Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

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.
25-OCT-2017, entry version 184.
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.
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: Peptidylproline (omega=180) = peptidylproline
(omega=0). {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 HCV NS5A. Interacts with ZFYVE27; may
negatively regulate ZFYVE27 phosphorylation.
{ECO:0000269|PubMed:12510191, ECO:0000269|PubMed:15733859,
ECO:0000269|PubMed:16844119, ECO:0000269|PubMed:17090549,
ECO:0000269|PubMed:18385096, ECO:0000269|PubMed:18459960,
ECO:0000305}.
-!- 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;
Q8TBM7:TMEM254; NbExp=4; IntAct=EBI-724839, EBI-11956809;
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";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
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; 99.
CORUM; Q14318; -.
DIP; DIP-42200N; -.
ELM; Q14318; -.
IntAct; Q14318; 68.
MINT; MINT-1338555; -.
STRING; 9606.ENSP00000222308; -.
iPTMnet; Q14318; -.
PhosphoSitePlus; Q14318; -.
SwissPalm; Q14318; -.
BioMuta; FKBP8; -.
DMDM; 193806337; -.
EPD; Q14318; -.
MaxQB; Q14318; -.
PaxDb; Q14318; -.
PeptideAtlas; Q14318; -.
PRIDE; Q14318; -.
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; ENSGT00900000140986; -.
HOVERGEN; HBG051626; -.
InParanoid; Q14318; -.
KO; K09574; -.
OMA; AIYRYKY; -.
OrthoDB; EOG091G0AS2; -.
PhylomeDB; Q14318; -.
TreeFam; TF105295; -.
BRENDA; 5.2.1.8; 2681.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
SIGNOR; Q14318; -.
ChiTaRS; FKBP8; human.
EvolutionaryTrace; Q14318; -.
GeneWiki; FKBP8; -.
GenomeRNAi; 23770; -.
PRO; PR:Q14318; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000105701; -.
CleanEx; HS_FKBP8; -.
ExpressionAtlas; Q14318; baseline and differential.
Genevisible; Q14318; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IDA:UniProtKB.
GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0043234; C:protein complex; IMP:CAFA.
GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
GO; GO:0005528; F:FK506 binding; IBA:GO_Central.
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; IBA:GO_Central.
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:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
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.
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}.
STRAND 208 211 {ECO:0000244|PDB:2D9F}.
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


Related products :

Catalog number Product name Quantity
20-372-60237 FK506 binding protein 3. 25kDa (FKBP3). mRNA - Mouse monoclonal anti-human FKBP3 antibody; EC 5.2.1.8; Peptidyl-prolyl cis-trans isomerase; PPIase; Rotamase; 25 kDa FKBP; FKBP-25; Rapamycin-selective 0.1 mg
18-003-43761 FK506-binding protein 6 - EC 5.2.1.8; Peptidyl-prolyl cis-trans isomerase; PPIase; Rotamase; 36 kDa FK506-binding protein; FKBP-36; Immunophilin FKBP36 Polyclonal 0.1 mg Protein A
18-271-81040 Peptidylprolyl Isomerase - Chicken Anti Peptidylprolyl Isomerase; EC 5.2.1.8; Peptidyl-prolyl cis-trans isomerase; PPIase; Rotamase; FKBP-21; NcFKBP22 Polyclonal 0.1 mg
26-205 FKBP11 belongs to the FKBP family of peptidyl-prolyl cis_trans isomerases, which catalyze the folding of proline-containing polypeptides. The peptidyl-prolyl isomerase activity of FKBP proteins is inh 0.05 mg
OETENZ-338 FKBP-Type Peptidyl-Prolyl Cis-Trans Isomerase E.Coli Recombinant 20
OETENZ-338 FKBP-Type Peptidyl-Prolyl Cis-Trans Isomerase E.Coli Recombinant 5
U0979p CLIA Cyclophilin A,Cyclosporin A-binding protein,Peptidyl-prolyl cis-trans isomerase A,Pig,PPIA,PPIase A,Rotamase A,Sus scrofa 96T
E0979p ELISA kit Cyclophilin A,Cyclosporin A-binding protein,Peptidyl-prolyl cis-trans isomerase A,Pig,PPIA,PPIase A,Rotamase A,Sus scrofa 96T
E0979p ELISA Cyclophilin A,Cyclosporin A-binding protein,Peptidyl-prolyl cis-trans isomerase A,Pig,PPIA,PPIase A,Rotamase A,Sus scrofa 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
E0979b ELISA Bos taurus,Bovine,Cyclophilin A,Cyclosporin A-binding protein,Peptidyl-prolyl cis-trans isomerase A,PPIA,PPIase A,Rotamase A 96T
CSB-EL008704HU Human Peptidyl-prolyl cis-trans isomerase FKBP8(FKBP8) ELISA kit 96T
CSB-EL008704MO Mouse Peptidyl-prolyl cis-trans isomerase FKBP8(FKBP8) ELISA kit 96T
CSB-EL008704RA Rat Peptidyl-prolyl cis-trans isomerase FKBP8(FKBP8) ELISA kit SpeciesRat 96T
CSB-EL008704RA Rat Peptidyl-prolyl cis-trans isomerase FKBP8(FKBP8) ELISA kit 96T
CSB-EL008704MO Mouse Peptidyl-prolyl cis-trans isomerase FKBP8(FKBP8) ELISA kit SpeciesMouse 96T
FKBP8_RAT ELISA Kit FOR Peptidyl-prolyl cis-trans isomerase FKBP8; organism: Rat; gene name: Fkbp8 96T
CSB-EL008704HU Human Peptidyl-prolyl cis-trans isomerase FKBP8(FKBP8) ELISA kit SpeciesHuman 96T
FKBP8_MOUSE ELISA Kit FOR Peptidyl-prolyl cis-trans isomerase FKBP8; organism: Mouse; gene name: Fkbp8 96T
U0979r CLIA Cyclophilin A,Cyclosporin A-binding protein,p1B15,p31,Peptidyl-prolyl cis-trans isomerase A,Ppia,PPIase A,Rat,Rattus norvegicus,Rotamase A 96T
E0979m ELISA kit Cyclophilin A,Cyclosporin A-binding protein,Mouse,Mus musculus,Peptidyl-prolyl cis-trans isomerase A,Ppia,PPIase A,Rotamase A,SP18 96T
E0979r ELISA Cyclophilin A,Cyclosporin A-binding protein,p1B15,p31,Peptidyl-prolyl cis-trans isomerase A,Ppia,PPIase A,Rat,Rattus norvegicus,Rotamase A 96T
U0979m CLIA Cyclophilin A,Cyclosporin A-binding protein,Mouse,Mus musculus,Peptidyl-prolyl cis-trans isomerase A,Ppia,PPIase A,Rotamase A,SP18 96T
E0979m ELISA Cyclophilin A,Cyclosporin A-binding protein,Mouse,Mus musculus,Peptidyl-prolyl cis-trans isomerase A,Ppia,PPIase A,Rotamase A,SP18 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur