Q9BVC4 (LST8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	MLST8
Synonyms:	GBL, LST8

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	326 AA.
Sequence status	Complete.
Protein existence	Evidence 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.11
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 component	Cytoplasm
Coding sequence diversity	Alternative splicing
Domain	Repeat WD repeat
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	T cell costimulation Traceable author statement. Source: Reactome fibroblast growth factor receptor signaling pathway Traceable author statement. Source: Reactome insulin receptor signaling pathway Traceable author statement. Source: Reactome nerve growth factor receptor signaling pathway Traceable author statement. Source: Reactome phosphatidylinositol-mediated signaling Traceable author statement. Source: Reactome positive regulation of TOR signaling cascade Inferred from mutant phenotype Ref.10. Source: UniProtKB
Cellular component	cytosol Traceable author statement. Source: Reactome
Molecular function	protein binding Inferred from physical interaction Ref.12. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MTOR	P42345	4	EBI-1387471,EBI-359260
RPTOR	Q8N122	3	EBI-1387471,EBI-1567928

Alternative products

This entry describes 3 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: Phosphorylated on Ser-7.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 326	326	Target of rapamycin complex subunit LST8		PRO_0000326499
Regions
	Repeat	1 – 37	37	WD 1
	Repeat	40 – 80	41	WD 2
	Repeat	83 – 122	40	WD 3
	Repeat	126 – 165	40	WD 4
	Repeat	168 – 207	40	WD 5
	Repeat	218 – 257	40	WD 6
	Repeat	268 – 309	42	WD 7
Amino acid modifications
	Modified residue	3	1	Phosphothreonine Ref.15
	Modified residue	4	1	Phosphoserine Ref.14 Ref.15
	Modified residue	7	1	Phosphothreonine Ref.14 Ref.15
Natural variations
	Alternative sequence	1 – 66	66	Missing in isoform 2.		VSP_032665
	Alternative sequence	1	1	M → MEHAPWSPGASSRARAGHTM in isoform 3.		VSP_032666
	Alternative sequence	192 – 198	7	GNCYVWN → APRHLLG in isoform 3.		VSP_032667
	Alternative sequence	199 – 326	128	Missing in isoform 3.		VSP_032668
Experimental info
	Mutagenesis	72	1	S → D: Impairs interaction with MTOR. Ref.8
	Mutagenesis	192	1	G → D: Abolishes interaction with MTOR. Ref.8
	Mutagenesis	320	1	F → S: Impairs interaction with MTOR. Ref.8
	Sequence conflict	44	1	Missing in BAG51036. Ref.2
	Sequence conflict	56	1	M → V in BAB13990. Ref.2
	Sequence conflict	153	1	H → Y in AAH88354. Ref.5
	Sequence conflict	248	1	R → G in AAO73410. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 43A600D4EF2B6543	FASTA	326	35,876
	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
	Isoform 2 [UniParc]. Checksum: 92BC4236276B1274	FASTA	260	28,728
	10 20 30 40 50 60 MYDLNSNNPN PIISYDGVNK NIASVGFHED GRWMYTGGED CTARIWDLRS RNLQCQRIFQ 70 80 90 100 110 120 VNAPINCVCL HPNQAELIVG DQSGAIHIWD LKTDHNEQLI PEPEVSITSA HIDPDASYMA 130 140 150 160 170 180 AVNSTGNCYV WNLTGGIGDE VTQLIPKTKI PAHTRYALQC RFSPDSTLLA TCSADQTCKI 190 200 210 220 230 240 WRTSNFSLMT ELSIKSGNPG ESSRGWMWGC AFSGDSQYIV TASSDNLARL WCVETGEIKR 250 260 EYGGHQKAVV CLAFNDSVLG
	Isoform 3 [UniParc]. Checksum: 3B611C65EAE88115	FASTA	217	23,850
	10 20 30 40 50 60 MEHAPWSPGA SSRARAGHTM NTSPGTVGSD PVILATAGYD HTVRFWQAHS GICTRTVQHQ 70 80 90 100 110 120 DSQVNALEVT PDRSMIAAAG YQHIRMYDLN SNNPNPIISY DGVNKNIASV GFHEDGRWMY 130 140 150 160 170 180 TGGEDCTARI WDLRSRNLQC QRIFQVNAPI NCVCLHPNQA ELIVGDQSGA IHIWDLKTDH 190 200 210 NEQLIPEPEV SITSAHIDPD ASYMAAVNST APRHLLG

References

	« Hide 'large scale' referencesShow '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. , 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: 14702039] [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: 15616553] [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. , 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: 15489334] [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: 12408816] [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: 12718876] [Abstract] Cited for: FUNCTION, INTERACTION WITH MTOR, IDENTIFICATION IN THE TORC1 COMPLEX, MUTAGENESIS OF SER-72; GLY-192 AND PHE-320, 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: 15268862] [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: 15467718] [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: 15854902] [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: 17461779] [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: 17510057] [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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7 (ISOFORM 3), MASS SPECTROMETRY. 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: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3; SER-4 AND THR-7, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7 (ISOFORM 3), MASS SPECTROMETRY.
+	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.
IPI	IPI00007182. IPI00102926. IPI00420058.
RefSeq	NP_001186102.1. NM_001199173.1. NP_001186103.1. NM_001199174.1. NP_001186104.1. NM_001199175.1. NP_071767.3. NM_022372.4.
UniGene	Hs.29203.
3D structure databases
ProteinModelPortal	Q9BVC4.
SMR	Q9BVC4. Positions 5-323.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9BVC4. 15 interactions.
STRING	Q9BVC4.
PTM databases
PhosphoSite	Q9BVC4.
Polymorphism databases
DMDM	74761285.
Proteomic databases
PRIDE	Q9BVC4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000382450; ENSP00000371888; ENSG00000167965. ENST00000397124; ENSP00000380313; ENSG00000167965.
GeneID	64223.
KEGG	hsa:64223.
UCSC	uc002coy.2. human. uc002coz.1. human. uc002cpb.1. human.
Organism-specific databases
CTD	64223.
GeneCards	GC16P002255.
H-InvDB	HIX0012725.
HGNC	HGNC:24825. MLST8.
HPA	CAB019935.
MIM	612190. gene.
neXtProt	NX_Q9BVC4.
PharmGKB	PA165450213.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG09047.
GeneTree	ENSGT00390000014795.
HOVERGEN	HBG054763.
OMA	NNKGNCY.
OrthoDB	EOG4TXBS3.
PhylomeDB	Q9BVC4.
Enzyme and pathway databases
Pathway_Interaction_DB	pi3kciaktpathway. Class I PI3K signaling events mediated by Akt. mtor_4pathway. mTOR signaling pathway.
Reactome	REACT_111102. Signal Transduction. REACT_6900. Immune System.
Gene expression databases
ArrayExpress	Q9BVC4.
Bgee	Q9BVC4.
Genevestigator	Q9BVC4.
Family and domain databases
InterPro	IPR020472. G-protein_beta_WD-40_rep. IPR015943. WD40/YVTN_repeat-like_dom. IPR001680. WD40_repeat. IPR011046. WD40_repeat-like_dom. IPR019775. WD40_repeat_CS. IPR017986. WD40_repeat_dom. [Graphical view]
Gene3D	G3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit.
KO	K08266.
Pfam	PF00400. WD40. 7 hits. [Graphical view]
PRINTS	PR00320. GPROTEINBRPT.
SMART	SM00320. WD40. 6 hits. [Graphical view]
SUPFAM	SSF50978. WD40_like. 1 hit.
PROSITE	PS00678. WD_REPEATS_1. 1 hit. PS50082. WD_REPEATS_2. 3 hits. PS50294. WD_REPEATS_REGION. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	66155.
SOURCE	Search...

Entry information

Entry name

LST8_HUMAN

Accession

Primary (citable) accession number: Q9BVC4
Secondary accession number(s): B3KMM4 , 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:	January 25, 2012
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.