TFE3_MOUSE
ID TFE3_MOUSE Reviewed; 572 AA.
AC Q64092; A2AEW3; A2AEW4; Q3U8H0; Q3UMV4; Q3UT52; Q7TNC1; Q8BN29;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Transcription factor E3 {ECO:0000303|PubMed:1732746};
DE Short=mTFE3 {ECO:0000303|PubMed:1732746};
GN Name=Tfe3 {ECO:0000303|PubMed:1732746, ECO:0000312|MGI:MGI:98511};
GN Synonyms=Tcfe3;
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 [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, Egg, Lung, and Spleen;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 127-572.
RX PubMed=1732746; DOI=10.1128/mcb.12.2.817-827.1992;
RA Roman C., Matera A.G., Cooper C., Artandi S., Blain S., Ward D.C.,
RA Calame K.;
RT "mTFE3, an X-linked transcriptional activator containing basic helix-loop-
RT helix and zipper domains, utilizes the zipper to stabilize both DNA binding
RT and multimerization.";
RL Mol. Cell. Biol. 12:817-827(1992).
RN [5]
RP FUNCTION, DNA-BINDING, AND TISSUE SPECIFICITY.
RX PubMed=16936731; DOI=10.1038/ni1378;
RA Huan C., Kelly M.L., Steele R., Shapira I., Gottesman S.R.S., Roman C.A.J.;
RT "Transcription factors TFE3 and TFEB are critical for CD40 ligand
RT expression and thymus-dependent humoral immunity.";
RL Nat. Immunol. 7:1082-1091(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-545; SER-551; SER-553 AND
RP SER-557, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, 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 [7]
RP SUBCELLULAR LOCATION.
RX PubMed=21209915; DOI=10.1371/journal.pone.0015793;
RA Hong S.B., Oh H., Valera V.A., Baba M., Schmidt L.S., Linehan W.M.;
RT "Inactivation of the FLCN tumor suppressor gene induces TFE3
RT transcriptional activity by increasing its nuclear localization.";
RL PLoS ONE 5:E15793-E15793(2010).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23582324; DOI=10.1016/j.cell.2013.03.012;
RA Betschinger J., Nichols J., Dietmann S., Corrin P.D., Paddison P.J.,
RA Smith A.;
RT "Exit from pluripotency is gated by intracellular redistribution of the
RT bHLH transcription factor Tfe3.";
RL Cell 153:335-347(2013).
RN [9]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-187, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-320, AND MUTAGENESIS
RP OF SER-320.
RX PubMed=27913603; DOI=10.1101/gad.287953.116;
RA Wada S., Neinast M., Jang C., Ibrahim Y.H., Lee G., Babu A., Li J.,
RA Hoshino A., Rowe G.C., Rhee J., Martina J.A., Puertollano R., Blenis J.,
RA Morley M., Baur J.A., Seale P., Arany Z.;
RT "The tumor suppressor FLCN mediates an alternate mTOR pathway to regulate
RT browning of adipose tissue.";
RL Genes Dev. 30:2551-2564(2016).
RN [11]
RP FUNCTION.
RX PubMed=29146937; DOI=10.1038/s41467-017-01871-z;
RA Willett R., Martina J.A., Zewe J.P., Wills R., Hammond G.R.V.,
RA Puertollano R.;
RT "TFEB regulates lysosomal positioning by modulating TMEM55B expression and
RT JIP4 recruitment to lysosomes.";
RL Nat. Commun. 8:1580-1580(2017).
RN [12]
RP FUNCTION, AND INTERACTION WITH RRAGC AND RRAGD.
RX PubMed=30595499; DOI=10.1016/j.stem.2018.11.021;
RA Villegas F., Lehalle D., Mayer D., Rittirsch M., Stadler M.B., Zinner M.,
RA Olivieri D., Vabres P., Duplomb-Jego L., De Bont E.S.J.M., Duffourd Y.,
RA Duijkers F., Avila M., Genevieve D., Houcinat N., Jouan T., Kuentz P.,
RA Lichtenbelt K.D., Thauvin-Robinet C., St-Onge J., Thevenon J.,
RA van Gassen K.L.I., van Haelst M., van Koningsbruggen S., Hess D.,
RA Smallwood S.A., Riviere J.B., Faivre L., Betschinger J.;
RT "Lysosomal signaling licenses embryonic stem cell differentiation via
RT inactivation of Tfe3.";
RL Cell Stem Cell 24:257-270(2019).
CC -!- FUNCTION: Transcription factor that acts as a master regulator of
CC lysosomal biogenesis and immune response (PubMed:16936731,
CC PubMed:29146937). Specifically recognizes and binds E-box sequences
CC (5'-CANNTG-3'); efficient DNA-binding requires dimerization with itself
CC or with another MiT/TFE family member such as TFEB or MITF
CC (PubMed:16936731). Involved in the cellular response to amino acid
CC availability by acting downstream of MTOR: in the presence of
CC nutrients, TFE3 phosphorylation by MTOR promotes its cytosolic
CC retention and subsequent inactivation (PubMed:27913603). Upon
CC starvation or lysosomal stress, inhibition of MTOR induces TFE3
CC dephosphorylation, resulting in nuclear localization and transcription
CC factor activity (PubMed:27913603). Maintains the pluripotent state of
CC embryonic stem cells by promoting the expression of genes such as
CC ESRRB; mTOR-dependent TFE3 cytosolic retention and inactivation
CC promotes exit from pluripotency (PubMed:23582324). Required to maintain
CC the naive pluripotent state of hematopoietic stem cell (By similarity).
CC TFE3 activity is also involved in the inhibition of neuronal progenitor
CC differentiation (PubMed:30595499). Acts as a positive regulator of
CC browning of adipose tissue by promoting expression of target genes;
CC mTOR-dependent phosphorylation and cytoplasmic retention of TFE3
CC inhibits browning of adipose tissue (PubMed:27913603). In association
CC with TFEB, activates the expression of CD40L in T-cells, thereby
CC playing a role in T-cell-dependent antibody responses in activated
CC CD4(+) T-cells and thymus-dependent humoral immunity (PubMed:16936731).
CC Specifically recognizes the MUE3 box, a subset of E-boxes, present in
CC the immunoglobulin enhancer (By similarity). It also binds very well to
CC a USF/MLTF site. May regulate lysosomal positioning in response to
CC nutrient deprivation by promoting the expression of PIP4P1
CC (PubMed:29146937). {ECO:0000250|UniProtKB:P19532,
CC ECO:0000269|PubMed:16936731, ECO:0000269|PubMed:23582324,
CC ECO:0000269|PubMed:27913603, ECO:0000269|PubMed:29146937,
CC ECO:0000269|PubMed:30595499}.
CC -!- SUBUNIT: Homodimer and heterodimer; with TFEB or MITF. Interacts with
CC RRAGC/RagC GDP-bound and RRAGD/RagD GDP-bound (PubMed:30595499).
CC {ECO:0000250|UniProtKB:P19532, ECO:0000269|PubMed:30595499}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:23582324,
CC ECO:0000269|PubMed:27913603, ECO:0000305|PubMed:21209915}. Nucleus
CC {ECO:0000269|PubMed:21209915, ECO:0000269|PubMed:23582324,
CC ECO:0000269|PubMed:27913603}. Note=When nutrients are present,
CC phosphorylation by MTOR prevents nuclear translocation and activity
CC (PubMed:23582324, PubMed:27913603). Conversely, inhibition of mTORC1,
CC starvation and lysosomal disruption, promotes dephosphorylation and
CC translocation to the nucleus (PubMed:23582324, PubMed:27913603).
CC {ECO:0000269|PubMed:23582324, ECO:0000269|PubMed:27913603}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q64092-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q64092-2; Sequence=VSP_022143;
CC Name=3;
CC IsoId=Q64092-3; Sequence=VSP_022143, VSP_022144;
CC Name=4;
CC IsoId=Q64092-4; Sequence=VSP_022144;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16936731}.
CC -!- PTM: Sumoylated; does not affect dimerization with MITF.
CC {ECO:0000250|UniProtKB:P19532}.
CC -!- PTM: Phosphorylation by MTOR regulates its subcellular location and
CC activity (PubMed:27913603). When nutrients are present, phosphorylation
CC by MTOR promotes retention in the cytosol (PubMed:27913603). Inhibition
CC of mTORC1, starvation and lysosomal disruption, promotes
CC dephosphorylation and translocation to the nucleus (PubMed:27913603).
CC {ECO:0000269|PubMed:27913603}.
CC -!- SIMILARITY: Belongs to the MiT/TFE family. {ECO:0000305}.
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DR EMBL; AK089762; BAC40955.1; -; mRNA.
DR EMBL; AK139756; BAE24128.1; -; mRNA.
DR EMBL; AK144657; BAE25994.1; -; mRNA.
DR EMBL; AK152221; BAE31048.1; -; mRNA.
DR EMBL; AL671995; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC056358; AAH56358.1; -; mRNA.
DR EMBL; BC063047; AAH63047.1; -; mRNA.
DR EMBL; S76673; AAB21130.1; -; mRNA.
DR CCDS; CCDS52984.1; -. [Q64092-1]
DR CCDS; CCDS52985.1; -. [Q64092-4]
DR CCDS; CCDS72332.1; -. [Q64092-2]
DR CCDS; CCDS72333.1; -. [Q64092-3]
DR PIR; A42029; A42029.
DR RefSeq; NP_001098666.1; NM_001105196.1.
DR RefSeq; NP_001098667.1; NM_001105197.1. [Q64092-2]
DR RefSeq; NP_001258418.1; NM_001271489.1. [Q64092-2]
DR RefSeq; NP_001258419.1; NM_001271490.1. [Q64092-2]
DR RefSeq; NP_001258420.1; NM_001271491.1. [Q64092-3]
DR RefSeq; NP_766060.2; NM_172472.3.
DR RefSeq; XP_006527641.1; XM_006527578.2. [Q64092-2]
DR RefSeq; XP_017173942.1; XM_017318453.1. [Q64092-2]
DR RefSeq; XP_017173943.1; XM_017318454.1. [Q64092-3]
DR AlphaFoldDB; Q64092; -.
DR SMR; Q64092; -.
DR BioGRID; 229078; 324.
DR IntAct; Q64092; 1.
DR STRING; 10090.ENSMUSP00000076864; -.
DR iPTMnet; Q64092; -.
DR PhosphoSitePlus; Q64092; -.
DR jPOST; Q64092; -.
DR MaxQB; Q64092; -.
DR PaxDb; Q64092; -.
DR PRIDE; Q64092; -.
DR ProteomicsDB; 263164; -. [Q64092-1]
DR ProteomicsDB; 263165; -. [Q64092-2]
DR ProteomicsDB; 263166; -. [Q64092-3]
DR ProteomicsDB; 263167; -. [Q64092-4]
DR Antibodypedia; 11943; 429 antibodies from 40 providers.
DR DNASU; 209446; -.
DR Ensembl; ENSMUST00000101695; ENSMUSP00000099219; ENSMUSG00000000134. [Q64092-2]
DR Ensembl; ENSMUST00000115677; ENSMUSP00000111341; ENSMUSG00000000134. [Q64092-2]
DR Ensembl; ENSMUST00000115678; ENSMUSP00000111342; ENSMUSG00000000134. [Q64092-3]
DR Ensembl; ENSMUST00000115679; ENSMUSP00000111343; ENSMUSG00000000134. [Q64092-2]
DR Ensembl; ENSMUST00000137467; ENSMUSP00000134125; ENSMUSG00000000134. [Q64092-2]
DR GeneID; 209446; -.
DR KEGG; mmu:209446; -.
DR UCSC; uc009smg.2; mouse. [Q64092-1]
DR UCSC; uc009smk.2; mouse. [Q64092-3]
DR CTD; 7030; -.
DR MGI; MGI:98511; Tfe3.
DR VEuPathDB; HostDB:ENSMUSG00000000134; -.
DR eggNOG; KOG1318; Eukaryota.
DR GeneTree; ENSGT00940000157503; -.
DR HOGENOM; CLU_031638_3_2_1; -.
DR InParanoid; Q64092; -.
DR OMA; DEMRWNK; -.
DR OrthoDB; 1211990at2759; -.
DR BioGRID-ORCS; 209446; 5 hits in 73 CRISPR screens.
DR PRO; PR:Q64092; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q64092; protein.
DR Bgee; ENSMUSG00000000134; Expressed in animal zygote and 220 other tissues.
DR ExpressionAtlas; Q64092; baseline and differential.
DR Genevisible; Q64092; MM.
DR GO; GO:0005737; C:cytoplasm; IMP:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IC:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0006959; P:humoral immune response; IMP:UniProtKB.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0090336; P:positive regulation of brown fat cell differentiation; IMP:UniProtKB.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0045670; P:regulation of osteoclast differentiation; IGI:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR021802; MiT/TFE_C.
DR InterPro; IPR031867; MiT/TFE_N.
DR InterPro; IPR024100; TFE3.
DR PANTHER; PTHR45776:SF3; PTHR45776:SF3; 1.
DR Pfam; PF11851; DUF3371; 1.
DR Pfam; PF00010; HLH; 1.
DR Pfam; PF15951; MITF_TFEB_C_3_N; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW Activator; Adaptive immunity; Alternative splicing; Cytoplasm; DNA-binding;
KW Immunity; Isopeptide bond; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..572
FT /note="Transcription factor E3"
FT /id="PRO_0000127472"
FT DOMAIN 345..398
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 87..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..270
FT /note="Strong transcription activation domain"
FT /evidence="ECO:0000255"
FT REGION 408..429
FT /note="Leucine-zipper"
FT REGION 439..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 187
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 320
FT /note="Phosphoserine; by MTOR"
FT /evidence="ECO:0000269|PubMed:27913603"
FT MOD_RES 539
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19532"
FT MOD_RES 545
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 551
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 553
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 557
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 565
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19532"
FT CROSSLNK 338
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P19532"
FT VAR_SEQ 1..105
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022143"
FT VAR_SEQ 260..294
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022144"
FT MUTAGEN 320
FT /note="S->A: Impaired phosphorylation by MTOR, leading to
FT constitutive nuclear localization."
FT /evidence="ECO:0000269|PubMed:27913603"
FT CONFLICT 73
FT /note="F -> S (in Ref. 1; BAE24128/BAE25994)"
FT /evidence="ECO:0000305"
FT CONFLICT 127..131
FT /note="QERRE -> TSGTR (in Ref. 4; AAB21130)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="S -> G (in Ref. 1; BAE25994)"
FT /evidence="ECO:0000305"
FT CONFLICT 558
FT /note="K -> N (in Ref. 4; AAB21130)"
FT /evidence="ECO:0000305"
FT CONFLICT 568
FT /note="M -> I (in Ref. 4; AAB21130)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 572 AA; 61536 MW; DAB0487EC0F6E92D CRC64;
MSHAAEPARD AVEASAEGPR AVFLLLEERR PAESAQLLSL NSLLPESGIV ADIELENILD
PDSFYELKSQ PLFLRSSLPI SLQATPTTPA TLSASSSAGG SRTPAMSSSS SRVLLRQQLM
RAQAQEQERR ERREQAAAAP FPSPAPASPA ISVIGVSAGG HTLSRPPPAQ VPREVLKVQT
HLENPTRYHL QQARRQQVKQ YLSTTLGPKL ASQALTPPPG PSSAQPLPAP ETAHATGPTG
SAPNSPMALL TIGSSSEKEI DDVIDEIISL ESSYNDEMLS YLPGGTAGLQ LPSTLPVSGN
LLDVYSSQGV ATPAITVSNS CPAELPNIKR EISETEAKAL LKERQKKDNH NLIERRRRFN
INDRIKELGT LIPKSNDPEM RWNKGTILKA SVDYIRKLQK EQQRSKDLES RQRSLEQANR
SLQLRIQELE LQAQIHGLPV PPNPGLLSLT TSSVSDSLKP EQLDIEEEGR PSTTFHVSGG
PAQNAPPQQP PAPPSDALLD LHFPSDHLGD LGDPFHLGLE DILMEEEGMV GGLSGGALSP
LRAASDPLLS SVSPAVSKAS SRRSSFSMEE ES
