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Protein

Tuberous sclerosis 1 protein homolog

Gene

tsc1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Together with tsc2, required for uptake of various amino acids from the environment and for proper conjugation. Involved in induction of gene expression of permeases and genes required for meiosis upon nitrogen starvation. May act as a GTPase-activating protein (GAP) for the small GTPase rhb1.3 Publications

GO - Biological processi

  • methionine import into cell Source: PomBase
  • negative regulation of G1/S transition of mitotic cell cycle Source: PomBase
  • regulation of amino acid transmembrane transport Source: PomBase
  • TOR signaling Source: PomBase
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Tuberous sclerosis 1 protein homolog
Gene namesi
Name:tsc1
ORF Names:SPAC22F3.13
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC22F3.13.
PomBaseiSPAC22F3.13. tsc1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • TSC1-TSC2 complex Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 899899Tuberous sclerosis 1 protein homologPRO_0000065653Add
BLAST

Proteomic databases

MaxQBiQ09778.

Interactioni

Subunit structurei

Interacts with tsc2.1 Publication

Protein-protein interaction databases

BioGridi278359. 83 interactions.
IntActiQ09778. 1 interaction.
MINTiMINT-4695004.

Structurei

Secondary structure

1
899
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 1413Combined sources
Helixi26 – 3813Combined sources
Helixi44 – 6017Combined sources
Beta strandi63 – 653Combined sources
Helixi66 – 7914Combined sources
Helixi80 – 823Combined sources
Helixi87 – 9610Combined sources
Helixi98 – 1036Combined sources
Helixi109 – 12315Combined sources
Turni128 – 1314Combined sources
Helixi135 – 15420Combined sources
Helixi165 – 18521Combined sources
Helixi187 – 19812Combined sources
Helixi201 – 2033Combined sources
Helixi204 – 21613Combined sources
Helixi222 – 2287Combined sources
Helixi230 – 24011Combined sources
Helixi244 – 25815Combined sources
Turni259 – 2613Combined sources
Turni264 – 2685Combined sources
Helixi269 – 28012Combined sources
Turni284 – 2863Combined sources
Helixi332 – 3343Combined sources
Helixi339 – 34911Combined sources
Helixi351 – 3577Combined sources
Helixi361 – 3666Combined sources
Turni367 – 3693Combined sources
Helixi378 – 38912Combined sources
Helixi396 – 3994Combined sources
Helixi403 – 4075Combined sources
Helixi412 – 42716Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4KK0X-ray2.90A/B/C/D/E/F/G/H/I/J1-431[»]
4KK1X-ray3.30A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T1-431[»]
ProteinModelPortaliQ09778.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili540 – 706167Sequence analysisAdd
BLAST
Coiled coili737 – 847111Sequence analysisAdd
BLAST

Keywords - Domaini

Coiled coil

Phylogenomic databases

InParanoidiQ09778.
OMAiLANIMEI.
OrthoDBiEOG71CFVC.
PhylomeDBiQ09778.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR007483. Hamartin.
[Graphical view]
PANTHERiPTHR15154. PTHR15154. 3 hits.
PfamiPF04388. Hamartin. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.

Sequencei

Sequence statusi: Complete.

Q09778-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPLQSLVKAL WNVLHEEESE GYPDLTELIA EVESYQQRYP KQNPTNSQKI
60 70 80 90 100
RHILDEIYEK TPFNNTRRRI LWLAVLKTVI PLLILDRQAV GEWWDQIFFP
110 120 130 140 150
FLNSPTQLKP VFSDLKSILF YILIFHDEDE WGGDLRRECA EETITRLVDL
160 170 180 190 200
YVSKAIENLG DVESQEQRNQ TIECLVNVLV HYGIQRPKEL SSCFCHHFLN
210 220 230 240 250
PPTRIPILSV MVEVIRRQGP RLYEIPQTGF YDLVLKCAEF DTSPILLSYA
260 270 280 290 300
LSFILMILSH ICNSLDDSLY RLFCIYLRFS MIDPTSGFPS STASGNWEVF
310 320 330 340 350
HDFMSTYAST TTSQTDSSYN DVHDIVGSSQ PDYLESLDYS QLFSILYALY
360 370 380 390 400
PINFLEFLRD PKLYASKHNF QIRYSFNQEL LSTKSDGLLG RHLAHSNFLK
410 420 430 440 450
YTAETELTDK SRWTRLDSIA VVALCNSLNA VGIAESVMDP FGGKLPTTYE
460 470 480 490 500
ETSSATGLLA YPNESHDIAS EPFSISWPQN PSISGSVHSA TTFDKAQLSN
510 520 530 540 550
TEDSYDNISH GTSYSEGVSS IHMVKGERGS NNLELTSESL SSTNDTIRRL
560 570 580 590 600
QRDLLFLQNE LRFEKFVRQQ HLQNIGKLHR EHILDMAVES ERQKLLLTNK
610 620 630 640 650
RYKAQIELLN SEIDKHRSES QAALNRRVKW ENDFNNKIKA LREEKKAWKS
660 670 680 690 700
EESELKSSIE SLISQLESIR NSQIDIAFSK NQLELKLQLY ETKLKEYEQH
710 720 730 740 750
LSCVNISKKQ VSSSSDTSFG NTKMDSSMIL SNSEAVSDEQ ERELIESEKH
760 770 780 790 800
RMKLESENLH LQANIELLKK DLEAINVVYE AKIFDLEKRL SSEANAPELH
810 820 830 840 850
NPVNLNYDAQ LSKISEIKEN YDELLTRYRE LEGKFLESQA EVEELKNFQK
860 870 880 890
PLVDTGSSIH SSPGLQQSKF IIRNDSLHPK VGPPRRQSTD TSRSTFRQY
Length:899
Mass (Da):103,435
Last modified:November 1, 1995 - v1
Checksum:i03D7E9CC8866ECAB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA91078.1.
PIRiS62428.
RefSeqiNP_593028.1. NM_001018427.2.

Genome annotation databases

EnsemblFungiiSPAC22F3.13.1; SPAC22F3.13.1:pep; SPAC22F3.13.
GeneIDi2541869.
KEGGispo:SPAC22F3.13.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA91078.1.
PIRiS62428.
RefSeqiNP_593028.1. NM_001018427.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4KK0X-ray2.90A/B/C/D/E/F/G/H/I/J1-431[»]
4KK1X-ray3.30A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T1-431[»]
ProteinModelPortaliQ09778.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278359. 83 interactions.
IntActiQ09778. 1 interaction.
MINTiMINT-4695004.

Proteomic databases

MaxQBiQ09778.

Protocols and materials databases

DNASUi2541869.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC22F3.13.1; SPAC22F3.13.1:pep; SPAC22F3.13.
GeneIDi2541869.
KEGGispo:SPAC22F3.13.

Organism-specific databases

EuPathDBiFungiDB:SPAC22F3.13.
PomBaseiSPAC22F3.13. tsc1.

Phylogenomic databases

InParanoidiQ09778.
OMAiLANIMEI.
OrthoDBiEOG71CFVC.
PhylomeDBiQ09778.

Miscellaneous databases

PROiQ09778.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR007483. Hamartin.
[Graphical view]
PANTHERiPTHR15154. PTHR15154. 3 hits.
PfamiPF04388. Hamartin. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "Role of the Tsc1-Tsc2 complex in signaling and transport across the cell membrane in the fission yeast Schizosaccharomyces pombe."
    Matsumoto S., Bandyopadhyay A., Kwiatkowski D.J., Maitra U., Matsumoto T.
    Genetics 161:1053-1063(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TSC2.
  3. "Tsc1+ and tsc2+ regulate arginine uptake and metabolism in Schizosaccharomyces pombe."
    van Slegtenhorst M., Carr E., Stoyanova R., Kruger W.D., Henske E.P.
    J. Biol. Chem. 279:12706-12713(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. "A defect in protein farnesylation suppresses a loss of Schizosaccharomyces pombe tsc2+, a homolog of the human gene predisposing to tuberous sclerosis complex."
    Nakase Y., Fukuda K., Chikashige Y., Tsutsumi C., Morita D., Kawamoto S., Ohnuki M., Hiraoka Y., Matsumoto T.
    Genetics 173:569-578(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTSC1_SCHPO
AccessioniPrimary (citable) accession number: Q09778
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 8, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.