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Protein

Tuberous sclerosis 2 protein homolog

Gene

tsc2

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

Functioni

Together with tsc1, 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 - Molecular functioni

GO - Biological processi

  • cellular protein localization Source: PomBase
  • negative regulation of G1/S transition of mitotic cell cycle Source: PomBase
  • negative regulation of protein binding Source: PomBase
  • negative regulation of TORC1 signaling Source: PomBase
  • positive regulation of GTPase activity Source: PomBase
  • regulation of amino acid transmembrane transport Source: PomBase
  • regulation of GTPase activity Source: PomBase
  • regulation of L-arginine import Source: PomBase
  • regulation of small GTPase mediated signal transduction Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Enzyme and pathway databases

ReactomeiR-SPO-392517. Rap1 signalling.

Names & Taxonomyi

Protein namesi
Recommended name:
Tuberous sclerosis 2 protein homolog
Gene namesi
Name:tsc2
ORF Names:SPAC630.13c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC630.13c.
PomBaseiSPAC630.13c. tsc2.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1191 – 11911N → K: Decreased arginine uptake. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13391339Tuberous sclerosis 2 protein homologPRO_0000065657Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1036 – 10361Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UUG9.

PTM databases

iPTMnetiQ9UUG9.

Interactioni

Subunit structurei

Interacts with tsc1.1 Publication

Protein-protein interaction databases

BioGridi279762. 105 interactions.
MINTiMINT-4713520.

Structurei

3D structure databases

ProteinModelPortaliQ9UUG9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1109 – 1303195Rap-GAPPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 Rap-GAP domain.PROSITE-ProRule annotation

Phylogenomic databases

InParanoidiQ9UUG9.
OrthoDBiEOG7966QS.
PhylomeDBiQ9UUG9.

Family and domain databases

InterProiIPR000331. Rap_GAP_dom.
IPR003913. Tuberin.
IPR018515. Tuberin-type_domain.
IPR024584. Tuberin_N.
[Graphical view]
PANTHERiPTHR10063:SF1. PTHR10063:SF1. 2 hits.
PfamiPF11864. DUF3384. 1 hit.
PF02145. Rap_GAP. 1 hit.
PF03542. Tuberin. 1 hit.
[Graphical view]
SUPFAMiSSF111347. SSF111347. 1 hit.
PROSITEiPS50085. RAPGAP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9UUG9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNNKSLLDLS SEPAIKDTDI LSYFDANLPF KKRHQIVRSI YHGLKYYIYS
60 70 80 90 100
STSIIQVWQN IQDFISTKND NAAFRELVYN LMMRYVSTQK HLSIIERHTF
110 120 130 140 150
FQTIEKDPFQ DIAELQLRLK SLSVLTDEGH KISGIENRVG PLLSAWFNQY
160 170 180 190 200
LQWQSQATEL QGKDADSKLV HLLFFKSLFK FSTNLVKFQW FLVPEPQMLQ
210 220 230 240 250
LVNSVVQICN HARLEDVVTE VLMFFDSMIR YSVIPKASLY DTVLILCSTY
260 270 280 290 300
ISTYSYSKLA QSVIFNLISS PVSNLAFENV FNILQYNRSN VNAVRGAVRL
310 320 330 340 350
MRFLMLQEVK NDAIASITLS SSIEFTEFPL GFNENVDFEI LGTVYLFLRT
360 370 380 390 400
PSILNRLNFL DWHRILNILM YCSQYLPLKA STSKEAFSKT AAFANIYDRV
410 420 430 440 450
LDFLDFEALI PLLQQFQVKL VFFLKDVLPV LKPKIRKKLL RLFETYNLIF
460 470 480 490 500
PCNQYWVFNL EFLLGIYQCK TFDLEDRALL FKLVEDACSV ADENSAPILC
510 520 530 540 550
SKFLFPVIES FSKESDDCVV SPVYNMLFFL SVNFQNPGLK DCIDHIFQQL
560 570 580 590 600
ISDTSSVTVR RLATSTLIRL FYYYYDLRDA VPIQETLAKM LEILETPSFP
610 620 630 640 650
FVSRMLCLQF FLRFRANGTS IYICENIDLN EPFKVLNVDS ELIPAVYPIS
660 670 680 690 700
DSFVNSATVE KHIWERKEND LIKISNHSTE YGKDFVTFPT SSLLRFYRKS
710 720 730 740 750
MATESNWTIL MFMITHLADQ ISNRSMFIGA LEEIYNLLDF MCDIVFERVS
760 770 780 790 800
ISAEIPSNIR KANIMIPILQ NVQMLFVYHD QFSRAQEDEL VSVFFAGLQK
810 820 830 840 850
WNEACHVSIH SLMLCCYELP VSIRKQLPAI LVTLSRLITK PDLSVHILEF
860 870 880 890 900
LCSLARLPDL IANFTDADYR QIFAIALKYI QHRDFTKESK DSNDTESILK
910 920 930 940 950
NSYSSYVLAL AYSVLQIWFL SLRLTERKKF VPWILRGLKL ASEGKPLEDL
960 970 980 990 1000
CLVQYDMMQQ FCYSNSDINN QTSTFVDSDV ESETWIRGNS LFTINVSVNS
1010 1020 1030 1040 1050
GFLEAVIRRP TGTTQYTFRN EASLQKFLWE ENLTSSKALT RGLLCTPSSF
1060 1070 1080 1090 1100
VSHFLDPHGI SLYNQPLLLP SNDDSVRRAI SVFDRIPVIE SLKAGLVYVG
1110 1120 1130 1140 1150
YQQRREADIL ANTNPSEDFL TFLNGLGTLF ELKTDQKVFA GGLDRENDID
1160 1170 1180 1190 1200
GAFAYCWKDK VTQMVFHCTT MMPTNIEHDP GCTLKKRHIG NDFVTIIFNE
1210 1220 1230 1240 1250
SGLEYDFDTI PSQFNFVNIV ITPESESIRR TGRQIKFYKV KALTKYDIDF
1260 1270 1280 1290 1300
SLFRRYKIVS SDALPAIVRD VTLNAAVFSH IYHRSAGDYV HIWAERLRQL
1310 1320 1330
KRLREKFQAS VLPEDYNLDE QTKTKLQNGT NFSDFTSYL
Length:1,339
Mass (Da):154,813
Last modified:May 1, 2000 - v1
Checksum:iB4D32AE6F0D100FE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB52735.1.
PIRiT38991.
RefSeqiNP_592909.1. NM_001018309.2.

Genome annotation databases

EnsemblFungiiSPAC630.13c.1; SPAC630.13c.1:pep; SPAC630.13c.
GeneIDi2543339.
KEGGispo:SPAC630.13c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB52735.1.
PIRiT38991.
RefSeqiNP_592909.1. NM_001018309.2.

3D structure databases

ProteinModelPortaliQ9UUG9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279762. 105 interactions.
MINTiMINT-4713520.

PTM databases

iPTMnetiQ9UUG9.

Proteomic databases

MaxQBiQ9UUG9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC630.13c.1; SPAC630.13c.1:pep; SPAC630.13c.
GeneIDi2543339.
KEGGispo:SPAC630.13c.

Organism-specific databases

EuPathDBiFungiDB:SPAC630.13c.
PomBaseiSPAC630.13c. tsc2.

Phylogenomic databases

InParanoidiQ9UUG9.
OrthoDBiEOG7966QS.
PhylomeDBiQ9UUG9.

Enzyme and pathway databases

ReactomeiR-SPO-392517. Rap1 signalling.

Miscellaneous databases

NextBioi20804355.
PROiQ9UUG9.

Family and domain databases

InterProiIPR000331. Rap_GAP_dom.
IPR003913. Tuberin.
IPR018515. Tuberin-type_domain.
IPR024584. Tuberin_N.
[Graphical view]
PANTHERiPTHR10063:SF1. PTHR10063:SF1. 2 hits.
PfamiPF11864. DUF3384. 1 hit.
PF02145. Rap_GAP. 1 hit.
PF03542. Tuberin. 1 hit.
[Graphical view]
SUPFAMiSSF111347. SSF111347. 1 hit.
PROSITEiPS50085. RAPGAP. 1 hit.
[Graphical view]
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 TSC1.
  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, MUTAGENESIS OF ASN-1191.
  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].
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1036, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiTSC2_SCHPO
AccessioniPrimary (citable) accession number: Q9UUG9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: May 1, 2000
Last modified: May 11, 2016
This is version 98 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

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

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.