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Q9DCJ1

- LST8_MOUSE

UniProt

Q9DCJ1 - LST8_MOUSE

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Protein
Target of rapamycin complex subunit LST8
Gene
Mlst8, Gbl, Lst8
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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'.1 Publication

GO - Biological processi

  1. positive regulation of TOR signaling Source: Ensembl
  2. positive regulation of actin filament polymerization Source: MGI
  3. positive regulation of peptidyl-tyrosine phosphorylation Source: MGI
  4. regulation of Rac GTPase activity Source: MGI
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
REACT_213550. HSF1-dependent transactivation.
REACT_226151. CD28 dependent PI3K/Akt signaling.
REACT_226341. PIP3 activates AKT signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Target of rapamycin complex subunit LST8
Short name:
TORC subunit LST8
Alternative name(s):
G protein beta subunit-like
Short name:
Protein GbetaL
Mammalian lethal with SEC13 protein 8
Short name:
mLST8
Gene namesi
Name:Mlst8
Synonyms:Gbl, Lst8
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 17

Organism-specific databases

MGIiMGI:1929514. Mlst8.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. TORC1 complex Source: MGI
  2. TORC2 complex Source: MGI
  3. cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Death around E10.5 due to multiple defects in vascular system development. In addition, they exhibit a delayed development of their cephalic region.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 326326Target of rapamycin complex subunit LST8
PRO_0000326500Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine By similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ9DCJ1.
PRIDEiQ9DCJ1.

PTM databases

PhosphoSiteiQ9DCJ1.

Expressioni

Gene expression databases

BgeeiQ9DCJ1.
GenevestigatoriQ9DCJ1.

Interactioni

Subunit structurei

Part of the mammalian target of rapamycin complex 1 (mTORC1) which contains MTOR, MLST8, RPTOR, AKT1S1/PRAS40 and DEPTOR By similarity. 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 By similarity. Contrary to mTORC1, mTORC2 does not bind to and is not sensitive to FKBP12-rapamycin. Interacts directly with MTOR and RPTOR. Interacts with RHEB By similarity. Interacts with MTOR.2 Publications

Protein-protein interaction databases

BioGridi208141. 3 interactions.
DIPiDIP-46976N.
IntActiQ9DCJ1. 3 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ9DCJ1.
SMRiQ9DCJ1. Positions 8-324.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati1 – 3737WD 1
Add
BLAST
Repeati40 – 8041WD 2
Add
BLAST
Repeati83 – 12240WD 3
Add
BLAST
Repeati126 – 16540WD 4
Add
BLAST
Repeati168 – 20740WD 5
Add
BLAST
Repeati218 – 25740WD 6
Add
BLAST
Repeati268 – 30942WD 7
Add
BLAST

Sequence similaritiesi

Belongs to the WD repeat LST8 family.
Contains 7 WD repeats.

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00390000014795.
HOGENOMiHOG000208395.
HOVERGENiHBG054763.
InParanoidiQ9DCJ1.
KOiK08266.
OMAiAGHHTVK.
OrthoDBiEOG7BCNBX.
PhylomeDBiQ9DCJ1.
TreeFamiTF318577.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR020472. G-protein_beta_WD-40_rep.
IPR011047. Quinonprotein_ADH-like_supfam.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 5 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF50998. SSF50998. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9DCJ1-1 [UniParc]FASTAAdd to Basket

« Hide

MNTTPGTVGS DPVILATAGY DHTVRFWQAH SGICTRTVQH QDSQVNALEI    50
TPDRSMIAAA GYQHIRMYDL NSNNPNPIIS YDGVSKNIAS VGFHEDGRWM 100
YTGGEDCTAR IWDLRSRNLQ CQRIFQVNAP INCVCLHPNQ AELIVGDQSG 150
AIHIWDLKTD HNEQLIPEPE SSITSAHIDP DASYMAAVNS AGNCYVWNLT 200
GGIGDDVTQL IPKTKIPAHT RYALQCRFSP DSTLLATCSA DQTCKIWRTS 250
NFSLMTELSI KSSNPGESSR GWMWGCAFSG DSQYIVTASS DNLARLWCVE 300
TGEIKREYGG HQKAVVCLAF NDSVLG 326
Length:326
Mass (Da):35,851
Last modified:June 1, 2001 - v1
Checksum:i2F6E75383905667A
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti24 – 241V → G in BAC39006. 1 Publication
Sequence conflicti127 – 1271V → G in BAC39006. 1 Publication
Sequence conflicti171 – 1711S → F in AAF37719. 1 Publication
Sequence conflicti195 – 1951Y → F in AAF37719. 1 Publication
Sequence conflicti206 – 2061D → E in AAF37719. 1 Publication
Sequence conflicti229 – 2291S → G in BAC33243. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF237676 mRNA. Translation: AAF37719.1.
AK002751 mRNA. Translation: BAB22328.1.
AK038515 mRNA. Translation: BAC30024.1.
AK040100 mRNA. Translation: BAC30510.1.
AK048102 mRNA. Translation: BAC33243.1.
AK077680 mRNA. Translation: BAC36952.1.
AK083731 mRNA. Translation: BAC39006.1.
BC015279 mRNA. Translation: AAH15279.1.
CCDSiCCDS28484.1.
RefSeqiNP_001239392.1. NM_001252463.1.
NP_001239393.1. NM_001252464.1.
NP_001239394.1. NM_001252465.1.
NP_064372.2. NM_019988.5.
UniGeneiMm.289516.

Genome annotation databases

EnsembliENSMUST00000070888; ENSMUSP00000065004; ENSMUSG00000024142.
ENSMUST00000179163; ENSMUSP00000136287; ENSMUSG00000024142.
GeneIDi56716.
KEGGimmu:56716.
UCSCiuc008awg.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF237676 mRNA. Translation: AAF37719.1 .
AK002751 mRNA. Translation: BAB22328.1 .
AK038515 mRNA. Translation: BAC30024.1 .
AK040100 mRNA. Translation: BAC30510.1 .
AK048102 mRNA. Translation: BAC33243.1 .
AK077680 mRNA. Translation: BAC36952.1 .
AK083731 mRNA. Translation: BAC39006.1 .
BC015279 mRNA. Translation: AAH15279.1 .
CCDSi CCDS28484.1.
RefSeqi NP_001239392.1. NM_001252463.1.
NP_001239393.1. NM_001252464.1.
NP_001239394.1. NM_001252465.1.
NP_064372.2. NM_019988.5.
UniGenei Mm.289516.

3D structure databases

ProteinModelPortali Q9DCJ1.
SMRi Q9DCJ1. Positions 8-324.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 208141. 3 interactions.
DIPi DIP-46976N.
IntActi Q9DCJ1. 3 interactions.

PTM databases

PhosphoSitei Q9DCJ1.

Proteomic databases

PaxDbi Q9DCJ1.
PRIDEi Q9DCJ1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000070888 ; ENSMUSP00000065004 ; ENSMUSG00000024142 .
ENSMUST00000179163 ; ENSMUSP00000136287 ; ENSMUSG00000024142 .
GeneIDi 56716.
KEGGi mmu:56716.
UCSCi uc008awg.3. mouse.

Organism-specific databases

CTDi 64223.
MGIi MGI:1929514. Mlst8.

Phylogenomic databases

eggNOGi COG2319.
GeneTreei ENSGT00390000014795.
HOGENOMi HOG000208395.
HOVERGENi HBG054763.
InParanoidi Q9DCJ1.
KOi K08266.
OMAi AGHHTVK.
OrthoDBi EOG7BCNBX.
PhylomeDBi Q9DCJ1.
TreeFami TF318577.

Enzyme and pathway databases

Reactomei REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
REACT_213550. HSF1-dependent transactivation.
REACT_226151. CD28 dependent PI3K/Akt signaling.
REACT_226341. PIP3 activates AKT signaling.

Miscellaneous databases

NextBioi 313187.
PROi Q9DCJ1.
SOURCEi Search...

Gene expression databases

Bgeei Q9DCJ1.
Genevestigatori Q9DCJ1.

Family and domain databases

Gene3Di 2.130.10.10. 1 hit.
InterProi IPR020472. G-protein_beta_WD-40_rep.
IPR011047. Quinonprotein_ADH-like_supfam.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view ]
Pfami PF00400. WD40. 5 hits.
[Graphical view ]
PRINTSi PR00320. GPROTEINBRPT.
SMARTi SM00320. WD40. 6 hits.
[Graphical view ]
SUPFAMi SSF50998. SSF50998. 1 hit.
PROSITEi PS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Insulin regulation of a novel WD-40 repeat protein in adipocytes."
    Rodgers B.D., Levine M.A., Bernier M., Montrose-Rafizadeh C.
    J. Endocrinol. 168:325-332(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Head, Hypothalamus, Kidney and Thymus.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Kidney.
  4. "GbetaL, a positive regulator of the rapamycin-sensitive pathway required for the nutrient-sensitive interaction between raptor and mTOR."
    Kim D.-H., Sarbassov D.D., Ali S.M., Latek R.R., Guntur K.V.P., Erdjument-Bromage H., Tempst P., Sabatini D.M.
    Mol. Cell 11:895-904(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MTOR.
  5. "Ablation in mice of the mTORC components raptor, rictor, or mLST8 reveals that mTORC2 is required for signaling to Akt-FOXO and PKCalpha, but not S6K1."
    Guertin D.A., Stevens D.M., Thoreen C.C., Burds A.A., Kalaany N.Y., Moffat J., Brown M., Fitzgerald K.J., Sabatini D.M.
    Dev. Cell 11:859-871(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  6. "Tel2 structure and function in the Hsp90-dependent maturation of mTOR and ATR complexes."
    Takai H., Xie Y., de Lange T., Pavletich N.P.
    Genes Dev. 24:2019-2030(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MTOR.

Entry informationi

Entry nameiLST8_MOUSE
AccessioniPrimary (citable) accession number: Q9DCJ1
Secondary accession number(s): Q8BNG8, Q8C882, Q9JKK6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: June 1, 2001
Last modified: September 3, 2014
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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