S.V., Chodavarapu R.S.
Acta Crystallogr. D 56:266-271(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRJC2188.
RefSeqNP_004107.1. NM_004116.3.
NP_473374.1. NM_054033.2.
UniGeneHs.709461.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1C9HX-ray2.00A2-108[»]
4C02X-ray2.17B1-108[»]
4IQ2X-ray1.70A/B2-108[»]
4IQCX-ray1.90A/B2-108[»]
ProteinModelPortalP68106.
SMRP68106. Positions 2-108.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108571. 2 interactions.
DIPDIP-48796N.
IntActP68106. 4 interactions.
STRING9606.ENSP00000370373.

Chemistry

BindingDBP68106.
ChEMBLCHEMBL2430.

PTM databases

PhosphoSiteP68106.

Polymorphism databases

DMDM61224185.

Proteomic databases

PaxDbP68106.
PRIDEP68106.

Protocols and materials databases

DNASU2281.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000380986; ENSP00000370373; ENSG00000119782. [P68106-1]
ENST00000380991; ENSP00000370379; ENSG00000119782. [P68106-2]
GeneID2281.
KEGGhsa:2281.
UCSCuc002rer.3. human.
uc002res.3. human. [P68106-2]

Organism-specific databases

CTD2281.
GeneCardsGC02P024272.
HGNCHGNC:3712. FKBP1B.
HPAHPA051798.
MIM600620. gene.
neXtProtNX_P68106.
PharmGKBPA28154.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0545.
HOGENOMHOG000154887.
HOVERGENHBG051623.
InParanoidP68106.
KOK09568.
OMAQLAYGEK.
OrthoDBEOG7ZGX5T.
PhylomeDBP68106.
TreeFamTF105291.

Gene expression databases

BgeeP68106.
CleanExHS_FKBP1B.
HS_FKBP9.
GenevestigatorP68106.

Family and domain databases

InterProIPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view]
PANTHERPTHR10516. PTHR10516. 1 hit.
PfamPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP68106.
GeneWikiFKBP1B.
GenomeRNAi2281.
NextBio9275.
PROP68106.
SOURCESearch...

Entry information

Entry nameFKB1B_HUMAN
AccessionPrimary (citable) accession number: P68106
Secondary accession number(s): Q13664 expand/collapse secondary AC list , Q16645, Q53TM2, Q9BQ40
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2004
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM