ID   1433E_HUMAN             Reviewed;         255 AA.
AC   P62258; B3KY71; D3DTH5; P29360; P42655; Q4VJB6; Q53XZ5; Q63631; Q7M4R4;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   12-OCT-2022, entry version 198.
DE   RecName: Full=14-3-3 protein epsilon;
DE            Short=14-3-3E;
GN   Name=YWHAE;
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).
RX   PubMed=7644510; DOI=10.1073/pnas.92.17.7892;
RA   Conklin D.S., Galaktionov K., Beach D.;
RT   "14-3-3 proteins associate with cdc25 phosphatases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:7892-7896(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Liver;
RX   PubMed=8858348; DOI=10.1101/gr.6.8.735;
RA   Chong S.S., Tanigami A., Roschke A.V., Ledbetter D.H.;
RT   "14-3-3 epsilon has no homology to LIS1 and lies telomeric to it on
RT   chromosome 17p13.3 outside the Miller-Dieker syndrome chromosome region.";
RL   Genome Res. 6:735-741(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=8684458; DOI=10.1038/382308a0;
RA   Jin D.-Y., Lyu M.S., Kozak C.A., Jeang K.-T.;
RT   "Function of 14-3-3 proteins.";
RL   Nature 382:308-308(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SV), AND ALTERNATIVE SPLICING.
RC   TISSUE=Brain;
RX   PubMed=20417184; DOI=10.1016/j.bbrc.2010.04.104;
RA   Han D., Ye G., Liu T., Chen C., Yang X., Wan B., Pan Y., Yu L.;
RT   "Functional identification of a novel 14-3-3 epsilon splicing variant
RT   suggests dimerization is not necessary for 14-3-3 epsilon to inhibit UV-
RT   induced apoptosis.";
RL   Biochem. Biophys. Res. Commun. 396:401-406(2010).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Heart;
RA   Luk S.C.W., Lee C.Y., Waye M.M.Y.;
RT   "Sequence determination of human epsilon 14-3-3 protein.";
RL   Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Tanigami A., Chong S.S., Ledbetter D.H.;
RT   "14-3-3 epsilon genomic sequence.";
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND SV).
RC   TISSUE=Caudate nucleus, Heart, and Subthalamic nucleus;
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   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Placenta;
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   [11]
RP   PROTEIN SEQUENCE OF 1-19.
RC   TISSUE=Platelet;
RX   PubMed=12665801; DOI=10.1038/nbt810;
RA   Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA   Vandekerckhove J.;
RT   "Exploring proteomes and analyzing protein processing by mass spectrometric
RT   identification of sorted N-terminal peptides.";
RL   Nat. Biotechnol. 21:566-569(2003).
RN   [12]
RP   PROTEIN SEQUENCE OF 1-56; 62-73; 95-118; 131-193 AND 197-255, INTERACTION
RP   WITH PI4KB; TBC1D22A AND TBC1D22B, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=23572552; DOI=10.1128/mbio.00098-13;
RA   Greninger A.L., Knudsen G.M., Betegon M., Burlingame A.L., DeRisi J.L.;
RT   "ACBD3 interaction with TBC1 domain 22 protein is differentially affected
RT   by enteroviral and kobuviral 3A protein binding.";
RL   MBio 4:E00098-E00098(2013).
RN   [13]
RP   PROTEIN SEQUENCE OF 1-19; 30-50 AND 131-170, ACETYLATION AT MET-1, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RA   Bienvenut W.V.;
RL   Submitted (MAY-2005) to UniProtKB.
RN   [14]
RP   PROTEIN SEQUENCE OF 50-60, AND INTERACTION WITH KSR1.
RX   PubMed=10409742; DOI=10.1128/mcb.19.8.5523;
RA   Stewart S., Sundaram M., Zhang Y., Lee J., Han M., Guan K.L.;
RT   "Kinase suppressor of Ras forms a multiprotein signaling complex and
RT   modulates MEK localization.";
RL   Mol. Cell. Biol. 19:5523-5534(1999).
RN   [15]
RP   PROTEIN SEQUENCE OF 103-108; 120-123; 131-141 AND 143-153.
RC   TISSUE=Histiocytic lymphoma;
RX   PubMed=2026444;
RA   Demeter J., Medzihradszky D., Kha H., Goetzl E.J., Turck C.W.;
RT   "Isolation and partial characterization of the structures of fibroblast
RT   activating factor-related proteins from U937 cells.";
RL   Immunology 72:350-354(1991).
RN   [16]
RP   PROTEIN SEQUENCE OF 131-141 AND 154-190, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain, and Cajal-Retzius cell;
RA   Lubec G., Afjehi-Sadat L.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [17]
RP   INTERACTION WITH HCV CORE PROTEIN (MICROBIAL INFECTION).
RX   PubMed=10644344; DOI=10.1128/jvi.74.4.1736-1741.2000;
RA   Aoki H., Hayashi J., Moriyama M., Arakawa Y., Hino O.;
RT   "Hepatitis C virus core protein interacts with 14-3-3 protein and activates
RT   the kinase Raf-1.";
RL   J. Virol. 74:1736-1741(2000).
RN   [18]
RP   INTERACTION WITH AANAT.
RX   PubMed=11427721; DOI=10.1073/pnas.141118798;
RA   Ganguly S., Gastel J.A., Weller J.L., Schwartz C., Jaffe H.,
RA   Namboodiri M.A., Coon S.L., Hickman A.B., Rollag M., Obsil T.,
RA   Beauverger P., Ferry G., Boutin J.A., Klein D.C.;
RT   "Role of a pineal cAMP-operated arylalkylamine N-acetyltransferase/14-3-3-
RT   binding switch in melatonin synthesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:8083-8088(2001).
RN   [19]
RP   INTERACTION WITH CDKN1B, AND SUBCELLULAR LOCATION.
RX   PubMed=12042314; DOI=10.1074/jbc.m203668200;
RA   Fujita N., Sato S., Katayama K., Tsuruo T.;
RT   "Akt-dependent phosphorylation of p27Kip1 promotes binding to 14-3-3 and
RT   cytoplasmic localization.";
RL   J. Biol. Chem. 277:28706-28713(2002).
RN   [20]
RP   FUNCTION, INTERACTION WITH HSF1, AND SUBCELLULAR LOCATION.
RX   PubMed=12917326; DOI=10.1128/mcb.23.17.6013-6026.2003;
RA   Wang X., Grammatikakis N., Siganou A., Calderwood S.K.;
RT   "Regulation of molecular chaperone gene transcription involves the serine
RT   phosphorylation, 14-3-3 epsilon binding, and cytoplasmic sequestration of
RT   heat shock factor 1.";
RL   Mol. Cell. Biol. 23:6013-6026(2003).
RN   [21]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Lymphoblast;
RX   PubMed=14654843; DOI=10.1038/nature02166;
RA   Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT   "Proteomic characterization of the human centrosome by protein correlation
RT   profiling.";
RL   Nature 426:570-574(2003).
RN   [22]
RP   INTERACTION WITH GRB10.
RX   PubMed=15722337; DOI=10.1074/jbc.m501477200;
RA   Urschel S., Bassermann F., Bai R.Y., Munch S., Peschel C., Duyster J.;
RT   "Phosphorylation of grb10 regulates its interaction with 14-3-3.";
RL   J. Biol. Chem. 280:16987-16993(2005).
RN   [23]
RP   INTERACTION WITH ABL1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=15696159; DOI=10.1038/ncb1228;
RA   Yoshida K., Yamaguchi T., Natsume T., Kufe D., Miki Y.;
RT   "JNK phosphorylation of 14-3-3 proteins regulates nuclear targeting of c-
RT   Abl in the apoptotic response to DNA damage.";
RL   Nat. Cell Biol. 7:278-285(2005).
RN   [24]
RP   INTERACTION WITH YWHAZ.
RX   PubMed=16376338; DOI=10.1016/j.febslet.2005.12.024;
RA   Gu Y.-M., Jin Y.-H., Choi J.-K., Baek K.-H., Yeo C.-Y., Lee K.-Y.;
RT   "Protein kinase A phosphorylates and regulates dimerization of 14-3-3
RT   epsilon.";
RL   FEBS Lett. 580:305-310(2006).
RN   [25]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   TISSUE=Melanoma;
RX   PubMed=17081065; DOI=10.1021/pr060363j;
RA   Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J.,
RA   Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S.,
RA   Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
RT   "Proteomic and bioinformatic characterization of the biogenesis and
RT   function of melanosomes.";
RL   J. Proteome Res. 5:3135-3144(2006).
RN   [26]
RP   INTERACTION WITH ATP2B1 AND ATP2B3.
RX   PubMed=18029012; DOI=10.1016/j.ceca.2007.09.003;
RA   Linde C.I., Di Leva F., Domi T., Tosatto S.C., Brini M., Carafoli E.;
RT   "Inhibitory interaction of the 14-3-3 proteins with ubiquitous (PMCA1) and
RT   tissue-specific (PMCA3) isoforms of the plasma membrane Ca2+ pump.";
RL   Cell Calcium 43:550-561(2008).
RN   [27]
RP   INTERACTION WITH GAB2.
RX   PubMed=19172738; DOI=10.1038/emboj.2008.159;
RA   Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P.,
RA   Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D., Guilhaus M.,
RA   James D.E., Daly R.J.;
RT   "Phosphorylation-dependent binding of 14-3-3 terminates signalling by the
RT   Gab2 docking protein.";
RL   EMBO J. 27:2305-2316(2008).
RN   [28]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=18318008; DOI=10.1002/pmic.200700884;
RA   Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA   Zou H., Gu J.;
RT   "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT   and fractionation of phosphopeptides with strong anion exchange
RT   chromatography.";
RL   Proteomics 8:1346-1361(2008).
RN   [29]
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   [30]
RP   INTERACTION WITH SLITRK1.
RX   PubMed=19640509; DOI=10.1016/j.biopsych.2009.05.033;
RA   Kajiwara Y., Buxbaum J.D., Grice D.E.;
RT   "SLITRK1 binds 14-3-3 and regulates neurite outgrowth in a phosphorylation-
RT   dependent manner.";
RL   Biol. Psychiatry 66:918-925(2009).
RN   [31]
RP   INTERACTION WITH SRPK2.
RX   PubMed=19592491; DOI=10.1074/jbc.m109.026237;
RA   Jang S.W., Liu X., Fu H., Rees H., Yepes M., Levey A., Ye K.;
RT   "Interaction of Akt-phosphorylated SRPK2 with 14-3-3 mediates cell cycle
RT   and cell death in neurons.";
RL   J. Biol. Chem. 284:24512-24525(2009).
RN   [32]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-50; LYS-69; LYS-118 AND LYS-123,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [33]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, AND IDENTIFICATION BY
RP   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   [34]
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   [35]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [36]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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   [37]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-232, AND IDENTIFICATION BY
RP   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   [38]
RP   INTERACTION WITH DAPK2.
RX   PubMed=26047703; DOI=10.1016/j.bbrc.2015.05.105;
RA   Yuasa K., Ota R., Matsuda S., Isshiki K., Inoue M., Tsuji A.;
RT   "Suppression of death-associated protein kinase 2 by interaction with 14-3-
RT   3 proteins.";
RL   Biochem. Biophys. Res. Commun. 464:70-75(2015).
RN   [39]
RP   INTERACTION WITH DENND1A.
RX   PubMed=26055712; DOI=10.1074/jbc.m115.636712;
RA   Kulasekaran G., Nossova N., Marat A.L., Lund I., Cremer C., Ioannou M.S.,
RA   McPherson P.S.;
RT   "Phosphorylation-dependent regulation of Connecdenn/DENND1 guanine
RT   nucleotide exchange factors.";
RL   J. Biol. Chem. 290:17999-18008(2015).
RN   [40]
RP   INTERACTION WITH RIPOR2.
RX   PubMed=25588844; DOI=10.1242/jcs.161497;
RA   Gao K., Tang W., Li Y., Zhang P., Wang D., Yu L., Wang C., Wu D.;
RT   "Front-signal-dependent accumulation of the RHOA inhibitor FAM65B at
RT   leading edges polarizes neutrophils.";
RL   J. Cell Sci. 128:992-1000(2015).
RN   [41]
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   [42]
RP   INTERACTION WITH MEFV.
RX   PubMed=27030597; DOI=10.1126/scitranslmed.aaf1471;
RA   Masters S.L., Lagou V., Jeru I., Baker P.J., Van Eyck L., Parry D.A.,
RA   Lawless D., De Nardo D., Garcia-Perez J.E., Dagley L.F., Holley C.L.,
RA   Dooley J., Moghaddas F., Pasciuto E., Jeandel P.Y., Sciot R., Lyras D.,
RA   Webb A.I., Nicholson S.E., De Somer L., van Nieuwenhove E., Ruuth-Praz J.,
RA   Copin B., Cochet E., Medlej-Hashim M., Megarbane A., Schroder K., Savic S.,
RA   Goris A., Amselem S., Wouters C., Liston A.;
RT   "Familial autoinflammation with neutrophilic dermatosis reveals a
RT   regulatory mechanism of pyrin activation.";
RL   Sci. Transl. Med. 8:332ra45-332ra45(2016).
RN   [43]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-50, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [44]
RP   INTERACTION WITH CRTC1; CRTC2 AND CRTC3.
RX   PubMed=30611118; DOI=10.1016/j.isci.2018.12.012;
RA   Sonntag T., Ostojic J., Vaughan J.M., Moresco J.J., Yoon Y.S.,
RA   Yates J.R. III, Montminy M.;
RT   "Mitogenic Signals Stimulate the CREB Coactivator CRTC3 through PP2A
RT   Recruitment.";
RL   IScience 11:134-145(2018).
RN   [45]
RP   INTERACTION WITH KLHL22.
RX   PubMed=29769719; DOI=10.1038/s41586-018-0128-9;
RA   Chen J., Ou Y., Yang Y., Li W., Xu Y., Xie Y., Liu Y.;
RT   "KLHL22 activates amino-acid-dependent mTORC1 signalling to promote
RT   tumorigenesis and ageing.";
RL   Nature 557:585-589(2018).
RN   [46]
RP   X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 1-233, IDENTIFICATION BY MASS
RP   SPECTROMETRY, INTERACTION WITH PHOSPHOSERINE MOTIFS, AND SUBUNIT.
RX   PubMed=17085597; DOI=10.1073/pnas.0605779103;
RA   Yang X., Lee W.H., Sobott F., Papagrigoriou E., Robinson C.V.,
RA   Grossmann J.G., Sundstroem M., Doyle D.A., Elkins J.M.;
RT   "Structural basis for protein-protein interactions in the 14-3-3 protein
RT   family.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:17237-17242(2006).
CC   -!- FUNCTION: Adapter protein implicated in the regulation of a large
CC       spectrum of both general and specialized signaling pathways. Binds to a
CC       large number of partners, usually by recognition of a phosphoserine or
CC       phosphothreonine motif. Binding generally results in the modulation of
CC       the activity of the binding partner (By similarity). Positively
CC       regulates phosphorylated protein HSF1 nuclear export to the cytoplasm
CC       (PubMed:12917326). {ECO:0000250|UniProtKB:P62261,
CC       ECO:0000269|PubMed:12917326}.
CC   -!- SUBUNIT: Homodimer (PubMed:17085597). Heterodimerizes with YWHAZ
CC       (PubMed:16376338). Interacts with PKA-phosphorylated AANAT
CC       (PubMed:11427721). Interacts with ABL1 (phosphorylated form); the
CC       interaction retains it in the cytoplasm (PubMed:15696159). Interacts
CC       with ARHGEF28 (By similarity). Interacts with BEX3 (By similarity).
CC       Weakly interacts with CDKN1B (PubMed:12042314). Interacts with the
CC       'Thr-369' phosphorylated form of DAPK2 (PubMed:26047703). Interacts
CC       with DENND1A (PubMed:26055712). Interacts with GAB2 (PubMed:19172738).
CC       Interacts with phosphorylated GRB10 (PubMed:15722337). Interacts with
CC       KSR1 (PubMed:10409742). Interacts with NDEL1 (By similarity). Interacts
CC       with PI4KB, TBC1D22A and TBC1D22B (PubMed:23572552). Interacts with the
CC       phosphorylated (by AKT1) form of SRPK2 (PubMed:19592491). Interacts
CC       with TIAM2. Interacts with the 'Ser-1134' and 'Ser-1161' phosphorylated
CC       form of SOS1 (By similarity). Interacts with ZFP36 (via phosphorylated
CC       form) (By similarity). Interacts with SLITRK1 (PubMed:19640509).
CC       Interacts with HSF1 (via phosphorylated form); this interaction
CC       promotes HSF1 sequestration in the cytoplasm in a ERK-dependent manner
CC       (PubMed:12917326). Interacts with RIPOR2 isoform 2 (PubMed:25588844).
CC       Interacts with KLHL22; required for the nuclear localization of KLHL22
CC       upon amino acid starvation (PubMed:29769719). Interacts with CRTC1
CC       (PubMed:30611118). Interacts with CRTC2 (probably when phosphorylated
CC       at 'Ser-171') (PubMed:30611118). Interacts with CRTC3 (probably when
CC       phosphorylated at 'Ser-162' and/or 'Ser-273') (PubMed:30611118).
CC       Interacts with ATP2B1 and ATP2B3; this interaction inhibits calcium-
CC       transporting ATPase activity (PubMed:18029012). Interacts with MEFV
CC       (PubMed:27030597). {ECO:0000250|UniProtKB:P62259,
CC       ECO:0000250|UniProtKB:P62260, ECO:0000269|PubMed:10409742,
CC       ECO:0000269|PubMed:11427721, ECO:0000269|PubMed:12042314,
CC       ECO:0000269|PubMed:12917326, ECO:0000269|PubMed:15696159,
CC       ECO:0000269|PubMed:15722337, ECO:0000269|PubMed:16376338,
CC       ECO:0000269|PubMed:17085597, ECO:0000269|PubMed:18029012,
CC       ECO:0000269|PubMed:19172738, ECO:0000269|PubMed:19592491,
CC       ECO:0000269|PubMed:19640509, ECO:0000269|PubMed:23572552,
CC       ECO:0000269|PubMed:25588844, ECO:0000269|PubMed:26047703,
CC       ECO:0000269|PubMed:26055712, ECO:0000269|PubMed:27030597,
CC       ECO:0000269|PubMed:29769719, ECO:0000269|PubMed:30611118}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with HCV core protein.
CC       {ECO:0000269|PubMed:10644344}.
CC   -!- INTERACTION:
CC       P62258; Q96AP0: ACD; NbExp=2; IntAct=EBI-356498, EBI-717666;
CC       P62258; O14727: APAF1; NbExp=2; IntAct=EBI-356498, EBI-446492;
CC       P62258; P10398: ARAF; NbExp=4; IntAct=EBI-356498, EBI-365961;
CC       P62258; P54253: ATXN1; NbExp=8; IntAct=EBI-356498, EBI-930964;
CC       P62258; Q92934: BAD; NbExp=4; IntAct=EBI-356498, EBI-700771;
CC       P62258; O00257-3: CBX4; NbExp=2; IntAct=EBI-356498, EBI-4392727;
CC       P62258; Q9Y3M2: CBY1; NbExp=3; IntAct=EBI-356498, EBI-947308;
CC       P62258; Q86Z20: CCDC125; NbExp=3; IntAct=EBI-356498, EBI-11977221;
CC       P62258; O94921: CDK14; NbExp=3; IntAct=EBI-356498, EBI-1043945;
CC       P62258; Q9NRI5: DISC1; NbExp=3; IntAct=EBI-356498, EBI-529989;
CC       P62258; P09622: DLD; NbExp=5; IntAct=EBI-356498, EBI-353366;
CC       P62258; P36957: DLST; NbExp=4; IntAct=EBI-356498, EBI-351007;
CC       P62258; Q9UKT5: FBXO4; NbExp=5; IntAct=EBI-356498, EBI-960409;
CC       P62258; P56524: HDAC4; NbExp=4; IntAct=EBI-356498, EBI-308629;
CC       P62258; P56524-2: HDAC4; NbExp=3; IntAct=EBI-356498, EBI-11953488;
CC       P62258; Q14678-2: KANK1; NbExp=3; IntAct=EBI-356498, EBI-6173812;
CC       P62258; Q5S007: LRRK2; NbExp=8; IntAct=EBI-356498, EBI-5323863;
CC       P62258; Q99759: MAP3K3; NbExp=3; IntAct=EBI-356498, EBI-307281;
CC       P62258; O15151: MDM4; NbExp=3; IntAct=EBI-356498, EBI-398437;
CC       P62258; P58340: MLF1; NbExp=3; IntAct=EBI-356498, EBI-721328;
CC       P62258; Q9NXR1: NDE1; NbExp=2; IntAct=EBI-356498, EBI-941227;
CC       P62258; Q7L804: RAB11FIP2; NbExp=3; IntAct=EBI-356498, EBI-1049676;
CC       P62258; P04049: RAF1; NbExp=6; IntAct=EBI-356498, EBI-365996;
CC       P62258; Q13671: RIN1; NbExp=3; IntAct=EBI-356498, EBI-366017;
CC       P62258; Q99469: STAC; NbExp=3; IntAct=EBI-356498, EBI-2652799;
CC       P62258; P21796: VDAC1; NbExp=5; IntAct=EBI-356498, EBI-354158;
CC       P62258; Q9GZV5: WWTR1; NbExp=3; IntAct=EBI-356498, EBI-747743;
CC       P62258; P46937: YAP1; NbExp=5; IntAct=EBI-356498, EBI-1044059;
CC       P62258; P31946: YWHAB; NbExp=6; IntAct=EBI-356498, EBI-359815;
CC       P62258; P62258: YWHAE; NbExp=3; IntAct=EBI-356498, EBI-356498;
CC       P62258; P61981: YWHAG; NbExp=7; IntAct=EBI-356498, EBI-359832;
CC       P62258; Q04917: YWHAH; NbExp=5; IntAct=EBI-356498, EBI-306940;
CC       P62258; P27348: YWHAQ; NbExp=7; IntAct=EBI-356498, EBI-359854;
CC       P62258; P63104: YWHAZ; NbExp=9; IntAct=EBI-356498, EBI-347088;
CC       P62258; P61588: Rnd3; Xeno; NbExp=2; IntAct=EBI-356498, EBI-6930266;
CC       P62258; PRO_0000278742 [O92972]; Xeno; NbExp=5; IntAct=EBI-356498, EBI-9213553;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12917326}. Cytoplasm
CC       {ECO:0000269|PubMed:12917326}. Melanosome {ECO:0000269|PubMed:12042314,
CC       ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in
CC       melanosome fractions from stage I to stage IV.
CC       {ECO:0000269|PubMed:12042314, ECO:0000269|PubMed:17081065}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P62258-1; Sequence=Displayed;
CC       Name=SV;
CC         IsoId=P62258-2; Sequence=VSP_040621;
CC   -!- MISCELLANEOUS: [Isoform SV]: Unable to dimerize with YWHAZ.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
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DR   EMBL; U20972; AAC50175.1; -; mRNA.
DR   EMBL; U54778; AAC50710.1; -; mRNA.
DR   EMBL; U43399; AAC50625.1; -; mRNA.
DR   EMBL; U43430; AAD00026.1; -; mRNA.
DR   EMBL; U28936; AAA75301.1; -; mRNA.
DR   EMBL; AB017103; BAA32538.1; -; Genomic_DNA.
DR   EMBL; AY883089; AAX68683.1; -; mRNA.
DR   EMBL; AK128785; BAG54733.1; -; mRNA.
DR   EMBL; AK295260; BAG58249.1; -; mRNA.
DR   EMBL; AK316185; BAH14556.1; -; mRNA.
DR   EMBL; BT007161; AAP35825.1; -; mRNA.
DR   EMBL; CH471108; EAW90628.1; -; Genomic_DNA.
DR   EMBL; CH471108; EAW90629.1; -; Genomic_DNA.
DR   EMBL; BC000179; AAH00179.1; -; mRNA.
DR   EMBL; BC001440; AAH01440.1; -; mRNA.
DR   CCDS; CCDS11001.1; -. [P62258-1]
DR   PIR; A61235; A61235.
DR   PIR; I38947; I38947.
DR   RefSeq; NP_006752.1; NM_006761.4. [P62258-1]
DR   PDB; 2BR9; X-ray; 1.75 A; A=1-233.
DR   PDB; 3UAL; X-ray; 1.80 A; A=1-232.
DR   PDB; 3UBW; X-ray; 1.90 A; A=1-234.
DR   PDB; 6EIH; X-ray; 2.70 A; A=3-232.
DR   PDB; 7C8E; X-ray; 3.16 A; A/B=1-232.
DR   PDBsum; 2BR9; -.
DR   PDBsum; 3UAL; -.
DR   PDBsum; 3UBW; -.
DR   PDBsum; 6EIH; -.
DR   PDBsum; 7C8E; -.
DR   AlphaFoldDB; P62258; -.
DR   SMR; P62258; -.
DR   BioGRID; 113363; 939.
DR   CORUM; P62258; -.
DR   DIP; DIP-36676N; -.
DR   ELM; P62258; -.
DR   IntAct; P62258; 290.
DR   MINT; P62258; -.
DR   STRING; 9606.ENSP00000264335; -.
DR   ChEMBL; CHEMBL3329082; -.
DR   DrugBank; DB01780; Fusicoccin.
DR   DrugBank; DB12695; Phenethyl Isothiocyanate.
DR   MoonDB; P62258; Predicted.
DR   GlyGen; P62258; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P62258; -.
DR   MetOSite; P62258; -.
DR   PhosphoSitePlus; P62258; -.
DR   SwissPalm; P62258; -.
DR   BioMuta; YWHAE; -.
DR   DMDM; 51702210; -.
DR   OGP; P42655; -.
DR   UCD-2DPAGE; P62258; -.
DR   EPD; P62258; -.
DR   jPOST; P62258; -.
DR   MassIVE; P62258; -.
DR   MaxQB; P62258; -.
DR   PaxDb; P62258; -.
DR   PeptideAtlas; P62258; -.
DR   PRIDE; P62258; -.
DR   ProteomicsDB; 57377; -.
DR   ProteomicsDB; 57378; -. [P62258-2]
DR   TopDownProteomics; P62258-1; -. [P62258-1]
DR   Antibodypedia; 1898; 503 antibodies from 39 providers.
DR   CPTC; P62258; 3 antibodies.
DR   DNASU; 7531; -.
DR   Ensembl; ENST00000264335.13; ENSP00000264335.8; ENSG00000108953.17. [P62258-1]
DR   Ensembl; ENST00000571732.5; ENSP00000461762.1; ENSG00000108953.17. [P62258-2]
DR   Ensembl; ENST00000616643.3; ENSP00000481059.2; ENSG00000274474.3. [P62258-2]
DR   Ensembl; ENST00000627231.2; ENSP00000487356.1; ENSG00000274474.3. [P62258-1]
DR   GeneID; 7531; -.
DR   KEGG; hsa:7531; -.
DR   MANE-Select; ENST00000264335.13; ENSP00000264335.8; NM_006761.5; NP_006752.1.
DR   UCSC; uc002fsk.4; human. [P62258-1]
DR   CTD; 7531; -.
DR   DisGeNET; 7531; -.
DR   GeneCards; YWHAE; -.
DR   HGNC; HGNC:12851; YWHAE.
DR   HPA; ENSG00000108953; Low tissue specificity.
DR   MalaCards; YWHAE; -.
DR   MIM; 605066; gene.
DR   neXtProt; NX_P62258; -.
DR   OpenTargets; ENSG00000108953; -.
DR   Orphanet; 217385; 17p13.3 microduplication syndrome.
DR   Orphanet; 457246; Clear cell sarcoma of kidney.
DR   Orphanet; 261257; Distal 17p13.3 microdeletion syndrome.
DR   Orphanet; 213711; Endometrial stromal sarcoma.
DR   Orphanet; 531; Miller-Dieker syndrome.
DR   PharmGKB; PA37440; -.
DR   VEuPathDB; HostDB:ENSG00000108953; -.
DR   eggNOG; KOG0841; Eukaryota.
DR   GeneTree; ENSGT01050000244964; -.
DR   HOGENOM; CLU_058290_0_0_1; -.
DR   InParanoid; P62258; -.
DR   OMA; IPCATTG; -.
DR   PhylomeDB; P62258; -.
DR   TreeFam; TF102003; -.
DR   PathwayCommons; P62258; -.
DR   Reactome; R-HSA-111447; Activation of BAD and translocation to mitochondria.
DR   Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
DR   Reactome; R-HSA-2028269; Signaling by Hippo.
DR   Reactome; R-HSA-205025; NADE modulates death signalling.
DR   Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR   Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
DR   Reactome; R-HSA-3371511; HSF1 activation.
DR   Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
DR   Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR   Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR   Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR   Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
DR   Reactome; R-HSA-5625740; RHO GTPases activate PKNs.
DR   Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
DR   Reactome; R-HSA-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
DR   Reactome; R-HSA-8854518; AURKA Activation by TPX2.
DR   Reactome; R-HSA-8862803; Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models.
DR   Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR   Reactome; R-HSA-9755779; SARS-CoV-2 targets host intracellular signalling and regulatory pathways.
DR   SignaLink; P62258; -.
DR   SIGNOR; P62258; -.
DR   BioGRID-ORCS; 7531; 201 hits in 1049 CRISPR screens.
DR   ChiTaRS; YWHAE; human.
DR   EvolutionaryTrace; P62258; -.
DR   GeneWiki; YWHAE; -.
DR   GenomeRNAi; 7531; -.
DR   Pharos; P62258; Tbio.
DR   PRO; PR:P62258; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; P62258; protein.
DR   Bgee; ENSG00000108953; Expressed in superior frontal gyrus and 114 other tissues.
DR   ExpressionAtlas; P62258; baseline and differential.
DR   Genevisible; P62258; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR   GO; GO:0005246; F:calcium channel regulator activity; IDA:SynGO-UCL.
DR   GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR   GO; GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0023026; F:MHC class II protein complex binding; HDA:UniProtKB.
DR   GO; GO:0051219; F:phosphoprotein binding; IPI:BHF-UCL.
DR   GO; GO:0050815; F:phosphoserine residue binding; IPI:BHF-UCL.
DR   GO; GO:0015459; F:potassium channel regulator activity; IDA:BHF-UCL.
DR   GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL.
DR   GO; GO:0019903; F:protein phosphatase binding; IEA:Ensembl.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0097110; F:scaffold protein binding; IPI:UniProtKB.
DR   GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
DR   GO; GO:0034605; P:cellular response to heat; IDA:UniProtKB.
DR   GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR   GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR   GO; GO:0035556; P:intracellular signal transduction; TAS:ProtInc.
DR   GO; GO:0000165; P:MAPK cascade; IDA:UniProtKB.
DR   GO; GO:0086013; P:membrane repolarization during cardiac muscle cell action potential; IC:BHF-UCL.
DR   GO; GO:1905913; P:negative regulation of calcium ion export across plasma membrane; IDA:SynGO-UCL.
DR   GO; GO:1901020; P:negative regulation of calcium ion transmembrane transporter activity; IDA:SynGO-UCL.
DR   GO; GO:1902309; P:negative regulation of peptidyl-serine dephosphorylation; IDA:BHF-UCL.
DR   GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR   GO; GO:0046827; P:positive regulation of protein export from nucleus; IDA:UniProtKB.
DR   GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR   GO; GO:0034504; P:protein localization to nucleus; IMP:UniProtKB.
DR   GO; GO:0006605; P:protein targeting; IEA:Ensembl.
DR   GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IDA:SynGO-UCL.
DR   GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IC:BHF-UCL.
DR   GO; GO:0003064; P:regulation of heart rate by hormone; NAS:BHF-UCL.
DR   GO; GO:0060306; P:regulation of membrane repolarization; IDA:BHF-UCL.
DR   GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:1901016; P:regulation of potassium ion transmembrane transporter activity; IDA:BHF-UCL.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   GO; GO:0021762; P:substantia nigra development; HEP:UniProtKB.
DR   Gene3D; 1.20.190.20; -; 1.
DR   IDEAL; IID00512; -.
DR   InterPro; IPR000308; 14-3-3.
DR   InterPro; IPR023409; 14-3-3_CS.
DR   InterPro; IPR036815; 14-3-3_dom_sf.
DR   InterPro; IPR023410; 14-3-3_domain.
DR   PANTHER; PTHR18860; PTHR18860; 1.
DR   Pfam; PF00244; 14-3-3; 1.
DR   PIRSF; PIRSF000868; 14-3-3; 1.
DR   PRINTS; PR00305; 1433ZETA.
DR   SMART; SM00101; 14_3_3; 1.
DR   SUPFAM; SSF48445; SSF48445; 1.
DR   PROSITE; PS00796; 1433_1; 1.
DR   PROSITE; PS00797; 1433_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW   Direct protein sequencing; Host-virus interaction; Isopeptide bond;
KW   Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT   CHAIN           1..255
FT                   /note="14-3-3 protein epsilon"
FT                   /id="PRO_0000058618"
FT   REGION          234..255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..255
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            57
FT                   /note="Interaction with phosphoserine on interacting
FT                   protein"
FT   SITE            130
FT                   /note="Interaction with phosphoserine on interacting
FT                   protein"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000269|Ref.13, ECO:0007744|PubMed:19413330"
FT   MOD_RES         50
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         65
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P62260"
FT   MOD_RES         69
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         118
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         123
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         131
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62260"
FT   MOD_RES         137
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P62260"
FT   MOD_RES         210
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   MOD_RES         232
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   CROSSLNK        50
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         1..22
FT                   /note="Missing (in isoform SV)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:20417184"
FT                   /id="VSP_040621"
FT   CONFLICT        106..107
FT                   /note="KH -> NY (in Ref. 15; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        143
FT                   /note="E -> F (in Ref. 15; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        148
FT                   /note="S -> T (in Ref. 15; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   HELIX           4..17
FT                   /evidence="ECO:0007829|PDB:2BR9"
FT   HELIX           20..31
FT                   /evidence="ECO:0007829|PDB:2BR9"
FT   HELIX           39..73
FT                   /evidence="ECO:0007829|PDB:2BR9"
FT   HELIX           76..106
FT                   /evidence="ECO:0007829|PDB:2BR9"
FT   HELIX           108..111
FT                   /evidence="ECO:0007829|PDB:2BR9"
FT   HELIX           115..135
FT                   /evidence="ECO:0007829|PDB:2BR9"
FT   HELIX           138..162
FT                   /evidence="ECO:0007829|PDB:2BR9"
FT   HELIX           168..183
FT                   /evidence="ECO:0007829|PDB:2BR9"
FT   HELIX           188..204
FT                   /evidence="ECO:0007829|PDB:2BR9"
FT   HELIX           205..208
FT                   /evidence="ECO:0007829|PDB:2BR9"
FT   TURN            211..213
FT                   /evidence="ECO:0007829|PDB:2BR9"
FT   HELIX           214..231
FT                   /evidence="ECO:0007829|PDB:2BR9"
SQ   SEQUENCE   255 AA;  29174 MW;  07817CCBD1F75B26 CRC64;
     MDDREDLVYQ AKLAEQAERY DEMVESMKKV AGMDVELTVE ERNLLSVAYK NVIGARRASW
     RIISSIEQKE ENKGGEDKLK MIREYRQMVE TELKLICCDI LDVLDKHLIP AANTGESKVF
     YYKMKGDYHR YLAEFATGND RKEAAENSLV AYKAASDIAM TELPPTHPIR LGLALNFSVF
     YYEILNSPDR ACRLAKAAFD DAIAELDTLS EESYKDSTLI MQLLRDNLTL WTSDMQGDGE
     EQNKEALQDV EDENQ
//