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Protein

Serine/threonine-protein kinase tor2

Gene

tor2

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

Phosphatidylinositol 3-kinase homolog, component of TORC1, which regulates multiple cellular processes to control cell growth in response to environmental signals. TORC1 controls the switch between cell proliferation and differentiation by sensing nutrient availability. Nutrient limitation and environmental stress signals cause inactivation of TORC1. Active TORC1 positively controls cell growth and ribosome biogenesis by regulating ribosomal protein gene expression (PubMed:17121544, PubMed:17179073, PubMed:17261596). In nutrient rich conditions, responsible for the phosphorylation of AGC S6 kinase (S6K) psk1 at 'Thr-392' and 'Thr-415', activating psk1 kinase activity and promoting phosphorylation of ribosomal protein S6. Also catalyzes the nutrient-dependent phosphorylation of sck1 and sck2 (PubMed:20144990, PubMed:22976295). TORC1 negatively controls G1 cell-cycle arrest, sexual development and amino acid uptake. Represses mating, meiosis and sporulation efficiency by interfering with the functions of the transcription factor ste11 and the meiosis-promoting RNA-binding protein mei2 (PubMed:17046992).6 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • macromolecular complex binding Source: InterPro
  • protein kinase activity Source: PomBase
  • protein serine/threonine kinase activity Source: PomBase

GO - Biological processi

  • DNA repair Source: GO_Central
  • meiotic cell cycle Source: UniProtKB-KW
  • mitotic G1 cell cycle arrest in response to nitrogen starvation Source: PomBase
  • negative regulation of autophagy Source: PomBase
  • negative regulation of induction of conjugation with cellular fusion Source: PomBase
  • peptidyl-threonine phosphorylation Source: PomBase
  • positive regulation of mitotic cell cycle Source: PomBase
  • signal transduction Source: PomBase
  • sporulation resulting in formation of a cellular spore Source: UniProtKB-KW
  • TORC1 signaling Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, Meiosis, Sporulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.1.137. 5613.
ReactomeiR-SPO-3371571. HSF1-dependent transactivation.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase tor21 Publication (EC:2.7.11.11 Publication)
Alternative name(s):
Phosphatidylinositol kinase homolog tor2
Target of rapamycin kinase 2
Gene namesi
Name:tor21 Publication
ORF Names:SPBC216.07cImported, SPBC646.01c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC216.07c.
PomBaseiSPBC216.07c. tor2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
  • nuclear chromatin Source: PomBase
  • perinuclear region of cytoplasm Source: PomBase
  • Tor2-Mei2-Ste11 complex Source: PomBase
  • TORC1 complex Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 23372337Serine/threonine-protein kinase tor2PRO_0000088814Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1539 – 15391Phosphoserine1 Publication
Modified residuei2238 – 22381Phosphoserine1 Publication
Modified residuei2240 – 22401Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9Y7K2.

PTM databases

iPTMnetiQ9Y7K2.

Interactioni

Subunit structurei

The target of rapamycin complex 1 (TORC1) is composed of at least mip1, pop3/wat1, tco89, toc1 and tor2 (PubMed:17046992, PubMed:18076573, PubMed:17261596). Tor2 interacts with the small GTPase rhb1 (PubMed:17121544). Tor2 interacts with ste11 and mei2 (PubMed:17046992).4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
tel2Q9P3W53EBI-2014299,EBI-2014377

Protein-protein interaction databases

BioGridi277243. 34 interactions.
IntActiQ9Y7K2. 7 interactions.
MINTiMINT-4716528.

Structurei

3D structure databases

ProteinModelPortaliQ9Y7K2.
SMRiQ9Y7K2. Positions 1817-1916, 2306-2337.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati163 – 20038HEAT 1Add
BLAST
Repeati249 – 28638HEAT 2Add
BLAST
Repeati290 – 32637HEAT 3Add
BLAST
Repeati409 – 44638HEAT 4Add
BLAST
Repeati474 – 51239HEAT 5Add
BLAST
Repeati559 – 59638HEAT 6Add
BLAST
Repeati642 – 67938HEAT 7Add
BLAST
Repeati683 – 72139HEAT 8Add
BLAST
Repeati727 – 76539HEAT 9Add
BLAST
Repeati802 – 84039HEAT 10Add
BLAST
Repeati844 – 88037HEAT 11Add
BLAST
Repeati881 – 92141HEAT 12Add
BLAST
Repeati965 – 100440HEAT 13Add
BLAST
Repeati1006 – 104338HEAT 14Add
BLAST
Domaini1228 – 1784557FATPROSITE-ProRule annotationAdd
BLAST
Domaini1990 – 2304315PI3K/PI4KPROSITE-ProRule annotationAdd
BLAST
Domaini2305 – 233733FATCPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the PI3/PI4-kinase family.Curated
Contains 1 FAT domain.PROSITE-ProRule annotation
Contains 1 FATC domain.PROSITE-ProRule annotation
Contains 14 HEAT repeats.PROSITE-ProRule annotation
Contains 1 PI3K/PI4K domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

HOGENOMiHOG000163215.
InParanoidiQ9Y7K2.
KOiK07203.
OMAiPAMEPHI.
OrthoDBiEOG7Z3FCR.
PhylomeDBiQ9Y7K2.

Family and domain databases

Gene3Di1.10.1070.11. 3 hits.
1.25.10.10. 6 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR024585. DUF3385_TOR.
IPR003152. FATC_dom.
IPR009076. FRB_dom.
IPR000357. HEAT.
IPR021133. HEAT_type_2.
IPR011009. Kinase-like_dom.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR003151. PIK-rel_kinase_FAT.
IPR014009. PIK_FAT.
IPR026683. TOR.
[Graphical view]
PANTHERiPTHR11139:SF9. PTHR11139:SF9. 1 hit.
PfamiPF11865. DUF3385. 1 hit.
PF02259. FAT. 1 hit.
PF02260. FATC. 1 hit.
PF02985. HEAT. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
PF08771. Rapamycin_bind. 1 hit.
[Graphical view]
SMARTiSM01346. DUF3385. 1 hit.
SM01343. FATC. 1 hit.
SM00146. PI3Kc. 1 hit.
[Graphical view]
SUPFAMiSSF47212. SSF47212. 1 hit.
SSF48371. SSF48371. 5 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS51189. FAT. 1 hit.
PS51190. FATC. 1 hit.
PS50077. HEAT_REPEAT. 1 hit.
PS00915. PI3_4_KINASE_1. 1 hit.
PS00916. PI3_4_KINASE_2. 1 hit.
PS50290. PI3_4_KINASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Y7K2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKEFPGLKSR NEEIRNKAAN DLYEYVIAYS RELSGEALVQ FNNDVNKYVY
60 70 80 90 100
TLIHSTDPLD RLAGVTAINR LIDYEGEDTT RITRFANYLR IILPGTDQKA
110 120 130 140 150
TVLAAKALGR LAVPGGALTS EFVNFEVKRA LEWLQGERNE NRRYAAVLIL
160 170 180 190 200
KELAKNTSTL IYAHIDSIFE LLWHGLRDPK VTIRIASADA LSEFLKIVRQ
210 220 230 240 250
RDSSIRLQWY TSILNEAQRG VAQGSSDYIH GSLLVYRQLF LKAGMFMHER
260 270 280 290 300
YREVSDIILQ FRDHKDLLIR KTVTELIATL AAYNPDEFVS NYLHVCMLHL
310 320 330 340 350
LNLLKKENVK MLAFATIGKV AVAITNSIIP YLDPICDSIK ESLKIHIRNK
360 370 380 390 400
SASDAAIFQC ISLLSIALGQ AFSNYAYDLF DLIFASGLSE ASYRALSDLA
410 420 430 440 450
HNIPPLLPVI QERLLDMLSK ILSGRPFIPP GCPPQYVARS LKSSKSASLK
460 470 480 490 500
TGFFPNDVYI LALKVLGNFD FSGYILNEFV KDCVVVYLEN NDPEVRKTAS
510 520 530 540 550
ITCSQLFARD PILSQTSDHA IQVVAEVLEK LLTVGICDTV PDIRLTVLNS
560 570 580 590 600
LDSRFNKHLA QADKIRLLFI AINDENFAVR ESALRIIGRL NVYNPAYVMP
610 620 630 640 650
YLRKIMLKTL TILDYSTIIR TKEENAKLLC LLIAAAPRLI ESHVEPILQI
660 670 680 690 700
LLPKAKDSSS IVAASIVNSL GEICQISGEV IVPFIKDLMP LIIEALQDQS
710 720 730 740 750
SPIRRAAALK ALGNLSSSTG YVIDPYIEFP SLLDILIGIT KTEQDITIRR
760 770 780 790 800
ETIKLIGTLG ALDPNRHRVL EKGTEKVVPE QKNIPPDISL LMSGIGPSSD
810 820 830 840 850
EYYPTVVITA LMSILKDPSL TIHHTAVIQA VMYIFKTMGL RCAPFLSQII
860 870 880 890 900
PEFIAVMRTC PTNILEFYFQ QLSILVLIVR QHIRSFLPDL FKLIKDFWNP
910 920 930 940 950
HSNLQFTILS LIESLARAMQ GEFKPYLPSL LVMMLQIFDS DVSVDSVSTK
960 970 980 990 1000
KVLHAFIVFG DTLADYFHML LDPILRLYER NDVSIGIKES IMITIGRLSM
1010 1020 1030 1040 1050
VINLSEYASR IIHPVMRMLS CNNASLIRVS MDTVCALIYQ LNVDFAIFIP
1060 1070 1080 1090 1100
MIDKCLKMNG VTHETYSILV EQFLQEQPLP IKLNPYEKYD KPKLDVVASA
1110 1120 1130 1140 1150
ADITSKKLPV NQEILRNAWE ASQRSTKDDW QEWIRRLGVA LLRESPSHAL
1160 1170 1180 1190 1200
RACAALAAAY QPLARDLFNA SFVSCWSELY DHFQEELVKS IEIALTSPHI
1210 1220 1230 1240 1250
SPEIIQILLN LAEFMEHDDK PLPIDIRTLG AYAAKCHAFA KALHYKELEF
1260 1270 1280 1290 1300
IEEELVTKPS VDTIEALISI NNQLQQPDAA IGILKHAQQH DKMNLKETWY
1310 1320 1330 1340 1350
EKLQRWEDAL SAYEKREAAG AGNFEITMGK LRCLHALGEW DRLSQLAQEN
1360 1370 1380 1390 1400
WIHAGHDARR YIAPLSVAAA WGLGQWEQMD EYISVMKSES PDKAFFNAIV
1410 1420 1430 1440 1450
ALHRSQFEEA ASYITRARDL LDTELTALVG ESYNRAYSVA VRVQMLSELE
1460 1470 1480 1490 1500
EIITYKKAED KPEVREMIKK TWVRRLKGCQ RNVDVWQRML RIRSLVISPR
1510 1520 1530 1540 1550
DNMEMWIKFA NLCRKSGRIS LAKKSLNLLL EDDENLDNSL VLKKTHPSIV
1560 1570 1580 1590 1600
YANLKFLWAV DDKRKALNSM QEFTSQLISD INVDPALFVQ STSVNTQKSQ
1610 1620 1630 1640 1650
EEIQYYFHLL ARCYHKQGQW QQEIENNWSE GSFDGVLQSY MYATQFDSKW
1660 1670 1680 1690 1700
YKAWHSWALA NFEAVKFLEQ SEEQIPSAAY EQYIIPAVKG FFKSIALSKG
1710 1720 1730 1740 1750
NLQDTLRLLN LWFKFGNNSN VINTLNVGIS TVNIDIWLDV IPQLIARIHA
1760 1770 1780 1790 1800
SSLSVRKSVH QLLSDVGRAH PQALVYPLTV AAKSQSSARQ NAALAIMDSL
1810 1820 1830 1840 1850
KTHSPRLVEQ ARLVSHELIR AAILWHEQWH EGLEEASRLY FGDHNIEGMF
1860 1870 1880 1890 1900
AVLRPLHEML ERGPETLREI SFQQAFGRDL VEARDCCIRF EQTGDISDLN
1910 1920 1930 1940 1950
QAWDLYYQVF KKIRKQLPQL TTLDLQYVSP KLLHVHDLEL AVPGTYVSGK
1960 1970 1980 1990 2000
PVIRIVKFYP TFNVITSKQR PRRLSIKGSD GKDYQYVLKG HEDIRQDERV
2010 2020 2030 2040 2050
MQLFGLCNNL LLADPETFKR LLSIQRYPVI PLSPDSGLLG WVLDSDTLHV
2060 2070 2080 2090 2100
LIRDYRESRK ILLNIEHRLI IQMAPDYDRL TLLQKVEVFE YALLSTTGQD
2110 2120 2130 2140 2150
LYRVLWLKSR SSEAWLNRRT NYSRTLAVMS MVGYILGLGD RHPSNLMLDR
2160 2170 2180 2190 2200
YTGNIIHIDF GDCFEVAMHR EKFPEKIPFR LTRMLVNAME VSGIEGTFRI
2210 2220 2230 2240 2250
TCEHVMRVLR TNKESVMAVL EAFVYDPLIN WRLAPAYSPS IDEKQSNEPN
2260 2270 2280 2290 2300
TLLGETIDGL HRKRLNEEGI TLEERQKPEI LNQRAITVLN RVSNKLTGRD
2310 2320 2330
FKPQQQLDVP SQVEKLILQA TSIENLCLCY IGWCSFW
Length:2,337
Mass (Da):266,379
Last modified:December 6, 2002 - v2
Checksum:i190F448DA04FD2D9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAB40167.1.
PIRiT39913. T40577.
RefSeqiNP_595359.2. NM_001021266.3.

Genome annotation databases

EnsemblFungiiSPBC216.07c.1; SPBC216.07c.1:pep; SPBC216.07c.
GeneIDi2540720.
KEGGispo:SPBC216.07c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAB40167.1.
PIRiT39913. T40577.
RefSeqiNP_595359.2. NM_001021266.3.

3D structure databases

ProteinModelPortaliQ9Y7K2.
SMRiQ9Y7K2. Positions 1817-1916, 2306-2337.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277243. 34 interactions.
IntActiQ9Y7K2. 7 interactions.
MINTiMINT-4716528.

PTM databases

iPTMnetiQ9Y7K2.

Proteomic databases

MaxQBiQ9Y7K2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC216.07c.1; SPBC216.07c.1:pep; SPBC216.07c.
GeneIDi2540720.
KEGGispo:SPBC216.07c.

Organism-specific databases

EuPathDBiFungiDB:SPBC216.07c.
PomBaseiSPBC216.07c. tor2.

Phylogenomic databases

HOGENOMiHOG000163215.
InParanoidiQ9Y7K2.
KOiK07203.
OMAiPAMEPHI.
OrthoDBiEOG7Z3FCR.
PhylomeDBiQ9Y7K2.

Enzyme and pathway databases

BRENDAi2.7.1.137. 5613.
ReactomeiR-SPO-3371571. HSF1-dependent transactivation.

Miscellaneous databases

PROiQ9Y7K2.

Family and domain databases

Gene3Di1.10.1070.11. 3 hits.
1.25.10.10. 6 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR024585. DUF3385_TOR.
IPR003152. FATC_dom.
IPR009076. FRB_dom.
IPR000357. HEAT.
IPR021133. HEAT_type_2.
IPR011009. Kinase-like_dom.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR003151. PIK-rel_kinase_FAT.
IPR014009. PIK_FAT.
IPR026683. TOR.
[Graphical view]
PANTHERiPTHR11139:SF9. PTHR11139:SF9. 1 hit.
PfamiPF11865. DUF3385. 1 hit.
PF02259. FAT. 1 hit.
PF02260. FATC. 1 hit.
PF02985. HEAT. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
PF08771. Rapamycin_bind. 1 hit.
[Graphical view]
SMARTiSM01346. DUF3385. 1 hit.
SM01343. FATC. 1 hit.
SM00146. PI3Kc. 1 hit.
[Graphical view]
SUPFAMiSSF47212. SSF47212. 1 hit.
SSF48371. SSF48371. 5 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS51189. FAT. 1 hit.
PS51190. FATC. 1 hit.
PS50077. HEAT_REPEAT. 1 hit.
PS00915. PI3_4_KINASE_1. 1 hit.
PS00916. PI3_4_KINASE_2. 1 hit.
PS50290. PI3_4_KINASE_3. 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. "The fission yeast TOR homolog, tor1+, is required for the response to starvation and other stresses via a conserved serine."
    Weisman R., Choder M.
    J. Biol. Chem. 276:7027-7032(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  3. "Fission yeast Tor2 links nitrogen signals to cell proliferation and acts downstream of the Rheb GTPase."
    Uritani M., Hidaka H., Hotta Y., Ueno M., Ushimaru T., Toda T.
    Genes Cells 11:1367-1379(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RHB1.
  4. "Fission yeast Tor2 promotes cell growth and represses cell differentiation."
    Alvarez B., Moreno S.
    J. Cell Sci. 119:4475-4485(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MIP1; POP3; STE11 AND MEI2.
  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. "Rapamycin sensitivity of the Schizosaccharomyces pombe tor2 mutant and organization of two highly phosphorylated TOR complexes by specific and common subunits."
    Hayashi T., Hatanaka M., Nagao K., Nakaseko Y., Kanoh J., Kokubu A., Ebe M., Yanagida M.
    Genes Cells 12:1357-1370(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE TORC1 COMPLEX, PHOSPHORYLATION AT SER-1539, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
  7. "Opposite effects of tor1 and tor2 on nitrogen starvation responses in fission yeast."
    Weisman R., Roitburg I., Schonbrun M., Harari R., Kupiec M.
    Genetics 175:1153-1162(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Loss of the TOR kinase Tor2 mimics nitrogen starvation and activates the sexual development pathway in fission yeast."
    Matsuo T., Otsubo Y., Urano J., Tamanoi F., Yamamoto M.
    Mol. Cell. Biol. 27:3154-3164(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MIP1.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2238 AND SER-2240, IDENTIFICATION BY MASS SPECTROMETRY.
  10. "Fission yeast TORC1 regulates phosphorylation of ribosomal S6 proteins in response to nutrients and its activity is inhibited by rapamycin."
    Nakashima A., Sato T., Tamanoi F.
    J. Cell Sci. 123:777-786(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Psk1, an AGC kinase family member in fission yeast, is directly phosphorylated and controlled by TORC1 and functions as S6 kinase."
    Nakashima A., Otsubo Y., Yamashita A., Sato T., Yamamoto M., Tamanoi F.
    J. Cell Sci. 125:5840-5849(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.

Entry informationi

Entry nameiTOR2_SCHPO
AccessioniPrimary (citable) accession number: Q9Y7K2
Secondary accession number(s): O94507
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: December 6, 2002
Last modified: July 6, 2016
This is version 126 of the entry and version 2 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.