FKB1B_HUMAN
ID FKB1B_HUMAN Reviewed; 108 AA.
AC P68106; Q13664; Q16645; Q53TM2; Q9BQ40;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP1B {ECO:0000305};
DE Short=PPIase FKBP1B;
DE EC=5.2.1.8 {ECO:0000269|PubMed:7513996, ECO:0000269|PubMed:7592869};
DE AltName: Full=12.6 kDa FK506-binding protein;
DE Short=12.6 kDa FKBP;
DE Short=FKBP-12.6;
DE AltName: Full=FK506-binding protein 1B;
DE Short=FKBP-1B;
DE AltName: Full=Immunophilin FKBP12.6;
DE AltName: Full=Rotamase;
DE AltName: Full=h-FKBP-12;
GN Name=FKBP1B {ECO:0000312|HGNC:HGNC:3712};
GN Synonyms=FKBP12.6, FKBP1L, FKBP9, OTK4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND CATALYTIC
RP ACTIVITY.
RC TISSUE=Fetal brain;
RX PubMed=7513996; DOI=10.1006/bbrc.1994.1527;
RA Arakawa H., Nagase H., Hayashi N., Fujiwara T., Ogawa M., Shin S.,
RA Nakamura Y.;
RT "Molecular cloning and expression of a novel human gene that is highly
RT homologous to human FK506-binding protein 12kDa (hFKBP-12) and
RT characterization of two alternatively spliced transcripts.";
RL Biochem. Biophys. Res. Commun. 200:836-843(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND CATALYTIC ACTIVITY.
RC TISSUE=Brain, and Heart muscle;
RX PubMed=7592869; DOI=10.1074/jbc.270.44.26511;
RA Lam E., Martin M.M., Timerman A.P., Sabers C., Fleischer S., Lukas T.,
RA Abraham R.T., O'Keefe S.J., O'Neill E.A., Wiederrecht G.J.;
RT "A novel FK506 binding protein can mediate the immunosuppressive effects of
RT FK506 and is associated with the cardiac ryanodine receptor.";
RL J. Biol. Chem. 270:26511-26522(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Seidler T., Kussebi N., Prestle J.;
RT "FKBP9: an alternative splice variant of the FK506-binding protein FKBP12.6
RT expressed in the human heart.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16122887; DOI=10.1016/j.gene.2005.07.004;
RA Nakazawa T., Takasawa S., Noguchi N., Nata K., Tohgo A., Mori M.,
RA Nakagawara K., Akiyama T., Ikeda T., Yamauchi A., Takahashi I.,
RA Yoshikawa T., Okamoto H.;
RT "Genomic organization, chromosomal localization, and promoter of human gene
RT for FK506-binding protein 12.6.";
RL Gene 360:55-64(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP IDENTIFICATION IN A COMPLEX WITH RYR2; PP1; PP2A AKAP6 AND PKA, INTERACTION
RP WITH RYR2, AND TISSUE SPECIFICITY.
RX PubMed=10830164; DOI=10.1016/s0092-8674(00)80847-8;
RA Marx S.O., Reiken S., Hisamatsu Y., Jayaraman T., Burkhoff D.,
RA Rosemblit N., Marks A.R.;
RT "PKA phosphorylation dissociates FKBP12.6 from the calcium release channel
RT (ryanodine receptor): defective regulation in failing hearts.";
RL Cell 101:365-376(2000).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=10713512; DOI=10.1107/s0907444999016571;
RA Deivanayagam C.C., Carson M., Thotakura A., Narayana S.V.,
RA Chodavarapu R.S.;
RT "Structure of FKBP12.6 in complex with rapamycin.";
RL Acta Crystallogr. D 56:266-271(2000).
CC -!- FUNCTION: Has the potential to contribute to the immunosuppressive and
CC toxic effects of FK506 and rapamycin. PPIases accelerate the folding of
CC proteins. It catalyzes the cis-trans isomerization of proline imidic
CC peptide bonds in oligopeptides. {ECO:0000269|PubMed:7513996,
CC ECO:0000269|PubMed:7592869}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence={ECO:0000269|PubMed:7513996,
CC ECO:0000269|PubMed:7592869};
CC -!- ACTIVITY REGULATION: Inhibited by both FK506 and rapamycin.
CC -!- SUBUNIT: Identified in a complex composed of RYR2, FKBP1B, PKA
CC catalytic subunit, PRKAR2A, AKAP6, and the protein phosphatases PP2A
CC and PP1. Interacts directly with RYR2. {ECO:0000269|PubMed:10830164}.
CC -!- INTERACTION:
CC P68106; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-6693977, EBI-10173507;
CC P68106; Q13557: CAMK2D; NbExp=3; IntAct=EBI-6693977, EBI-351018;
CC P68106; Q53SE7: FLJ13057; NbExp=3; IntAct=EBI-6693977, EBI-10172181;
CC P68106; Q15323: KRT31; NbExp=3; IntAct=EBI-6693977, EBI-948001;
CC P68106; Q6A162: KRT40; NbExp=3; IntAct=EBI-6693977, EBI-10171697;
CC P68106; Q04864: REL; NbExp=3; IntAct=EBI-6693977, EBI-307352;
CC P68106; Q92736: RYR2; NbExp=5; IntAct=EBI-6693977, EBI-1170425;
CC P68106; Q86WT6: TRIM69; NbExp=3; IntAct=EBI-6693977, EBI-749955;
CC P68106-1; P62161: Calm3; Xeno; NbExp=2; IntAct=EBI-15766566, EBI-397530;
CC P68106-1; P11716: RYR1; Xeno; NbExp=2; IntAct=EBI-15766566, EBI-6477441;
CC P68106-2; Q15323: KRT31; NbExp=3; IntAct=EBI-11998976, EBI-948001;
CC P68106-2; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-11998976, EBI-11959885;
CC P68106-2; Q04864-2: REL; NbExp=3; IntAct=EBI-11998976, EBI-10829018;
CC P68106-2; Q86WT6-2: TRIM69; NbExp=3; IntAct=EBI-11998976, EBI-11525489;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Sarcoplasmic reticulum
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P68106-1, Q16645-1;
CC Sequence=Displayed;
CC Name=2;
CC IsoId=P68106-2, Q16645-2;
CC Sequence=VSP_005184;
CC -!- TISSUE SPECIFICITY: Detected in heart muscle (at protein level).
CC Isoform 1 and isoform 2 are ubiquitous with highest levels in brain and
CC thymus. {ECO:0000269|PubMed:10830164}.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP1 subfamily.
CC {ECO:0000305}.
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DR EMBL; S69815; AAB30684.1; -; mRNA.
DR EMBL; D38037; BAA07232.1; -; mRNA.
DR EMBL; L37086; AAC37581.1; -; mRNA.
DR EMBL; S69800; AAB30685.1; -; mRNA.
DR EMBL; AF322070; AAK11191.1; -; mRNA.
DR EMBL; AB190793; BAE44300.1; -; Genomic_DNA.
DR EMBL; AC008073; AAY14663.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00769.1; -; Genomic_DNA.
DR EMBL; BC002614; AAH02614.1; -; mRNA.
DR CCDS; CCDS1706.1; -.
DR CCDS; CCDS33153.1; -. [P68106-2]
DR PIR; JC2188; JC2188.
DR RefSeq; NP_004107.1; NM_004116.4. [P68106-1]
DR RefSeq; NP_473374.1; NM_054033.3. [P68106-2]
DR PDB; 1C9H; X-ray; 2.00 A; A=2-108.
DR PDB; 4C02; X-ray; 2.17 A; B=1-108.
DR PDB; 4IQ2; X-ray; 1.70 A; A/B=2-108.
DR PDB; 4IQC; X-ray; 1.90 A; A/B=2-108.
DR PDB; 5HKG; X-ray; 1.50 A; A=2-108.
DR PDB; 5L1D; EM; 10.50 A; B/D/F/H=2-108.
DR PDB; 5T15; EM; 3.80 A; A/F/H/J=1-108.
DR PDB; 5T9M; EM; 3.80 A; A/F/H/J=1-108.
DR PDB; 5T9N; EM; 3.80 A; A/F/H/J=1-108.
DR PDB; 5T9R; EM; 3.80 A; A/F/H/J=1-108.
DR PDB; 5T9S; EM; 3.80 A; A/F/H/J=1-108.
DR PDB; 5T9V; EM; 3.80 A; A/F/H/J=1-108.
DR PDB; 5TA3; EM; 3.80 A; A/F/H/J=1-108.
DR PDB; 5TAL; EM; 3.80 A; A/F/H/J=1-108.
DR PDB; 5TAM; EM; 3.80 A; A/F/H/J=1-108.
DR PDB; 5TAN; EM; 3.80 A; A/F/H/J=1-108.
DR PDB; 5TAP; EM; 3.80 A; A/F/H/J=1-108.
DR PDB; 5TAQ; EM; 3.80 A; A/F/H/J=1-108.
DR PDB; 5TAS; EM; 3.80 A; A/F/H/J=1-108.
DR PDB; 5TAT; EM; 3.80 A; A/F/H/J=1-108.
DR PDB; 5TAU; EM; 3.80 A; A/F/H/J=1-108.
DR PDB; 5TAV; EM; 3.80 A; A/F/H/J=1-108.
DR PDB; 5TAW; EM; 3.80 A; A/F/H/J=1-108.
DR PDB; 5TAX; EM; 3.80 A; A/F/H/J=1-108.
DR PDB; 5TAY; EM; 3.80 A; A/F/H/J=1-108.
DR PDB; 5TAZ; EM; 3.80 A; A/F/H/J=1-108.
DR PDB; 5TB0; EM; 4.40 A; A/F/H/J=1-108.
DR PDB; 5TB1; EM; 3.80 A; A/F/H/J=1-108.
DR PDB; 5TB2; EM; 3.80 A; A/F/H/J=1-108.
DR PDB; 5TB3; EM; 3.80 A; A/F/H/J=1-108.
DR PDB; 5TB4; EM; 3.80 A; A/F/H/J=1-108.
DR PDB; 6JGZ; EM; 4.60 A; A/C/E/G=1-108.
DR PDB; 6JH6; EM; 4.80 A; A/C/E/G=1-108.
DR PDB; 6JHN; EM; 4.50 A; B/D/F/H=1-108.
DR PDB; 6JI0; EM; 4.20 A; B/D/F/H=1-108.
DR PDB; 6JI8; EM; 3.60 A; B/E/H/K=1-108.
DR PDB; 6JII; EM; 4.20 A; A/D/G/J=1-108.
DR PDB; 6JIU; EM; 4.20 A; B/E/H/K=1-108.
DR PDB; 6JIY; EM; 3.90 A; B/E/H/K=1-108.
DR PDB; 6JRR; EM; 3.90 A; B/D/F/H=1-108.
DR PDB; 6JRS; EM; 3.70 A; B/E/H/K=1-108.
DR PDB; 6M2W; EM; 3.80 A; B/E/H/K=2-108.
DR PDB; 6PV6; EM; 4.50 A; A/F/H/J=1-108.
DR PDB; 6W1N; EM; 4.00 A; A/C/E/G=2-108.
DR PDB; 6WOT; EM; 3.54 A; E/F/G/H=2-108.
DR PDB; 6WOU; EM; 3.27 A; E/F/G/H=2-108.
DR PDB; 6WOV; EM; 5.10 A; E/F/G/H=2-108.
DR PDB; 6X32; EM; 3.80 A; A/D/G/J=2-108.
DR PDB; 6X33; EM; 4.20 A; A/D/G/J=2-108.
DR PDB; 6X34; EM; 4.70 A; A/C/E/G=2-107.
DR PDB; 6X35; EM; 4.20 A; A/D/G/J=2-108.
DR PDB; 6X36; EM; 4.70 A; A/D/G/J=2-108.
DR PDB; 7CF9; EM; 4.70 A; B/D/F/H=2-108.
DR PDB; 7JMF; EM; 4.50 A; A/F/H/J=1-108.
DR PDB; 7JMG; EM; 4.50 A; A/F/H/J=2-108.
DR PDB; 7JMH; EM; 4.50 A; A/F/H/J=2-108.
DR PDB; 7JMI; EM; 4.50 A; A/F/H/J=2-108.
DR PDB; 7JMJ; EM; 4.50 A; A/F/H/J=2-108.
DR PDB; 7M6A; EM; 3.36 A; F/H/J/O=1-108.
DR PDB; 7M6L; EM; 3.98 A; F/H/J/O=1-108.
DR PDBsum; 1C9H; -.
DR PDBsum; 4C02; -.
DR PDBsum; 4IQ2; -.
DR PDBsum; 4IQC; -.
DR PDBsum; 5HKG; -.
DR PDBsum; 5L1D; -.
DR PDBsum; 5T15; -.
DR PDBsum; 5T9M; -.
DR PDBsum; 5T9N; -.
DR PDBsum; 5T9R; -.
DR PDBsum; 5T9S; -.
DR PDBsum; 5T9V; -.
DR PDBsum; 5TA3; -.
DR PDBsum; 5TAL; -.
DR PDBsum; 5TAM; -.
DR PDBsum; 5TAN; -.
DR PDBsum; 5TAP; -.
DR PDBsum; 5TAQ; -.
DR PDBsum; 5TAS; -.
DR PDBsum; 5TAT; -.
DR PDBsum; 5TAU; -.
DR PDBsum; 5TAV; -.
DR PDBsum; 5TAW; -.
DR PDBsum; 5TAX; -.
DR PDBsum; 5TAY; -.
DR PDBsum; 5TAZ; -.
DR PDBsum; 5TB0; -.
DR PDBsum; 5TB1; -.
DR PDBsum; 5TB2; -.
DR PDBsum; 5TB3; -.
DR PDBsum; 5TB4; -.
DR PDBsum; 6JGZ; -.
DR PDBsum; 6JH6; -.
DR PDBsum; 6JHN; -.
DR PDBsum; 6JI0; -.
DR PDBsum; 6JI8; -.
DR PDBsum; 6JII; -.
DR PDBsum; 6JIU; -.
DR PDBsum; 6JIY; -.
DR PDBsum; 6JRR; -.
DR PDBsum; 6JRS; -.
DR PDBsum; 6M2W; -.
DR PDBsum; 6PV6; -.
DR PDBsum; 6W1N; -.
DR PDBsum; 6WOT; -.
DR PDBsum; 6WOU; -.
DR PDBsum; 6WOV; -.
DR PDBsum; 6X32; -.
DR PDBsum; 6X33; -.
DR PDBsum; 6X34; -.
DR PDBsum; 6X35; -.
DR PDBsum; 6X36; -.
DR PDBsum; 7CF9; -.
DR PDBsum; 7JMF; -.
DR PDBsum; 7JMG; -.
DR PDBsum; 7JMH; -.
DR PDBsum; 7JMI; -.
DR PDBsum; 7JMJ; -.
DR PDBsum; 7M6A; -.
DR PDBsum; 7M6L; -.
DR AlphaFoldDB; P68106; -.
DR BMRB; P68106; -.
DR SMR; P68106; -.
DR BioGRID; 108571; 32.
DR DIP; DIP-48796N; -.
DR IntAct; P68106; 13.
DR STRING; 9606.ENSP00000370373; -.
DR BindingDB; P68106; -.
DR ChEMBL; CHEMBL2430; -.
DR DrugCentral; P68106; -.
DR iPTMnet; P68106; -.
DR PhosphoSitePlus; P68106; -.
DR BioMuta; FKBP1B; -.
DR DMDM; 61224185; -.
DR EPD; P68106; -.
DR jPOST; P68106; -.
DR MassIVE; P68106; -.
DR MaxQB; P68106; -.
DR PaxDb; P68106; -.
DR PeptideAtlas; P68106; -.
DR PRIDE; P68106; -.
DR ProteomicsDB; 57530; -.
DR ProteomicsDB; 57531; -. [P68106-2]
DR Antibodypedia; 27417; 134 antibodies from 29 providers.
DR DNASU; 2281; -.
DR Ensembl; ENST00000380986.9; ENSP00000370373.4; ENSG00000119782.14. [P68106-1]
DR Ensembl; ENST00000380991.8; ENSP00000370379.4; ENSG00000119782.14. [P68106-2]
DR GeneID; 2281; -.
DR KEGG; hsa:2281; -.
DR MANE-Select; ENST00000380986.9; ENSP00000370373.4; NM_004116.5; NP_004107.1.
DR UCSC; uc002rer.4; human.
DR CTD; 2281; -.
DR DisGeNET; 2281; -.
DR GeneCards; FKBP1B; -.
DR HGNC; HGNC:3712; FKBP1B.
DR HPA; ENSG00000119782; Tissue enhanced (brain).
DR MIM; 600620; gene.
DR neXtProt; NX_P68106; -.
DR OpenTargets; ENSG00000119782; -.
DR PharmGKB; PA28154; -.
DR VEuPathDB; HostDB:ENSG00000119782; -.
DR eggNOG; KOG0544; Eukaryota.
DR GeneTree; ENSGT00940000153311; -.
DR HOGENOM; CLU_196166_0_0_1; -.
DR InParanoid; P68106; -.
DR OMA; RVIAGWD; -.
DR OrthoDB; 1328688at2759; -.
DR PhylomeDB; P68106; -.
DR TreeFam; TF105291; -.
DR PathwayCommons; P68106; -.
DR Reactome; R-HSA-2672351; Stimuli-sensing channels.
DR Reactome; R-HSA-5578775; Ion homeostasis.
DR SignaLink; P68106; -.
DR BioGRID-ORCS; 2281; 8 hits in 1072 CRISPR screens.
DR ChiTaRS; FKBP1B; human.
DR EvolutionaryTrace; P68106; -.
DR GeneWiki; FKBP1B; -.
DR GenomeRNAi; 2281; -.
DR Pharos; P68106; Tchem.
DR PRO; PR:P68106; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P68106; protein.
DR Bgee; ENSG00000119782; Expressed in cortical plate and 96 other tissues.
DR ExpressionAtlas; P68106; baseline and differential.
DR Genevisible; P68106; HS.
DR GO; GO:0034704; C:calcium channel complex; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IC:BHF-UCL.
DR GO; GO:0016020; C:membrane; IDA:BHF-UCL.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0030018; C:Z disc; IDA:BHF-UCL.
DR GO; GO:0019855; F:calcium channel inhibitor activity; IDA:BHF-UCL.
DR GO; GO:0030551; F:cyclic nucleotide binding; IEA:Ensembl.
DR GO; GO:0005528; F:FK506 binding; IDA:BHF-UCL.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:BHF-UCL.
DR GO; GO:0005102; F:signaling receptor binding; IPI:BHF-UCL.
DR GO; GO:0044325; F:transmembrane transporter binding; ISS:BHF-UCL.
DR GO; GO:0006458; P:'de novo' protein folding; TAS:BHF-UCL.
DR GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; TAS:BHF-UCL.
DR GO; GO:0086064; P:cell communication by electrical coupling involved in cardiac conduction; TAS:BHF-UCL.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
DR GO; GO:0035773; P:insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:0010459; P:negative regulation of heart rate; ISS:BHF-UCL.
DR GO; GO:0061179; P:negative regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; IDA:BHF-UCL.
DR GO; GO:0051280; P:negative regulation of release of sequestered calcium ion into cytosol; IDA:BHF-UCL.
DR GO; GO:0060315; P:negative regulation of ryanodine-sensitive calcium-release channel activity; IDA:BHF-UCL.
DR GO; GO:0019227; P:neuronal action potential propagation; IEA:Ensembl.
DR GO; GO:0048680; P:positive regulation of axon regeneration; IEA:Ensembl.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
DR GO; GO:0051284; P:positive regulation of sequestering of calcium ion; IDA:BHF-UCL.
DR GO; GO:0022417; P:protein maturation by protein folding; TAS:BHF-UCL.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IDA:BHF-UCL.
DR GO; GO:0042026; P:protein refolding; TAS:BHF-UCL.
DR GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; ISS:BHF-UCL.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IDA:BHF-UCL.
DR GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IDA:BHF-UCL.
DR GO; GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; IDA:BHF-UCL.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IEA:Ensembl.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:0051775; P:response to redox state; IDA:BHF-UCL.
DR GO; GO:0033197; P:response to vitamin E; IEA:Ensembl.
DR GO; GO:0006939; P:smooth muscle contraction; IEA:Ensembl.
DR GO; GO:0042098; P:T cell proliferation; IEA:Ensembl.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR Pfam; PF00254; FKBP_C; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Isomerase;
KW Reference proteome; Rotamase; Sarcoplasmic reticulum.
FT CHAIN 1..108
FT /note="Peptidyl-prolyl cis-trans isomerase FKBP1B"
FT /id="PRO_0000075295"
FT DOMAIN 20..108
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT VAR_SEQ 67..108
FT /note="MSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE -> LGPLSP
FT LPICPHPC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:7513996, ECO:0000303|Ref.3"
FT /id="VSP_005184"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:5HKG"
FT STRAND 22..31
FT /evidence="ECO:0007829|PDB:5HKG"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:5HKG"
FT TURN 40..44
FT /evidence="ECO:0007829|PDB:5HKG"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:5HKG"
FT TURN 51..54
FT /evidence="ECO:0007829|PDB:5HKG"
FT HELIX 58..65
FT /evidence="ECO:0007829|PDB:5HKG"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:5HKG"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:5HKG"
FT TURN 82..86
FT /evidence="ECO:0007829|PDB:5HKG"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:5HKG"
FT STRAND 98..108
FT /evidence="ECO:0007829|PDB:5HKG"
SQ SEQUENCE 108 AA; 11783 MW; BAC2A25945F63AC4 CRC64;
MGVEIETISP GDGRTFPKKG QTCVVHYTGM LQNGKKFDSS RDRNKPFKFR IGKQEVIKGF
EEGAAQMSLG QRAKLTCTPD VAYGATGHPG VIPPNATLIF DVELLNLE
