ID DPTOR_HUMAN Reviewed; 409 AA.
AC Q8TB45; B2RCL9; B4DN97; E7EV87; Q96EQ1; Q9H0R7; Q9H894; Q9HA07;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 24-JAN-2024, entry version 162.
DE RecName: Full=DEP domain-containing mTOR-interacting protein {ECO:0000305};
DE Short=hDEPTOR {ECO:0000303|PubMed:33865870};
DE AltName: Full=DEP domain-containing protein 6 {ECO:0000303|PubMed:29382726};
GN Name=DEPTOR {ECO:0000303|PubMed:19446321, ECO:0000312|HGNC:HGNC:22953};
GN Synonyms=DEPDC6 {ECO:0000303|PubMed:29382726};
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 [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-204.
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP SER-204 AND ASN-389.
RC TISSUE=Heart, Mammary gland, and Thyroid;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS SER-204
RP AND ASN-389.
RC TISSUE=Cervix, and Colon;
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 [6]
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 [7]
RP FUNCTION, INTERACTION WITH MTOR, INDUCTION, PHOSPHORYLATION AT THR-241;
RP SER-244; SER-258; THR-259; SER-263; SER-265; SER-282; SER-283; SER-287;
RP SER-293; SER-297; SER-298 AND SER-299, MUTAGENESIS OF THR-241; SER-244;
RP SER-258; THR-259; SER-263; SER-265; SER-282; SER-283; SER-287; SER-293;
RP SER-297; SER-298 AND SER-299, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19446321; DOI=10.1016/j.cell.2009.03.046;
RA Peterson T.R., Laplante M., Thoreen C.C., Sancak Y., Kang S.A., Kuehl W.M.,
RA Gray N.S., Sabatini D.M.;
RT "DEPTOR is an mTOR inhibitor frequently overexpressed in multiple myeloma
RT cells and required for their survival.";
RL Cell 137:873-886(2009).
RN [8]
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 [9]
RP FUNCTION, ACTIVITY REGULATION, PHOSPHORYLATION AT SER-265; SER-286;
RP SER-287; SER-293; THR-295 AND SER-299, UBIQUITINATION, AND MUTAGENESIS OF
RP SER-286; SER-293 AND 295-THR--SER-299.
RX PubMed=22017875; DOI=10.1016/j.molcel.2011.08.030;
RA Gao D., Inuzuka H., Tan M.K., Fukushima H., Locasale J.W., Liu P., Wan L.,
RA Zhai B., Chin Y.R., Shaik S., Lyssiotis C.A., Gygi S.P., Toker A.,
RA Cantley L.C., Asara J.M., Harper J.W., Wei W.;
RT "mTOR drives its own activation via SCF(betaTrCP)-dependent degradation of
RT the mTOR inhibitor DEPTOR.";
RL Mol. Cell 44:290-303(2011).
RN [10]
RP FUNCTION, ACTIVITY REGULATION, PHOSPHORYLATION AT SER-286; SER-287 AND
RP SER-291, UBIQUITINATION, AND MUTAGENESIS OF SER-286; SER-287 AND SER-291.
RX PubMed=22017876; DOI=10.1016/j.molcel.2011.08.029;
RA Zhao Y., Xiong X., Sun Y.;
RT "DEPTOR, an mTOR inhibitor, is a physiological substrate of SCF(betaTrCP)
RT E3 ubiquitin ligase and regulates survival and autophagy.";
RL Mol. Cell 44:304-316(2011).
RN [11]
RP FUNCTION, ACTIVITY REGULATION, PHOSPHORYLATION AT SER-286; SER-287 AND
RP SER-291, UBIQUITINATION, AND MUTAGENESIS OF 286-SER--SER-291; SER-286;
RP SER-287 AND SER-291.
RX PubMed=22017877; DOI=10.1016/j.molcel.2011.09.005;
RA Duan S., Skaar J.R., Kuchay S., Toschi A., Kanarek N., Ben-Neriah Y.,
RA Pagano M.;
RT "mTOR generates an auto-amplification loop by triggering the betaTrCP- and
RT CK1alpha-dependent degradation of DEPTOR.";
RL Mol. Cell 44:317-324(2011).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [14]
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 [15]
RP FUNCTION, ACTIVITY REGULATION, IDENTIFICATION IN THE MTORC1 COMPLEX,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF THR-241; SER-244; SER-258;
RP THR-259; SER-263; SER-265; SER-282; SER-283; SER-287; SER-293; SER-297;
RP SER-298 AND SER-299.
RX PubMed=25936805; DOI=10.1016/j.molcel.2015.03.028;
RA Yoon M.S., Rosenberger C.L., Wu C., Truong N., Sweedler J.V., Chen J.;
RT "Rapid mitogenic regulation of the mTORC1 inhibitor, DEPTOR, by
RT phosphatidic acid.";
RL Mol. Cell 58:549-556(2015).
RN [16]
RP FUNCTION, AND DEUBIQUITINATION.
RX PubMed=29382726; DOI=10.1074/jbc.m117.809533;
RA Zhao L., Wang X., Yu Y., Deng L., Chen L., Peng X., Jiao C., Gao G.,
RA Tan X., Pan W., Ge X., Wang P.;
RT "OTUB1 protein suppresses mTOR complex 1 (mTORC1) activity by
RT deubiquitinating the mTORC1 inhibitor DEPTOR.";
RL J. Biol. Chem. 293:4883-4892(2018).
RN [17]
RP INTERACTION WITH MINAR1, AND UBIQUITINATION.
RX PubMed=30080879; DOI=10.1371/journal.pgen.1007583;
RA Zhang H., Zhang Q., Gao G., Wang X., Wang T., Kong Z., Wang G., Zhang C.,
RA Wang Y., Peng G.;
RT "UBTOR/KIAA1024 regulates neurite outgrowth and neoplasia through mTOR
RT signaling.";
RL PLoS Genet. 14:E1007583-E1007583(2018).
RN [18]
RP INTERACTION WITH SIK3.
RX PubMed=30232230; DOI=10.1126/scitranslmed.aat9356;
RA Csukasi F., Duran I., Barad M., Barta T., Gudernova I., Trantirek L.,
RA Martin J.H., Kuo C.Y., Woods J., Lee H., Cohn D.H., Krejci P., Krakow D.;
RT "The PTH/PTHrP-SIK3 pathway affects skeletogenesis through altered mTOR
RT signaling.";
RL Sci. Transl. Med. 10:0-0(2018).
RN [19]
RP UBIQUITINATION.
RX PubMed=33110214; DOI=10.1038/s41418-020-00649-z;
RA Cho J.H., Kim K., Kim S.A., Park S., Park B.O., Kim J.H., Kim S.Y.,
RA Kwon M.J., Han M.H., Lee S.B., Park B.C., Park S.G., Kim J.H., Kim S.;
RT "Deubiquitinase OTUD5 is a positive regulator of mTORC1 and mTORC2
RT signaling pathways.";
RL Cell Death Differ. 28:900-914(2021).
RN [20]
RP PHOSPHORYLATION AT TYR-289, AND MUTAGENESIS OF TYR-289 AND TYR-326.
RX PubMed=34634301; DOI=10.1016/j.jbc.2021.101291;
RA M Gagne L., Morin N., Lavoie N., Bisson N., Lambert J.P., Mallette F.A.,
RA Huot M.E.;
RT "Tyrosine phosphorylation of DEPTOR functions as a molecular switch to
RT activate mTOR signaling.";
RL J. Biol. Chem. 297:101291-101291(2021).
RN [21]
RP PHOSPHORYLATION AT SER-235, DEUBIQUITINATION, AND MUTAGENESIS OF SER-235.
RX PubMed=35216969; DOI=10.1016/j.jbc.2022.101750;
RA Vega M., Chen Y., Shi Y., Gera J., Lichtenstein A.;
RT "Turnover of the mTOR inhibitor, DEPTOR, and downstream AKT phosphorylation
RT in multiple myeloma cells, is dependent on ERK1-mediated phosphorylation.";
RL J. Biol. Chem. 298:101750-101750(2022).
RN [22] {ECO:0007744|PDB:7DKL}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 21-235, ACTIVITY REGULATION, AND
RP MUTAGENESIS OF ARG-53; ARG-54; LYS-58; ARG-225 AND LEU-231.
RX PubMed=33865870; DOI=10.1016/j.jmb.2021.166989;
RA Weng Z., Shen X., Zheng J., Liang H., Liu Y.;
RT "Structural basis of DEPTOR to recognize phosphatidic acid using its tandem
RT DEP domains.";
RL J. Mol. Biol. 433:166989-166989(2021).
RN [23] {ECO:0007744|PDB:7PE7, ECO:0007744|PDB:7PE8, ECO:0007744|PDB:7PE9, ECO:0007744|PDB:7PEA, ECO:0007744|PDB:7PEB, ECO:0007744|PDB:7PEC, ECO:0007744|PDB:7PED}
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 1-230 IN COMPLEX WITH DEPTOR;
RP MLST8; MAPKAP1; RICTOR AND RPTOR, FUNCTION, IDENTIFICATION IN THE MTORC1
RP COMPLEX, AND IDENTIFICATION IN THE MTORC2 COMPLEX.
RX PubMed=34519268; DOI=10.7554/elife.70871;
RA Waelchli M., Berneiser K., Mangia F., Imseng S., Craigie L.M.,
RA Stuttfeld E., Hall M.N., Maier T.;
RT "Regulation of human mTOR complexes by DEPTOR.";
RL Elife 10:0-0(2021).
RN [24] {ECO:0007744|PDB:7OWG}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.70 ANGSTROMS) IN COMPLEX WITH MTOR;
RP MLST8 AND RPTOR, FUNCTION, AND IDENTIFICATION IN THE MTORC1 COMPLEX.
RX PubMed=34519269; DOI=10.7554/elife.68799;
RA Heimhalt M., Berndt A., Wagstaff J., Anandapadamanaban M., Perisic O.,
RA Maslen S., McLaughlin S., Yu C.W., Masson G.R., Boland A., Ni X.,
RA Yamashita K., Murshudov G.N., Skehel M., Freund S.M., Williams R.L.;
RT "Bipartite binding and partial inhibition links DEPTOR and mTOR in a
RT mutually antagonistic embrace.";
RL Elife 10:0-0(2021).
CC -!- FUNCTION: Negative regulator of the mTORC1 and mTORC2 complexes:
CC inhibits the protein kinase activity of MTOR, thereby inactivating both
CC complexes (PubMed:19446321, PubMed:22017875, PubMed:22017876,
CC PubMed:22017877, PubMed:25936805, PubMed:29382726, PubMed:34519269,
CC PubMed:34519268). DEPTOR inhibits mTORC1 and mTORC2 to induce autophagy
CC (PubMed:22017875, PubMed:22017876, PubMed:22017877). In contrast to
CC AKT1S1/PRAS40, only partially inhibits mTORC1 activity
CC (PubMed:34519269, PubMed:34519268). {ECO:0000269|PubMed:19446321,
CC ECO:0000269|PubMed:22017875, ECO:0000269|PubMed:22017876,
CC ECO:0000269|PubMed:22017877, ECO:0000269|PubMed:25936805,
CC ECO:0000269|PubMed:29382726, ECO:0000269|PubMed:34519268,
CC ECO:0000269|PubMed:34519269}.
CC -!- ACTIVITY REGULATION: Inhibited upon phosphatidic acid-binding:
CC phosphatidic acid produced upon mitogenic stimulation promotes DEPTOR
CC dissociatiom from the mTORC1 and mTORC2 complexes, leading to their
CC activation (PubMed:25936805, PubMed:33865870). Specifically binds
CC unsaturated phosphatidic acid, such as 16:0-18:1, 18:0-18:1 and di-18:1
CC (PubMed:25936805). Inhibited when nutrients are present via a feedback
CC loop: phosphorylation by MTOR promotes DEPTOR ubiquitination and
CC degradation (PubMed:22017875, PubMed:22017876, PubMed:22017877).
CC {ECO:0000269|PubMed:22017875, ECO:0000269|PubMed:22017876,
CC ECO:0000269|PubMed:22017877, ECO:0000269|PubMed:25936805,
CC ECO:0000269|PubMed:33865870}.
CC -!- SUBUNIT: Associated component of the mechanistic target of rapamycin
CC complex 1 (mTORC1) which contains MTOR, MLST8 and RPTOR
CC (PubMed:19446321, PubMed:25936805, PubMed:34519269, PubMed:34519268).
CC Associated component of the mechanistic target of rapamycin complex 2
CC (mTORC2) which contains MTOR, MLST8, PROTOR1, RICTOR, MAPKAP1 and
CC DEPTOR (PubMed:19446321, PubMed:34519268). Interacts (via PDZ domain)
CC with MTOR; interacts with MTOR within both mTORC1 and mTORC2
CC (PubMed:19446321). Interacts (via PDZ domain) with MINAR1 (via N-
CC terminus) (PubMed:30080879). Interacts with SIK3 (PubMed:30232230).
CC {ECO:0000269|PubMed:19446321, ECO:0000269|PubMed:25936805,
CC ECO:0000269|PubMed:30080879, ECO:0000269|PubMed:30232230,
CC ECO:0000269|PubMed:34519268, ECO:0000269|PubMed:34519269}.
CC -!- INTERACTION:
CC Q8TB45; X5D778: ANKRD11; NbExp=3; IntAct=EBI-2359040, EBI-17183751;
CC Q8TB45; Q8TBZ0: CCDC110; NbExp=3; IntAct=EBI-2359040, EBI-2837012;
CC Q8TB45; P42345: MTOR; NbExp=5; IntAct=EBI-2359040, EBI-359260;
CC Q8TB45; Q13077: TRAF1; NbExp=3; IntAct=EBI-2359040, EBI-359224;
CC Q8TB45; P42346: Mtor; Xeno; NbExp=2; IntAct=EBI-2359040, EBI-1571489;
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000305|PubMed:25936805}.
CC Note=Localizes to the lysosomal membrane when associated with the
CC mTORC1 and mTORC2 complexes. {ECO:0000305|PubMed:25936805}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8TB45-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TB45-2; Sequence=VSP_054681;
CC -!- INDUCTION: Expression is negatively regulated by both mTORC1 and mTORC2
CC (at protein level). {ECO:0000269|PubMed:19446321}.
CC -!- PTM: Phosphorylation weakens interaction with MTOR within mTORC1 and
CC mTORC2 (PubMed:19446321). Phosphorylated at Ser-286, Ser-287 and Ser-
CC 291 in response to mitogenic stimulation by MTOR: DEPTOR is either
CC directly phosphorylated by MTOR or indirectly via proteins kinases that
CC are activated by MTOR, such as CK1/CSNK1A1 (PubMed:22017875,
CC PubMed:22017876, PubMed:22017877). Phosphorylation at Ser-286, Ser-287
CC and Ser-291 promotes ubiquitination by the SCF(BTRC) complex, followed
CC by degradation (PubMed:22017875, PubMed:22017876, PubMed:22017877).
CC Phosphorylation at Ser-235 by MAPK3/ERK1 promotes deubiquitination by
CC USP7, enhancing its stability (PubMed:35216969). Phosphorylation at
CC Tyr-289 by SYK impairs its interaction with MTOR, promoting mTORC1 and
CC mTORC2 signaling (PubMed:34634301). {ECO:0000269|PubMed:19446321,
CC ECO:0000269|PubMed:22017875, ECO:0000269|PubMed:22017876,
CC ECO:0000269|PubMed:22017877, ECO:0000269|PubMed:34634301,
CC ECO:0000269|PubMed:35216969}.
CC -!- PTM: Ubiquitinated; leading to proteasomal degradation
CC (PubMed:22017875, PubMed:22017876, PubMed:22017877, PubMed:30080879,
CC PubMed:33110214). Ubiquitination by the SCF(BTRC) and SCF(FBXW11)
CC complexes following phosphorylation at Ser-286, Ser-287 and Ser-291 by
CC MTOR, leads to its degradation by the proteasome (PubMed:22017875,
CC PubMed:22017876, PubMed:22017877, PubMed:33110214). Deubiquitinated by
CC OTUB1 in response to amino acid via a non-canonical mechanism, leading
CC to DEPTOR stability (PubMed:29382726). Deubiquitinated by USP7
CC following phosphorylation at Ser-235, promoting its stability
CC (PubMed:35216969). {ECO:0000269|PubMed:22017875,
CC ECO:0000269|PubMed:22017876, ECO:0000269|PubMed:22017877,
CC ECO:0000269|PubMed:29382726, ECO:0000269|PubMed:30080879,
CC ECO:0000269|PubMed:33110214, ECO:0000269|PubMed:35216969}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14723.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL136678; CAB66613.1; -; mRNA.
DR EMBL; AK022490; BAB14054.1; -; mRNA.
DR EMBL; AK023916; BAB14723.1; ALT_INIT; mRNA.
DR EMBL; AK297822; BAG60159.1; -; mRNA.
DR EMBL; AK315175; BAG37616.1; -; mRNA.
DR EMBL; AC091563; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP005717; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471060; EAW91997.1; -; Genomic_DNA.
DR EMBL; BC012040; AAH12040.1; -; mRNA.
DR EMBL; BC024746; AAH24746.1; -; mRNA.
DR CCDS; CCDS6331.1; -. [Q8TB45-1]
DR CCDS; CCDS64960.1; -. [Q8TB45-2]
DR RefSeq; NP_001269941.1; NM_001283012.1. [Q8TB45-2]
DR RefSeq; NP_073620.2; NM_022783.3. [Q8TB45-1]
DR PDB; 7DKL; X-ray; 1.50 A; A=21-235.
DR PDB; 7OWG; EM; 4.70 A; O=1-409.
DR PDB; 7PE7; EM; 3.41 A; I/J=1-409.
DR PDB; 7PE8; EM; 3.20 A; I=1-409.
DR PDB; 7PE9; EM; 3.70 A; I=1-409.
DR PDB; 7PEA; EM; 4.07 A; I/J=1-409.
DR PDB; 7PEB; EM; 3.67 A; I=1-409.
DR PDB; 7PEC; EM; 4.24 A; I=1-409.
DR PDB; 7PED; X-ray; 1.93 A; A/B=1-230.
DR PDBsum; 7DKL; -.
DR PDBsum; 7OWG; -.
DR PDBsum; 7PE7; -.
DR PDBsum; 7PE8; -.
DR PDBsum; 7PE9; -.
DR PDBsum; 7PEA; -.
DR PDBsum; 7PEB; -.
DR PDBsum; 7PEC; -.
DR PDBsum; 7PED; -.
DR AlphaFoldDB; Q8TB45; -.
DR EMDB; EMD-13097; -.
DR EMDB; EMD-13347; -.
DR EMDB; EMD-13348; -.
DR EMDB; EMD-13349; -.
DR EMDB; EMD-13350; -.
DR EMDB; EMD-13351; -.
DR EMDB; EMD-13352; -.
DR SMR; Q8TB45; -.
DR BioGRID; 122304; 82.
DR IntAct; Q8TB45; 11.
DR MINT; Q8TB45; -.
DR STRING; 9606.ENSP00000286234; -.
DR BindingDB; Q8TB45; -.
DR ChEMBL; CHEMBL4105866; -.
DR GlyGen; Q8TB45; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8TB45; -.
DR PhosphoSitePlus; Q8TB45; -.
DR BioMuta; DEPTOR; -.
DR DMDM; 251757257; -.
DR EPD; Q8TB45; -.
DR jPOST; Q8TB45; -.
DR MassIVE; Q8TB45; -.
DR MaxQB; Q8TB45; -.
DR PaxDb; 9606-ENSP00000286234; -.
DR PeptideAtlas; Q8TB45; -.
DR ProteomicsDB; 18583; -.
DR ProteomicsDB; 73961; -. [Q8TB45-1]
DR Pumba; Q8TB45; -.
DR Antibodypedia; 13704; 331 antibodies from 32 providers.
DR DNASU; 64798; -.
DR Ensembl; ENST00000286234.6; ENSP00000286234.5; ENSG00000155792.10. [Q8TB45-1]
DR Ensembl; ENST00000523492.5; ENSP00000430457.1; ENSG00000155792.10. [Q8TB45-2]
DR GeneID; 64798; -.
DR KEGG; hsa:64798; -.
DR MANE-Select; ENST00000286234.6; ENSP00000286234.5; NM_022783.4; NP_073620.2.
DR UCSC; uc003yow.6; human. [Q8TB45-1]
DR AGR; HGNC:22953; -.
DR CTD; 64798; -.
DR DisGeNET; 64798; -.
DR GeneCards; DEPTOR; -.
DR HGNC; HGNC:22953; DEPTOR.
DR HPA; ENSG00000155792; Tissue enhanced (skeletal muscle, tongue).
DR MIM; 612974; gene.
DR neXtProt; NX_Q8TB45; -.
DR OpenTargets; ENSG00000155792; -.
DR PharmGKB; PA134897957; -.
DR VEuPathDB; HostDB:ENSG00000155792; -.
DR eggNOG; ENOG502QS4Y; Eukaryota.
DR GeneTree; ENSGT00520000055667; -.
DR HOGENOM; CLU_042535_0_0_1; -.
DR InParanoid; Q8TB45; -.
DR OMA; HVCDDHL; -.
DR OrthoDB; 2953750at2759; -.
DR PhylomeDB; Q8TB45; -.
DR PathwayCommons; Q8TB45; -.
DR SignaLink; Q8TB45; -.
DR SIGNOR; Q8TB45; -.
DR BioGRID-ORCS; 64798; 10 hits in 1146 CRISPR screens.
DR ChiTaRS; DEPTOR; human.
DR GeneWiki; DEPTOR; -.
DR GenomeRNAi; 64798; -.
DR Pharos; Q8TB45; Tchem.
DR PRO; PR:Q8TB45; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q8TB45; Protein.
DR Bgee; ENSG00000155792; Expressed in parotid gland and 203 other cell types or tissues.
DR Genevisible; Q8TB45; HS.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0070300; F:phosphatidic acid binding; IDA:UniProtKB.
DR GO; GO:0004860; F:protein kinase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0030291; F:protein serine/threonine kinase inhibitor activity; IDA:UniProt.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0045792; P:negative regulation of cell size; IMP:UniProtKB.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IMP:UniProtKB.
DR GO; GO:0032007; P:negative regulation of TOR signaling; IMP:UniProtKB.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IDA:UniProtKB.
DR GO; GO:1903940; P:negative regulation of TORC2 signaling; IDA:UniProtKB.
DR GO; GO:0010508; P:positive regulation of autophagy; IDA:UniProtKB.
DR GO; GO:2001236; P:regulation of extrinsic apoptotic signaling pathway; IMP:UniProtKB.
DR CDD; cd04442; DEP_1_DEP6; 1.
DR CDD; cd04441; DEP_2_DEP6; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR037335; DEPTOR_DEP_1.
DR InterPro; IPR037336; DEPTOR_DEP_2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR22829; DEP DOMAIN PROTEIN; 1.
DR PANTHER; PTHR22829:SF18; DEP DOMAIN-CONTAINING MTOR-INTERACTING PROTEIN; 1.
DR Pfam; PF00610; DEP; 2.
DR SMART; SM00049; DEP; 2.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 2.
DR PROSITE; PS50186; DEP; 2.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Lipid-binding; Lysosome;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..409
FT /note="DEP domain-containing mTOR-interacting protein"
FT /id="PRO_0000284784"
FT DOMAIN 36..119
FT /note="DEP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT DOMAIN 145..219
FT /note="DEP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT DOMAIN 330..407
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 217..235
FT /note="DDEX motif"
FT /evidence="ECO:0000269|PubMed:33865870"
FT MOTIF 286..291
FT /note="BetaTrCP degron motif"
FT /evidence="ECO:0000269|PubMed:22017877"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 235
FT /note="Phosphoserine; by MAPK3"
FT /evidence="ECO:0000269|PubMed:35216969"
FT MOD_RES 241
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19446321"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19446321,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19446321"
FT MOD_RES 259
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19446321"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19446321"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19446321,
FT ECO:0000269|PubMed:22017875"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q570Y9"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19446321"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19446321"
FT MOD_RES 286
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000269|PubMed:22017875,
FT ECO:0000269|PubMed:22017876, ECO:0000269|PubMed:22017877"
FT MOD_RES 287
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000269|PubMed:19446321,
FT ECO:0000269|PubMed:22017875, ECO:0000269|PubMed:22017876,
FT ECO:0000269|PubMed:22017877"
FT MOD_RES 289
FT /note="Phosphotyrosine; by SYK"
FT /evidence="ECO:0000269|PubMed:34634301"
FT MOD_RES 291
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000269|PubMed:22017876,
FT ECO:0000269|PubMed:22017877"
FT MOD_RES 293
FT /note="Phosphoserine; by MTOR"
FT /evidence="ECO:0000269|PubMed:19446321,
FT ECO:0000269|PubMed:22017875"
FT MOD_RES 295
FT /note="Phosphothreonine; by MTOR"
FT /evidence="ECO:0000269|PubMed:22017875"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19446321"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19446321"
FT MOD_RES 299
FT /note="Phosphoserine; by MTOR"
FT /evidence="ECO:0000269|PubMed:19446321,
FT ECO:0000269|PubMed:22017875"
FT VAR_SEQ 42..142
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054681"
FT VARIANT 148
FT /note="N -> S (in dbSNP:rs34057546)"
FT /id="VAR_031816"
FT VARIANT 204
FT /note="N -> S (in dbSNP:rs2271900)"
FT /evidence="ECO:0000269|PubMed:11230166,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334"
FT /id="VAR_031817"
FT VARIANT 389
FT /note="S -> N (in dbSNP:rs4871827)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_031818"
FT MUTAGEN 53
FT /note="R->A: Decreased phosphatidic acid-binding."
FT /evidence="ECO:0000269|PubMed:33865870"
FT MUTAGEN 54
FT /note="R->A: Decreased phosphatidic acid-binding."
FT /evidence="ECO:0000269|PubMed:33865870"
FT MUTAGEN 58
FT /note="K->A: Decreased phosphatidic acid-binding."
FT /evidence="ECO:0000269|PubMed:33865870"
FT MUTAGEN 225
FT /note="R->A: Decreased phosphatidic acid-binding."
FT /evidence="ECO:0000269|PubMed:33865870"
FT MUTAGEN 231
FT /note="L->D: Decreased phosphatidic acid-binding."
FT /evidence="ECO:0000269|PubMed:33865870"
FT MUTAGEN 235
FT /note="S->A: Decreased phosphorylation, leading to impaired
FT deubiquitination by USP7."
FT /evidence="ECO:0000269|PubMed:35216969"
FT MUTAGEN 235
FT /note="S->D: Mimics phosphorylation, leading to slightly
FT increased stability."
FT /evidence="ECO:0000269|PubMed:35216969"
FT MUTAGEN 241
FT /note="T->A: In mutant 13A; abolished phosphorylation,
FT leading to promote interaction with MTOR without affecting
FT ability to bind phosphatidic acid; when associated with A-
FT 244, A-258, A-259, A-263, A-265, A-282, A-283, A-287, A-
FT 293, A-297, A-298 and A-299."
FT /evidence="ECO:0000269|PubMed:19446321,
FT ECO:0000269|PubMed:25936805"
FT MUTAGEN 244
FT /note="S->A: In mutant 13A; abolished phosphorylation,
FT leading to promote interaction with MTOR without affecting
FT ability to bind phosphatidic acid; when associated with A-
FT 241, A-258, A-259, A-263, A-265, A-282, A-283, A-287, A-
FT 293, A-297, A-298 and A-299."
FT /evidence="ECO:0000269|PubMed:19446321,
FT ECO:0000269|PubMed:25936805"
FT MUTAGEN 258
FT /note="S->A: In mutant 13A; abolished phosphorylation,
FT leading to promote interaction with MTOR without affecting
FT ability to bind phosphatidic acid; when associated with A-
FT 241, A-244, A-259, A-263, A-265, A-282, A-283, A-287, A-
FT 293, A-297, A-298 and A-299."
FT /evidence="ECO:0000269|PubMed:19446321,
FT ECO:0000269|PubMed:25936805"
FT MUTAGEN 259
FT /note="T->A: In mutant 13A; abolished phosphorylation,
FT leading to promote interaction with MTOR without affecting
FT ability to bind phosphatidic acid; when associated with A-
FT 241, A-244, A-258, A-263, A-265, A-282, A-283, A-287, A-
FT 293, A-297, A-298 and A-299."
FT /evidence="ECO:0000269|PubMed:19446321,
FT ECO:0000269|PubMed:25936805"
FT MUTAGEN 263
FT /note="S->A: In mutant 13A; abolished phosphorylation,
FT leading to promote interaction with MTOR without affecting
FT ability to bind phosphatidic acid; when associated with A-
FT 241, A-244, A-258, A-259, A-265, A-282, A-283, A-287, A-
FT 293, A-297, A-298 and A-299."
FT /evidence="ECO:0000269|PubMed:19446321,
FT ECO:0000269|PubMed:25936805"
FT MUTAGEN 265
FT /note="S->A: In mutant 13A; abolished phosphorylation,
FT leading to promote interaction with MTOR without affecting
FT ability to bind phosphatidic acid; when associated with A-
FT 241, A-244, A-258, A-259, A-263, A-282, A-283, A-287, A-
FT 293, A-297, A-298 and A-299."
FT /evidence="ECO:0000269|PubMed:19446321,
FT ECO:0000269|PubMed:25936805"
FT MUTAGEN 282
FT /note="S->A: In mutant 13A; abolished phosphorylation,
FT leading to promote interaction with MTOR without affecting
FT ability to bind phosphatidic acid; when associated with A-
FT 241, A-244, A-258, A-259, A-263, A-265, A-283, A-287, A-
FT 293, A-297, A-298 and A-299."
FT /evidence="ECO:0000269|PubMed:19446321,
FT ECO:0000269|PubMed:25936805"
FT MUTAGEN 283
FT /note="S->A: In mutant 13A; abolished phosphorylation,
FT leading to promote interaction with MTOR without affecting
FT ability to bind phosphatidic acid; when associated with A-
FT 241, A-244, A-258, A-259, A-263, A-265, A-282, A-287, A-
FT 293, A-297, A-298 and A-299."
FT /evidence="ECO:0000269|PubMed:19446321,
FT ECO:0000269|PubMed:25936805"
FT MUTAGEN 286..291
FT /note="SSGYFS->DDGYFD: Mimics phosphorylation; promoting
FT association with the SCF(BTRC) complex."
FT /evidence="ECO:0000269|PubMed:22017877"
FT MUTAGEN 286
FT /note="S->A: Reduced ubiquitination by the SCF(BTRC)
FT complex."
FT /evidence="ECO:0000269|PubMed:22017875,
FT ECO:0000269|PubMed:22017876, ECO:0000269|PubMed:22017877"
FT MUTAGEN 287
FT /note="S->A: In mutant 13A; abolished phosphorylation,
FT leading to promote interaction with MTOR without affecting
FT ability to bind phosphatidic acid; when associated with A-
FT 241, A-244, A-258, A-259, A-263, A-265, A-282, A-283, A-
FT 293, A-297, A-298 and A-299. Reduced ubiquitination by the
FT SCF(BTRC) complex."
FT /evidence="ECO:0000269|PubMed:19446321,
FT ECO:0000269|PubMed:22017876, ECO:0000269|PubMed:22017877,
FT ECO:0000269|PubMed:25936805"
FT MUTAGEN 289
FT /note="Y->E: Mimics phosphorylation, leading to slightly
FT decreased interaction with MTOR."
FT /evidence="ECO:0000269|PubMed:34634301"
FT MUTAGEN 289
FT /note="Y->F: Decreased phosphorylation, leading to
FT increased interaction with MTOR."
FT /evidence="ECO:0000269|PubMed:34634301"
FT MUTAGEN 291
FT /note="S->A: Reduced ubiquitination by the SCF(BTRC)
FT complex."
FT /evidence="ECO:0000269|PubMed:22017876,
FT ECO:0000269|PubMed:22017877"
FT MUTAGEN 293
FT /note="S->A: In mutant 13A; abolished phosphorylation,
FT leading to promote interaction with MTOR without affecting
FT ability to bind phosphatidic acid; when associated with A-
FT 241, A-244, A-258, A-259, A-263, A-265, A-282, A-283, A-
FT 287, A-297, A-298 and A-299. Reduced ubiquitination by the
FT SCF(BTRC) complex."
FT /evidence="ECO:0000269|PubMed:19446321,
FT ECO:0000269|PubMed:22017875, ECO:0000269|PubMed:25936805"
FT MUTAGEN 295..299
FT /note="TLSSS->ALSSA: Reduced ubiquitination by the
FT SCF(BTRC) complex."
FT /evidence="ECO:0000269|PubMed:22017875"
FT MUTAGEN 297
FT /note="S->A: In mutant 13A; abolished phosphorylation,
FT leading to promote interaction with MTOR without affecting
FT ability to bind phosphatidic acid; when associated with A-
FT 241, A-244, A-258, A-259, A-263, A-265, A-282, A-283, A-
FT 287, A-293, A-298 and A-299."
FT /evidence="ECO:0000269|PubMed:19446321,
FT ECO:0000269|PubMed:25936805"
FT MUTAGEN 298
FT /note="S->A: In mutant 13A; abolished phosphorylation,
FT leading to promote interaction with MTOR without affecting
FT ability to bind phosphatidic acid; when associated with A-
FT 241, A-244, A-258, A-259, A-263, A-265, A-282, A-283, A-
FT 287, A-293, A-297 and A-299."
FT /evidence="ECO:0000269|PubMed:19446321,
FT ECO:0000269|PubMed:25936805"
FT MUTAGEN 299
FT /note="S->A: In mutant 13A; abolished phosphorylation,
FT leading to promote interaction with MTOR without affecting
FT ability to bind phosphatidic acid; when associated with A-
FT 241, A-244, A-258, A-259, A-263, A-265, A-282, A-283, A-
FT 287, A-293, A-297 and A-298."
FT /evidence="ECO:0000269|PubMed:19446321,
FT ECO:0000269|PubMed:25936805"
FT MUTAGEN 326
FT /note="Y->F: Does not affect phosphorylation."
FT /evidence="ECO:0000269|PubMed:34634301"
FT CONFLICT 166
FT /note="M -> V (in Ref. 2; BAB14054)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="R -> G (in Ref. 1; CAB66613)"
FT /evidence="ECO:0000305"
FT HELIX 22..46
FT /evidence="ECO:0007829|PDB:7DKL"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:7DKL"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:7DKL"
FT HELIX 66..75
FT /evidence="ECO:0007829|PDB:7DKL"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:7PED"
FT HELIX 82..94
FT /evidence="ECO:0007829|PDB:7DKL"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:7DKL"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:7DKL"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:7DKL"
FT HELIX 118..121
FT /evidence="ECO:0007829|PDB:7DKL"
FT HELIX 128..143
FT /evidence="ECO:0007829|PDB:7DKL"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:7DKL"
FT STRAND 159..166
FT /evidence="ECO:0007829|PDB:7DKL"
FT HELIX 167..176
FT /evidence="ECO:0007829|PDB:7DKL"
FT HELIX 183..195
FT /evidence="ECO:0007829|PDB:7DKL"
FT STRAND 198..204
FT /evidence="ECO:0007829|PDB:7DKL"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:7DKL"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:7DKL"
FT HELIX 227..231
FT /evidence="ECO:0007829|PDB:7DKL"
FT HELIX 316..320
FT /evidence="ECO:0007829|PDB:7PE8"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:7PE7"
FT STRAND 329..333
FT /evidence="ECO:0007829|PDB:7PE8"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:7PE8"
FT STRAND 347..349
FT /evidence="ECO:0007829|PDB:7PE8"
FT STRAND 351..355
FT /evidence="ECO:0007829|PDB:7PE8"
FT HELIX 360..363
FT /evidence="ECO:0007829|PDB:7PE8"
FT STRAND 371..375
FT /evidence="ECO:0007829|PDB:7PE7"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:7PE8"
FT HELIX 385..394
FT /evidence="ECO:0007829|PDB:7PE8"
FT STRAND 397..403
FT /evidence="ECO:0007829|PDB:7PE8"
SQ SEQUENCE 409 AA; 46294 MW; AD132F0E9AFFB90C CRC64;
MEEGGSTGSA GSDSSTSGSG GAQQRELERM AEVLVTGEQL RLRLHEEKVI KDRRHHLKTY
PNCFVAKELI DWLIEHKEAS DRETAIKLMQ KLADRGIIHH VCDEHKEFKD VKLFYRFRKD
DGTFPLDNEV KAFMRGQRLY EKLMSPENTL LQPREEEGVK YERTFMASEF LDWLVQEGEA
TTRKEAEQLC HRLMEHGIIQ HVSNKHPFVD SNLLYQFRMN FRRRRRLMEL LNEKSPSSQE
THDSPFCLRK QSHDNRKSTS FMSVSPSKEI KIVSAVRRSS MSSCGSSGYF SSSPTLSSSP
PVLCNPKSVL KRPVTSEELL TPGAPYARKT FTIVGDAVGW GFVVRGSKPC HIQAVDPSGP
AAAAGMKVCQ FVVSVNGLNV LHVDYRTVSN LILTGPRTIV MEVMEELEC
//
