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Q9BVC4

- LST8_HUMAN

UniProt

Q9BVC4 - LST8_HUMAN

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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

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 - 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
Complete GO annotation...

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_228016. VEGFR2 mediated vascular permeability.
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
Complete GO annotation...

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

BgeeiQ9BVC4.
ExpressionAtlasiQ9BVC4. baseline and differential.
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. 39 interactions.
DIPiDIP-39481N.
IntActiQ9BVC4. 14 interactions.
MINTiMINT-3046622.
STRINGi9606.ENSP00000371888.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000014795.
HOVERGENiHBG054763.
InParanoidiQ9BVC4.
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

        10         20         30         40         50
MNTSPGTVGS DPVILATAGY DHTVRFWQAH SGICTRTVQH QDSQVNALEV
60 70 80 90 100
TPDRSMIAAA GYQHIRMYDL NSNNPNPIIS YDGVNKNIAS VGFHEDGRWM
110 120 130 140 150
YTGGEDCTAR IWDLRSRNLQ CQRIFQVNAP INCVCLHPNQ AELIVGDQSG
160 170 180 190 200
AIHIWDLKTD HNEQLIPEPE VSITSAHIDP DASYMAAVNS TGNCYVWNLT
210 220 230 240 250
GGIGDEVTQL IPKTKIPAHT RYALQCRFSP DSTLLATCSA DQTCKIWRTS
260 270 280 290 300
NFSLMTELSI KSGNPGESSR GWMWGCAFSG DSQYIVTASS DNLARLWCVE
310 320
TGEIKREYGG HQKAVVCLAF NDSVLG
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. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 39 interactions.
DIPi DIP-39481N.
IntActi Q9BVC4. 14 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.
GeneTreei ENSGT00390000014795.
HOVERGENi HBG054763.
InParanoidi Q9BVC4.
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_228016. VEGFR2 mediated vascular permeability.
REACT_6754. S6K1-mediated signalling.
REACT_6836. Release of eIF4E.
REACT_6838. mTOR signalling.
REACT_75829. PIP3 activates AKT signaling.
SignaLinki Q9BVC4.

Miscellaneous databases

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

Gene expression databases

Bgeei Q9BVC4.
ExpressionAtlasi Q9BVC4. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 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
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