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Q9BVC4 (LST8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:MLST8
Synonyms:GBL, LST8
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length326 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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'. Ref.8 Ref.10

Subunit structure

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. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.17

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Broadly expressed, with highest levels in skeletal muscle, heart and kidney. Ref.7

Sequence similarities

Belongs to the WD repeat LST8 family.

Contains 7 WD repeats.

Sequence caution

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

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   DomainRepeat
WD repeat
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

T cell costimulation

Traceable author statement. Source: Reactome

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

insulin receptor signaling pathway

Traceable author statement. Source: Reactome

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

phosphatidylinositol-mediated signaling

Traceable author statement. Source: Reactome

positive regulation of TOR signaling

Inferred from mutant phenotype Ref.10. Source: UniProtKB

positive regulation of actin filament polymerization

Inferred from electronic annotation. Source: Ensembl

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from electronic annotation. Source: Ensembl

regulation of Rac GTPase activity

Inferred from electronic annotation. Source: Ensembl

regulation of actin cytoskeleton organization

Inferred from mutant phenotype Ref.10. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

   Molecular_functionprotein binding

Inferred from physical interaction Ref.7Ref.12PubMed 20562859. Source: IntAct

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BVC4-1)

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.
Isoform 2 (identifier: Q9BVC4-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-66: Missing.
Isoform 3 (identifier: Q9BVC4-4)

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.
Isoform 4 (identifier: Q9BVC4-5)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 326326Target of rapamycin complex subunit LST8
PRO_0000326499

Regions

Repeat1 – 3737WD 1
Repeat40 – 8041WD 2
Repeat83 – 12240WD 3
Repeat126 – 16540WD 4
Repeat168 – 20740WD 5
Repeat218 – 25740WD 6
Repeat268 – 30942WD 7

Amino acid modifications

Modified residue11N-acetylmethionine Ref.15 Ref.16

Natural variations

Alternative sequence1 – 6666Missing in isoform 2.
VSP_032665
Alternative sequence11M → MEHAPWSPGASSRARAGHTM in isoform 3.
VSP_032666
Alternative sequence441Missing in isoform 4.
VSP_047368
Alternative sequence192 – 1987GNCYVWN → APRHLLG in isoform 3.
VSP_032667
Alternative sequence199 – 326128Missing in isoform 3.
VSP_032668

Experimental info

Mutagenesis721S → D: Impairs interaction with MTOR. Ref.8
Mutagenesis1921G → D: Abolishes interaction with MTOR. Ref.8
Mutagenesis3201F → S: Impairs interaction with MTOR. Ref.8
Sequence conflict561M → V in BAB13990. Ref.2
Sequence conflict1531H → Y in AAH88354. Ref.5
Sequence conflict2481R → G in AAO73410. Ref.1

Secondary structure

.................................................................. 326
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 43A600D4EF2B6543

FASTA32635,876
        10         20         30         40         50         60 
MNTSPGTVGS DPVILATAGY DHTVRFWQAH SGICTRTVQH QDSQVNALEV TPDRSMIAAA 

        70         80         90        100        110        120 
GYQHIRMYDL NSNNPNPIIS YDGVNKNIAS VGFHEDGRWM YTGGEDCTAR IWDLRSRNLQ 

       130        140        150        160        170        180 
CQRIFQVNAP INCVCLHPNQ AELIVGDQSG AIHIWDLKTD HNEQLIPEPE VSITSAHIDP 

       190        200        210        220        230        240 
DASYMAAVNS TGNCYVWNLT GGIGDEVTQL IPKTKIPAHT RYALQCRFSP DSTLLATCSA 

       250        260        270        280        290        300 
DQTCKIWRTS NFSLMTELSI KSGNPGESSR GWMWGCAFSG DSQYIVTASS DNLARLWCVE 

       310        320 
TGEIKREYGG HQKAVVCLAF NDSVLG 

« Hide

Isoform 2 [UniParc].

Checksum: 92BC4236276B1274
Show »

FASTA26028,728
Isoform 3 [UniParc].

Checksum: 3B611C65EAE88115
Show »

FASTA21723,850
Isoform 4 [UniParc].

Checksum: CF41EB9312C1788A
Show »

FASTA32535,748

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]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. expand/collapse author list , 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
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]"Rheb binds and regulates the mTOR kinase."
Long X., Lin Y., Ortiz-Vega S., Yonezawa K., Avruch J.
Curr. Biol. 15:702-713(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RHEB.
[12]"Identification of Protor as a novel Rictor-binding component of mTOR complex-2."
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.
Biochem. J. 405:513-522(2007) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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]"mTOR kinase structure, mechanism and regulation."
Yang H., Rudge D.G., Koos J.D., Vaidialingam B., Yang H.J., Pavletich N.P.
Nature 497:217-223(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH MTOR, WD REPEATS, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS10462.2. [Q9BVC4-1]
CCDS58409.1. [Q9BVC4-5]
RefSeqNP_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.
UniGeneHs.29203.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ9BVC4.
SMRQ9BVC4. Positions 8-324.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122113. 21 interactions.
DIPDIP-39481N.
IntActQ9BVC4. 14 interactions.
MINTMINT-3046622.
STRING9606.ENSP00000371888.

PTM databases

PhosphoSiteQ9BVC4.

Polymorphism databases

DMDM74761285.

Proteomic databases

MaxQBQ9BVC4.
PaxDbQ9BVC4.
PRIDEQ9BVC4.

Protocols and materials databases

DNASU64223.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000301725; ENSP00000301725; ENSG00000167965. [Q9BVC4-4]
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]
GeneID64223.
KEGGhsa:64223.
UCSCuc002coy.3. human. [Q9BVC4-1]

Organism-specific databases

CTD64223.
GeneCardsGC16P002254.
H-InvDBHIX0012725.
HGNCHGNC:24825. MLST8.
HPACAB019935.
HPA041841.
MIM612190. gene.
neXtProtNX_Q9BVC4.
PharmGKBPA165450213.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2319.
HOVERGENHBG054763.
KOK08266.
OMAAGHHTVK.
PhylomeDBQ9BVC4.
TreeFamTF318577.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_120956. Cellular responses to stress.
REACT_6900. Immune System.
SignaLinkQ9BVC4.

Gene expression databases

ArrayExpressQ9BVC4.
BgeeQ9BVC4.
GenevestigatorQ9BVC4.

Family and domain databases

Gene3D2.130.10.10. 2 hits.
InterProIPR020472. 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]
PfamPF00400. WD40. 5 hits.
[Graphical view]
PRINTSPR00320. GPROTEINBRPT.
SMARTSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMSSF50998. SSF50998. 1 hit.
PROSITEPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiMLST8.
GenomeRNAi64223.
NextBio66155.
PROQ9BVC4.
SOURCESearch...

Entry information

Entry nameLST8_HUMAN
AccessionPrimary (citable) accession number: Q9BVC4
Secondary accession number(s): B3KMM4 expand/collapse secondary AC list , B4DY00, D3DU88, Q5M800, Q86Y18, Q8WUI5, Q9HA66, Q9UJV6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM