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Peptidyl-prolyl cis-trans isomerase FKBP8 (PPIase FKBP8) (EC 5.2.1.8) (38 kDa FK506-binding protein) (38 kDa FKBP) (FKBP-38) (hFKBP38) (FK506-binding protein 8) (FKBP-8) (FKBPR38) (Rotamase)

 FKBP8_HUMAN             Reviewed;         412 AA.
Q14318; C8C9T5; Q53GU3; Q7Z349; Q86YK6;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-JUL-2008, sequence version 2.
13-FEB-2019, entry version 197.
RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP8;
Short=PPIase FKBP8;
EC=5.2.1.8;
AltName: Full=38 kDa FK506-binding protein;
Short=38 kDa FKBP;
Short=FKBP-38;
Short=hFKBP38;
AltName: Full=FK506-binding protein 8;
Short=FKBP-8;
AltName: Full=FKBPR38;
AltName: Full=Rotamase;
Name=FKBP8; Synonyms=FKBP38;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH
BCL2 AND BCL2L1/BCLXL, AND SUBCELLULAR LOCATION.
PubMed=12510191; DOI=10.1038/ncb894;
Shirane M., Nakayama K.I.;
"Inherent calcineurin inhibitor FKBP38 targets Bcl-2 to mitochondria
and inhibits apoptosis.";
Nat. Cell Biol. 5:28-37(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=15105374; DOI=10.1242/dev.01122;
Bulgakov O.V., Eggenschwiler J.T., Hong D.-H., Anderson K.V., Li T.;
"FKBP8 is a negative regulator of mouse sonic hedgehog signaling in
neural tissues.";
Development 131:2149-2159(2004).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), SUBCELLULAR LOCATION,
INTERACTION WITH BCL2L1, AND TISSUE SPECIFICITY.
TISSUE=Retinal pigment epithelium;
PubMed=18385096; DOI=10.1167/iovs.07-1121;
Chen Y., Sternberg P., Cai J.;
"Characterization of a Bcl-XL-interacting protein FKBP8 and its splice
variant in human RPE cells.";
Invest. Ophthalmol. Vis. Sci. 49:1721-1727(2008).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Colon endothelium;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 35-412 (ISOFORM 1).
PubMed=7543869; DOI=10.1016/0378-1119(95)00216-S;
Lam E., Martin M., Wiederrecht G.;
"Isolation of a cDNA encoding a novel human FK506-binding protein
homolog containing leucine zipper and tetratricopeptide repeat
motifs.";
Gene 160:297-302(1995).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 42-412 (ISOFORM 2).
TISSUE=Liver;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 54-412 (ISOFORM 1).
TISSUE=Pancreas;
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).
[10]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16176796; DOI=10.1016/j.bbrc.2005.09.023;
Kang C.B., Feng L., Chia J., Yoon H.S.;
"Molecular characterization of FK-506 binding protein 38 and its
potential regulatory role on the anti-apoptotic protein Bcl-2.";
Biochem. Biophys. Res. Commun. 337:30-38(2005).
[11]
CATALYTIC ACTIVITY, AND COFACTOR.
PubMed=15990872; DOI=10.1038/sj.emboj.7600739;
Edlich F., Weiwad M., Erdmann F., Fanghaenel J., Jarczowski F.,
Rahfeld J.-U., Fischer G.;
"Bcl-2 regulator FKBP38 is activated by Ca2+/calmodulin.";
EMBO J. 24:2688-2699(2005).
[12]
FUNCTION, AND ABSENCE OF DIRECT INTERACTION WITH CALCINEURIN.
PubMed=15757646; DOI=10.1016/j.febslet.2004.12.098;
Weiwad M., Edlich F., Erdmann F., Jarczowski F., Kilka S., Dorn M.,
Pechstein A., Fischer G.;
"A reassessment of the inhibitory capacity of human FKBP38 on
calcineurin.";
FEBS Lett. 579:1591-1596(2005).
[13]
INTERACTION WITH BCL2.
PubMed=15733859; DOI=10.1016/j.febslet.2005.01.053;
Kang C.B., Tai J., Chia J., Yoon H.S.;
"The flexible loop of Bcl-2 is required for molecular interaction with
immunosuppressant FK-506 binding protein 38 (FKBP38).";
FEBS Lett. 579:1469-1476(2005).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[15]
INTERACTION WITH BCL2.
PubMed=17090549; DOI=10.1074/jbc.M606181200;
Portier B.P., Taglialatela G.;
"Bcl-2 localized at the nuclear compartment induces apoptosis after
transient overexpression.";
J. Biol. Chem. 281:40493-40502(2006).
[16]
INTERACTION WITH HCV NS5A (MICROBIAL INFECTION).
PubMed=16844119; DOI=10.1016/j.febslet.2006.07.002;
Wang J., Tong W., Zhang X., Chen L., Yi Z., Pan T., Hu Y., Xiang L.,
Yuan Z.;
"Hepatitis C virus non-structural protein NS5A interacts with FKBP38
and inhibits apoptosis in Huh7 hepatoma cells.";
FEBS Lett. 580:4392-4400(2006).
[17]
INTERACTION WITH ZFYVE27.
PubMed=18459960; DOI=10.1111/j.1365-2443.2008.01194.x;
Shirane M., Ogawa M., Motoyama J., Nakayama K.I.;
"Regulation of apoptosis and neurite extension by FKBP38 is required
for neural tube formation in the mouse.";
Genes Cells 13:635-651(2008).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
UBIQUITINATION AT LYS-249; LYS-271; LYS-273; LYS-284; LYS-307;
LYS-314; LYS-334; LYS-340; LYS-348; LYS-351 AND LYS-352.
PubMed=25621951; DOI=10.1038/ncb3097;
Cunningham C.N., Baughman J.M., Phu L., Tea J.S., Yu C., Coons M.,
Kirkpatrick D.S., Bingol B., Corn J.E.;
"USP30 and parkin homeostatically regulate atypical ubiquitin chains
on mitochondria.";
Nat. Cell Biol. 17:160-169(2015).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[22]
STRUCTURE BY NMR OF 92-210.
PubMed=16604427; DOI=10.1007/s10858-006-0018-6;
Maestre-Martinez M., Edlich F., Jarczowski F., Weiwad M., Fischer G.,
Luecke C.;
"Solution structure of the FK506-binding domain of human FKBP38.";
J. Biomol. NMR 34:197-202(2006).
[23]
STRUCTURE BY NMR OF 91-205.
RIKEN structural genomics initiative (RSGI);
"Solution structure of RSGI RUH-047, an FKBP domain from human cDNA.";
Submitted (JUN-2006) to the PDB data bank.
[24]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 90-205.
Structural genomics consortium (SGC);
"Structure of the human FK-506 binding protein 8.";
Submitted (OCT-2006) to the PDB data bank.
[25]
X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) OF 92-210, METAL-BINDING SITES,
AND MUTAGENESIS OF ASP-149 AND ASP-151.
PubMed=20140889; DOI=10.1002/jmr.1020;
Maestre-Martinez M., Haupt K., Edlich F., Neumann P., Parthier C.,
Stubbs M.T., Fischer G., Lucke C.;
"A charge-sensitive loop in the FKBP38 catalytic domain modulates Bcl-
2 binding.";
J. Mol. Recognit. 24:23-34(2011).
-!- FUNCTION: Constitutively inactive PPiase, which becomes active
when bound to calmodulin and calcium. Seems to act as a chaperone
for BCL2, targets it to the mitochondria and modulates its
phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex
probably interferes with the binding of BCL2 to its targets. The
active form of FKBP8 may therefore play a role in the regulation
of apoptosis. {ECO:0000269|PubMed:12510191,
ECO:0000269|PubMed:15757646, ECO:0000269|PubMed:16176796}.
-!- CATALYTIC ACTIVITY:
Reaction=[protein]-peptidylproline (omega=180) = [protein]-
peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
ChEBI:CHEBI:83834; EC=5.2.1.8;
Evidence={ECO:0000269|PubMed:15990872};
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:15990872};
-!- SUBUNIT: Homomultimers or heteromultimers (Potential). Forms
heterodimer with calmodulin. When activated by calmodulin and
calcium, interacts with the BH4 domain of BCL2 and weakly with
BCL2L1/BCLX isoform Bcl-X(L). Does not bind and inhibit
calcineurin. Interacts with ZFYVE27; may negatively regulate
ZFYVE27 phosphorylation. {ECO:0000269|PubMed:12510191,
ECO:0000269|PubMed:15733859, ECO:0000269|PubMed:17090549,
ECO:0000269|PubMed:18385096, ECO:0000269|PubMed:18459960,
ECO:0000305}.
-!- SUBUNIT: (Microbial infection) Interacts with hepatitis C/HCV
protein NS5A. {ECO:0000269|PubMed:16844119}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-724839, EBI-724839;
Q9WMX2:- (xeno); NbExp=11; IntAct=EBI-724839, EBI-6863748;
P00533:EGFR; NbExp=3; IntAct=EBI-724839, EBI-297353;
Q9GZT9:EGLN1; NbExp=6; IntAct=EBI-724839, EBI-1174818;
O75344:FKBP6; NbExp=2; IntAct=EBI-724839, EBI-744771;
P07900:HSP90AA1; NbExp=7; IntAct=EBI-724839, EBI-296047;
O39474:NS5A (xeno); NbExp=16; IntAct=EBI-724839, EBI-7016711;
C5E526:PB1 (xeno); NbExp=5; IntAct=EBI-724839, EBI-12577179;
P03431:PB1 (xeno); NbExp=5; IntAct=EBI-724839, EBI-2547514;
Q1K9H5:PB1 (xeno); NbExp=5; IntAct=EBI-724839, EBI-6050669;
Q5EP37:PB1 (xeno); NbExp=3; IntAct=EBI-724839, EBI-12577201;
Q5T4F4:ZFYVE27; NbExp=4; IntAct=EBI-724839, EBI-3892947;
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16176796}.
Mitochondrion membrane {ECO:0000305}; Single-pass membrane
protein; Cytoplasmic side {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Isoform 1: Mitochondrion membrane
{ECO:0000269|PubMed:12510191, ECO:0000269|PubMed:18385096};
Single-pass membrane protein; Cytoplasmic side {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Isoform 3: Mitochondrion membrane
{ECO:0000269|PubMed:18385096}; Single-pass membrane protein;
Cytoplasmic side {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q14318-1; Sequence=Displayed;
Name=2;
IsoId=Q14318-2; Sequence=VSP_034486;
Name=3;
IsoId=Q14318-3; Sequence=VSP_047717;
Note=Interacts with BCL2L1/BCLX.;
-!- TISSUE SPECIFICITY: Widely expressed. Highest levels seen in the
brain. Highly abundant in the retina.
{ECO:0000269|PubMed:18385096}.
-!- PTM: Ubiquitinated by PRKN during mitophagy, leading to its
degradation and enhancement of mitophagy. Deubiquitinated by
USP30. {ECO:0000269|PubMed:25621951}.
-!- MISCELLANEOUS: Binds the immunosuppressant FK506 only in its
calmodulin/calcium activated form.
-!- CAUTION: It is uncertain whether Met-1 or Met-58 is the initiator.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB00102.1; Type=Miscellaneous discrepancy; Note=The first part of the cDNA maps to the same locus, but in opposite orientation.; Evidence={ECO:0000305};
Sequence=AAH09966.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAD98028.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/FKBP8ID40579ch19p13.html";
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EMBL; AY225339; AAO39020.1; -; mRNA.
EMBL; AY278607; AAQ84561.1; -; mRNA.
EMBL; GQ372970; ACU65096.1; -; mRNA.
EMBL; BX538124; CAD98028.1; ALT_INIT; mRNA.
EMBL; BX647405; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AC005387; AAC28753.1; -; Genomic_DNA.
EMBL; CH471106; EAW84709.1; -; Genomic_DNA.
EMBL; L37033; AAB00102.1; ALT_SEQ; mRNA.
EMBL; AK222838; BAD96558.1; -; mRNA.
EMBL; BC009966; AAH09966.1; ALT_INIT; mRNA.
CCDS; CCDS32961.1; -. [Q14318-2]
CCDS; CCDS77266.1; -. [Q14318-1]
RefSeq; NP_001295302.1; NM_001308373.1. [Q14318-1]
RefSeq; NP_036313.3; NM_012181.4. [Q14318-2]
RefSeq; XP_011526165.1; XM_011527863.1. [Q14318-2]
UniGene; Hs.173464; -.
PDB; 2AWG; X-ray; 1.60 A; A=90-205.
PDB; 2D9F; NMR; -; A=91-211.
PDB; 2F2D; NMR; -; A=92-210.
PDB; 2MF9; NMR; -; A=58-205.
PDB; 3EY6; X-ray; 1.05 A; A=92-210.
PDB; 5MGX; X-ray; 2.18 A; E/F/G/H=91-380.
PDBsum; 2AWG; -.
PDBsum; 2D9F; -.
PDBsum; 2F2D; -.
PDBsum; 2MF9; -.
PDBsum; 3EY6; -.
PDBsum; 5MGX; -.
ProteinModelPortal; Q14318; -.
SMR; Q14318; -.
BioGrid; 117270; 103.
CORUM; Q14318; -.
DIP; DIP-42200N; -.
ELM; Q14318; -.
IntAct; Q14318; 94.
MINT; Q14318; -.
STRING; 9606.ENSP00000222308; -.
iPTMnet; Q14318; -.
PhosphoSitePlus; Q14318; -.
SwissPalm; Q14318; -.
BioMuta; FKBP8; -.
DMDM; 193806337; -.
EPD; Q14318; -.
jPOST; Q14318; -.
MaxQB; Q14318; -.
PaxDb; Q14318; -.
PeptideAtlas; Q14318; -.
PRIDE; Q14318; -.
ProteomicsDB; 59962; -.
ProteomicsDB; 59963; -. [Q14318-2]
DNASU; 23770; -.
Ensembl; ENST00000222308; ENSP00000222308; ENSG00000105701. [Q14318-1]
Ensembl; ENST00000596558; ENSP00000472302; ENSG00000105701. [Q14318-1]
Ensembl; ENST00000597960; ENSP00000471700; ENSG00000105701. [Q14318-2]
Ensembl; ENST00000608443; ENSP00000476767; ENSG00000105701. [Q14318-2]
GeneID; 23770; -.
KEGG; hsa:23770; -.
UCSC; uc002njj.2; human. [Q14318-1]
CTD; 23770; -.
DisGeNET; 23770; -.
EuPathDB; HostDB:ENSG00000105701.15; -.
GeneCards; FKBP8; -.
HGNC; HGNC:3724; FKBP8.
HPA; CAB025346; -.
HPA; HPA045177; -.
MIM; 604840; gene.
neXtProt; NX_Q14318; -.
OpenTargets; ENSG00000105701; -.
PharmGKB; PA28165; -.
eggNOG; KOG0543; Eukaryota.
eggNOG; COG0545; LUCA.
GeneTree; ENSGT00940000156705; -.
HOVERGEN; HBG051626; -.
InParanoid; Q14318; -.
KO; K09574; -.
OMA; AIYRYKY; -.
OrthoDB; 787673at2759; -.
PhylomeDB; Q14318; -.
TreeFam; TF105295; -.
BRENDA; 5.2.1.8; 2681.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
SABIO-RK; Q14318; -.
SIGNOR; Q14318; -.
ChiTaRS; FKBP8; human.
EvolutionaryTrace; Q14318; -.
GeneWiki; FKBP8; -.
GenomeRNAi; 23770; -.
PRO; PR:Q14318; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000105701; Expressed in 211 organ(s), highest expression level in anterior cingulate cortex.
ExpressionAtlas; Q14318; baseline and differential.
Genevisible; Q14318; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IEA:Ensembl.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0032991; C:protein-containing complex; IMP:CAFA.
GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0043010; P:camera-type eye development; IEA:Ensembl.
GO; GO:0001708; P:cell fate specification; IEA:Ensembl.
GO; GO:0021904; P:dorsal/ventral neural tube patterning; IEA:Ensembl.
GO; GO:0035556; P:intracellular signal transduction; TAS:ProtInc.
GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:CAFA.
GO; GO:0030513; P:positive regulation of BMP signaling pathway; IEA:Ensembl.
GO; GO:0007224; P:smoothened signaling pathway; IEA:Ensembl.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 1.25.40.10; -; 1.
InterPro; IPR023566; PPIase_FKBP.
InterPro; IPR001179; PPIase_FKBP_dom.
InterPro; IPR013026; TPR-contain_dom.
InterPro; IPR011990; TPR-like_helical_dom_sf.
InterPro; IPR013105; TPR_2.
InterPro; IPR019734; TPR_repeat.
PANTHER; PTHR10516; PTHR10516; 1.
Pfam; PF00254; FKBP_C; 1.
Pfam; PF07719; TPR_2; 1.
SMART; SM00028; TPR; 3.
SUPFAM; SSF48452; SSF48452; 1.
PROSITE; PS50059; FKBP_PPIASE; 1.
PROSITE; PS50005; TPR; 2.
PROSITE; PS50293; TPR_REGION; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Apoptosis; Calcium;
Complete proteome; Host-virus interaction; Isomerase; Isopeptide bond;
Membrane; Metal-binding; Mitochondrion; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Rotamase; TPR repeat; Transmembrane;
Transmembrane helix; Ubl conjugation.
CHAIN 1 412 Peptidyl-prolyl cis-trans isomerase
FKBP8.
/FTId=PRO_0000075331.
TRANSMEM 390 410 Helical. {ECO:0000255}.
DOMAIN 120 204 PPIase FKBP-type. {ECO:0000255|PROSITE-
ProRule:PRU00277}.
REPEAT 221 254 TPR 1.
REPEAT 272 305 TPR 2.
REPEAT 306 339 TPR 3.
COMPBIAS 22 92 Glu-rich.
METAL 149 149 Calcium.
METAL 151 151 Calcium.
MOD_RES 296 296 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 249 249 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:25621951}.
CROSSLNK 271 271 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:25621951}.
CROSSLNK 273 273 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:25621951}.
CROSSLNK 284 284 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:25621951}.
CROSSLNK 307 307 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:25621951}.
CROSSLNK 314 314 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:25621951}.
CROSSLNK 334 334 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:25621951}.
CROSSLNK 340 340 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:25621951}.
CROSSLNK 348 348 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:25621951}.
CROSSLNK 351 351 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:25621951}.
CROSSLNK 352 352 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:25621951}.
VAR_SEQ 98 256 Missing (in isoform 3).
{ECO:0000303|PubMed:18385096}.
/FTId=VSP_047717.
VAR_SEQ 183 183 G -> GS (in isoform 2).
{ECO:0000303|PubMed:17974005,
ECO:0000303|Ref.8}.
/FTId=VSP_034486.
VARIANT 87 87 A -> V (in dbSNP:rs11574806).
/FTId=VAR_044225.
MUTAGEN 149 149 D->N: Abolishes calcium-binding and
reduces affinity for BCL2; when
associated with Asn-151.
{ECO:0000269|PubMed:20140889}.
MUTAGEN 151 151 D->N: Abolishes calcium-binding and
reduces affinity for BCL2; when
associated with Asn-149.
{ECO:0000269|PubMed:20140889}.
CONFLICT 144 144 V -> A (in Ref. 4; CAD98028).
{ECO:0000305}.
CONFLICT 191 191 H -> R (in Ref. 4; CAD98028).
{ECO:0000305}.
CONFLICT 206 206 G -> R (in Ref. 8; BAD96558).
{ECO:0000305}.
STRAND 94 108 {ECO:0000244|PDB:3EY6}.
STRAND 111 113 {ECO:0000244|PDB:2MF9}.
STRAND 121 131 {ECO:0000244|PDB:3EY6}.
STRAND 136 146 {ECO:0000244|PDB:3EY6}.
TURN 147 150 {ECO:0000244|PDB:2MF9}.
HELIX 154 157 {ECO:0000244|PDB:3EY6}.
HELIX 160 162 {ECO:0000244|PDB:3EY6}.
STRAND 168 173 {ECO:0000244|PDB:3EY6}.
HELIX 175 177 {ECO:0000244|PDB:3EY6}.
HELIX 180 182 {ECO:0000244|PDB:3EY6}.
TURN 185 187 {ECO:0000244|PDB:3EY6}.
STRAND 190 192 {ECO:0000244|PDB:2F2D}.
STRAND 194 204 {ECO:0000244|PDB:3EY6}.
HELIX 209 211 {ECO:0000244|PDB:5MGX}.
HELIX 214 233 {ECO:0000244|PDB:5MGX}.
HELIX 237 252 {ECO:0000244|PDB:5MGX}.
HELIX 261 284 {ECO:0000244|PDB:5MGX}.
HELIX 288 301 {ECO:0000244|PDB:5MGX}.
HELIX 306 319 {ECO:0000244|PDB:5MGX}.
HELIX 322 335 {ECO:0000244|PDB:5MGX}.
HELIX 340 354 {ECO:0000244|PDB:5MGX}.
SEQUENCE 412 AA; 44562 MW; 887C25ADE71EBA8D CRC64;
MASCAEPSEP SAPLPAGVPP LEDFEVLDGV EDAEGEEEEE EEEEEEDDLS ELPPLEDMGQ
PPAEEAEQPG ALAREFLAAM EPEPAPAPAP EEWLDILGNG LLRKKTLVPG PPGSSRPVKG
QVVTVHLQTS LENGTRVQEE PELVFTLGDC DVIQALDLSV PLMDVGETAM VTADSKYCYG
PQGRSPYIPP HAALCLEVTL KTAVDGPDLE MLTGQERVAL ANRKRECGNA HYQRADFVLA
ANSYDLAIKA ITSSAKVDMT FEEEAQLLQL KVKCLNNLAA SQLKLDHYRA ALRSCSLVLE
HQPDNIKALF RKGKVLAQQG EYSEAIPILR AALKLEPSNK TIHAELSKLV KKHAAQRSTE
TALYRKMLGN PSRLPAKCPG KGAWSIPWKW LFGATAVALG GVALSVVIAA RN


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Pathways :
WP1531: Vitamin D synthesis
WP1616: ABC transporters
WP2292: Chemokine signaling pathway
WP731: Sterol regulatory element binding protein related
WP1493: Carbon assimilation C4 pathway
WP1049: G Protein Signaling Pathways
WP1058: Senescence and Autophagy
WP1165: G Protein Signaling Pathways
WP1174: Senescence and Autophagy
WP1371: G Protein Signaling Pathways
WP1378: Senescence and Autophagy
WP1438: Influenza A virus infection
WP1502: Mitochondrial biogenesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation

Related Genes :
[FKBP8 FKBP38] Peptidyl-prolyl cis-trans isomerase FKBP8 (PPIase FKBP8) (EC 5.2.1.8) (38 kDa FK506-binding protein) (38 kDa FKBP) (FKBP-38) (hFKBP38) (FK506-binding protein 8) (FKBP-8) (FKBPR38) (Rotamase)
[Fkbp8 Fkbp38 Sam11] Peptidyl-prolyl cis-trans isomerase FKBP8 (PPIase FKBP8) (EC 5.2.1.8) (38 kDa FK506-binding protein) (38 kDa FKBP) (FKBP-38) (mFKBP38) (FK506-binding protein 8) (FKBP-8) (FKBPR38) (Rotamase)
[Fkbp8] Peptidyl-prolyl cis-trans isomerase FKBP8 (PPIase FKBP8) (EC 5.2.1.8) (FK506-binding protein 8) (FKBP-8) (Rotamase)
[FKBP4 FKBP52] Peptidyl-prolyl cis-trans isomerase FKBP4 (PPIase FKBP4) (EC 5.2.1.8) (51 kDa FK506-binding protein) (FKBP51) (52 kDa FK506-binding protein) (52 kDa FKBP) (FKBP-52) (59 kDa immunophilin) (p59) (FK506-binding protein 4) (FKBP-4) (FKBP59) (HSP-binding immunophilin) (HBI) (Immunophilin FKBP52) (Rotamase) [Cleaved into: Peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed]
[FKBP4 P59] Peptidyl-prolyl cis-trans isomerase FKBP4 (PPIase FKBP4) (EC 5.2.1.8) (52 kDa FK506-binding protein) (52 kDa FKBP) (FKBP-52) (59 kDa immunophilin) (p59) (FK506-binding protein 4) (FKBP-4) (FKBP59) (HSP-binding immunophilin) (HBI) (Immunophilin FKBP52) (Rotamase) [Cleaved into: Peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed]
[FKBP1A FKBP1] Peptidyl-prolyl cis-trans isomerase FKBP1A (PPIase FKBP1A) (EC 5.2.1.8) (12 kDa FK506-binding protein) (12 kDa FKBP) (FKBP-12) (Calstabin-1) (FK506-binding protein 1A) (FKBP-1A) (Immunophilin FKBP12) (Rotamase)
[Fkbp4 Fkpb52] Peptidyl-prolyl cis-trans isomerase FKBP4 (PPIase FKBP4) (EC 5.2.1.8) (52 kDa FK506-binding protein) (52 kDa FKBP) (FKBP-52) (59 kDa immunophilin) (p59) (FK506-binding protein 4) (FKBP-4) (FKBP59) (HSP-binding immunophilin) (HBI) (Immunophilin FKBP52) (Rotamase) [Cleaved into: Peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed]
[FKBP6 FKBP36] Inactive peptidyl-prolyl cis-trans isomerase FKBP6 (Inactive PPIase FKBP6) (36 kDa FK506-binding protein) (36 kDa FKBP) (FKBP-36) (FK506-binding protein 6) (FKBP-6) (Immunophilin FKBP36)
[Fkbp4 Fkbp52] Peptidyl-prolyl cis-trans isomerase FKBP4 (PPIase FKBP4) (EC 5.2.1.8) (52 kDa FK506-binding protein) (52 kDa FKBP) (FKBP-52) (59 kDa immunophilin) (p59) (FK506-binding protein 4) (FKBP-4) (FKBP59) (HSP-binding immunophilin) (HBI) (Immunophilin FKBP52) (Rotamase) [Cleaved into: Peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed]
[Fkbp10 Fkbp-rs Fkbp1-rs Fkbp6 Fkbp65 Fkbprp] Peptidyl-prolyl cis-trans isomerase FKBP10 (PPIase FKBP10) (EC 5.2.1.8) (65 kDa FK506-binding protein) (65 kDa FKBP) (FKBP-65) (FK506-binding protein 10) (FKBP-10) (Immunophilin FKBP65) (Rotamase)
[FKBP10 FKBP65 PSEC0056] Peptidyl-prolyl cis-trans isomerase FKBP10 (PPIase FKBP10) (EC 5.2.1.8) (65 kDa FK506-binding protein) (65 kDa FKBP) (FKBP-65) (FK506-binding protein 10) (FKBP-10) (Immunophilin FKBP65) (Rotamase)
[FKBP4] Peptidyl-prolyl cis-trans isomerase FKBP4 (PPIase FKBP4) (EC 5.2.1.8) (52 kDa FK506-binding protein) (52 kDa FKBP) (FKBP-52) (FK506-binding protein 4) (FKBP-4) (HSP-binding immunophilin) (HBI) (Immunophilin FKBP52) (Rotamase) [Cleaved into: Peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed]
[FK506-bp1 FKBP39 CG6226] 39 kDa FK506-binding nuclear protein (EC 5.2.1.8) (Peptidyl-prolyl cis-trans isomerase) (PPIase) (Rotamase)
[FKBP42 TWD1 UCU2 At3g21640 MIL23.21] Peptidyl-prolyl cis-trans isomerase FKBP42 (PPIase FKBP42) (EC 5.2.1.8) (42 kDa peptidyl-prolyl isomerase) (FK506-binding protein 42) (AtFKBP42) (Immunophilin FKBP42) (Protein TWISTED DWARF 1) (Protein ULTRACURVATA 2) (Rotamase)
[FPR3 NPI46 YML074C] FK506-binding nuclear protein (EC 5.2.1.8) (FKBP-70) (Nucleolar proline isomerase) (Peptidyl-prolyl cis-trans isomerase) (PPIase) (Proline rotamase)
[Fkbp7 Fkbp23] Peptidyl-prolyl cis-trans isomerase FKBP7 (PPIase FKBP7) (EC 5.2.1.8) (23 kDa FK506-binding protein) (23 kDa FKBP) (FKBP-23) (FK506-binding protein 7) (FKBP-7) (Rotamase)
[FKBP59 CG4535] FK506-binding protein 59 (EC 5.2.1.8) (Peptidyl-prolyl cis-trans isomerase) (PPIase) (Rotamase) (dFKBP59)
[FKS1 CND1 CWH53 ETG1 GLS1 GSC1 PBR1 YLR342W L8300.6] 1,3-beta-glucan synthase component FKS1 (EC 2.4.1.34) (1,3-beta-D-glucan-UDP glucosyltransferase) (Calcineurin dependent protein 1) (Calcofluor white hypersensitivity protein 53) (Echinocandin target gene protein 1) (FK506 sensitivity protein 1) (Glucan synthase of cerevisiae protein 1) (Papulacandin B resistance protein 1)
[fkr-2 9G6.180 NCU04140] FK506-binding protein 1A (FKBP-1A) (EC 5.2.1.8) (FK506-resistance protein 2) (NcFKBP13) (Peptidyl-prolyl cis-trans isomerase fkr-2) (PPIase fkr-2)
[slyD b3349 JW3311] FKBP-type peptidyl-prolyl cis-trans isomerase SlyD (PPIase) (EC 5.2.1.8) (Histidine-rich protein) (Metallochaperone SlyD) (Rotamase) (Sensitivity to lysis protein D) (WHP)
[MTOR FRAP FRAP1 FRAP2 RAFT1 RAPT1] Serine/threonine-protein kinase mTOR (EC 2.7.11.1) (FK506-binding protein 12-rapamycin complex-associated protein 1) (FKBP12-rapamycin complex-associated protein) (Mammalian target of rapamycin) (mTOR) (Mechanistic target of rapamycin) (Rapamycin and FKBP12 target 1) (Rapamycin target protein 1)
[Ppid] Peptidyl-prolyl cis-trans isomerase D (PPIase D) (EC 5.2.1.8) (40 kDa peptidyl-prolyl cis-trans isomerase) (Cyclophilin-40) (CYP-40) (Rotamase D)
[Mtor Frap Frap1] Serine/threonine-protein kinase mTOR (EC 2.7.11.1) (FK506-binding protein 12-rapamycin complex-associated protein 1) (FKBP12-rapamycin complex-associated protein) (Mammalian target of rapamycin) (mTOR) (Mechanistic target of rapamycin) (Rapamycin target protein 1) (RAPT1)
[Mtor Frap1 Raft1] Serine/threonine-protein kinase mTOR (EC 2.7.11.1) (FK506-binding protein 12-rapamycin complex-associated protein 1) (FKBP12-rapamycin complex-associated protein) (Mammalian target of rapamycin) (mTOR) (Mechanistic target of rapamycin) (Rapamycin target protein 1) (RAPT1)
[HSP90AA1 HSP90A HSPC1 HSPCA] Heat shock protein HSP 90-alpha (Heat shock 86 kDa) (HSP 86) (HSP86) (Lipopolysaccharide-associated protein 2) (LAP-2) (LPS-associated protein 2) (Renal carcinoma antigen NY-REN-38)
[fkr-5 NCU02455] FK506-binding protein 2 (FKBP2) (EC 5.2.1.8) (FK506-resistance protein 5) (NcFKBP22) (Peptidyl-prolyl cis-trans isomerase fkr-5) (PPIase fkr-5)
[fkr-4 NCU03241] FK506-binding protein 4 (FKBP4) (EC 5.2.1.8) (FK506-resistance protein 4) (Histone proline isomerase) (Peptidyl-prolyl cis-trans isomerase fkr-4) (PPIase fkr-4) (Rotamase)
[BCL2] Apoptosis regulator Bcl-2
[GSC2 FKS2 GLS2 YGR032W] 1,3-beta-glucan synthase component GSC2 (EC 2.4.1.34) (1,3-beta-D-glucan-UDP glucosyltransferase) (FK506 sensitivity protein 2) (Glucan synthase of cerevisiae protein 2)
[fkr-3 29E8.450 NCU04371] FK506-binding protein 1B (FKBP-1B) (EC 5.2.1.8) (FK506-resistance protein 3) (Peptidyl-prolyl cis-trans isomerase fkr-3) (PPIase fkr-3) (Rapamycin-binding protein)

Bibliography :
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