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Target of rapamycin complex subunit LST8 (TORC subunit LST8) (G protein beta subunit-like) (Gable) (Protein GbetaL) (Mammalian lethal with SEC13 protein 8) (mLST8)

 LST8_HUMAN              Reviewed;         326 AA.
Q9BVC4; B3KMM4; B4DY00; D3DU88; Q5M800; Q86Y18; Q8WUI5; Q9HA66;
Q9UJV6;
08-APR-2008, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
10-OCT-2018, entry version 151.
RecName: Full=Target of rapamycin complex subunit LST8;
Short=TORC subunit LST8;
AltName: Full=G protein beta subunit-like;
Short=Gable;
Short=Protein GbetaL;
AltName: Full=Mammalian lethal with SEC13 protein 8;
Short=mLST8;
Name=MLST8; Synonyms=GBL, LST8;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Mao Y., Li Y., Xie Y., Huo K., Hu Q.;
"Cloning and characterization of human LST8 gene.";
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=Embryo, Mammary gland, and Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lymph, Placenta, Skin, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 97-326 (ISOFORMS 1/2).
TISSUE=Promyelocytic leukemia;
Ramachandiran S., Lau S.S., Monks T.J.;
"A novel G protein beta subunit (G beta 6) in human promyelocytic
leukemia (HL-60) cells.";
Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
[7]
INTERACTION WITH MTOR AND RPTOR, IDENTIFICATION IN THE TORC1 COMPLEX,
AND TISSUE SPECIFICITY.
PubMed=12408816; DOI=10.1016/S1097-2765(02)00636-6;
Loewith R., Jacinto E., Wullschleger S., Lorberg A., Crespo J.L.,
Bonenfant D., Oppliger W., Jenoe P., Hall M.N.;
"Two TOR complexes, only one of which is rapamycin sensitive, have
distinct roles in cell growth control.";
Mol. Cell 10:457-468(2002).
[8]
FUNCTION, INTERACTION WITH MTOR, IDENTIFICATION IN THE TORC1 COMPLEX,
MUTAGENESIS OF SER-72; GLY-192 AND PHE-320, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=12718876; DOI=10.1016/S1097-2765(03)00114-X;
Kim D.-H., Sarbassov D.D., Ali S.M., Latek R.R., Guntur K.V.P.,
Erdjument-Bromage H., Tempst P., Sabatini D.M.;
"GbetaL, a positive regulator of the rapamycin-sensitive pathway
required for the nutrient-sensitive interaction between raptor and
mTOR.";
Mol. Cell 11:895-904(2003).
[9]
IDENTIFICATION IN THE TORC1 AND TORC2 COMPLEXES.
PubMed=15268862; DOI=10.1016/j.cub.2004.06.054;
Sarbassov D.D., Ali S.M., Kim D.-H., Guertin D.A., Latek R.R.,
Erdjument-Bromage H., Tempst P., Sabatini D.M.;
"Rictor, a novel binding partner of mTOR, defines a rapamycin-
insensitive and raptor-independent pathway that regulates the
cytoskeleton.";
Curr. Biol. 14:1296-1302(2004).
[10]
IDENTIFICATION IN THE TORC2 COMPLEX, AND FUNCTION.
PubMed=15467718; DOI=10.1038/ncb1183;
Jacinto E., Loewith R., Schmidt A., Lin S., Ruegg M.A., Hall A.,
Hall M.N.;
"Mammalian TOR complex 2 controls the actin cytoskeleton and is
rapamycin insensitive.";
Nat. Cell Biol. 6:1122-1128(2004).
[11]
INTERACTION WITH RHEB.
PubMed=15854902; DOI=10.1016/j.cub.2005.02.053;
Long X., Lin Y., Ortiz-Vega S., Yonezawa K., Avruch J.;
"Rheb binds and regulates the mTOR kinase.";
Curr. Biol. 15:702-713(2005).
[12]
IDENTIFICATION IN THE TORC2 COMPLEX.
PubMed=17461779; DOI=10.1042/BJ20070540;
Pearce L.R., Huang X., Boudeau J., Pawlowski R., Wullschleger S.,
Deak M., Ibrahim A.F.M., Gourlay R., Magnuson M.A., Alessi D.R.;
"Identification of Protor as a novel Rictor-binding component of mTOR
complex-2.";
Biochem. J. 405:513-522(2007).
[13]
IDENTIFICATION IN THE TORC1 AND TORC2 COMPLEXES.
PubMed=17510057; DOI=10.1074/jbc.M702376200;
Wang L., Harris T.E., Roth R.A., Lawrence J.C. Jr.;
"PRAS40 regulates mTORC1 kinase activity by functioning as a direct
inhibitor of substrate binding.";
J. Biol. Chem. 282:20036-20044(2007).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, ACETYLATION [LARGE SCALE
ANALYSIS] AT MET-1 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS]
AT SER-7 (ISOFORM 3), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[18]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH MTOR, WD
REPEATS, AND SUBUNIT.
PubMed=23636326; DOI=10.1038/nature12122;
Yang H., Rudge D.G., Koos J.D., Vaidialingam B., Yang H.J.,
Pavletich N.P.;
"mTOR kinase structure, mechanism and regulation.";
Nature 497:217-223(2013).
-!- FUNCTION: Subunit of both mTORC1 and mTORC2, which regulates cell
growth and survival in response to nutrient and hormonal signals.
mTORC1 is activated in response to growth factors or amino acids.
Growth factor-stimulated mTORC1 activation involves a AKT1-
mediated phosphorylation of TSC1-TSC2, which leads to the
activation of the RHEB GTPase that potently activates the protein
kinase activity of mTORC1. Amino acid-signaling to mTORC1 requires
its relocalization to the lysosomes mediated by the Ragulator
complex and the Rag GTPases. Activated mTORC1 up-regulates protein
synthesis by phosphorylating key regulators of mRNA translation
and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and
releases it from inhibiting the elongation initiation factor 4E
(eiF4E). mTORC1 phosphorylates and activates S6K1 at 'Thr-389',
which then promotes protein synthesis by phosphorylating PDCD4 and
targeting it for degradation. Within mTORC1, LST8 interacts
directly with MTOR and enhances its kinase activity. In nutrient-
poor conditions, stabilizes the MTOR-RPTOR interaction and favors
RPTOR-mediated inhibition of MTOR activity. mTORC2 is also
activated by growth factors, but seems to be nutrient-insensitive.
mTORC2 seems to function upstream of Rho GTPases to regulate the
actin cytoskeleton, probably by activating one or more Rho-type
guanine nucleotide exchange factors. mTORC2 promotes the serum-
induced formation of stress-fibers or F-actin. mTORC2 plays a
critical role in AKT1 'Ser-473' phosphorylation, which may
facilitate the phosphorylation of the activation loop of AKT1 on
'Thr-308' by PDK1 which is a prerequisite for full activation.
mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2
also modulates the phosphorylation of PRKCA on 'Ser-657'.
{ECO:0000269|PubMed:12718876, ECO:0000269|PubMed:15467718}.
-!- SUBUNIT: Part of the mammalian target of rapamycin complex 1
(mTORC1) which contains MTOR, MLST8, RPTOR, AKT1S1/PRAS40 and
DEPTOR. mTORC1 binds to and is inhibited by FKBP12-rapamycin. Part
of the mammalian target of rapamycin complex 2 (mTORC2) which
contains MTOR, MLST8, PRR5, RICTOR, MAPKAP1 and DEPTOR. Contrary
to mTORC1, mTORC2 does not bind to and is not sensitive to FKBP12-
rapamycin. Interacts directly with MTOR and RPTOR. Interacts with
RHEB. {ECO:0000269|PubMed:12408816, ECO:0000269|PubMed:12718876,
ECO:0000269|PubMed:15268862, ECO:0000269|PubMed:15467718,
ECO:0000269|PubMed:15854902, ECO:0000269|PubMed:17461779,
ECO:0000269|PubMed:17510057, ECO:0000269|PubMed:23636326}.
-!- INTERACTION:
P42345:MTOR; NbExp=7; IntAct=EBI-16056342, EBI-359260;
Q8N122:RPTOR; NbExp=3; IntAct=EBI-1387471, EBI-1567928;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q9BVC4-1; Sequence=Displayed;
Name=2;
IsoId=Q9BVC4-3; Sequence=VSP_032665;
Name=3;
IsoId=Q9BVC4-4; Sequence=VSP_032666, VSP_032667, VSP_032668;
Note=Contains a phosphoserine at position 7. Contains a
N-acetylmethionine at position 1. {ECO:0000244|PubMed:19369195};
Name=4;
IsoId=Q9BVC4-5; Sequence=VSP_047368;
-!- TISSUE SPECIFICITY: Broadly expressed, with highest levels in
skeletal muscle, heart and kidney. {ECO:0000269|PubMed:12408816}.
-!- SIMILARITY: Belongs to the WD repeat LST8 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=EAW85539.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AY223837; AAO73410.1; -; mRNA.
EMBL; AK021536; BAG51036.1; -; mRNA.
EMBL; AK022227; BAB13990.1; -; mRNA.
EMBL; AK302201; BAG63562.1; -; mRNA.
EMBL; AC009065; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471112; EAW85538.1; -; Genomic_DNA.
EMBL; CH471112; EAW85539.1; ALT_SEQ; Genomic_DNA.
EMBL; CH471112; EAW85541.1; -; Genomic_DNA.
EMBL; CH471112; EAW85542.1; -; Genomic_DNA.
EMBL; BC001313; AAH01313.1; -; mRNA.
EMBL; BC017119; AAH17119.1; -; mRNA.
EMBL; BC052292; AAH52292.1; -; mRNA.
EMBL; BC088354; AAH88354.1; -; mRNA.
EMBL; AF195883; AAF04308.1; -; mRNA.
CCDS; CCDS10462.2; -. [Q9BVC4-1]
CCDS; CCDS58409.1; -. [Q9BVC4-5]
RefSeq; NP_001186102.1; NM_001199173.1. [Q9BVC4-1]
RefSeq; NP_001186103.1; NM_001199174.1. [Q9BVC4-1]
RefSeq; NP_001186104.1; NM_001199175.1. [Q9BVC4-5]
RefSeq; NP_071767.3; NM_022372.4. [Q9BVC4-1]
RefSeq; XP_016879037.1; XM_017023548.1. [Q9BVC4-3]
RefSeq; XP_016879038.1; XM_017023549.1. [Q9BVC4-3]
UniGene; Hs.29203; -.
PDB; 4JSN; X-ray; 3.20 A; C/D=1-326.
PDB; 4JSP; X-ray; 3.30 A; C/D=1-326.
PDB; 4JSV; X-ray; 3.50 A; C/D=1-326.
PDB; 4JSX; X-ray; 3.50 A; C/D=1-326.
PDB; 4JT5; X-ray; 3.45 A; C/D=1-323.
PDB; 4JT6; X-ray; 3.60 A; C/D=1-326.
PDB; 5FLC; EM; 5.90 A; D/H=1-326.
PDB; 5H64; EM; 4.40 A; C/c=1-326.
PDB; 5WBU; X-ray; 3.42 A; C/D=1-326.
PDB; 5WBY; X-ray; 3.10 A; C/D=1-326.
PDB; 5ZCS; EM; 4.90 A; C/D=1-326.
PDB; 6BCU; EM; 3.43 A; D/E=1-326.
PDB; 6BCX; EM; 3.00 A; D/E=1-326.
PDBsum; 4JSN; -.
PDBsum; 4JSP; -.
PDBsum; 4JSV; -.
PDBsum; 4JSX; -.
PDBsum; 4JT5; -.
PDBsum; 4JT6; -.
PDBsum; 5FLC; -.
PDBsum; 5H64; -.
PDBsum; 5WBU; -.
PDBsum; 5WBY; -.
PDBsum; 5ZCS; -.
PDBsum; 6BCU; -.
PDBsum; 6BCX; -.
ProteinModelPortal; Q9BVC4; -.
SMR; Q9BVC4; -.
BioGrid; 122113; 57.
CORUM; Q9BVC4; -.
DIP; DIP-39481N; -.
IntAct; Q9BVC4; 26.
MINT; Q9BVC4; -.
STRING; 9606.ENSP00000380313; -.
iPTMnet; Q9BVC4; -.
PhosphoSitePlus; Q9BVC4; -.
BioMuta; MLST8; -.
DMDM; 74761285; -.
EPD; Q9BVC4; -.
MaxQB; Q9BVC4; -.
PaxDb; Q9BVC4; -.
PeptideAtlas; Q9BVC4; -.
PRIDE; Q9BVC4; -.
ProteomicsDB; 79194; -.
ProteomicsDB; 79195; -. [Q9BVC4-3]
ProteomicsDB; 79196; -. [Q9BVC4-4]
DNASU; 64223; -.
Ensembl; ENST00000382450; ENSP00000371888; ENSG00000167965. [Q9BVC4-5]
Ensembl; ENST00000397124; ENSP00000380313; ENSG00000167965. [Q9BVC4-1]
Ensembl; ENST00000564088; ENSP00000457870; ENSG00000167965. [Q9BVC4-1]
Ensembl; ENST00000565250; ENSP00000455046; ENSG00000167965. [Q9BVC4-1]
Ensembl; ENST00000569417; ENSP00000456405; ENSG00000167965. [Q9BVC4-1]
GeneID; 64223; -.
KEGG; hsa:64223; -.
UCSC; uc002coz.4; human. [Q9BVC4-1]
CTD; 64223; -.
DisGeNET; 64223; -.
EuPathDB; HostDB:ENSG00000167965.17; -.
GeneCards; MLST8; -.
H-InvDB; HIX0012725; -.
HGNC; HGNC:24825; MLST8.
HPA; CAB019935; -.
HPA; HPA041841; -.
MIM; 612190; gene.
neXtProt; NX_Q9BVC4; -.
OpenTargets; ENSG00000167965; -.
PharmGKB; PA165450213; -.
eggNOG; KOG0315; Eukaryota.
eggNOG; ENOG410XPVD; LUCA.
GeneTree; ENSGT00390000014795; -.
HOVERGEN; HBG054763; -.
InParanoid; Q9BVC4; -.
KO; K08266; -.
OMA; LISCDQA; -.
PhylomeDB; Q9BVC4; -.
TreeFam; TF318577; -.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-1632852; Macroautophagy.
Reactome; R-HSA-165159; mTOR signalling.
Reactome; R-HSA-166208; mTORC1-mediated signalling.
Reactome; R-HSA-3371571; HSF1-dependent transactivation.
Reactome; R-HSA-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
Reactome; R-HSA-389357; CD28 dependent PI3K/Akt signaling.
Reactome; R-HSA-5218920; VEGFR2 mediated vascular permeability.
Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
Reactome; R-HSA-5674400; Constitutive Signaling by AKT1 E17K in Cancer.
Reactome; R-HSA-6804757; Regulation of TP53 Degradation.
Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
SignaLink; Q9BVC4; -.
SIGNOR; Q9BVC4; -.
ChiTaRS; MLST8; human.
GeneWiki; MLST8; -.
GenomeRNAi; 64223; -.
PRO; PR:Q9BVC4; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000167965; Expressed in 203 organ(s), highest expression level in right hemisphere of cerebellum.
ExpressionAtlas; Q9BVC4; baseline and differential.
Genevisible; Q9BVC4; HS.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0031931; C:TORC1 complex; IDA:UniProtKB.
GO; GO:0031932; C:TORC2 complex; IDA:UniProtKB.
GO; GO:0043539; F:protein serine/threonine kinase activator activity; IDA:WormBase.
GO; GO:0032148; P:activation of protein kinase B activity; TAS:Reactome.
GO; GO:0007050; P:cell cycle arrest; TAS:Reactome.
GO; GO:0030838; P:positive regulation of actin filament polymerization; IEA:Ensembl.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
GO; GO:0032008; P:positive regulation of TOR signaling; IMP:UniProtKB.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:UniProtKB.
GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome.
GO; GO:0043087; P:regulation of GTPase activity; IEA:Ensembl.
GO; GO:0016241; P:regulation of macroautophagy; TAS:Reactome.
GO; GO:0038202; P:TORC1 signaling; IMP:WormBase.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR020472; G-protein_beta_WD-40_rep.
InterPro; IPR037588; MLST8.
InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
PANTHER; PTHR19842; PTHR19842; 1.
Pfam; PF00400; WD40; 5.
PRINTS; PR00320; GPROTEINBRPT.
SMART; SM00320; WD40; 6.
SUPFAM; SSF50998; SSF50998; 1.
PROSITE; PS00678; WD_REPEATS_1; 1.
PROSITE; PS50082; WD_REPEATS_2; 3.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Phosphoprotein; Reference proteome; Repeat; WD repeat.
CHAIN 1 326 Target of rapamycin complex subunit LST8.
/FTId=PRO_0000326499.
REPEAT 1 37 WD 1. {ECO:0000255|PROSITE-
ProRule:PRU00221,
ECO:0000269|PubMed:23636326}.
REPEAT 40 80 WD 2. {ECO:0000255|PROSITE-
ProRule:PRU00221,
ECO:0000269|PubMed:23636326}.
REPEAT 83 122 WD 3. {ECO:0000255|PROSITE-
ProRule:PRU00221,
ECO:0000269|PubMed:23636326}.
REPEAT 126 165 WD 4. {ECO:0000255|PROSITE-
ProRule:PRU00221,
ECO:0000269|PubMed:23636326}.
REPEAT 168 207 WD 5. {ECO:0000255|PROSITE-
ProRule:PRU00221,
ECO:0000269|PubMed:23636326}.
REPEAT 218 257 WD 6. {ECO:0000255|PROSITE-
ProRule:PRU00221,
ECO:0000269|PubMed:23636326}.
REPEAT 268 309 WD 7. {ECO:0000255|PROSITE-
ProRule:PRU00221,
ECO:0000269|PubMed:23636326}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:20068231}.
VAR_SEQ 1 66 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.1}.
/FTId=VSP_032665.
VAR_SEQ 1 1 M -> MEHAPWSPGASSRARAGHTM (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_032666.
VAR_SEQ 44 44 Missing (in isoform 4). {ECO:0000305}.
/FTId=VSP_047368.
VAR_SEQ 192 198 GNCYVWN -> APRHLLG (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_032667.
VAR_SEQ 199 326 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_032668.
MUTAGEN 72 72 S->D: Impairs interaction with MTOR.
{ECO:0000269|PubMed:12718876}.
MUTAGEN 192 192 G->D: Abolishes interaction with MTOR.
{ECO:0000269|PubMed:12718876}.
MUTAGEN 320 320 F->S: Impairs interaction with MTOR.
{ECO:0000269|PubMed:12718876}.
CONFLICT 56 56 M -> V (in Ref. 2; BAB13990).
{ECO:0000305}.
CONFLICT 153 153 H -> Y (in Ref. 5; AAH88354).
{ECO:0000305}.
CONFLICT 248 248 R -> G (in Ref. 1; AAO73410).
{ECO:0000305}.
STRAND 10 19 {ECO:0000244|PDB:5WBY}.
STRAND 22 27 {ECO:0000244|PDB:5WBY}.
TURN 29 31 {ECO:0000244|PDB:5WBY}.
STRAND 34 39 {ECO:0000244|PDB:5WBY}.
STRAND 47 50 {ECO:0000244|PDB:5WBY}.
STRAND 54 60 {ECO:0000244|PDB:5WBY}.
STRAND 65 72 {ECO:0000244|PDB:5WBY}.
STRAND 77 80 {ECO:0000244|PDB:5WBY}.
STRAND 86 93 {ECO:0000244|PDB:5WBY}.
STRAND 97 104 {ECO:0000244|PDB:5WBY}.
STRAND 107 113 {ECO:0000244|PDB:5WBY}.
STRAND 122 126 {ECO:0000244|PDB:5WBY}.
STRAND 131 136 {ECO:0000244|PDB:5WBY}.
STRAND 140 147 {ECO:0000244|PDB:5WBY}.
STRAND 152 156 {ECO:0000244|PDB:5WBY}.
TURN 157 159 {ECO:0000244|PDB:5WBY}.
STRAND 162 168 {ECO:0000244|PDB:5WBY}.
STRAND 173 178 {ECO:0000244|PDB:5WBY}.
STRAND 182 189 {ECO:0000244|PDB:5WBY}.
STRAND 194 199 {ECO:0000244|PDB:5WBY}.
TURN 203 206 {ECO:0000244|PDB:5WBY}.
STRAND 210 216 {ECO:0000244|PDB:5WBY}.
STRAND 223 228 {ECO:0000244|PDB:5WBY}.
STRAND 232 239 {ECO:0000244|PDB:5WBY}.
TURN 240 242 {ECO:0000244|PDB:5WBY}.
STRAND 243 248 {ECO:0000244|PDB:5WBY}.
TURN 249 251 {ECO:0000244|PDB:5WBY}.
STRAND 254 259 {ECO:0000244|PDB:5WBY}.
STRAND 263 265 {ECO:0000244|PDB:5WBY}.
STRAND 273 278 {ECO:0000244|PDB:5WBY}.
STRAND 282 289 {ECO:0000244|PDB:5WBY}.
STRAND 292 298 {ECO:0000244|PDB:5WBY}.
TURN 299 301 {ECO:0000244|PDB:5WBY}.
STRAND 304 309 {ECO:0000244|PDB:5WBY}.
STRAND 315 322 {ECO:0000244|PDB:5WBY}.
SEQUENCE 326 AA; 35876 MW; 43A600D4EF2B6543 CRC64;
MNTSPGTVGS DPVILATAGY DHTVRFWQAH SGICTRTVQH QDSQVNALEV TPDRSMIAAA
GYQHIRMYDL NSNNPNPIIS YDGVNKNIAS VGFHEDGRWM YTGGEDCTAR IWDLRSRNLQ
CQRIFQVNAP INCVCLHPNQ AELIVGDQSG AIHIWDLKTD HNEQLIPEPE VSITSAHIDP
DASYMAAVNS TGNCYVWNLT GGIGDEVTQL IPKTKIPAHT RYALQCRFSP DSTLLATCSA
DQTCKIWRTS NFSLMTELSI KSGNPGESSR GWMWGCAFSG DSQYIVTASS DNLARLWCVE
TGEIKREYGG HQKAVVCLAF NDSVLG


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