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Q9BVC4

- LST8_HUMAN

UniProt

Q9BVC4 - LST8_HUMAN

Protein

Target of rapamycin complex subunit LST8

Gene

MLST8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    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'.2 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. epidermal growth factor receptor signaling pathway Source: Reactome
    2. Fc-epsilon receptor signaling pathway Source: Reactome
    3. fibroblast growth factor receptor signaling pathway Source: Reactome
    4. innate immune response Source: Reactome
    5. insulin receptor signaling pathway Source: Reactome
    6. neurotrophin TRK receptor signaling pathway Source: Reactome
    7. phosphatidylinositol-mediated signaling Source: Reactome
    8. positive regulation of actin filament polymerization Source: Ensembl
    9. positive regulation of peptidyl-tyrosine phosphorylation Source: Ensembl
    10. positive regulation of TOR signaling Source: UniProtKB
    11. regulation of actin cytoskeleton organization Source: UniProtKB
    12. regulation of Rac GTPase activity Source: Ensembl
    13. T cell costimulation Source: Reactome

    Enzyme and pathway databases

    ReactomeiREACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_19358. CD28 dependent PI3K/Akt signaling.
    REACT_200775. HSF1-dependent transactivation.
    REACT_6754. S6K1-mediated signalling.
    REACT_6836. Release of eIF4E.
    REACT_6838. mTOR signalling.
    REACT_75829. PIP3 activates AKT signaling.
    SignaLinkiQ9BVC4.

    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:
    Gable
    Short name:
    Protein GbetaL
    Mammalian lethal with SEC13 protein 8
    Short name:
    mLST8
    Gene namesi
    Name:MLST8
    Synonyms:GBL, LST8
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:24825. MLST8.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi72 – 721S → D: Impairs interaction with MTOR. 1 Publication
    Mutagenesisi192 – 1921G → D: Abolishes interaction with MTOR. 1 Publication
    Mutagenesisi320 – 3201F → S: Impairs interaction with MTOR. 1 Publication

    Organism-specific databases

    PharmGKBiPA165450213.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 326326Target of rapamycin complex subunit LST8PRO_0000326499Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9BVC4.
    PaxDbiQ9BVC4.
    PRIDEiQ9BVC4.

    PTM databases

    PhosphoSiteiQ9BVC4.

    Expressioni

    Tissue specificityi

    Broadly expressed, with highest levels in skeletal muscle, heart and kidney.1 Publication

    Gene expression databases

    ArrayExpressiQ9BVC4.
    BgeeiQ9BVC4.
    GenevestigatoriQ9BVC4.

    Organism-specific databases

    HPAiCAB019935.
    HPA041841.

    Interactioni

    Subunit structurei

    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.8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MTORP423454EBI-1387471,EBI-359260
    RPTORQ8N1223EBI-1387471,EBI-1567928

    Protein-protein interaction databases

    BioGridi122113. 21 interactions.
    DIPiDIP-39481N.
    IntActiQ9BVC4. 15 interactions.
    MINTiMINT-3046622.
    STRINGi9606.ENSP00000371888.

    Structurei

    Secondary structure

    1
    326
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi10 – 1910
    Beta strandi22 – 276
    Turni29 – 313
    Beta strandi34 – 396
    Beta strandi47 – 504
    Beta strandi54 – 607
    Beta strandi65 – 728
    Beta strandi78 – 814
    Beta strandi86 – 938
    Beta strandi97 – 1048
    Beta strandi107 – 1137
    Beta strandi122 – 1265
    Beta strandi131 – 1366
    Beta strandi140 – 1478
    Beta strandi152 – 1565
    Turni157 – 1593
    Beta strandi162 – 1654
    Beta strandi173 – 1786
    Beta strandi182 – 1898
    Beta strandi194 – 1996
    Helixi203 – 2053
    Beta strandi210 – 2167
    Beta strandi223 – 2286
    Beta strandi232 – 2398
    Beta strandi242 – 2487
    Turni249 – 2513
    Beta strandi254 – 2596
    Beta strandi263 – 2653
    Beta strandi273 – 2786
    Beta strandi282 – 2898
    Beta strandi292 – 2987
    Turni299 – 3013
    Beta strandi304 – 3096
    Beta strandi315 – 3228

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4JSNX-ray3.20C/D1-326[»]
    4JSPX-ray3.30C/D1-326[»]
    4JSVX-ray3.50C/D1-326[»]
    4JSXX-ray3.50C/D1-326[»]
    4JT5X-ray3.45C/D1-323[»]
    4JT6X-ray3.60C/D1-326[»]
    ProteinModelPortaliQ9BVC4.
    SMRiQ9BVC4. Positions 8-324.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati1 – 3737WD 11 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati40 – 8041WD 21 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati83 – 12240WD 31 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati126 – 16540WD 41 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati168 – 20740WD 51 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati218 – 25740WD 61 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati268 – 30942WD 71 PublicationPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the WD repeat LST8 family.Curated
    Contains 7 WD repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, WD repeat

    Phylogenomic databases

    eggNOGiCOG2319.
    HOVERGENiHBG054763.
    KOiK08266.
    OMAiAGHHTVK.
    PhylomeDBiQ9BVC4.
    TreeFamiTF318577.

    Family and domain databases

    Gene3Di2.130.10.10. 2 hits.
    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]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9BVC4-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MNTSPGTVGS DPVILATAGY DHTVRFWQAH SGICTRTVQH QDSQVNALEV    50
    TPDRSMIAAA GYQHIRMYDL NSNNPNPIIS YDGVNKNIAS VGFHEDGRWM 100
    YTGGEDCTAR IWDLRSRNLQ CQRIFQVNAP INCVCLHPNQ AELIVGDQSG 150
    AIHIWDLKTD HNEQLIPEPE VSITSAHIDP DASYMAAVNS TGNCYVWNLT 200
    GGIGDEVTQL IPKTKIPAHT RYALQCRFSP DSTLLATCSA DQTCKIWRTS 250
    NFSLMTELSI KSGNPGESSR GWMWGCAFSG DSQYIVTASS DNLARLWCVE 300
    TGEIKREYGG HQKAVVCLAF NDSVLG 326
    Length:326
    Mass (Da):35,876
    Last modified:June 1, 2001 - v1
    Checksum:i43A600D4EF2B6543
    GO
    Isoform 2 (identifier: Q9BVC4-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-66: Missing.

    Show »
    Length:260
    Mass (Da):28,728
    Checksum:i92BC4236276B1274
    GO
    Isoform 3 (identifier: Q9BVC4-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MEHAPWSPGASSRARAGHTM
         192-198: GNCYVWN → APRHLLG
         199-326: Missing.

    Note: Contains a N-acetylmethionine at position 1. Contains a phosphoserine at position 7.

    Show »
    Length:217
    Mass (Da):23,850
    Checksum:i3B611C65EAE88115
    GO
    Isoform 4 (identifier: Q9BVC4-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         44-44: Missing.

    Show »
    Length:325
    Mass (Da):35,748
    Checksum:iCF41EB9312C1788A
    GO

    Sequence cautioni

    The sequence EAW85539.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti56 – 561M → V in BAB13990. (PubMed:14702039)Curated
    Sequence conflicti153 – 1531H → Y in AAH88354. (PubMed:15489334)Curated
    Sequence conflicti248 – 2481R → G in AAO73410. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6666Missing in isoform 2. 2 PublicationsVSP_032665Add
    BLAST
    Alternative sequencei1 – 11M → MEHAPWSPGASSRARAGHTM in isoform 3. 1 PublicationVSP_032666
    Alternative sequencei44 – 441Missing in isoform 4. CuratedVSP_047368
    Alternative sequencei192 – 1987GNCYVWN → APRHLLG in isoform 3. 1 PublicationVSP_032667
    Alternative sequencei199 – 326128Missing in isoform 3. 1 PublicationVSP_032668Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY223837 mRNA. Translation: AAO73410.1.
    AK021536 mRNA. Translation: BAG51036.1.
    AK022227 mRNA. Translation: BAB13990.1.
    AK302201 mRNA. Translation: BAG63562.1.
    AC009065 Genomic DNA. No translation available.
    CH471112 Genomic DNA. Translation: EAW85538.1.
    CH471112 Genomic DNA. Translation: EAW85539.1. Sequence problems.
    CH471112 Genomic DNA. Translation: EAW85541.1.
    CH471112 Genomic DNA. Translation: EAW85542.1.
    BC001313 mRNA. Translation: AAH01313.1.
    BC017119 mRNA. Translation: AAH17119.1.
    BC052292 mRNA. Translation: AAH52292.1.
    BC088354 mRNA. Translation: AAH88354.1.
    AF195883 mRNA. Translation: AAF04308.1.
    CCDSiCCDS10462.2. [Q9BVC4-1]
    CCDS58409.1. [Q9BVC4-5]
    RefSeqiNP_001186102.1. NM_001199173.1. [Q9BVC4-1]
    NP_001186103.1. NM_001199174.1. [Q9BVC4-1]
    NP_001186104.1. NM_001199175.1. [Q9BVC4-5]
    NP_071767.3. NM_022372.4. [Q9BVC4-1]
    XP_005255537.1. XM_005255480.2.
    UniGeneiHs.29203.

    Genome annotation databases

    EnsembliENST00000382450; ENSP00000371888; ENSG00000167965. [Q9BVC4-5]
    ENST00000397124; ENSP00000380313; ENSG00000167965. [Q9BVC4-1]
    ENST00000564088; ENSP00000457870; ENSG00000167965. [Q9BVC4-1]
    ENST00000565250; ENSP00000455046; ENSG00000167965. [Q9BVC4-1]
    ENST00000569417; ENSP00000456405; ENSG00000167965. [Q9BVC4-1]
    GeneIDi64223.
    KEGGihsa:64223.
    UCSCiuc002coy.3. human. [Q9BVC4-1]

    Polymorphism databases

    DMDMi74761285.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY223837 mRNA. Translation: AAO73410.1 .
    AK021536 mRNA. Translation: BAG51036.1 .
    AK022227 mRNA. Translation: BAB13990.1 .
    AK302201 mRNA. Translation: BAG63562.1 .
    AC009065 Genomic DNA. No translation available.
    CH471112 Genomic DNA. Translation: EAW85538.1 .
    CH471112 Genomic DNA. Translation: EAW85539.1 . Sequence problems.
    CH471112 Genomic DNA. Translation: EAW85541.1 .
    CH471112 Genomic DNA. Translation: EAW85542.1 .
    BC001313 mRNA. Translation: AAH01313.1 .
    BC017119 mRNA. Translation: AAH17119.1 .
    BC052292 mRNA. Translation: AAH52292.1 .
    BC088354 mRNA. Translation: AAH88354.1 .
    AF195883 mRNA. Translation: AAF04308.1 .
    CCDSi CCDS10462.2. [Q9BVC4-1 ]
    CCDS58409.1. [Q9BVC4-5 ]
    RefSeqi NP_001186102.1. NM_001199173.1. [Q9BVC4-1 ]
    NP_001186103.1. NM_001199174.1. [Q9BVC4-1 ]
    NP_001186104.1. NM_001199175.1. [Q9BVC4-5 ]
    NP_071767.3. NM_022372.4. [Q9BVC4-1 ]
    XP_005255537.1. XM_005255480.2.
    UniGenei Hs.29203.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4JSN X-ray 3.20 C/D 1-326 [» ]
    4JSP X-ray 3.30 C/D 1-326 [» ]
    4JSV X-ray 3.50 C/D 1-326 [» ]
    4JSX X-ray 3.50 C/D 1-326 [» ]
    4JT5 X-ray 3.45 C/D 1-323 [» ]
    4JT6 X-ray 3.60 C/D 1-326 [» ]
    ProteinModelPortali Q9BVC4.
    SMRi Q9BVC4. Positions 8-324.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122113. 21 interactions.
    DIPi DIP-39481N.
    IntActi Q9BVC4. 15 interactions.
    MINTi MINT-3046622.
    STRINGi 9606.ENSP00000371888.

    PTM databases

    PhosphoSitei Q9BVC4.

    Polymorphism databases

    DMDMi 74761285.

    Proteomic databases

    MaxQBi Q9BVC4.
    PaxDbi Q9BVC4.
    PRIDEi Q9BVC4.

    Protocols and materials databases

    DNASUi 64223.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000382450 ; ENSP00000371888 ; ENSG00000167965 . [Q9BVC4-5 ]
    ENST00000397124 ; ENSP00000380313 ; ENSG00000167965 . [Q9BVC4-1 ]
    ENST00000564088 ; ENSP00000457870 ; ENSG00000167965 . [Q9BVC4-1 ]
    ENST00000565250 ; ENSP00000455046 ; ENSG00000167965 . [Q9BVC4-1 ]
    ENST00000569417 ; ENSP00000456405 ; ENSG00000167965 . [Q9BVC4-1 ]
    GeneIDi 64223.
    KEGGi hsa:64223.
    UCSCi uc002coy.3. human. [Q9BVC4-1 ]

    Organism-specific databases

    CTDi 64223.
    GeneCardsi GC16P002254.
    H-InvDB HIX0012725.
    HGNCi HGNC:24825. MLST8.
    HPAi CAB019935.
    HPA041841.
    MIMi 612190. gene.
    neXtProti NX_Q9BVC4.
    PharmGKBi PA165450213.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2319.
    HOVERGENi HBG054763.
    KOi K08266.
    OMAi AGHHTVK.
    PhylomeDBi Q9BVC4.
    TreeFami TF318577.

    Enzyme and pathway databases

    Reactomei REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_19358. CD28 dependent PI3K/Akt signaling.
    REACT_200775. HSF1-dependent transactivation.
    REACT_6754. S6K1-mediated signalling.
    REACT_6836. Release of eIF4E.
    REACT_6838. mTOR signalling.
    REACT_75829. PIP3 activates AKT signaling.
    SignaLinki Q9BVC4.

    Miscellaneous databases

    GeneWikii MLST8.
    GenomeRNAii 64223.
    NextBioi 66155.
    PROi Q9BVC4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BVC4.
    Bgeei Q9BVC4.
    Genevestigatori Q9BVC4.

    Family and domain databases

    Gene3Di 2.130.10.10. 2 hits.
    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

    1. "Cloning and characterization of human LST8 gene."
      Mao Y., Li Y., Xie Y., Huo K., Hu Q.
      Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      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.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
      Tissue: Embryo, Mammary gland and Testis.
    3. "The sequence and analysis of duplication-rich human chromosome 16."
      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.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 1).
      Tissue: Lymph, Placenta, Skin and Uterus.
    6. "A novel G protein beta subunit (G beta 6) in human promyelocytic leukemia (HL-60) cells."
      Ramachandiran S., Lau S.S., Monks T.J.
      Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 97-326 (ISOFORMS 1/2).
      Tissue: Promyelocytic leukemia.
    7. "Two TOR complexes, only one of which is rapamycin sensitive, have distinct roles in cell growth control."
      Loewith R., Jacinto E., Wullschleger S., Lorberg A., Crespo J.L., Bonenfant D., Oppliger W., Jenoe P., Hall M.N.
      Mol. Cell 10:457-468(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MTOR AND RPTOR, IDENTIFICATION IN THE TORC1 COMPLEX, TISSUE SPECIFICITY.
    8. "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: FUNCTION, INTERACTION WITH MTOR, IDENTIFICATION IN THE TORC1 COMPLEX, MUTAGENESIS OF SER-72; GLY-192 AND PHE-320, IDENTIFICATION BY MASS SPECTROMETRY.
    9. "Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton."
      Sarbassov D.D., Ali S.M., Kim D.-H., Guertin D.A., Latek R.R., Erdjument-Bromage H., Tempst P., Sabatini D.M.
      Curr. Biol. 14:1296-1302(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE TORC1 AND TORC2 COMPLEXES.
    10. "Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive."
      Jacinto E., Loewith R., Schmidt A., Lin S., Ruegg M.A., Hall A., Hall M.N.
      Nat. Cell Biol. 6:1122-1128(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE TORC2 COMPLEX, FUNCTION.
    11. Cited for: INTERACTION WITH RHEB.
    12. Cited for: IDENTIFICATION IN THE TORC2 COMPLEX.
    13. "PRAS40 regulates mTORC1 kinase activity by functioning as a direct inhibitor of substrate binding."
      Wang L., Harris T.E., Roth R.A., Lawrence J.C. Jr.
      J. Biol. Chem. 282:20036-20044(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE TORC1 AND TORC2 COMPLEXES.
    14. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: 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), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      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.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH MTOR, WD REPEATS, SUBUNIT.

    Entry informationi

    Entry nameiLST8_HUMAN
    AccessioniPrimary (citable) accession number: Q9BVC4
    Secondary accession number(s): B3KMM4
    , B4DY00, D3DU88, Q5M800, Q86Y18, Q8WUI5, Q9HA66, Q9UJV6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 8, 2008
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 110 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3