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Peptidyl-prolyl cis-trans isomerase FKBP5 (PPIase FKBP5) (EC 5.2.1.8) (51 kDa FK506-binding protein) (51 kDa FKBP) (FKBP-51) (54 kDa progesterone receptor-associated immunophilin) (Androgen-regulated protein 6) (FF1 antigen) (FK506-binding protein 5) (FKBP-5) (FKBP54) (p54) (HSP90-binding immunophilin) (Rotamase)

 FKBP5_HUMAN             Reviewed;         457 AA.
Q13451; F5H7R1; Q59EB8; Q5TGM6;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
15-JUL-1998, sequence version 2.
22-NOV-2017, entry version 181.
RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP5;
Short=PPIase FKBP5;
EC=5.2.1.8;
AltName: Full=51 kDa FK506-binding protein;
Short=51 kDa FKBP;
Short=FKBP-51;
AltName: Full=54 kDa progesterone receptor-associated immunophilin;
AltName: Full=Androgen-regulated protein 6;
AltName: Full=FF1 antigen;
AltName: Full=FK506-binding protein 5;
Short=FKBP-5;
AltName: Full=FKBP54;
Short=p54;
AltName: Full=HSP90-binding immunophilin;
AltName: Full=Rotamase;
Name=FKBP5; Synonyms=AIG6, FKBP51;
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).
TISSUE=Thymus;
PubMed=9125197; DOI=10.1006/bbrc.1997.6307;
Baughman G., Wiederrecht G.J., Chang F., Martin M.M., Bourgeois S.;
"Tissue distribution and abundance of human FKBP51, an FK506-binding
protein that can mediate calcineurin inhibition.";
Biochem. Biophys. Res. Commun. 232:437-443(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Zhang J.S., Smith D.I.;
"Identification of AIG6 as an androgen response gene in human prostate
cancer cell line LNCaP.";
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Aortic endothelium;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
"Homo sapiens protein coding cDNA.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton 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 [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
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]
NUCLEOTIDE SEQUENCE [MRNA] OF 9-457 (ISOFORM 1).
PubMed=9001212; DOI=10.1128/MCB.17.2.594;
Nair S.C., Rimerman R.A., Toran E.J., Chen S., Prapapanich V.,
Butts R.N., Smith D.F.;
"Molecular cloning of human FKBP51 and comparisons of immunophilin
interactions with Hsp90 and progesterone receptor.";
Mol. Cell. Biol. 17:594-603(1997).
[9]
CHARACTERIZATION.
PubMed=7693698;
Smith D.F., Albers M.W., Schreiber S.L., Leach K.L., Deibel M.R. Jr.;
"FKBP54, a novel FK506-binding protein in avian progesterone receptor
complexes and HeLa extracts.";
J. Biol. Chem. 268:24270-24273(1993).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[15]
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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND SER-445, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and 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).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
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).
[19]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
PubMed=12538866; DOI=10.1073/pnas.0231020100;
Sinars C.R., Cheung-Flynn J., Rimerman R.A., Scammell J.G.,
Smith D.F., Clardy J.;
"Structure of the large FK506-binding protein FKBP51, an Hsp90-binding
protein and a component of steroid receptor complexes.";
Proc. Natl. Acad. Sci. U.S.A. 100:868-873(2003).
-!- FUNCTION: Immunophilin protein with PPIase and co-chaperone
activities. Component of unligated steroid receptors
heterocomplexes through interaction with heat-shock protein 90
(HSP90). Plays a role in the intracellular trafficking of
heterooligomeric forms of steroid hormone receptors maintaining
the complex into the cytoplasm when unliganded.
-!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
(omega=0).
-!- ENZYME REGULATION: Inhibited by FK506 but not cyclosporin.
-!- SUBUNIT: Part of a heteromultimeric cytoplasmic complex with
HSP90AA1, HSPA1A/HSPA1B and steroid receptors. Upon ligand binding
dissociates from the complex and FKBP4 takes its place. Interacts
with functionally mature heterooligomeric progesterone receptor
complexes along with HSP90 and TEBP.
-!- INTERACTION:
Q9WMX2:- (xeno); NbExp=4; IntAct=EBI-306914, EBI-9005440;
Q96Q40:CDK15; NbExp=2; IntAct=EBI-306914, EBI-1051975;
P50750:CDK9; NbExp=4; IntAct=EBI-306914, EBI-1383449;
O15111:CHUK; NbExp=2; IntAct=EBI-306914, EBI-81249;
P08238:HSP90AB1; NbExp=4; IntAct=EBI-306914, EBI-352572;
Q6VAB6:KSR2; NbExp=6; IntAct=EBI-306914, EBI-6424389;
Q9BTE3-2:MCMBP; NbExp=3; IntAct=EBI-306914, EBI-9384556;
Q15831:STK11; NbExp=4; IntAct=EBI-306914, EBI-306838;
Q70CQ1:USP49; NbExp=2; IntAct=EBI-306914, EBI-2511022;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q13451-1; Sequence=Displayed;
Name=2;
IsoId=Q13451-2; Sequence=VSP_044820, VSP_044821;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed, enriched in testis compared
to other tissues.
-!- INDUCTION: By androgen.
-!- SEQUENCE CAUTION:
Sequence=BAD93130.1; Type=Frameshift; Positions=29; Evidence={ECO:0000305};
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EMBL; U71321; AAC51189.1; -; mRNA.
EMBL; AF194172; AAL54872.1; -; mRNA.
EMBL; AK312422; BAG35332.1; -; mRNA.
EMBL; AB209893; BAD93130.1; ALT_FRAME; mRNA.
EMBL; AL033519; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL157823; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL590400; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471081; EAX03842.1; -; Genomic_DNA.
EMBL; BC042605; AAH42605.1; -; mRNA.
EMBL; U42031; AAA86245.1; -; mRNA.
CCDS; CCDS4808.1; -. [Q13451-1]
CCDS; CCDS54996.1; -. [Q13451-2]
PIR; JC5422; JC5422.
RefSeq; NP_001139247.1; NM_001145775.2. [Q13451-1]
RefSeq; NP_001139248.1; NM_001145776.1. [Q13451-1]
RefSeq; NP_001139249.1; NM_001145777.1. [Q13451-2]
RefSeq; NP_004108.1; NM_004117.3. [Q13451-1]
UniGene; Hs.407190; -.
PDB; 1KT0; X-ray; 2.70 A; A=1-457.
PDB; 3O5D; X-ray; 4.00 A; A/B=1-260.
PDB; 3O5E; X-ray; 1.60 A; A=1-140.
PDB; 3O5F; X-ray; 1.65 A; A=1-140.
PDB; 3O5G; X-ray; 2.00 A; A=16-140.
PDB; 3O5I; X-ray; 1.80 A; A/B=16-140.
PDB; 3O5J; X-ray; 1.70 A; A=16-140.
PDB; 3O5K; X-ray; 2.70 A; A/B/C/D=16-140.
PDB; 3O5L; X-ray; 1.30 A; A=16-140.
PDB; 3O5M; X-ray; 1.60 A; A/B=16-140.
PDB; 3O5O; X-ray; 1.15 A; A=16-140.
PDB; 3O5P; X-ray; 1.00 A; A=16-140.
PDB; 3O5Q; X-ray; 0.96 A; A=16-140.
PDB; 3O5R; X-ray; 1.10 A; A=16-140.
PDB; 4DRH; X-ray; 2.30 A; A/D=1-140.
PDB; 4DRI; X-ray; 1.45 A; A=1-140.
PDB; 4DRK; X-ray; 1.50 A; A/B=16-140.
PDB; 4DRM; X-ray; 1.48 A; A=16-140.
PDB; 4DRN; X-ray; 1.07 A; A=16-140.
PDB; 4DRO; X-ray; 1.10 A; A=16-140.
PDB; 4DRP; X-ray; 1.80 A; A=16-140.
PDB; 4DRQ; X-ray; 1.00 A; A=16-140.
PDB; 4JFI; X-ray; 1.05 A; A=16-139.
PDB; 4JFJ; X-ray; 1.08 A; A=16-140.
PDB; 4JFK; X-ray; 1.15 A; A=16-140.
PDB; 4JFL; X-ray; 1.20 A; A=16-140.
PDB; 4JFM; X-ray; 1.02 A; A=16-140.
PDB; 4R0X; X-ray; 1.20 A; A=20-140.
PDB; 4TW6; X-ray; 1.40 A; A=16-140.
PDB; 4TW7; X-ray; 1.25 A; A=16-140.
PDB; 4TX0; X-ray; 1.03 A; A=16-140.
PDB; 4W9O; X-ray; 1.27 A; A/E=16-140.
PDB; 4W9P; X-ray; 1.50 A; A/E=16-140.
PDB; 4W9Q; X-ray; 1.08 A; A=16-140.
PDB; 5BXJ; X-ray; 1.24 A; A=16-140.
PDB; 5DIT; X-ray; 2.25 A; A=16-140.
PDB; 5DIU; X-ray; 1.30 A; A=16-140.
PDB; 5DIV; X-ray; 1.65 A; A=16-139.
PDBsum; 1KT0; -.
PDBsum; 3O5D; -.
PDBsum; 3O5E; -.
PDBsum; 3O5F; -.
PDBsum; 3O5G; -.
PDBsum; 3O5I; -.
PDBsum; 3O5J; -.
PDBsum; 3O5K; -.
PDBsum; 3O5L; -.
PDBsum; 3O5M; -.
PDBsum; 3O5O; -.
PDBsum; 3O5P; -.
PDBsum; 3O5Q; -.
PDBsum; 3O5R; -.
PDBsum; 4DRH; -.
PDBsum; 4DRI; -.
PDBsum; 4DRK; -.
PDBsum; 4DRM; -.
PDBsum; 4DRN; -.
PDBsum; 4DRO; -.
PDBsum; 4DRP; -.
PDBsum; 4DRQ; -.
PDBsum; 4JFI; -.
PDBsum; 4JFJ; -.
PDBsum; 4JFK; -.
PDBsum; 4JFL; -.
PDBsum; 4JFM; -.
PDBsum; 4R0X; -.
PDBsum; 4TW6; -.
PDBsum; 4TW7; -.
PDBsum; 4TX0; -.
PDBsum; 4W9O; -.
PDBsum; 4W9P; -.
PDBsum; 4W9Q; -.
PDBsum; 5BXJ; -.
PDBsum; 5DIT; -.
PDBsum; 5DIU; -.
PDBsum; 5DIV; -.
ProteinModelPortal; Q13451; -.
SMR; Q13451; -.
BioGrid; 108579; 114.
CORUM; Q13451; -.
DIP; DIP-27597N; -.
IntAct; Q13451; 120.
MINT; MINT-1142816; -.
STRING; 9606.ENSP00000338160; -.
BindingDB; Q13451; -.
ChEMBL; CHEMBL2052031; -.
iPTMnet; Q13451; -.
PhosphoSitePlus; Q13451; -.
SwissPalm; Q13451; -.
BioMuta; FKBP5; -.
DMDM; 2851536; -.
EPD; Q13451; -.
PaxDb; Q13451; -.
PeptideAtlas; Q13451; -.
PRIDE; Q13451; -.
DNASU; 2289; -.
Ensembl; ENST00000357266; ENSP00000349811; ENSG00000096060. [Q13451-1]
Ensembl; ENST00000536438; ENSP00000444810; ENSG00000096060. [Q13451-1]
Ensembl; ENST00000539068; ENSP00000441205; ENSG00000096060. [Q13451-1]
Ensembl; ENST00000542713; ENSP00000442340; ENSG00000096060. [Q13451-2]
GeneID; 2289; -.
KEGG; hsa:2289; -.
UCSC; uc003okx.3; human. [Q13451-1]
CTD; 2289; -.
DisGeNET; 2289; -.
EuPathDB; HostDB:ENSG00000096060.14; -.
GeneCards; FKBP5; -.
HGNC; HGNC:3721; FKBP5.
HPA; CAB009315; -.
HPA; HPA031092; -.
HPA; HPA031093; -.
HPA; HPA031095; -.
MalaCards; FKBP5; -.
MIM; 602623; gene.
neXtProt; NX_Q13451; -.
OpenTargets; ENSG00000096060; -.
PharmGKB; PA28162; -.
eggNOG; KOG0543; Eukaryota.
eggNOG; COG0545; LUCA.
GeneTree; ENSGT00760000119159; -.
HOGENOM; HOG000256916; -.
HOVERGEN; HBG051624; -.
InParanoid; Q13451; -.
KO; K09571; -.
OMA; NSEETPM; -.
OrthoDB; EOG091G07OA; -.
PhylomeDB; Q13451; -.
TreeFam; TF105292; -.
Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
SIGNOR; Q13451; -.
ChiTaRS; FKBP5; human.
EvolutionaryTrace; Q13451; -.
GeneWiki; FKBP5; -.
GenomeRNAi; 2289; -.
PRO; PR:Q13451; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000096060; -.
CleanEx; HS_FKBP5; -.
Genevisible; Q13451; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005528; F:FK506 binding; IBA:GO_Central.
GO; GO:0031072; F:heat shock protein binding; IPI:UniProtKB.
GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:UniProtKB.
GO; GO:0061077; P:chaperone-mediated protein folding; IDA:UniProtKB.
GO; GO:0006457; P:protein folding; TAS:ProtInc.
Gene3D; 1.25.40.10; -; 2.
InterPro; IPR031210; FKBP5.
InterPro; IPR023566; PPIase_FKBP.
InterPro; IPR001179; PPIase_FKBP_dom.
InterPro; IPR013026; TPR-contain_dom.
InterPro; IPR011990; TPR-like_helical_dom_sf.
InterPro; IPR001440; TPR_1.
InterPro; IPR019734; TPR_repeat.
PANTHER; PTHR10516; PTHR10516; 1.
PANTHER; PTHR10516:SF26; PTHR10516:SF26; 1.
Pfam; PF00254; FKBP_C; 2.
Pfam; PF00515; TPR_1; 1.
Pfam; PF13181; TPR_8; 1.
SMART; SM00028; TPR; 2.
SUPFAM; SSF48452; SSF48452; 1.
PROSITE; PS50059; FKBP_PPIASE; 2.
PROSITE; PS50005; TPR; 3.
PROSITE; PS50293; TPR_REGION; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Chaperone;
Complete proteome; Cytoplasm; Isomerase; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Rotamase; TPR repeat.
CHAIN 1 457 Peptidyl-prolyl cis-trans isomerase
FKBP5.
/FTId=PRO_0000075324.
DOMAIN 42 130 PPIase FKBP-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00277}.
DOMAIN 157 243 PPIase FKBP-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00277}.
REPEAT 268 301 TPR 1.
REPEAT 317 350 TPR 2.
REPEAT 351 384 TPR 3.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 13 13 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 445 445 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 223 268 YGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKE
KLEQA -> PKNPGRWIPKKNWSRLPLSKRREPYTSRCVSP
YAILSISKNLFKCW (in isoform 2).
{ECO:0000303|Ref.4}.
/FTId=VSP_044820.
VAR_SEQ 269 457 Missing (in isoform 2).
{ECO:0000303|Ref.4}.
/FTId=VSP_044821.
HELIX 16 21 {ECO:0000244|PDB:3O5Q}.
STRAND 22 24 {ECO:0000244|PDB:4W9O}.
STRAND 26 28 {ECO:0000244|PDB:4DRH}.
STRAND 30 39 {ECO:0000244|PDB:3O5Q}.
STRAND 42 44 {ECO:0000244|PDB:3O5Q}.
STRAND 52 61 {ECO:0000244|PDB:3O5Q}.
STRAND 66 69 {ECO:0000244|PDB:3O5Q}.
HELIX 70 73 {ECO:0000244|PDB:3O5Q}.
STRAND 77 80 {ECO:0000244|PDB:3O5Q}.
STRAND 83 86 {ECO:0000244|PDB:3O5Q}.
HELIX 88 94 {ECO:0000244|PDB:3O5Q}.
STRAND 102 107 {ECO:0000244|PDB:3O5Q}.
HELIX 109 111 {ECO:0000244|PDB:3O5Q}.
TURN 112 116 {ECO:0000244|PDB:3O5Q}.
TURN 119 121 {ECO:0000244|PDB:3O5Q}.
STRAND 128 138 {ECO:0000244|PDB:3O5Q}.
STRAND 144 154 {ECO:0000244|PDB:1KT0}.
STRAND 167 176 {ECO:0000244|PDB:1KT0}.
STRAND 179 189 {ECO:0000244|PDB:1KT0}.
HELIX 193 196 {ECO:0000244|PDB:1KT0}.
HELIX 200 206 {ECO:0000244|PDB:1KT0}.
STRAND 214 219 {ECO:0000244|PDB:1KT0}.
HELIX 221 223 {ECO:0000244|PDB:1KT0}.
HELIX 231 233 {ECO:0000244|PDB:1KT0}.
STRAND 241 251 {ECO:0000244|PDB:1KT0}.
HELIX 256 258 {ECO:0000244|PDB:1KT0}.
HELIX 261 280 {ECO:0000244|PDB:1KT0}.
HELIX 284 298 {ECO:0000244|PDB:1KT0}.
HELIX 306 329 {ECO:0000244|PDB:1KT0}.
HELIX 333 346 {ECO:0000244|PDB:1KT0}.
HELIX 351 363 {ECO:0000244|PDB:1KT0}.
HELIX 367 378 {ECO:0000244|PDB:1KT0}.
HELIX 387 411 {ECO:0000244|PDB:1KT0}.
SEQUENCE 457 AA; 51212 MW; 18A86608C6891A73 CRC64;
MTTDEGAKNN EESPTATVAE QGEDITSKKD RGVLKIVKRV GNGEETPMIG DKVYVHYKGK
LSNGKKFDSS HDRNEPFVFS LGKGQVIKAW DIGVATMKKG EICHLLCKPE YAYGSAGSLP
KIPSNATLFF EIELLDFKGE DLFEDGGIIR RTKRKGEGYS NPNEGATVEI HLEGRCGGRM
FDCRDVAFTV GEGEDHDIPI GIDKALEKMQ REEQCILYLG PRYGFGEAGK PKFGIEPNAE
LIYEVTLKSF EKAKESWEMD TKEKLEQAAI VKEKGTVYFK GGKYMQAVIQ YGKIVSWLEM
EYGLSEKESK ASESFLLAAF LNLAMCYLKL REYTKAVECC DKALGLDSAN EKGLYRRGEA
QLLMNEFESA KGDFEKVLEV NPQNKAARLQ ISMCQKKAKE HNERDRRIYA NMFKKFAEQD
AKEEANKAMG KKTSEGVTNE KGTDSQAMEE EKPEGHV


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