RPTOR_MOUSE
ID RPTOR_MOUSE Reviewed; 1335 AA.
AC Q8K4Q0; Q8C9W9; Q8CBY4; Q8CDY8; Q9D4H3;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Regulatory-associated protein of mTOR {ECO:0000305};
DE Short=Raptor {ECO:0000303|PubMed:33495318};
DE AltName: Full=p150 target of rapamycin (TOR)-scaffold protein;
GN Name=Rptor {ECO:0000312|MGI:MGI:1921620};
GN Synonyms=Raptor {ECO:0000303|PubMed:33495318};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=12150926; DOI=10.1016/s0092-8674(02)00833-4;
RA Hara K., Maruki Y., Long X., Yoshino K., Oshiro N., Hidayat S.,
RA Tokunaga C., Avruch J., Yonezawa K.;
RT "Raptor, a binding partner of target of rapamycin (TOR), mediates TOR
RT action.";
RL Cell 110:177-189(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4 AND 5).
RC STRAIN=C57BL/6J; TISSUE=Diencephalon, Head, Testis, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [4]
RP PHOSPHORYLATION AT SER-722 AND SER-792, AND MUTAGENESIS OF SER-722 AND
RP SER-792.
RX PubMed=18439900; DOI=10.1016/j.molcel.2008.03.003;
RA Gwinn D.M., Shackelford D.B., Egan D.F., Mihaylova M.M., Mery A.,
RA Vasquez D.S., Turk B.E., Shaw R.J.;
RT "AMPK phosphorylation of raptor mediates a metabolic checkpoint.";
RL Mol. Cell 30:214-226(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859 AND SER-863, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION AT SER-859 AND SER-863 BY MTOR.
RX PubMed=19346248; DOI=10.1074/jbc.c109.002907;
RA Wang L., Lawrence J.C. Jr., Sturgill T.W., Harris T.E.;
RT "Mammalian target of rapamycin complex 1 (mTORC1) activity is associated
RT with phosphorylation of raptor by mTOR.";
RL J. Biol. Chem. 284:14693-14697(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859; SER-863; THR-865 AND
RP SER-877, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP INTERACTION WITH MTOR.
RX PubMed=20801936; DOI=10.1101/gad.1956410;
RA Takai H., Xie Y., de Lange T., Pavletich N.P.;
RT "Tel2 structure and function in the Hsp90-dependent maturation of mTOR and
RT ATR complexes.";
RL Genes Dev. 24:2019-2030(2010).
RN [9]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=33495318; DOI=10.1073/pnas.2020705118;
RA De Gregorio D., Popic J., Enns J.P., Inserra A., Skalecka A.,
RA Markopoulos A., Posa L., Lopez-Canul M., Qianzi H., Lafferty C.K.,
RA Britt J.P., Comai S., Aguilar-Valles A., Sonenberg N., Gobbi G.;
RT "Lysergic acid diethylamide (LSD) promotes social behavior through mTORC1
RT in the excitatory neurotransmission.";
RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021).
CC -!- FUNCTION: Involved in the control of the mammalian target of rapamycin
CC complex 1 (mTORC1) activity which regulates cell growth and survival,
CC and autophagy in response to nutrient and hormonal signals; functions
CC as a scaffold for recruiting mTORC1 substrates. mTORC1 is activated in
CC response to growth factors or amino acids. Growth factor-stimulated
CC mTORC1 activation involves a AKT1-mediated phosphorylation of TSC1-
CC TSC2, which leads to the activation of the RHEB GTPase that potently
CC activates the protein kinase activity of mTORC1. Amino acid-signaling
CC to mTORC1 requires its relocalization to the lysosomes mediated by the
CC Ragulator complex and the Rag GTPases. Activated mTORC1 up-regulates
CC protein synthesis by phosphorylating key regulators of mRNA translation
CC and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it
CC from inhibiting the elongation initiation factor 4E (eiF4E). mTORC1
CC phosphorylates and activates S6K1 at 'Thr-389', which then promotes
CC protein synthesis by phosphorylating PDCD4 and targeting it for
CC degradation. Involved in ciliogenesis. mTORC1 complex in excitatory
CC neuronal transmission is required for the prosocial behavior induced by
CC the psychoactive substance lysergic acid diethylamide (LSD)
CC (PubMed:33495318). {ECO:0000250|UniProtKB:Q8N122,
CC ECO:0000269|PubMed:33495318}.
CC -!- SUBUNIT: Part of the mammalian target of rapamycin complex 1 (mTORC1)
CC which contains MTOR, MLST8, RPTOR, AKT1S1/PRAS40 and DEPTOR
CC (PubMed:20801936). mTORC1 binds to and is inhibited by FKBP12-
CC rapamycin. Binds directly to 4EBP1 and RPS6KB1 independently of its
CC association with MTOR. Binds preferentially to poorly or non-
CC phosphorylated forms of EIF4EBP1, and this binding is critical to the
CC ability of MTOR to catalyze phosphorylation. Forms a complex with MTOR
CC under both leucine-rich and -poor conditions. Interacts with ULK1 in a
CC nutrient-dependent manner; the interaction is reduced during
CC starvation. Interacts (when phosphorylated by AMPK) with 14-3-3
CC protein, leading to inhibition of its activity. Interacts with SPAG5;
CC SPAG5 competes with MTOR for RPTOR-binding, resulting in decreased
CC mTORC1 formation. Interacts with WAC; WAC positively regulates MTOR
CC activity by promoting the assembly of the TTT complex composed of
CC TELO2, TTI1 and TTI2 and the RUVBL complex composed of RUVBL1 and
CC RUVBL2 into the TTT-RUVBL complex which leads to the dimerization of
CC the mTORC1 complex and its subsequent activation. Interacts with G3BP1.
CC The complex formed with G3BP1 AND SPAG5 is increased by oxidative
CC stress. Interacts with HTR6. Interacts with PIH1D1. Interacts with
CC LARP1. Interacts with BRAT1. Interacts with SIK3 (By similarity).
CC {ECO:0000250|UniProtKB:Q8N122, ECO:0000269|PubMed:20801936}.
CC -!- INTERACTION:
CC Q8K4Q0; Q9JLN9: Mtor; NbExp=9; IntAct=EBI-4567273, EBI-1571628;
CC Q8K4Q0; Q00899: Yy1; NbExp=3; IntAct=EBI-4567273, EBI-6921536;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Lysosome {ECO:0000250}.
CC Cytoplasmic granule {ECO:0000250|UniProtKB:Q8N122}. Note=Targeting to
CC lysosomes depends on amino acid availability. In arsenite-stressed
CC cells, accumulates in stress granules when associated with SPAG5 and
CC association with lysosomes is drastically decreased. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8K4Q0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K4Q0-2; Sequence=VSP_010175, VSP_010181, VSP_010182;
CC Name=3;
CC IsoId=Q8K4Q0-3; Sequence=VSP_010177, VSP_010179, VSP_010180;
CC Name=4;
CC IsoId=Q8K4Q0-4; Sequence=VSP_010176, VSP_010183, VSP_010184;
CC Name=5;
CC IsoId=Q8K4Q0-5; Sequence=VSP_010178;
CC -!- PTM: Insulin-stimulated phosphorylation at Ser-863 by MTOR and MAPK8
CC up-regulates mTORC1 activity. Osmotic stress also induces
CC phosphorylation at Ser-696, Thr-706 and Ser-863 by MAPK8. Ser-863
CC phosphorylation is required for phosphorylation at Ser-855 and Ser-859
CC (By similarity). In response to nutrient limitation, phosphorylated by
CC AMPK; phosphorylation promotes interaction with 14-3-3 proteins,
CC leading to negative regulation of the mTORC1 complex. In response to
CC growth factors, phosphorylated at Ser-719, Ser-721 and Ser-722 by
CC RPS6KA1, which stimulates mTORC1 activity.
CC {ECO:0000250|UniProtKB:Q8N122, ECO:0000269|PubMed:18439900,
CC ECO:0000269|PubMed:19346248}.
CC -!- DISRUPTION PHENOTYPE: Conditional knockout mice in excitatory neurons
CC do not show any prosocial effects of lysergic acid diethylamide (LSD)
CC unlike control mice. Conditional knockout mice in inhibitory neurons
CC show no different LSD-induced prosocial behavior compared to control
CC mice. {ECO:0000269|PubMed:33495318}.
CC -!- SIMILARITY: Belongs to the WD repeat RAPTOR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK029341; 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; AB082952; BAC06491.1; -; mRNA.
DR EMBL; AK016530; BAB30288.1; -; mRNA.
DR EMBL; AK029341; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK034306; BAC28669.1; -; mRNA.
DR EMBL; AK040288; BAC30561.1; -; mRNA.
DR CCDS; CCDS25720.1; -. [Q8K4Q0-1]
DR AlphaFoldDB; Q8K4Q0; -.
DR SMR; Q8K4Q0; -.
DR ComplexPortal; CPX-4473; mTORC1 complex.
DR DIP; DIP-46324N; -.
DR IntAct; Q8K4Q0; 7.
DR MINT; Q8K4Q0; -.
DR STRING; 10090.ENSMUSP00000026671; -.
DR iPTMnet; Q8K4Q0; -.
DR PhosphoSitePlus; Q8K4Q0; -.
DR EPD; Q8K4Q0; -.
DR jPOST; Q8K4Q0; -.
DR MaxQB; Q8K4Q0; -.
DR PaxDb; Q8K4Q0; -.
DR PeptideAtlas; Q8K4Q0; -.
DR PRIDE; Q8K4Q0; -.
DR ProteomicsDB; 299809; -. [Q8K4Q0-1]
DR ProteomicsDB; 299810; -. [Q8K4Q0-2]
DR ProteomicsDB; 299811; -. [Q8K4Q0-3]
DR ProteomicsDB; 299812; -. [Q8K4Q0-4]
DR ProteomicsDB; 299813; -. [Q8K4Q0-5]
DR UCSC; uc007mqw.1; mouse. [Q8K4Q0-5]
DR UCSC; uc007mra.1; mouse. [Q8K4Q0-1]
DR MGI; MGI:1921620; Rptor.
DR eggNOG; KOG1517; Eukaryota.
DR InParanoid; Q8K4Q0; -.
DR PhylomeDB; Q8K4Q0; -.
DR Reactome; R-MMU-1632852; Macroautophagy.
DR Reactome; R-MMU-165159; MTOR signalling.
DR Reactome; R-MMU-166208; mTORC1-mediated signalling.
DR Reactome; R-MMU-3371571; HSF1-dependent transactivation.
DR Reactome; R-MMU-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR Reactome; R-MMU-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-MMU-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-MMU-9639288; Amino acids regulate mTORC1.
DR ChiTaRS; Rptor; mouse.
DR PRO; PR:Q8K4Q0; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8K4Q0; protein.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0031931; C:TORC1 complex; ISS:UniProtKB.
DR GO; GO:0071889; F:14-3-3 protein binding; ISO:MGI.
DR GO; GO:0030295; F:protein kinase activator activity; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0030291; F:protein serine/threonine kinase inhibitor activity; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:MGI.
DR GO; GO:0001002; F:RNA polymerase III type 1 promoter sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0001003; F:RNA polymerase III type 2 promoter sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0001006; F:RNA polymerase III type 3 promoter sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0001156; F:TFIIIC-class transcription factor complex binding; ISO:MGI.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IC:ComplexPortal.
DR GO; GO:0071456; P:cellular response to hypoxia; IC:ComplexPortal.
DR GO; GO:0071233; P:cellular response to leucine; ISO:MGI.
DR GO; GO:0031669; P:cellular response to nutrient levels; ISO:MGI.
DR GO; GO:0071470; P:cellular response to osmotic stress; IC:ComplexPortal.
DR GO; GO:0009267; P:cellular response to starvation; IBA:GO_Central.
DR GO; GO:0010507; P:negative regulation of autophagy; IC:ComplexPortal.
DR GO; GO:0046676; P:negative regulation of insulin secretion; IMP:CACAO.
DR GO; GO:0016310; P:phosphorylation; ISO:MGI.
DR GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:MGI.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:0045821; P:positive regulation of glycolytic process; IC:ComplexPortal.
DR GO; GO:0046889; P:positive regulation of lipid biosynthetic process; IC:ComplexPortal.
DR GO; GO:1905857; P:positive regulation of pentose-phosphate shunt; IC:ComplexPortal.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; ISO:MGI.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0032008; P:positive regulation of TOR signaling; ISS:UniProtKB.
DR GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; ISO:MGI.
DR GO; GO:0010506; P:regulation of autophagy; IBA:GO_Central.
DR GO; GO:0001558; P:regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0008361; P:regulation of cell size; ISO:MGI.
DR GO; GO:0042325; P:regulation of phosphorylation; ISO:MGI.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IMP:CACAO.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:UniProtKB.
DR GO; GO:0035176; P:social behavior; IMP:UniProtKB.
DR GO; GO:0031929; P:TOR signaling; ISS:UniProtKB.
DR GO; GO:0038202; P:TORC1 signaling; ISO:MGI.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000357; HEAT.
DR InterPro; IPR004083; Raptor.
DR InterPro; IPR029347; Raptor_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR12848; PTHR12848; 1.
DR Pfam; PF02985; HEAT; 1.
DR Pfam; PF14538; Raptor_N; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM01302; Raptor_N; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Lysosome; Phosphoprotein;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN 1..1335
FT /note="Regulatory-associated protein of mTOR"
FT /id="PRO_0000051201"
FT REPEAT 1020..1061
FT /note="WD 1"
FT REPEAT 1065..1106
FT /note="WD 2"
FT REPEAT 1121..1160
FT /note="WD 3"
FT REPEAT 1164..1203
FT /note="WD 4"
FT REPEAT 1209..1249
FT /note="WD 5"
FT REPEAT 1251..1291
FT /note="WD 6"
FT REPEAT 1299..1335
FT /note="WD 7"
FT REGION 749..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 853..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..922
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..942
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 696
FT /note="Phosphoserine; by MAPK8"
FT /evidence="ECO:0000250|UniProtKB:Q8N122"
FT MOD_RES 706
FT /note="Phosphothreonine; by MAPK8"
FT /evidence="ECO:0000250|UniProtKB:Q8N122"
FT MOD_RES 719
FT /note="Phosphoserine; by RPS6KA1"
FT /evidence="ECO:0000250|UniProtKB:Q8N122"
FT MOD_RES 721
FT /note="Phosphoserine; by RPS6KA1"
FT /evidence="ECO:0000250|UniProtKB:Q8N122"
FT MOD_RES 722
FT /note="Phosphoserine; by AMPK and RPS6KA1"
FT /evidence="ECO:0000269|PubMed:18439900"
FT MOD_RES 738
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N122"
FT MOD_RES 792
FT /note="Phosphoserine; by AMPK"
FT /evidence="ECO:0000269|PubMed:18439900"
FT MOD_RES 855
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N122"
FT MOD_RES 859
FT /note="Phosphoserine; by MTOR"
FT /evidence="ECO:0000269|PubMed:19346248,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 863
FT /note="Phosphoserine; by MAPK8 and MTOR"
FT /evidence="ECO:0000269|PubMed:19346248,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 865
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 877
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..954
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010176"
FT VAR_SEQ 1..421
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010177"
FT VAR_SEQ 1..185
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010175"
FT VAR_SEQ 298..1335
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010178"
FT VAR_SEQ 701..728
FT /note="EGGSLTPVRDSPCTPRLRSVSSYGNIRA -> GTGVAGSLGPPSGPSPGQSV
FT AWVQPGQV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010179"
FT VAR_SEQ 729..1335
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010180"
FT VAR_SEQ 841..843
FT /note="ATV -> VCI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010181"
FT VAR_SEQ 844..1335
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010182"
FT VAR_SEQ 1202
FT /note="C -> W (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010183"
FT VAR_SEQ 1203..1335
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010184"
FT MUTAGEN 722
FT /note="S->A: Abolishes AMPK-mediated phosphorylation; when
FT associated with A-792."
FT /evidence="ECO:0000269|PubMed:18439900"
FT MUTAGEN 792
FT /note="S->A: Abolishes AMPK-mediated phosphorylation; when
FT associated with A-722."
FT /evidence="ECO:0000269|PubMed:18439900"
FT CONFLICT 630
FT /note="S -> F (in Ref. 2; AK029341/BAB30288)"
FT /evidence="ECO:0000305"
FT CONFLICT 970
FT /note="A -> P (in Ref. 2; BAC30561)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1335 AA; 149471 MW; 26702199FF7C8136 CRC64;
MESEMLQSPL MGLGEEDEAD LTDWNLPLAF MKKRHCEKIE GSKSLAQSWR MKDRMKTVSV
ALVLCLNVGV DPPDVVKTTP CARLECWIDP LSMGPQKALE TIGANLQKQY ENWQPRARYK
QSLDPTVDEV KKLCTSLRRN AKEERVLFHY NGHGVPRPTV NGEVWVFNKN YTQYIPLSIY
DLQTWMGSPS IFVYDCSNAG LIVKSFKQFA LQREQELEVA AINPNHPLAQ MPLPPSMKNC
IQLAACEAHE LLPMIPDLPA DLFTSCLTTP IKIALRWFCM QKCVSLVPGV TLDLIEKIPG
RLNDRRTPLG ELNWIFTAIT DTIAWNVLPR DLFQKLFRQD LLVASLFRNF LLAERIMRSY
NCTPVSSPRL PPTYMHAMWQ AWDLAVDICL SQLPTIIEEG TAFRHSPFFA EQLTAFQVWL
TMGVENRSPP EQLPIVLQVL LSQVHRLRAL DLLGRFLDLG PWAVSLALSV GIFPYVLKLL
QSSARELRPL LVFIWAKILA VDSSCQADLV KDNGHKYFLS VLADPYMPAE HRTMTAFILA
VIVNSYTTGQ EACLQGNLIA ICLEQLSDPH PLLRQWVAIC LGRIWQNFDS ARWCGVRDSA
HEKLYSLLSD PIPEVRCAAV FALGTFVGNS AERTDHSTTI DHNVAMMLAQ LINDGSPMVR
KELVVALSHL VVQYESNFCT VALQFMEEEK NYPLPSPAAT EGGSLTPVRD SPCTPRLRSV
SSYGNIRAVT TARNLNKSLQ NLSLTEESGS SVAFSPGNLS TSSSASSTLG SPENEEYILS
FETIDKMRRV SSYSALNSLI GVSFNSVYTQ IWRVLLHLAA DPYPDVSDLA MKVLNSIAYK
ATVNARPQRI LDTSSLTQSA PASPTNKGMH MHQVGGSPPA SSTSSCSLTN DVAKQTVSRD
LPSSRPGTAG PTGAQYTPHS HQFPRTRKMF DKGPDQTTDD ADDAAGHKSF ICASMQTGFC
DWSARYFAQA VMKIPEEHDL ESQIRKEREW RFLRNTRVRK QAQQVIQKGI TRLDDQIFLN
RNPGVPSVVK FHPFTPCIAV ADKDSICFWD WEKGEKLDYF HNGNPRYTRV TAMEYLNGQD
CSLLLTATDD GAIRVWKNFA DLEKNPEMVT AWQGLSDMLP TTRGAGMVVD WEQETGLLMS
SGDVRIVRIW DTDRETKVQD IPTGADSCVT SLSCDSHRSL IVAGLGDGSI RVYDRRMALS
ECRVMTYREH TAWVVKAYLQ KHPEGHIVSV SVNGDVRFFD PRMPESVNVM QIVKGLTALD
IHPQANLIAC GSMNQFTAIY NGNGELINNI KYYDGFMGQR VGAISCLAFH PHWPHLAVGS
NDYYISVYSV EKRVR
