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P40061

- TSC11_YEAST

UniProt

P40061 - TSC11_YEAST

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Protein

Target of rapamycin complex 2 subunit TSC11

Gene

TSC11

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 SLM1.1 Publication

GO - Molecular functioni

  1. guanyl-nucleotide exchange factor activity Source: UniProtKB-KW

GO - Biological processi

  1. establishment or maintenance of actin cytoskeleton polarity Source: SGD
  2. fungal-type cell wall organization Source: SGD
  3. regulation of cell growth Source: SGD
  4. sphingolipid biosynthetic process Source: SGD
  5. TOR signaling Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Enzyme and pathway databases

BioCyciYEAST:G3O-30260-MONOMER.
ReactomeiREACT_188925. CD28 dependent PI3K/Akt signaling.
REACT_188931. PIP3 activates AKT signaling.
REACT_223756. Constitutive PI3K/AKT Signaling in Cancer.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:TSC11
Synonyms:AVO3
Ordered Locus Names:YER093C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome V

Organism-specific databases

CYGDiYER093c.
SGDiS000000895. TSC11.

Subcellular locationi

Cell membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication. Vacuole membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication

GO - Cellular componenti

  1. plasma membrane Source: UniProtKB-KW
  2. TORC2 complex Source: SGD
  3. vacuole Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14301430Target of rapamycin complex 2 subunit TSC11PRO_0000202640Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191Phosphoserine2 Publications
Modified residuei81 – 811Phosphoserine1 Publication
Modified residuei84 – 841Phosphoserine1 Publication
Modified residuei87 – 871Phosphoserine1 Publication
Modified residuei141 – 1411Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated by TOR2; when part of TORC2.4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP40061.
PaxDbiP40061.
PeptideAtlasiP40061.

Expressioni

Gene expression databases

GenevestigatoriP40061.

Interactioni

Subunit structurei

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.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
LST8P413182EBI-22621,EBI-28598
TOR2P326005EBI-22621,EBI-19385

Protein-protein interaction databases

BioGridi36838. 180 interactions.
DIPiDIP-4957N.
IntActiP40061. 10 interactions.
MINTiMINT-486144.
STRINGi4932.YER093C.

Structurei

3D structure databases

ProteinModelPortaliP40061.
SMRiP40061. Positions 627-658, 1148-1215.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini995 – 1100106N-terminal Ras-GEFAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili91 – 18090Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the pianissimo family.Curated
Contains 1 N-terminal Ras-GEF domain.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG305760.
GeneTreeiENSGT00390000002096.
HOGENOMiHOG000141815.
InParanoidiP40061.
OMAiGRNDTYV.
OrthoDBiEOG71VT21.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR028268. Pianissimo_fam.
IPR028267. Pianissimo_N.
IPR029453. Rictor_IV.
IPR029451. RICTOR_M.
IPR029452. RICTOR_V.
[Graphical view]
PANTHERiPTHR13298. PTHR13298. 1 hit.
PfamiPF14663. RasGEF_N_2. 1 hit.
PF14666. RICTOR_M. 1 hit.
PF14664. RICTOR_N. 1 hit.
PF14668. RICTOR_V. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 4 hits.

Sequencei

Sequence statusi: Complete.

P40061-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSIPHSAKQS SPLSSRRRSV TNTTPLLTPR HSRDNSSTQI SSAKNITSSS
60 70 80 90 100
PSTITNESSK RNKQNLVLST SFISTKRLEN SAPSPTSPLM ARRTRSTMTK
110 120 130 140 150
ALLNLKAEIN NQYQELARLR KKKDDIEHLR DSTISDIYSG SYSTNHLQKH
160 170 180 190 200
SMRIRANTQL REIDNSIKRV EKHIFDLKQQ FDKKRQRSLT TSSSIKADVG
210 220 230 240 250
SIRNDDGQNN DSEELGDHDS LTDQVTLDDE YLTTPTSGTE RNSQQNLNRN
260 270 280 290 300
STVNSRNNEN HSTLSIPDLD GSNKVNLTGD TEKDLGDLEN ENQIFTSTTT
310 320 330 340 350
EAATWLVSDY MQSFQEKNVN PDFIAQKANG LVTLLKEHSE IRKDLVLTSF
360 370 380 390 400
MSSIQNLLLN GNKLIAASAY RVCRYLINSS IFIDELLELR LDAFIIISLA
410 420 430 440 450
KDNSFQIERE QALKMVRRFI EYNNGVTQGI MQAIISCVEK PEDSLRHMAL
460 470 480 490 500
ETLLELCFVA PEMVKECRGM RVIEGFLQDY TSFSLASVIL DTILQLMATH
510 520 530 540 550
KTRQHFLEDF NVSVLTTVFS DTNTKSNVNV EKMQNASTLI SITLNSYNGF
560 570 580 590 600
MLFSNNNFKP LKQLVSFFQI PICAQYLIDI FLDVLKIKPL PYKPRGRHSH
610 620 630 640 650
SFKPIPSQYY KECMSVNQRL ALIVLILENS EFVPHLLELL NEEDRDDHLV
660 670 680 690 700
AKGRYLLTEY FNLRMNLVDK KYTSVSKPIY KENFTYVNET FQFKKIAYKM
710 720 730 740 750
NRNRNTIGMS GIDYAQNIKS FSKNIKENTL LREVDDFRFR RMVYDSKVLQ
760 770 780 790 800
TKDFTRWNWN IINELLEGPL LNKKQLEELV KSTKFIRRLL VFYRPLRLRF
810 820 830 840 850
SNVNKGAKLS QKYVQVGCQF FKTLTATPEG MKILMDDTKI IPQLASLMFR
860 870 880 890 900
AMEGNISGNI FNKNKLREKI IFGYFKFIGI LTQSKNGVHI LTRWNFFTVI
910 920 930 940 950
YKMFQFESKL GLEFLLLTIP ELDLKYSSHC RVIIGKALVV ANEKVRIEAT
960 970 980 990 1000
KHIGDKLKEL LSTKESDLKL KANKVKLQQF KMEMLTRQLY DLSPSVVAVA
1010 1020 1030 1040 1050
DQALYECIVA GNGSEELGTS FRMFLNQMVF IRSPILFELL SRPYGFQLLN
1060 1070 1080 1090 1100
EINFVKEERD SWLSKKNIEY VHIVEEFLKK NESINAKSLT FQQKSRLPLH
1110 1120 1130 1140 1150
FYESLTKTED GILLLSQTGD LVTFMNVIKK YVNGNNMATV ENAKEILDLK
1160 1170 1180 1190 1200
AALWCVGFIG STELGIGLLD NYSLVEDIIE VAYNASVTSV RFTAFYVLGL
1210 1220 1230 1240 1250
ISMTREGCEI LDEMGWNCCV SVQDEPIGIA LPNRLDRFLS YNEHKWSAFG
1260 1270 1280 1290 1300
EYSDEMIVFN KSDGDLIEKC LPIEFDLDKL LKEKDTAENP LNEKIITNKY
1310 1320 1330 1340 1350
DNDITSQTIT VSGENSSLFA NEGLSSPYVT QYRNDDDSIE SKVLHIVSQL
1360 1370 1380 1390 1400
GNHILSNHAV KEITEINNKY GPRLFENEKM FFKVFNMMSK YRFKPHVRKF
1410 1420 1430
LCGLFINNRA LENVIRHDNK RDKRPANFTR
Length:1,430
Mass (Da):164,368
Last modified:February 1, 1995 - v1
Checksum:i07BB5D75BA204E50
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U18839 Genomic DNA. Translation: AAB64648.1.
U32508 Genomic DNA. Translation: AAB60298.1.
BK006939 Genomic DNA. Translation: DAA07754.1.
PIRiS50596.
RefSeqiNP_011018.1. NM_001178984.1.

Genome annotation databases

EnsemblFungiiYER093C; YER093C; YER093C.
GeneIDi856828.
KEGGisce:YER093C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U18839 Genomic DNA. Translation: AAB64648.1 .
U32508 Genomic DNA. Translation: AAB60298.1 .
BK006939 Genomic DNA. Translation: DAA07754.1 .
PIRi S50596.
RefSeqi NP_011018.1. NM_001178984.1.

3D structure databases

ProteinModelPortali P40061.
SMRi P40061. Positions 627-658, 1148-1215.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 36838. 180 interactions.
DIPi DIP-4957N.
IntActi P40061. 10 interactions.
MINTi MINT-486144.
STRINGi 4932.YER093C.

Proteomic databases

MaxQBi P40061.
PaxDbi P40061.
PeptideAtlasi P40061.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YER093C ; YER093C ; YER093C .
GeneIDi 856828.
KEGGi sce:YER093C.

Organism-specific databases

CYGDi YER093c.
SGDi S000000895. TSC11.

Phylogenomic databases

eggNOGi NOG305760.
GeneTreei ENSGT00390000002096.
HOGENOMi HOG000141815.
InParanoidi P40061.
OMAi GRNDTYV.
OrthoDBi EOG71VT21.

Enzyme and pathway databases

BioCyci YEAST:G3O-30260-MONOMER.
Reactomei REACT_188925. CD28 dependent PI3K/Akt signaling.
REACT_188931. PIP3 activates AKT signaling.
REACT_223756. Constitutive PI3K/AKT Signaling in Cancer.

Miscellaneous databases

NextBioi 983121.

Gene expression databases

Genevestigatori P40061.

Family and domain databases

Gene3Di 1.25.10.10. 1 hit.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR028268. Pianissimo_fam.
IPR028267. Pianissimo_N.
IPR029453. Rictor_IV.
IPR029451. RICTOR_M.
IPR029452. RICTOR_V.
[Graphical view ]
PANTHERi PTHR13298. PTHR13298. 1 hit.
Pfami PF14663. RasGEF_N_2. 1 hit.
PF14666. RICTOR_M. 1 hit.
PF14664. RICTOR_N. 1 hit.
PF14668. RICTOR_V. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 4 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. 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. 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].

Entry informationi

Entry nameiTSC11_YEAST
AccessioniPrimary (citable) accession number: P40061
Secondary accession number(s): D3DM00
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: October 29, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1840 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome V
    Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

External Data

Dasty 3