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Peptidyl-prolyl cis-trans isomerase FKBP1B (PPIase FKBP1B) (EC 5.2.1.8) (12.6 kDa FK506-binding protein) (12.6 kDa FKBP) (FKBP-12.6) (FK506-binding protein 1B) (FKBP-1B) (Immunophilin FKBP12.6) (Rotamase) (h-FKBP-12)

 FKB1B_HUMAN             Reviewed;         108 AA.
P68106; Q13664; Q16645; Q53TM2; Q9BQ40;
25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
25-OCT-2017, entry version 138.
RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP1B;
Short=PPIase FKBP1B;
EC=5.2.1.8;
AltName: Full=12.6 kDa FK506-binding protein;
Short=12.6 kDa FKBP;
Short=FKBP-12.6;
AltName: Full=FK506-binding protein 1B;
Short=FKBP-1B;
AltName: Full=Immunophilin FKBP12.6;
AltName: Full=Rotamase;
AltName: Full=h-FKBP-12;
Name=FKBP1B; Synonyms=FKBP12.6, FKBP1L, FKBP9, OTK4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Fetal brain;
PubMed=7513996; DOI=10.1006/bbrc.1994.1527;
Arakawa H., Nagase H., Hayashi N., Fujiwara T., Ogawa M., Shin S.,
Nakamura Y.;
"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.";
Biochem. Biophys. Res. Commun. 200:836-843(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain, and Heart muscle;
PubMed=7592869; DOI=10.1074/jbc.270.44.26511;
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.;
"A novel FK506 binding protein can mediate the immunosuppressive
effects of FK506 and is associated with the cardiac ryanodine
receptor.";
J. Biol. Chem. 270:26511-26522(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Seidler T., Kussebi N., Prestle J.;
"FKBP9: an alternative splice variant of the FK506-binding protein
FKBP12.6 expressed in the human heart.";
Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=16122887; DOI=10.1016/j.gene.2005.07.004;
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.;
"Genomic organization, chromosomal localization, and promoter of human
gene for FK506-binding protein 12.6.";
Gene 360:55-64(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
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., 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.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
IDENTIFICATION IN A COMPLEX WITH RYR2; PP1; PP2A AKAP6 AND PKA,
INTERACTION WITH RYR2, AND TISSUE SPECIFICITY.
PubMed=10830164; DOI=10.1016/S0092-8674(00)80847-8;
Marx S.O., Reiken S., Hisamatsu Y., Jayaraman T., Burkhoff D.,
Rosemblit N., Marks A.R.;
"PKA phosphorylation dissociates FKBP12.6 from the calcium release
channel (ryanodine receptor): defective regulation in failing
hearts.";
Cell 101:365-376(2000).
[9]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=10713512; DOI=10.1107/S0907444999016571;
Deivanayagam C.C., Carson M., Thotakura A., Narayana S.V.,
Chodavarapu R.S.;
"Structure of FKBP12.6 in complex with rapamycin.";
Acta Crystallogr. D 56:266-271(2000).
-!- 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: Identified in a complex composed of RYR2, FKBP1B, PKA
catalytic subunit, PRKAR2A, AKAP6, and the protein phosphatases
PP2A and PP1. Interacts directly with RYR2.
{ECO:0000269|PubMed:10830164}.
-!- INTERACTION:
Q6UY14-3:ADAMTSL4; NbExp=3; IntAct=EBI-6693977, EBI-10173507;
P62161:Calm3 (xeno); NbExp=2; IntAct=EBI-15766566, EBI-397530;
Q13557:CAMK2D; NbExp=3; IntAct=EBI-6693977, EBI-351018;
Q53SE7:FLJ13057; NbExp=3; IntAct=EBI-6693977, EBI-10172181;
Q15323:KRT31; NbExp=3; IntAct=EBI-6693977, EBI-948001;
Q6A162:KRT40; NbExp=3; IntAct=EBI-6693977, EBI-10171697;
Q04864:REL; NbExp=3; IntAct=EBI-6693977, EBI-307352;
P11716:RYR1 (xeno); NbExp=2; IntAct=EBI-15766566, EBI-6477441;
Q92736:RYR2; NbExp=5; IntAct=EBI-6693977, EBI-1170425;
Q86WT6:TRIM69; NbExp=3; IntAct=EBI-6693977, EBI-749955;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Sarcoplasmic
reticulum {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P68106-1, Q16645-1;
Sequence=Displayed;
Name=2;
IsoId=P68106-2, Q16645-2;
Sequence=VSP_005184;
-!- TISSUE SPECIFICITY: Detected in heart muscle (at protein level).
Isoform 1 and isoform 2 are ubiquitous with highest levels in
brain and thymus. {ECO:0000269|PubMed:10830164}.
-!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP1
subfamily. {ECO:0000305}.
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EMBL; S69815; AAB30684.1; -; mRNA.
EMBL; D38037; BAA07232.1; -; mRNA.
EMBL; L37086; AAC37581.1; -; mRNA.
EMBL; S69800; AAB30685.1; -; mRNA.
EMBL; AF322070; AAK11191.1; -; mRNA.
EMBL; AB190793; BAE44300.1; -; Genomic_DNA.
EMBL; AC008073; AAY14663.1; -; Genomic_DNA.
EMBL; CH471053; EAX00769.1; -; Genomic_DNA.
EMBL; BC002614; AAH02614.1; -; mRNA.
CCDS; CCDS1706.1; -.
CCDS; CCDS33153.1; -. [P68106-2]
PIR; JC2188; JC2188.
RefSeq; NP_004107.1; NM_004116.4. [P68106-1]
RefSeq; NP_473374.1; NM_054033.3. [P68106-2]
UniGene; Hs.709461; -.
PDB; 1C9H; X-ray; 2.00 A; A=2-108.
PDB; 4C02; X-ray; 2.17 A; B=1-108.
PDB; 4IQ2; X-ray; 1.70 A; A/B=2-108.
PDB; 4IQC; X-ray; 1.90 A; A/B=2-108.
PDB; 5HKG; X-ray; 1.50 A; A=2-108.
PDB; 5L1D; EM; 10.50 A; B/D/F/H=2-108.
PDB; 5T15; EM; 3.80 A; A/F/H/J=1-108.
PDB; 5T9M; EM; 3.80 A; A/F/H/J=1-108.
PDB; 5T9N; EM; 3.80 A; A/F/H/J=1-108.
PDB; 5T9R; EM; 3.80 A; A/F/H/J=1-108.
PDB; 5T9S; EM; 3.80 A; A/F/H/J=1-108.
PDB; 5T9V; EM; 3.80 A; A/F/H/J=1-108.
PDB; 5TA3; EM; 3.80 A; A/F/H/J=1-108.
PDB; 5TAL; EM; 3.80 A; A/F/H/J=1-108.
PDB; 5TAM; EM; 3.80 A; A/F/H/J=1-108.
PDB; 5TAN; EM; 3.80 A; A/F/H/J=1-108.
PDB; 5TAP; EM; 3.80 A; A/F/H/J=1-108.
PDB; 5TAQ; EM; 3.80 A; A/F/H/J=1-108.
PDB; 5TAS; EM; 3.80 A; A/F/H/J=1-108.
PDB; 5TAT; EM; 3.80 A; A/F/H/J=1-108.
PDB; 5TAU; EM; 3.80 A; A/F/H/J=1-108.
PDB; 5TAV; EM; 3.80 A; A/F/H/J=1-108.
PDB; 5TAW; EM; 3.80 A; A/F/H/J=1-108.
PDB; 5TAX; EM; 3.80 A; A/F/H/J=1-108.
PDB; 5TAY; EM; 3.80 A; A/F/H/J=1-108.
PDB; 5TAZ; EM; 3.80 A; A/F/H/J=1-108.
PDB; 5TB0; EM; 4.40 A; A/F/H/J=1-108.
PDB; 5TB1; EM; 3.80 A; A/F/H/J=1-108.
PDB; 5TB2; EM; 3.80 A; A/F/H/J=1-108.
PDB; 5TB3; EM; 3.80 A; A/F/H/J=1-108.
PDB; 5TB4; EM; 3.80 A; A/F/H/J=1-108.
PDBsum; 1C9H; -.
PDBsum; 4C02; -.
PDBsum; 4IQ2; -.
PDBsum; 4IQC; -.
PDBsum; 5HKG; -.
PDBsum; 5L1D; -.
PDBsum; 5T15; -.
PDBsum; 5T9M; -.
PDBsum; 5T9N; -.
PDBsum; 5T9R; -.
PDBsum; 5T9S; -.
PDBsum; 5T9V; -.
PDBsum; 5TA3; -.
PDBsum; 5TAL; -.
PDBsum; 5TAM; -.
PDBsum; 5TAN; -.
PDBsum; 5TAP; -.
PDBsum; 5TAQ; -.
PDBsum; 5TAS; -.
PDBsum; 5TAT; -.
PDBsum; 5TAU; -.
PDBsum; 5TAV; -.
PDBsum; 5TAW; -.
PDBsum; 5TAX; -.
PDBsum; 5TAY; -.
PDBsum; 5TAZ; -.
PDBsum; 5TB0; -.
PDBsum; 5TB1; -.
PDBsum; 5TB2; -.
PDBsum; 5TB3; -.
PDBsum; 5TB4; -.
ProteinModelPortal; P68106; -.
SMR; P68106; -.
BioGrid; 108571; 28.
DIP; DIP-48796N; -.
IntAct; P68106; 14.
STRING; 9606.ENSP00000370373; -.
BindingDB; P68106; -.
ChEMBL; CHEMBL2430; -.
PhosphoSitePlus; P68106; -.
BioMuta; FKBP1B; -.
DMDM; 61224185; -.
EPD; P68106; -.
MaxQB; P68106; -.
PaxDb; P68106; -.
PeptideAtlas; P68106; -.
PRIDE; P68106; -.
DNASU; 2281; -.
Ensembl; ENST00000380986; ENSP00000370373; ENSG00000119782. [P68106-1]
Ensembl; ENST00000380991; ENSP00000370379; ENSG00000119782. [P68106-2]
GeneID; 2281; -.
KEGG; hsa:2281; -.
UCSC; uc002rer.4; human.
CTD; 2281; -.
DisGeNET; 2281; -.
EuPathDB; HostDB:ENSG00000119782.13; -.
GeneCards; FKBP1B; -.
HGNC; HGNC:3712; FKBP1B.
HPA; HPA051798; -.
HPA; HPA057830; -.
MIM; 600620; gene.
neXtProt; NX_P68106; -.
OpenTargets; ENSG00000119782; -.
PharmGKB; PA28154; -.
eggNOG; KOG0544; Eukaryota.
eggNOG; COG0545; LUCA.
GeneTree; ENSGT00760000119159; -.
HOGENOM; HOG000154887; -.
HOVERGEN; HBG051623; -.
InParanoid; P68106; -.
KO; K09568; -.
OMA; WGIMPNS; -.
OrthoDB; EOG091G02W1; -.
PhylomeDB; P68106; -.
TreeFam; TF105291; -.
Reactome; R-HSA-2672351; Stimuli-sensing channels.
Reactome; R-HSA-5578775; Ion homeostasis.
EvolutionaryTrace; P68106; -.
GeneWiki; FKBP1B; -.
GenomeRNAi; 2281; -.
PRO; PR:P68106; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000119782; -.
CleanEx; HS_FKBP1B; -.
CleanEx; HS_FKBP9; -.
ExpressionAtlas; P68106; baseline and differential.
Genevisible; P68106; HS.
GO; GO:0034704; C:calcium channel complex; IDA:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; IC:BHF-UCL.
GO; GO:0016020; C:membrane; IDA:BHF-UCL.
GO; GO:0033017; C:sarcoplasmic reticulum membrane; IBA:GO_Central.
GO; GO:0030018; C:Z disc; IDA:BHF-UCL.
GO; GO:0019855; F:calcium channel inhibitor activity; IDA:BHF-UCL.
GO; GO:0030551; F:cyclic nucleotide binding; IEA:Ensembl.
GO; GO:0005528; F:FK506 binding; IDA:BHF-UCL.
GO; GO:0044325; F:ion channel binding; ISS:BHF-UCL.
GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:BHF-UCL.
GO; GO:0005102; F:receptor binding; IPI:BHF-UCL.
GO; GO:0006458; P:'de novo' protein folding; TAS:BHF-UCL.
GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; TAS:BHF-UCL.
GO; GO:0086064; P:cell communication by electrical coupling involved in cardiac conduction; TAS:BHF-UCL.
GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
GO; GO:0030073; P:insulin secretion; IEA:Ensembl.
GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
GO; GO:0010459; P:negative regulation of heart rate; ISS:BHF-UCL.
GO; GO:0061179; P:negative regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; IDA:BHF-UCL.
GO; GO:0051280; P:negative regulation of release of sequestered calcium ion into cytosol; IDA:BHF-UCL.
GO; GO:0060315; P:negative regulation of ryanodine-sensitive calcium-release channel activity; IDA:BHF-UCL.
GO; GO:0019227; P:neuronal action potential propagation; IEA:Ensembl.
GO; GO:0048680; P:positive regulation of axon regeneration; IEA:Ensembl.
GO; GO:0051284; P:positive regulation of sequestering of calcium ion; IDA:BHF-UCL.
GO; GO:0022417; P:protein maturation by protein folding; TAS:BHF-UCL.
GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IDA:BHF-UCL.
GO; GO:0042026; P:protein refolding; TAS:BHF-UCL.
GO; GO:1903779; P:regulation of cardiac conduction; TAS:Reactome.
GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; ISS:BHF-UCL.
GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IDA:BHF-UCL.
GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IDA:BHF-UCL.
GO; GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; IDA:BHF-UCL.
GO; GO:0014808; P:release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IEA:Ensembl.
GO; GO:0009749; P:response to glucose; IEA:Ensembl.
GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0051775; P:response to redox state; IDA:BHF-UCL.
GO; GO:0033197; P:response to vitamin E; IEA:Ensembl.
GO; GO:0006939; P:smooth muscle contraction; IEA:Ensembl.
GO; GO:0042098; P:T cell proliferation; IEA:Ensembl.
InterPro; IPR023566; PPIase_FKBP.
InterPro; IPR001179; PPIase_FKBP_dom.
PANTHER; PTHR10516; PTHR10516; 1.
Pfam; PF00254; FKBP_C; 1.
PROSITE; PS50059; FKBP_PPIASE; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Isomerase; Reference proteome; Rotamase; Sarcoplasmic reticulum.
CHAIN 1 108 Peptidyl-prolyl cis-trans isomerase
FKBP1B.
/FTId=PRO_0000075295.
DOMAIN 20 108 PPIase FKBP-type. {ECO:0000255|PROSITE-
ProRule:PRU00277}.
VAR_SEQ 67 108 MSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNL
E -> LGPLSPLPICPHPC (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:7513996,
ECO:0000303|Ref.3}.
/FTId=VSP_005184.
STRAND 3 9 {ECO:0000244|PDB:5HKG}.
STRAND 22 31 {ECO:0000244|PDB:5HKG}.
STRAND 36 39 {ECO:0000244|PDB:5HKG}.
TURN 40 44 {ECO:0000244|PDB:5HKG}.
STRAND 47 50 {ECO:0000244|PDB:5HKG}.
TURN 51 54 {ECO:0000244|PDB:5HKG}.
HELIX 58 65 {ECO:0000244|PDB:5HKG}.
STRAND 72 77 {ECO:0000244|PDB:5HKG}.
HELIX 79 81 {ECO:0000244|PDB:5HKG}.
TURN 82 86 {ECO:0000244|PDB:5HKG}.
TURN 89 91 {ECO:0000244|PDB:5HKG}.
STRAND 98 108 {ECO:0000244|PDB:5HKG}.
SEQUENCE 108 AA; 11783 MW; BAC2A25945F63AC4 CRC64;
MGVEIETISP GDGRTFPKKG QTCVVHYTGM LQNGKKFDSS RDRNKPFKFR IGKQEVIKGF
EEGAAQMSLG QRAKLTCTPD VAYGATGHPG VIPPNATLIF DVELLNLE


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FKB1B_RAT ELISA Kit FOR Peptidyl-prolyl cis-trans isomerase FKBP1B; organism: Rat; gene name: Fkbp1b 96T
CSB-EL008692MO Mouse Peptidyl-prolyl cis-trans isomerase FKBP1B(FKBP1B) ELISA kit SpeciesMouse 96T
CSB-EL008692BO Bovine Peptidyl-prolyl cis-trans isomerase FKBP1B(FKBP1B) ELISA kit SpeciesBovine 96T
FKB1B_MOUSE ELISA Kit FOR Peptidyl-prolyl cis-trans isomerase FKBP1B; organism: Mouse; gene name: Fkbp1b 96T
U0979b CLIA Bos taurus,Bovine,Cyclophilin A,Cyclosporin A-binding protein,Peptidyl-prolyl cis-trans isomerase A,PPIA,PPIase A,Rotamase A 96T
E0979b ELISA kit Bos taurus,Bovine,Cyclophilin A,Cyclosporin A-binding protein,Peptidyl-prolyl cis-trans isomerase A,PPIA,PPIase A,Rotamase A 96T


 

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