Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P40061 (TSC11_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Target of rapamycin complex 2 subunit TSC11

Short name=TORC2 subunit TSC11
Alternative name(s):
Adheres voraciously to TOR2 protein 3
Temperature-sensitive CSG2 suppressor protein 11
Gene names
Name:TSC11
Synonyms:AVO3
Ordered Locus Names:YER093C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1430 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential component of TORC2, which regulates cell cycle-dependent polarization of the actin-cytoskeleton and cell wall integrity. TORC2 controls polarity of the actin cytoskeleton, which is required for orienting the secretory pathway toward discrete growth sites, via the RHO1/PKC1/MAPK cell integrity pathway. TSC11 may exert its functions through two distinct mechanisms, one mediated by AVO1 and the other mediated by AVO2 and SLM1. Ref.8

Subunit structure

The target of rapamycin complex 2 (TORC2) is composed of at least AVO1, AVO2, BIT61, LST8, TOR2 and TSC11. TORC2 likely forms a homodimer. Contrary to TORC1, TORC2 does not bind to and is not sensitive to FKBP-rapamycin. TSC11 binds to the N-terminal HEAT repeat region in TOR2 and is required for TORC2 integrity by tethering AVO1 and AVO2 to the complex. Ref.4 Ref.5 Ref.7

Subcellular location

Cell membrane; Peripheral membrane protein; Cytoplasmic side. Vacuole membrane; Peripheral membrane protein; Cytoplasmic side Ref.5.

Post-translational modification

Phosphorylated by TOR2; when part of TORC2. Ref.7

Miscellaneous

Present with 1840 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the pianissimo family.

Contains 1 N-terminal Ras-GEF domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

LST8P413182EBI-22621,EBI-28598
TOR2P326005EBI-22621,EBI-19385

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14301430Target of rapamycin complex 2 subunit TSC11
PRO_0000202640

Regions

Domain995 – 1100106N-terminal Ras-GEF
Coiled coil91 – 18090 Potential

Amino acid modifications

Modified residue191Phosphoserine Ref.9 Ref.11
Modified residue811Phosphoserine Ref.11
Modified residue841Phosphoserine Ref.10
Modified residue871Phosphoserine Ref.11
Modified residue1411Phosphoserine Ref.11

Sequences

Sequence LengthMass (Da)Tools
P40061 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 07BB5D75BA204E50

FASTA1,430164,368
        10         20         30         40         50         60 
MSIPHSAKQS SPLSSRRRSV TNTTPLLTPR HSRDNSSTQI SSAKNITSSS PSTITNESSK 

        70         80         90        100        110        120 
RNKQNLVLST SFISTKRLEN SAPSPTSPLM ARRTRSTMTK ALLNLKAEIN NQYQELARLR 

       130        140        150        160        170        180 
KKKDDIEHLR DSTISDIYSG SYSTNHLQKH SMRIRANTQL REIDNSIKRV EKHIFDLKQQ 

       190        200        210        220        230        240 
FDKKRQRSLT TSSSIKADVG SIRNDDGQNN DSEELGDHDS LTDQVTLDDE YLTTPTSGTE 

       250        260        270        280        290        300 
RNSQQNLNRN STVNSRNNEN HSTLSIPDLD GSNKVNLTGD TEKDLGDLEN ENQIFTSTTT 

       310        320        330        340        350        360 
EAATWLVSDY MQSFQEKNVN PDFIAQKANG LVTLLKEHSE IRKDLVLTSF MSSIQNLLLN 

       370        380        390        400        410        420 
GNKLIAASAY RVCRYLINSS IFIDELLELR LDAFIIISLA KDNSFQIERE QALKMVRRFI 

       430        440        450        460        470        480 
EYNNGVTQGI MQAIISCVEK PEDSLRHMAL ETLLELCFVA PEMVKECRGM RVIEGFLQDY 

       490        500        510        520        530        540 
TSFSLASVIL DTILQLMATH KTRQHFLEDF NVSVLTTVFS DTNTKSNVNV EKMQNASTLI 

       550        560        570        580        590        600 
SITLNSYNGF MLFSNNNFKP LKQLVSFFQI PICAQYLIDI FLDVLKIKPL PYKPRGRHSH 

       610        620        630        640        650        660 
SFKPIPSQYY KECMSVNQRL ALIVLILENS EFVPHLLELL NEEDRDDHLV AKGRYLLTEY 

       670        680        690        700        710        720 
FNLRMNLVDK KYTSVSKPIY KENFTYVNET FQFKKIAYKM NRNRNTIGMS GIDYAQNIKS 

       730        740        750        760        770        780 
FSKNIKENTL LREVDDFRFR RMVYDSKVLQ TKDFTRWNWN IINELLEGPL LNKKQLEELV 

       790        800        810        820        830        840 
KSTKFIRRLL VFYRPLRLRF SNVNKGAKLS QKYVQVGCQF FKTLTATPEG MKILMDDTKI 

       850        860        870        880        890        900 
IPQLASLMFR AMEGNISGNI FNKNKLREKI IFGYFKFIGI LTQSKNGVHI LTRWNFFTVI 

       910        920        930        940        950        960 
YKMFQFESKL GLEFLLLTIP ELDLKYSSHC RVIIGKALVV ANEKVRIEAT KHIGDKLKEL 

       970        980        990       1000       1010       1020 
LSTKESDLKL KANKVKLQQF KMEMLTRQLY DLSPSVVAVA DQALYECIVA GNGSEELGTS 

      1030       1040       1050       1060       1070       1080 
FRMFLNQMVF IRSPILFELL SRPYGFQLLN EINFVKEERD SWLSKKNIEY VHIVEEFLKK 

      1090       1100       1110       1120       1130       1140 
NESINAKSLT FQQKSRLPLH FYESLTKTED GILLLSQTGD LVTFMNVIKK YVNGNNMATV 

      1150       1160       1170       1180       1190       1200 
ENAKEILDLK AALWCVGFIG STELGIGLLD NYSLVEDIIE VAYNASVTSV RFTAFYVLGL 

      1210       1220       1230       1240       1250       1260 
ISMTREGCEI LDEMGWNCCV SVQDEPIGIA LPNRLDRFLS YNEHKWSAFG EYSDEMIVFN 

      1270       1280       1290       1300       1310       1320 
KSDGDLIEKC LPIEFDLDKL LKEKDTAENP LNEKIITNKY DNDITSQTIT VSGENSSLFA 

      1330       1340       1350       1360       1370       1380 
NEGLSSPYVT QYRNDDDSIE SKVLHIVSQL GNHILSNHAV KEITEINNKY GPRLFENEKM 

      1390       1400       1410       1420       1430 
FFKVFNMMSK YRFKPHVRKF LCGLFINNRA LENVIRHDNK RDKRPANFTR 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome V."
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. expand/collapse author list , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.
Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Structure and regulation of MET6, the vitamin B12-independent methionine synthase gene of Saccharomyces cerevisiae."
Korch C., Mountain H.A., Wenzlau J.M.
Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 967-1430.
Strain: ATCC 204508 / S288c.
[4]"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: IDENTIFICATION IN TORC2, IDENTIFICATION BY MASS SPECTROMETRY.
[5]"Tor kinases are in distinct membrane-associated protein complexes in Saccharomyces cerevisiae."
Wedaman K.P., Reinke A., Anderson S., Yates J.R. III, McCaffery J.M., Powers T.
Mol. Biol. Cell 14:1204-1220(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, IDENTIFICATION IN TORC2, IDENTIFICATION BY MASS SPECTROMETRY.
[6]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]"Molecular organization of target of rapamycin complex 2."
Wullschleger S., Loewith R., Oppliger W., Hall M.N.
J. Biol. Chem. 280:30697-30704(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, INTERACTION WITH TOR2, PHOSPHORYLATION.
[8]"Saccharomyces cerevisiae TSC11/AVO3 participates in regulating cell integrity and functionally interacts with components of the Tor2 complex."
Ho H.-L., Shiau Y.-S., Chen M.-Y.
Curr. Genet. 47:273-288(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[10]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-81; SER-87 AND SER-141, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U18839 Genomic DNA. Translation: AAB64648.1.
U32508 Genomic DNA. Translation: AAB60298.1.
BK006939 Genomic DNA. Translation: DAA07754.1.
PIRS50596.
RefSeqNP_011018.1. NM_001178984.1.

3D structure databases

ProteinModelPortalP40061.
SMRP40061. Positions 627-658, 1148-1215.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36838. 179 interactions.
DIPDIP-4957N.
IntActP40061. 10 interactions.
MINTMINT-486144.
STRING4932.YER093C.

Proteomic databases

PaxDbP40061.
PeptideAtlasP40061.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYER093C; YER093C; YER093C.
GeneID856828.
KEGGsce:YER093C.

Organism-specific databases

CYGDYER093c.
SGDS000000895. TSC11.

Phylogenomic databases

eggNOGNOG305760.
GeneTreeENSGT00390000002096.
HOGENOMHOG000141815.
OMAGRNDTYV.
OrthoDBEOG71VT21.

Enzyme and pathway databases

BioCycYEAST:G3O-30260-MONOMER.

Gene expression databases

GenevestigatorP40061.

Family and domain databases

Gene3D1.25.10.10. 1 hit.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR028268. Pianissimo_fam.
IPR028267. Pianissimo_N.
IPR028270. TORC2_TSC11.
[Graphical view]
PANTHERPTHR13298. PTHR13298. 1 hit.
PTHR13298:SF3. PTHR13298:SF3. 1 hit.
PfamPF14664. RICTOR_N. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 4 hits.
ProtoNetSearch...

Other

NextBio983121.

Entry information

Entry nameTSC11_YEAST
AccessionPrimary (citable) accession number: P40061
Secondary accession number(s): D3DM00
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome V

Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families