ID FKBP5_HUMAN Reviewed; 457 AA. AC Q13451; F5H7R1; Q59EB8; Q5TGM6; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 28-JAN-2026, entry version 233. DE RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP5; DE Short=PPIase FKBP5; DE EC=5.2.1.8 {ECO:0000269|PubMed:11350175}; DE AltName: Full=51 kDa FK506-binding protein; DE Short=51 kDa FKBP; DE Short=FKBP-51; DE AltName: Full=54 kDa progesterone receptor-associated immunophilin; DE AltName: Full=Androgen-regulated protein 6; DE AltName: Full=FF1 antigen; DE AltName: Full=FK506-binding protein 5; DE Short=FKBP-5; DE AltName: Full=FKBP54; DE Short=p54; DE AltName: Full=HSP90-binding immunophilin; DE AltName: Full=Rotamase; GN Name=FKBP5; Synonyms=AIG6, FKBP51 {ECO:0000303|PubMed:28147277}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Thymus; RX PubMed=9125197; DOI=10.1006/bbrc.1997.6307; RA Baughman G., Wiederrecht G.J., Chang F., Martin M.M., Bourgeois S.; RT "Tissue distribution and abundance of human FKBP51, an FK506-binding RT protein that can mediate calcineurin inhibition."; RL Biochem. Biophys. Res. Commun. 232:437-443(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Zhang J.S., Smith D.I.; RT "Identification of AIG6 as an androgen response gene in human prostate RT cancer cell line LNCaP."; RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Aortic endothelium; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RT "Homo sapiens protein coding cDNA."; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-457 (ISOFORM 1). RX PubMed=9001212; DOI=10.1128/mcb.17.2.594; RA Nair S.C., Rimerman R.A., Toran E.J., Chen S., Prapapanich V., Butts R.N., RA Smith D.F.; RT "Molecular cloning of human FKBP51 and comparisons of immunophilin RT interactions with Hsp90 and progesterone receptor."; RL Mol. Cell. Biol. 17:594-603(1997). RN [9] RP SUBUNIT. RX PubMed=7693698; DOI=10.1016/s0021-9258(20)80520-1; RA Smith D.F., Albers M.W., Schreiber S.L., Leach K.L., Deibel M.R. Jr.; RT "FKBP54, a novel FK506-binding protein in avian progesterone receptor RT complexes and HeLa extracts."; RL J. Biol. Chem. 268:24270-24273(1993). RN [10] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=11350175; DOI=10.1006/jmbi.2001.4595; RA Pirkl F., Buchner J.; RT "Functional analysis of the Hsp90-associated human peptidyl prolyl RT cis/trans isomerases FKBP51, FKBP52 and Cyp40."; RL J. Mol. Biol. 308:795-806(2001). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND SER-445, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [20] RP FUNCTION, AND INTERACTION WITH IKBKB AND IKBKE. RX PubMed=26101251; DOI=10.1093/nar/gkv615; RA Romano S., Xiao Y., Nakaya M., D'Angelillo A., Chang M., Jin J., Hausch F., RA Masullo M., Feng X., Romano M.F., Sun S.C.; RT "FKBP51 employs both scaffold and isomerase functions to promote NF-kappaB RT activation in melanoma."; RL Nucleic Acids Res. 43:6983-6993(2015). RN [21] RP FUNCTION, INTERACTION WITH AKT1 AND PHLPP1, ACETYLATION AT LYS-28 AND RP LYS-155, AND MUTAGENESIS OF LYS-28 AND LYS-155. RX PubMed=28147277; DOI=10.1016/j.celrep.2017.01.009; RA Yu J., Qin B., Wu F., Qin S., Nowsheen S., Shan S., Zayas J., Pei H., RA Lou Z., Wang L.; RT "Regulation of serine-threonine kinase Akt activation by NAD+-dependent RT deacetylase SIRT7."; RL Cell Rep. 18:1229-1240(2017). RN [22] RP FUNCTION, AND DEUBIQUITINATION BY USP49. RX PubMed=28363942; DOI=10.15252/embj.201695669; RA Luo K., Li Y., Yin Y., Li L., Wu C., Chen Y., Nowsheen S., Hu Q., Zhang L., RA Lou Z., Yuan J.; RT "USP49 negatively regulates tumorigenesis and chemoresistance through RT FKBP51-AKT signaling."; RL EMBO J. 36:1434-1446(2017). RN [23] RP FUNCTION, AND INTERACTION WITH IFI44L; IKBKB AND IKBKE. RX PubMed=31434731; DOI=10.1128/jvi.01159-19; RA DeDiego M.L., Martinez-Sobrido L., Topham D.J.; RT "Novel Functions of IFI44L as a Feedback Regulator of Host Antiviral RT Responses."; RL J. Virol. 93:0-0(2019). RN [24] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), AND FUNCTION. RX PubMed=12538866; DOI=10.1073/pnas.0231020100; RA Sinars C.R., Cheung-Flynn J., Rimerman R.A., Scammell J.G., Smith D.F., RA Clardy J.; RT "Structure of the large FK506-binding protein FKBP51, an Hsp90-binding RT protein and a component of steroid receptor complexes."; RL Proc. Natl. Acad. Sci. U.S.A. 100:868-873(2003). CC -!- FUNCTION: Immunophilin protein with PPIase and co-chaperone activities CC (PubMed:11350175). Component of unligated steroid receptors CC heterocomplexes through interaction with heat-shock protein 90 (HSP90). CC Plays a role in the intracellular trafficking of heterooligomeric forms CC of steroid hormone receptors maintaining the complex into the cytoplasm CC when unliganded (PubMed:12538866). Acts as a regulator of Akt/AKT1 CC activity by promoting the interaction between Akt/AKT1 and PHLPP1, CC thereby enhancing dephosphorylation and subsequent activation of CC Akt/AKT1 (PubMed:28147277, PubMed:28363942). Interacts with IKBKE and CC IKBKB which facilitates IKK complex assembly leading to increased IKBKE CC and IKBKB kinase activity, NF-kappa-B activation, and IFN production CC (PubMed:26101251, PubMed:31434731). {ECO:0000269|PubMed:11350175, CC ECO:0000269|PubMed:12538866, ECO:0000269|PubMed:26101251, CC ECO:0000269|PubMed:28147277, ECO:0000269|PubMed:28363942, CC ECO:0000269|PubMed:31434731}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[protein]-peptidylproline (omega=180) = [protein]- CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA- CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, CC ChEBI:CHEBI:83834; EC=5.2.1.8; CC Evidence={ECO:0000269|PubMed:11350175}; CC -!- ACTIVITY REGULATION: Inhibited by both FK506 and rapamycin. CC {ECO:0000250|UniProtKB:Q64378}. CC -!- SUBUNIT: Part of a heteromultimeric cytoplasmic complex with HSP90AA1, CC HSPA1A/HSPA1B and steroid receptors. Upon ligand binding dissociates CC from the complex and FKBP4 takes its place (By similarity). Interacts CC with functionally mature heterooligomeric progesterone receptor CC complexes along with HSP90 and TEBP (PubMed:7693698). Interacts with CC NR3C1 (By similarity). Interacts with Akt/AKT1 and PHLPP1; enhancing CC dephosphorylation and subsequent activation of Akt/AKT1 CC (PubMed:28147277). Interacts with IFI44L; this interaction modulates CC the kinase activity of IKBKB and IKBKE (PubMed:31434731). Interacts CC with IKBKB and IKBKE (PubMed:26101251, PubMed:31434731). CC {ECO:0000250|UniProtKB:Q64378, ECO:0000269|PubMed:28147277, CC ECO:0000269|PubMed:31434731, ECO:0000269|PubMed:7693698}. CC -!- INTERACTION: CC Q13451; Q96Q40: CDK15; NbExp=5; IntAct=EBI-306914, EBI-1051975; CC Q13451; P50750: CDK9; NbExp=11; IntAct=EBI-306914, EBI-1383449; CC Q13451; O15111: CHUK; NbExp=6; IntAct=EBI-306914, EBI-81249; CC Q13451; Q9UPZ9: CILK1; NbExp=3; IntAct=EBI-306914, EBI-6381479; CC Q13451; P00533: EGFR; NbExp=2; IntAct=EBI-306914, EBI-297353; CC Q13451; P07900: HSP90AA1; NbExp=9; IntAct=EBI-306914, EBI-296047; CC Q13451; P08238: HSP90AB1; NbExp=17; IntAct=EBI-306914, EBI-352572; CC Q13451; Q6VAB6: KSR2; NbExp=7; IntAct=EBI-306914, EBI-6424389; CC Q13451; P10636-8: MAPT; NbExp=8; IntAct=EBI-306914, EBI-366233; CC Q13451; P33993: MCM7; NbExp=2; IntAct=EBI-306914, EBI-355924; CC Q13451; Q9BTE3-2: MCMBP; NbExp=4; IntAct=EBI-306914, EBI-9384556; CC Q13451; P00540: MOS; NbExp=5; IntAct=EBI-306914, EBI-1757866; CC Q13451; P11216: PYGB; NbExp=2; IntAct=EBI-306914, EBI-1047231; CC Q13451; O00141: SGK1; NbExp=2; IntAct=EBI-306914, EBI-1042854; CC Q13451; Q15831: STK11; NbExp=11; IntAct=EBI-306914, EBI-306838; CC Q13451; Q6PHR2: ULK3; NbExp=3; IntAct=EBI-306914, EBI-1383475; CC Q13451; Q70CQ1: USP49; NbExp=2; IntAct=EBI-306914, EBI-2511022; CC Q13451; PRO_0000037552 [Q9WMX2]; Xeno; NbExp=4; IntAct=EBI-306914, EBI-9005440; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q64378}. Nucleus CC {ECO:0000250|UniProtKB:Q64378}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q13451-1; Sequence=Displayed; CC Name=2; CC IsoId=Q13451-2; Sequence=VSP_044820, VSP_044821; CC -!- TISSUE SPECIFICITY: Widely expressed, enriched in testis compared to CC other tissues. CC -!- INDUCTION: By androgen. CC -!- PTM: Acetylation impairs ability to promote interaction between CC Akt/AKT1 and PHLPP1 (PubMed:28147277). Deacetylation by SIRT7 promotes CC interaction between Akt/AKT1 and PHLPP1, leading to suppress Akt/AKT1 CC activation (PubMed:28147277). {ECO:0000269|PubMed:28147277}. CC -!- PTM: Ubiquitinated, leading to degradation in a proteasome-dependent CC manner. Deubiquitinated by USP49, leading to stabilization. CC {ECO:0000269|PubMed:28363942}. CC -!- SEQUENCE CAUTION: CC Sequence=BAD93130.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U71321; AAC51189.1; -; mRNA. DR EMBL; AF194172; AAL54872.1; -; mRNA. DR EMBL; AK312422; BAG35332.1; -; mRNA. DR EMBL; AB209893; BAD93130.1; ALT_FRAME; mRNA. DR EMBL; AL033519; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL157823; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL590400; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471081; EAX03842.1; -; Genomic_DNA. DR EMBL; BC042605; AAH42605.1; -; mRNA. DR EMBL; U42031; AAA86245.1; -; mRNA. DR CCDS; CCDS4808.1; -. [Q13451-1] DR CCDS; CCDS54996.1; -. [Q13451-2] DR PIR; JC5422; JC5422. DR RefSeq; NP_001139247.1; NM_001145775.3. [Q13451-1] DR RefSeq; NP_001139248.1; NM_001145776.2. [Q13451-1] DR RefSeq; NP_001139249.1; NM_001145777.2. [Q13451-2] DR RefSeq; NP_004108.1; NM_004117.4. [Q13451-1] DR PDB; 1KT0; X-ray; 2.70 A; A=1-457. DR PDB; 3O5D; X-ray; 4.00 A; A/B=1-260. DR PDB; 3O5E; X-ray; 1.60 A; A=1-140. DR PDB; 3O5F; X-ray; 1.65 A; A=1-140. DR PDB; 3O5G; X-ray; 2.00 A; A=16-140. DR PDB; 3O5I; X-ray; 1.80 A; A/B=16-140. DR PDB; 3O5J; X-ray; 1.70 A; A=16-140. DR PDB; 3O5K; X-ray; 2.70 A; A/B/C/D=16-140. DR PDB; 3O5L; X-ray; 1.30 A; A=16-140. DR PDB; 3O5M; X-ray; 1.60 A; A/B=16-140. DR PDB; 3O5O; X-ray; 1.15 A; A=16-140. DR PDB; 3O5P; X-ray; 1.00 A; A=16-140. DR PDB; 3O5Q; X-ray; 0.96 A; A=16-140. DR PDB; 3O5R; X-ray; 1.10 A; A=16-140. DR PDB; 4DRH; X-ray; 2.30 A; A/D=1-140. DR PDB; 4DRI; X-ray; 1.45 A; A=1-140. DR PDB; 4DRK; X-ray; 1.50 A; A/B=16-140. DR PDB; 4DRM; X-ray; 1.48 A; A=16-140. DR PDB; 4DRN; X-ray; 1.07 A; A=16-140. DR PDB; 4DRO; X-ray; 1.10 A; A=16-140. DR PDB; 4DRP; X-ray; 1.80 A; A=16-140. DR PDB; 4DRQ; X-ray; 1.00 A; A=16-140. DR PDB; 4JFI; X-ray; 1.05 A; A=16-139. DR PDB; 4JFJ; X-ray; 1.08 A; A=16-140. DR PDB; 4JFK; X-ray; 1.15 A; A=16-140. DR PDB; 4JFL; X-ray; 1.20 A; A=16-140. DR PDB; 4JFM; X-ray; 1.02 A; A=16-140. DR PDB; 4R0X; X-ray; 1.20 A; A=20-140. DR PDB; 4TW6; X-ray; 1.40 A; A=16-140. DR PDB; 4TW7; X-ray; 1.25 A; A=16-140. DR PDB; 4TX0; X-ray; 1.03 A; A=16-140. DR PDB; 4W9O; X-ray; 1.27 A; A/E=16-140. DR PDB; 4W9P; X-ray; 1.50 A; A/E=16-140. DR PDB; 4W9Q; X-ray; 1.08 A; A=16-140. DR PDB; 5BXJ; X-ray; 1.24 A; A=16-140. DR PDB; 5DIT; X-ray; 2.25 A; A=16-140. DR PDB; 5DIU; X-ray; 1.30 A; A=16-140. DR PDB; 5DIV; X-ray; 1.65 A; A=16-139. DR PDB; 5NJX; X-ray; 2.49 A; A=1-457. DR PDB; 5OBK; X-ray; 1.00 A; A=16-140. DR PDB; 5OMP; X-ray; 1.88 A; A=1-457. DR PDB; 6SAF; X-ray; 2.05 A; A=16-140. DR PDB; 6TX4; X-ray; 1.06 A; A=16-140. DR PDB; 6TX5; X-ray; 1.08 A; A=16-140. DR PDB; 6TX6; X-ray; 0.98 A; A=16-140. DR PDB; 6TX7; X-ray; 1.13 A; A=16-140. DR PDB; 6TX8; X-ray; 1.20 A; A=16-140. DR PDB; 6TX9; X-ray; 1.42 A; A=16-140. DR PDB; 6TXX; X-ray; 2.10 A; A/B=16-140. DR PDB; 7A6W; X-ray; 1.85 A; AAA/BBB=16-140. DR PDB; 7A6X; X-ray; 1.67 A; AAA=16-140. DR PDB; 7AOT; X-ray; 0.85 A; A=16-140. DR PDB; 7AOU; X-ray; 1.16 A; A=16-140. DR PDB; 7APQ; X-ray; 1.09 A; A=16-140. DR PDB; 7APS; X-ray; 0.94 A; A/B=16-140. DR PDB; 7APT; X-ray; 1.13 A; A=16-140. DR PDB; 7APW; X-ray; 0.89 A; A=16-140. DR PDB; 7AWF; X-ray; 1.40 A; A=16-140. DR PDB; 7AWX; X-ray; 2.20 A; A/B=16-140. DR PDB; 7B9Y; X-ray; 1.35 A; A=16-140. DR PDB; 7B9Z; X-ray; 1.44 A; A=16-140. DR PDB; 7BA0; X-ray; 1.14 A; A=16-140. DR PDB; 7ETT; X-ray; 1.50 A; A=16-140. DR PDB; 7ETU; X-ray; 1.39 A; A=16-140. DR PDB; 7ETV; X-ray; 1.31 A; A=16-140. DR PDB; 7L7I; EM; 3.30 A; C=1-457. DR PDB; 7R0L; X-ray; 1.10 A; A=16-140. DR PDB; 8BA6; X-ray; 1.10 A; A=16-140. DR PDB; 8BAJ; X-ray; 1.20 A; A=16-140. DR PDB; 8CCA; X-ray; 1.33 A; A=16-140. DR PDB; 8CCB; X-ray; 1.70 A; A=16-140. DR PDB; 8CCC; X-ray; 1.55 A; A=16-140. DR PDB; 8CCD; X-ray; 2.10 A; A=16-140. DR PDB; 8CCE; X-ray; 1.40 A; A=16-140. DR PDB; 8CCF; X-ray; 2.00 A; A=16-140. DR PDB; 8CCG; X-ray; 1.30 A; A=16-140. DR PDB; 8CCH; X-ray; 1.73 A; A=16-140. DR PDB; 8CHN; X-ray; 0.99 A; A=16-140. DR PDB; 8CHP; X-ray; 1.00 A; A=16-140. DR PDB; 8CHQ; X-ray; 1.01 A; A=16-140. DR PDB; 8CHR; X-ray; 1.10 A; A=16-140. DR PDB; 8FFW; EM; 3.23 A; D=2-457. DR PDB; 8PC2; X-ray; 2.80 A; G/H=16-140. DR PDB; 8PJ8; X-ray; 1.50 A; A=16-140. DR PDB; 8PJA; X-ray; 1.60 A; A=16-140. DR PDB; 8R5K; X-ray; 0.89 A; A=16-140. DR PDB; 9EU6; X-ray; 1.54 A; A/B=16-140. DR PDB; 9EU7; X-ray; 2.21 A; A/B=16-140. DR PDB; 9EU8; X-ray; 2.30 A; A/B=16-140. DR PDB; 9EU9; X-ray; 1.80 A; A/B=16-140. DR PDB; 9EUA; X-ray; 2.50 A; A/B=16-140. DR PDB; 9EUB; X-ray; 2.00 A; A/B=16-140. DR PDB; 9EUC; X-ray; 2.40 A; A/B=16-140. DR PDB; 9EUD; X-ray; 2.02 A; A/B=16-140. DR PDB; 9EUE; X-ray; 2.00 A; A/B=16-140. DR PDB; 9EY3; X-ray; 1.16 A; A=16-140. DR PDB; 9EY4; X-ray; 1.16 A; A=16-140. DR PDB; 9GPK; X-ray; 1.75 A; A/B=16-140. DR PDB; 9GPL; X-ray; 1.80 A; A/B=16-140. DR PDB; 9GPM; X-ray; 1.55 A; A/B=16-140. DR PDB; 9GPN; X-ray; 1.80 A; A/B=16-140. DR PDB; 9GPO; X-ray; 1.68 A; A/B=16-140. DR PDB; 9GPP; X-ray; 2.10 A; A/B=16-140. DR PDB; 9GPQ; X-ray; 1.35 A; A/B=16-140. DR PDB; 9GPR; X-ray; 1.75 A; A/B=16-140. DR PDB; 9GPS; X-ray; 1.90 A; A/B=16-140. DR PDB; 9GPT; X-ray; 2.00 A; A/B=16-140. DR PDB; 9GPU; X-ray; 1.36 A; A/B=16-140. DR PDB; 9GPV; X-ray; 1.70 A; A/B=16-140. DR PDB; 9GPW; X-ray; 1.74 A; A/B=16-140. DR PDB; 9GPX; X-ray; 1.80 A; A/B=16-140. DR PDB; 9GPY; X-ray; 1.50 A; A/B/C=16-140. DR PDB; 9GPZ; X-ray; 1.80 A; A/B=16-140. DR PDB; 9GQ2; X-ray; 2.30 A; A/B=16-140. DR PDB; 9GQ3; X-ray; 2.30 A; A/B=16-140. DR PDB; 9GQ4; X-ray; 1.80 A; A/B=16-140. DR PDB; 9GQ5; X-ray; 1.93 A; A/B=16-140. DR PDB; 9GQ6; X-ray; 1.88 A; A/B=16-140. DR PDB; 9GQ7; X-ray; 2.30 A; A/B=16-140. DR PDB; 9GQ8; X-ray; 2.16 A; A/B=16-140. DR PDB; 9GQ9; X-ray; 2.00 A; A/B=16-140. DR PDB; 9GQA; X-ray; 1.93 A; A/B=16-140. DR PDB; 9GQB; X-ray; 2.00 A; A/B=16-140. DR PDB; 9GQC; X-ray; 2.50 A; A/B=16-140. DR PDB; 9GQD; X-ray; 2.50 A; A/B=16-140. DR PDB; 9GQE; X-ray; 2.50 A; A/B=16-140. DR PDB; 9GQF; X-ray; 1.80 A; A/B=16-140. DR PDB; 9GQG; X-ray; 2.00 A; A/B=16-140. DR PDB; 9GQH; X-ray; 2.60 A; A/B=16-140. DR PDB; 9GQI; X-ray; 1.50 A; A/B=16-140. DR PDB; 9GQJ; X-ray; 1.65 A; A/B=16-140. DR PDB; 9GQK; X-ray; 1.70 A; A/B=16-140. DR PDBsum; 1KT0; -. DR PDBsum; 3O5D; -. DR PDBsum; 3O5E; -. DR PDBsum; 3O5F; -. DR PDBsum; 3O5G; -. DR PDBsum; 3O5I; -. DR PDBsum; 3O5J; -. DR PDBsum; 3O5K; -. DR PDBsum; 3O5L; -. DR PDBsum; 3O5M; -. DR PDBsum; 3O5O; -. DR PDBsum; 3O5P; -. DR PDBsum; 3O5Q; -. DR PDBsum; 3O5R; -. DR PDBsum; 4DRH; -. DR PDBsum; 4DRI; -. DR PDBsum; 4DRK; -. DR PDBsum; 4DRM; -. DR PDBsum; 4DRN; -. DR PDBsum; 4DRO; -. DR PDBsum; 4DRP; -. DR PDBsum; 4DRQ; -. DR PDBsum; 4JFI; -. DR PDBsum; 4JFJ; -. DR PDBsum; 4JFK; -. DR PDBsum; 4JFL; -. DR PDBsum; 4JFM; -. DR PDBsum; 4R0X; -. DR PDBsum; 4TW6; -. DR PDBsum; 4TW7; -. DR PDBsum; 4TX0; -. DR PDBsum; 4W9O; -. DR PDBsum; 4W9P; -. DR PDBsum; 4W9Q; -. DR PDBsum; 5BXJ; -. DR PDBsum; 5DIT; -. DR PDBsum; 5DIU; -. DR PDBsum; 5DIV; -. DR PDBsum; 5NJX; -. DR PDBsum; 5OBK; -. DR PDBsum; 5OMP; -. DR PDBsum; 6SAF; -. DR PDBsum; 6TX4; -. DR PDBsum; 6TX5; -. DR PDBsum; 6TX6; -. DR PDBsum; 6TX7; -. DR PDBsum; 6TX8; -. DR PDBsum; 6TX9; -. DR PDBsum; 6TXX; -. DR PDBsum; 7A6W; -. DR PDBsum; 7A6X; -. DR PDBsum; 7AOT; -. DR PDBsum; 7AOU; -. DR PDBsum; 7APQ; -. DR PDBsum; 7APS; -. DR PDBsum; 7APT; -. DR PDBsum; 7APW; -. DR PDBsum; 7AWF; -. DR PDBsum; 7AWX; -. DR PDBsum; 7B9Y; -. DR PDBsum; 7B9Z; -. DR PDBsum; 7BA0; -. DR PDBsum; 7ETT; -. DR PDBsum; 7ETU; -. DR PDBsum; 7ETV; -. DR PDBsum; 7L7I; -. DR PDBsum; 7R0L; -. DR PDBsum; 8BA6; -. DR PDBsum; 8BAJ; -. DR PDBsum; 8CCA; -. DR PDBsum; 8CCB; -. DR PDBsum; 8CCC; -. DR PDBsum; 8CCD; -. DR PDBsum; 8CCE; -. DR PDBsum; 8CCF; -. DR PDBsum; 8CCG; -. DR PDBsum; 8CCH; -. DR PDBsum; 8CHN; -. DR PDBsum; 8CHP; -. DR PDBsum; 8CHQ; -. DR PDBsum; 8CHR; -. DR PDBsum; 8FFW; -. DR PDBsum; 8PC2; -. DR PDBsum; 8PJ8; -. DR PDBsum; 8PJA; -. DR PDBsum; 8R5K; -. DR PDBsum; 9EU6; -. DR PDBsum; 9EU7; -. DR PDBsum; 9EU8; -. DR PDBsum; 9EU9; -. DR PDBsum; 9EUA; -. DR PDBsum; 9EUB; -. DR PDBsum; 9EUC; -. DR PDBsum; 9EUD; -. DR PDBsum; 9EUE; -. DR PDBsum; 9EY3; -. DR PDBsum; 9EY4; -. DR PDBsum; 9GPK; -. DR PDBsum; 9GPL; -. DR PDBsum; 9GPM; -. DR PDBsum; 9GPN; -. DR PDBsum; 9GPO; -. DR PDBsum; 9GPP; -. DR PDBsum; 9GPQ; -. DR PDBsum; 9GPR; -. DR PDBsum; 9GPS; -. DR PDBsum; 9GPT; -. DR PDBsum; 9GPU; -. DR PDBsum; 9GPV; -. DR PDBsum; 9GPW; -. DR PDBsum; 9GPX; -. DR PDBsum; 9GPY; -. DR PDBsum; 9GPZ; -. DR PDBsum; 9GQ2; -. DR PDBsum; 9GQ3; -. DR PDBsum; 9GQ4; -. DR PDBsum; 9GQ5; -. DR PDBsum; 9GQ6; -. DR PDBsum; 9GQ7; -. DR PDBsum; 9GQ8; -. DR PDBsum; 9GQ9; -. DR PDBsum; 9GQA; -. DR PDBsum; 9GQB; -. DR PDBsum; 9GQC; -. DR PDBsum; 9GQD; -. DR PDBsum; 9GQE; -. DR PDBsum; 9GQF; -. DR PDBsum; 9GQG; -. DR PDBsum; 9GQH; -. DR PDBsum; 9GQI; -. DR PDBsum; 9GQJ; -. DR PDBsum; 9GQK; -. DR AlphaFoldDB; Q13451; -. DR EMDB; EMD-23213; -. DR EMDB; EMD-29069; -. DR SMR; Q13451; -. DR BioGRID; 108579; 438. DR CORUM; Q13451; -. DR DIP; DIP-27597N; -. DR FunCoup; Q13451; 2990. DR IntAct; Q13451; 384. DR MINT; Q13451; -. DR STRING; 9606.ENSP00000444810; -. DR BindingDB; Q13451; -. DR ChEMBL; CHEMBL2052031; -. DR DrugCentral; Q13451; -. DR GuidetoPHARMACOLOGY; 3175; -. DR GlyGen; Q13451; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q13451; -. DR MetOSite; Q13451; -. DR PhosphoSitePlus; Q13451; -. DR SwissPalm; Q13451; -. DR BioMuta; FKBP5; -. DR DMDM; 2851536; -. DR CPTAC; CPTAC-506; -. DR CPTAC; CPTAC-507; -. DR jPOST; Q13451; -. DR MassIVE; Q13451; -. DR PaxDb; 9606-ENSP00000444810; -. DR PeptideAtlas; Q13451; -. DR ProteomicsDB; 27564; -. DR ProteomicsDB; 59455; -. [Q13451-1] DR Pumba; Q13451; -. DR Antibodypedia; 3988; 465 antibodies from 36 providers. DR DNASU; 2289; -. DR Ensembl; ENST00000357266.9; ENSP00000349811.3; ENSG00000096060.16. [Q13451-1] DR Ensembl; ENST00000536438.5; ENSP00000444810.1; ENSG00000096060.16. [Q13451-1] DR Ensembl; ENST00000539068.5; ENSP00000441205.1; ENSG00000096060.16. [Q13451-1] DR Ensembl; ENST00000542713.1; ENSP00000442340.1; ENSG00000096060.16. [Q13451-2] DR GeneID; 2289; -. DR KEGG; hsa:2289; -. DR MANE-Select; ENST00000357266.9; ENSP00000349811.3; NM_004117.4; NP_004108.1. DR UCSC; uc003okx.3; human. [Q13451-1] DR AGR; HGNC:3721; -. DR ClinPGx; PA28162; -. DR CTD; 2289; -. DR DisGeNET; 2289; -. DR GeneCards; FKBP5; -. DR HGNC; HGNC:3721; FKBP5. DR HPA; ENSG00000096060; Tissue enhanced (skeletal muscle, tongue). DR MalaCards; FKBP5; -. DR MIM; 602623; gene. DR OpenTargets; ENSG00000096060; -. DR VEuPathDB; HostDB:ENSG00000096060; -. DR eggNOG; KOG0543; Eukaryota. DR GeneTree; ENSGT00940000158726; -. DR HOGENOM; CLU_013615_13_1_1; -. DR InParanoid; Q13451; -. DR OMA; QAILTIH; -. DR OrthoDB; 433738at2759; -. DR PAN-GO; Q13451; 4 GO annotations based on evolutionary models. DR PhylomeDB; Q13451; -. DR PathwayCommons; Q13451; -. DR Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand. DR Reactome; R-HSA-8939211; ESR-mediated signaling. DR Reactome; R-HSA-9022699; MECP2 regulates neuronal receptors and channels. DR Reactome; R-HSA-9909505; Modulation of host responses by IFN-stimulated genes. DR SignaLink; Q13451; -. DR SIGNOR; Q13451; -. DR Agora; ENSG00000096060; Agora Nominated Target for Alzheimer's Disease. DR BioGRID-ORCS; 2289; 13 hits in 1167 CRISPR screens. DR ChiTaRS; FKBP5; human. DR EvolutionaryTrace; Q13451; -. DR GeneWiki; FKBP5; -. DR GenomeRNAi; 2289; -. DR Pharos; Q13451; Tchem. DR PRO; PR:Q13451; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q13451; protein. DR Bgee; ENSG00000096060; Expressed in mucosa of stomach and 192 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IC:UniProt. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005528; F:FK506 binding; TAS:ProtInc. DR GO; GO:0031072; F:heat shock protein binding; IPI:UniProtKB. DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:UniProtKB. DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:UniProt. DR GO; GO:0051898; P:negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IDA:UniProt. DR GO; GO:0006457; P:protein folding; IDA:UniProtKB. DR GO; GO:0097305; P:response to alcohol; IEA:Ensembl. DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl. DR GO; GO:0042220; P:response to cocaine; IEA:Ensembl. DR DisProt; DP01845; -. DR FunFam; 1.25.40.10:FF:000008; Peptidylprolyl isomerase; 1. DR FunFam; 3.10.50.40:FF:000011; Peptidylprolyl isomerase; 1. DR FunFam; 3.10.50.40:FF:000013; Peptidylprolyl isomerase; 1. DR Gene3D; 3.10.50.40; -; 2. DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1. DR IDEAL; IID00073; -. DR InterPro; IPR050754; FKBP4/5/8-like. DR InterPro; IPR046357; PPIase_dom_sf. DR InterPro; IPR001179; PPIase_FKBP_dom. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR InterPro; IPR019734; TPR_rpt. DR PANTHER; PTHR46512; PEPTIDYLPROLYL ISOMERASE; 1. DR PANTHER; PTHR46512:SF9; PEPTIDYLPROLYL ISOMERASE; 1. DR Pfam; PF00254; FKBP_C; 2. DR Pfam; PF00515; TPR_1; 1. DR Pfam; PF13181; TPR_8; 1. DR SMART; SM00028; TPR; 2. DR SUPFAM; SSF54534; FKBP-like; 2. DR SUPFAM; SSF48452; TPR-like; 1. DR PROSITE; PS50059; FKBP_PPIASE; 2. DR PROSITE; PS50005; TPR; 3. DR PROSITE; PS50293; TPR_REGION; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Chaperone; Cytoplasm; KW Isomerase; Nucleus; Phosphoprotein; Proteomics identification; KW Reference proteome; Repeat; Rotamase; TPR repeat; Ubl conjugation. FT CHAIN 1..457 FT /note="Peptidyl-prolyl cis-trans isomerase FKBP5" FT /id="PRO_0000075324" FT DOMAIN 42..130 FT /note="PPIase FKBP-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277" FT DOMAIN 157..243 FT /note="PPIase FKBP-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277" FT REPEAT 268..301 FT /note="TPR 1" FT REPEAT 317..350 FT /note="TPR 2" FT REPEAT 351..384 FT /note="TPR 3" FT REGION 1..24 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 420..457 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..11 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:19413330" FT MOD_RES 13 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 28 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:28147277" FT MOD_RES 155 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:28147277" FT MOD_RES 445 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17525332, FT ECO:0007744|PubMed:23186163" FT VAR_SEQ 223..268 FT /note="YGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQA -> PK FT NPGRWIPKKNWSRLPLSKRREPYTSRCVSPYAILSISKNLFKCW (in isoform FT 2)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_044820" FT VAR_SEQ 269..457 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_044821" FT MUTAGEN 28 FT /note="K->Q: Mimics acetylation; impaired interaction with FT AKT1 and PHLPP1; when associated with Q-155." FT /evidence="ECO:0000269|PubMed:28147277" FT MUTAGEN 28 FT /note="K->R: Decreased acetylation; promotes interaction FT with AKT1 and PHLPP1; when associated with R-155." FT /evidence="ECO:0000269|PubMed:28147277" FT MUTAGEN 155 FT /note="K->Q: Mimics acetylation; impaired interaction with FT AKT1 and PHLPP1; when associated with Q-28." FT /evidence="ECO:0000269|PubMed:28147277" FT MUTAGEN 155 FT /note="K->R: Decreased acetylation; promotes interaction FT with AKT1 and PHLPP1; when associated with R-28." FT /evidence="ECO:0000269|PubMed:28147277" FT HELIX 16..21 FT /evidence="ECO:0007829|PDB:7AOT" FT STRAND 22..24 FT /evidence="ECO:0007829|PDB:7BA0" FT STRAND 26..28 FT /evidence="ECO:0007829|PDB:4DRH" FT STRAND 33..39 FT /evidence="ECO:0007829|PDB:7AOT" FT STRAND 42..44 FT /evidence="ECO:0007829|PDB:7AOT" FT STRAND 52..61 FT /evidence="ECO:0007829|PDB:7AOT" FT STRAND 66..70 FT /evidence="ECO:0007829|PDB:7APW" FT STRAND 73..75 FT /evidence="ECO:0007829|PDB:7AOT" FT STRAND 77..80 FT /evidence="ECO:0007829|PDB:7AOT" FT STRAND 83..86 FT /evidence="ECO:0007829|PDB:7AOT" FT HELIX 88..94 FT /evidence="ECO:0007829|PDB:7AOT" FT STRAND 102..107 FT /evidence="ECO:0007829|PDB:7AOT" FT HELIX 109..111 FT /evidence="ECO:0007829|PDB:7AOT" FT TURN 112..116 FT /evidence="ECO:0007829|PDB:7AOT" FT TURN 119..121 FT /evidence="ECO:0007829|PDB:7AOT" FT STRAND 128..138 FT /evidence="ECO:0007829|PDB:7AOT" FT STRAND 144..154 FT /evidence="ECO:0007829|PDB:5OMP" FT STRAND 167..176 FT /evidence="ECO:0007829|PDB:5OMP" FT STRAND 179..189 FT /evidence="ECO:0007829|PDB:5OMP" FT HELIX 193..196 FT /evidence="ECO:0007829|PDB:5OMP" FT HELIX 200..206 FT /evidence="ECO:0007829|PDB:5OMP" FT STRAND 214..219 FT /evidence="ECO:0007829|PDB:5OMP" FT TURN 221..223 FT /evidence="ECO:0007829|PDB:5OMP" FT HELIX 226..228 FT /evidence="ECO:0007829|PDB:5NJX" FT HELIX 231..233 FT /evidence="ECO:0007829|PDB:5OMP" FT TURN 236..239 FT /evidence="ECO:0007829|PDB:8FFW" FT STRAND 241..251 FT /evidence="ECO:0007829|PDB:5OMP" FT HELIX 256..258 FT /evidence="ECO:0007829|PDB:5OMP" FT HELIX 261..280 FT /evidence="ECO:0007829|PDB:5OMP" FT HELIX 284..298 FT /evidence="ECO:0007829|PDB:5OMP" FT HELIX 306..329 FT /evidence="ECO:0007829|PDB:5OMP" FT HELIX 333..346 FT /evidence="ECO:0007829|PDB:5OMP" FT HELIX 351..363 FT /evidence="ECO:0007829|PDB:5OMP" FT HELIX 367..380 FT /evidence="ECO:0007829|PDB:5OMP" FT HELIX 385..423 FT /evidence="ECO:0007829|PDB:5OMP" SQ 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 //