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O14356

- TOR1_SCHPO

UniProt

O14356 - TOR1_SCHPO

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Protein

Phosphatidylinositol 3-kinase tor1

Gene

tor1

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

Functioni

Phosphatidylinositol 3-kinase homolog required for G1 progression and entry into stationary phase. Also required for the onset of meiosis and sporulation under nitrogen and carbon starvation conditions.1 Publication

Catalytic activityi

ATP + 1-phosphatidyl-1D-myo-inositol = ADP + 1-phosphatidyl-1D-myo-inositol 3-phosphate.

GO - Molecular functioni

  1. 1-phosphatidylinositol-3-kinase activity Source: UniProtKB-EC
  2. ATP binding Source: UniProtKB-KW
  3. drug binding Source: InterPro
  4. protein serine/threonine kinase activity Source: PomBase

GO - Biological processi

  1. cell aging Source: PomBase
  2. cell cycle Source: UniProtKB-KW
  3. cellular response to nitrogen starvation Source: PomBase
  4. cellular response to osmotic stress Source: PomBase
  5. cellular response to starvation Source: PomBase
  6. induction of conjugation upon nitrogen starvation Source: PomBase
  7. phosphatidylinositol-mediated signaling Source: PomBase
  8. positive regulation of conjugation with cellular fusion Source: PomBase
  9. protein phosphorylation Source: GOC
  10. regulation of conjugation with cellular fusion Source: PomBase
  11. response to temperature stimulus Source: PomBase
  12. TOR signaling Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Cell cycle

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.1.137. 5615.
ReactomeiREACT_188268. CD28 dependent PI3K/Akt signaling.
REACT_188279. PIP3 activates AKT signaling.
REACT_207307. HSF1-dependent transactivation.
REACT_227968. Constitutive PI3K/AKT Signaling in Cancer.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylinositol 3-kinase tor1 (EC:2.7.1.137)
Short name:
PI3-kinase tor1
Short name:
PI3K tor1
Short name:
PtdIns-3-kinase tor1
Gene namesi
Name:tor1
ORF Names:SPBC30D10.10c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485: Chromosome II

Organism-specific databases

PomBaseiSPBC30D10.10c.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: PomBase
  2. cytosol Source: PomBase
  3. TORC2 complex Source: PomBase
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1972 – 19721T → A: Increased mTOR kinase activity and stress resistance. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 23352335Phosphatidylinositol 3-kinase tor1PRO_0000088812Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1972 – 19721Phosphothreonine; by PKB/AKT11 Publication

Post-translational modificationi

Phosphorylation at Thr-1972 in the ATP-binding region by AKT1 strongly reduces kinase activity.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO14356.

Expressioni

Inductioni

By nitrogen and/or carbon starvation, cold, osmotic and oxidative stress.1 Publication

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
tel2Q9P3W53EBI-2014420,EBI-2014377

Protein-protein interaction databases

BioGridi277001. 162 interactions.
IntActiO14356. 7 interactions.
MINTiMINT-4672581.
STRINGi4896.SPBC30D10.10c-1.

Structurei

3D structure databases

ProteinModelPortaliO14356.
SMRiO14356. Positions 2303-2335.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati1 – 3131HEAT 1Add
BLAST
Repeati164 – 20138HEAT 2Add
BLAST
Repeati331 – 37141HEAT 3Add
BLAST
Repeati410 – 44940HEAT 4Add
BLAST
Repeati474 – 51239HEAT 5Add
BLAST
Repeati522 – 56039HEAT 6Add
BLAST
Repeati562 – 59635HEAT 7Add
BLAST
Repeati642 – 67938HEAT 8Add
BLAST
Repeati684 – 72239HEAT 9Add
BLAST
Repeati728 – 76639HEAT 10Add
BLAST
Repeati843 – 88038HEAT 11Add
BLAST
Repeati904 – 92320HEAT 12Add
BLAST
Repeati924 – 96138HEAT 13Add
BLAST
Repeati964 – 100340HEAT 14Add
BLAST
Repeati1005 – 104238HEAT 15Add
BLAST
Domaini1226 – 1781556FATPROSITE-ProRule annotationAdd
BLAST
Domaini1987 – 2302316PI3K/PI4KPROSITE-ProRule annotationAdd
BLAST
Domaini2303 – 233533FATCPROSITE-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 15 HEAT repeats.Curated
Contains 1 PI3K/PI4K domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5032.
HOGENOMiHOG000163215.
InParanoidiO14356.
KOiK07203.
OMAiNIYSARE.
OrthoDBiEOG7Z3FCR.
PhylomeDBiO14356.

Family and domain databases

Gene3Di1.10.1070.11. 3 hits.
1.25.10.10. 5 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR024585. DUF3385_TOR.
IPR003152. FATC.
IPR011009. Kinase-like_dom.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR003151. PIK-rel_kinase_FAT.
IPR014009. PIK_FAT.
IPR009076. Rapamycin-bd_dom.
[Graphical view]
PfamiPF11865. DUF3385. 1 hit.
PF02259. FAT. 1 hit.
PF02260. FATC. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
PF08771. Rapamycin_bind. 1 hit.
[Graphical view]
SMARTiSM00146. PI3Kc. 1 hit.
[Graphical view]
SUPFAMiSSF47212. SSF47212. 1 hit.
SSF48371. SSF48371. 4 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS51189. FAT. 1 hit.
PS51190. FATC. 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.

O14356-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEYFSDLKNK NESIQLAAAD QLKEFVHSST KELSGESLAR FNNDINRRIF
60 70 80 90 100
ELIHSHDSHE RFGGILAIGK LIEFESEGDV TNLSRYANYL RMTLPSTDWH
110 120 130 140 150
SMELSAKVLG HLAASGGTLA AEFVEFEVQR AFEWLQGDRQ EQKRMAAILI
160 170 180 190 200
IKALAQNSPT LVYLYISEIF QNLWTGLRDP KPLIRETAAD ALGASLDVVC
210 220 230 240 250
QREAKVQLQC FNEVLLQAEH GLRQSSVEYL HGSLLAYKEL FEKSGSFIRE
260 270 280 290 300
HYTEFCDLAL RLREHRDNSI RRCIVFLLPT LSEYNPKKFQ QRYLDSFMVY
310 320 330 340 350
LLSHIRKDKE KSLAFEAIGR IAMAVNEAMI PYLQNILKVI RDTLTAKVRE
360 370 380 390 400
KTQYEKPVFE CIGMLAAAVK LELLEDSRSL LGLIFSCELS VHLRQALVKM
410 420 430 440 450
AENIPPLLAP IQERLLNMVS QILTGKNFEI RTNDTYTPSF TNIYSAREPD
460 470 480 490 500
QRSKSTESII LALETLGTFN FTGYSLISFI QESVLSYLEN DNSEIRIAAA
510 520 530 540 550
RTCCQVFARD PICRKTNPLA VESVAEVLEK LLTLGIADSD PKIRETVLSL
560 570 580 590 600
LDERFDRHLA HPDNIRCLFI ALNDEVFSIR EIAIIIIGRL ALYNPAHVMP
610 620 630 640 650
SLRKTIIQLL SDMEYSGNSR QKEESAQLLK LLVSKARTLI KPYIQSIIHV
660 670 680 690 700
ILPKAADTSP GVSSAIISAL GELASVEGED MPVDVRGSFM KLILVNLQDQ
710 720 730 740 750
SSTLKRLASL KCLRKLCGRS GYVIQPYLDY PPLLGALIGI LQSEQPTPIR
760 770 780 790 800
REVLRTLGVL GALDPYTYLT TEEVSDDLQS SHNNAHGVPQ ISAAQYPSLE
810 820 830 840 850
NYAMVAVVTL IGILKDSSLS MHHSSVVQAV MHICSQMGSK STVFLPQVVP
860 870 880 890 900
TFLQVMQSLS ASSAEFYFQQ LTTLTSIIGP NIRDYVSDIF NLSKVFWEST
910 920 930 940 950
TSLLLVILEL IDAIAIALQD EFKFYLPQIL SCMLKAFSLD NTSSRSVSYK
960 970 980 990 1000
VLQSFVIFGS NIEEYMHLVL PVIIRSFERD TIPLGFRKSA LKCIAQLFQS
1010 1020 1030 1040 1050
VNFSDHASRI IHPLVRMLGK SNGDLRAVIM DTLCAIVSQL GYDYSIFIPM
1060 1070 1080 1090 1100
VNKVLVSHKI SHPAYELLVS RLLKGEPLPK DVVVKEFKPR PSTKPFSTQD
1110 1120 1130 1140 1150
EVLTKLPVDQ ASLKAAWESS QKLTRDDWQD WIRRISIELL KESPSSALRS
1160 1170 1180 1190 1200
CSTLAGIYHP LARDLFNVSF LSCWDELTES NKKNLVKSIE LAMNAPNISV
1210 1220 1230 1240 1250
EILQTLLNLA EYMEREDHTL PIPIKVISAH ASKCNVYAKA LHYTELQFVQ
1260 1270 1280 1290 1300
ETKEEVSIST IESLITINNH LQQSDAAVGM LQYTKEHKQF SLKETWYEKL
1310 1320 1330 1340 1350
HRWDDALAAY EHREREGDSS FEINIGKLRC YYALGDWDHL SELAQKAWVT
1360 1370 1380 1390 1400
SEQEHREAIA PLAAAAAWGL GQWNLISEYV SAMDRDPQDK EFFSAISAVH
1410 1420 1430 1440 1450
LGQYNKAYGH IERHRDILVN DLSSIIGESY NRAYGIMVKS QMLSELEEII
1460 1470 1480 1490 1500
DYKKNMQYEN NLDSLKKTWR KRLEGCQKNV DVWHNTLRFR ALVLSPQDSP
1510 1520 1530 1540 1550
EMWIKLADLC RRSDRLKLSN QCLTYLMGRD PSNAYPLDSL KLLNPHVVYT
1560 1570 1580 1590 1600
YLKYLWATDQ KNIAVSELEE FTSYLSSKHG YKMGDSSKLV DILASSSVSS
1610 1620 1630 1640 1650
EERSFLARCF HKLGKWKKSL QDSVNQESVR DILNCYFYAT LFDKSWYKAW
1660 1670 1680 1690 1700
HSWALANFEV VGYYEQTEHG VTQDMYEQYI VPAIKGFFHS SVLNQKNSLQ
1710 1720 1730 1740 1750
DILRLLNLWF KFGEHSDVAA AIVEGFSNVP MDTWLEVIPQ LIARIHTSSS
1760 1770 1780 1790 1800
SVRASVHQLL SDIGRVHPQA LVYSLTVSSK STNPQQKHSA KSIMDSMLSH
1810 1820 1830 1840 1850
SDTLVRQALL VSQELIRVAI LWHELWYEGL EEASQAYFSD HDISLMIDIV
1860 1870 1880 1890 1900
KPLHETLEKG PSTLSEISFA QTFGYDLRKA RSYWQKFLQD GDPTELNQSW
1910 1920 1930 1940 1950
DLYYQVFRRI QKQLPRIKHL ELQYVSPKLL DACDLELAVP GTYGHNKPVI
1960 1970 1980 1990 2000
RISHFHHTFE VISSKQRPRR LTIHGSDGKD YQYVLKGHED LRQDERVMQL
2010 2020 2030 2040 2050
FGLCNTLLTT DSETFKRRLN IERYTVIPLS PNSGLLGWVP HSDTLHFLIK
2060 2070 2080 2090 2100
EFRSKRNILL NLEHRMMLQM APDCDSLTLL QKLEVFEYVM ANTDGYDLYH
2110 2120 2130 2140 2150
VLWLKSRSSE AWLDRRTSYT QSLAVMSMVG YILGLGDRHP SNLMMDRYSG
2160 2170 2180 2190 2200
KIIHIDFGDC FEVAMHREKF PEKIPFRLTR MLINAMEVSG IQGTYKITCE
2210 2220 2230 2240 2250
LVMRVLRSNT ESLMAVLEAF VYDPLINWRL MTKSSFGAST TLRPTSSSVE
2260 2270 2280 2290 2300
EKGRSYTHRA RHADYAALSE TNGVNAEGLN ERSIQVLKRV SNKLTGKDFD
2310 2320 2330
LKEQLPVKAQ VEKLIQQATA PENLCRCYVG WCSFW
Length:2,335
Mass (Da):266,184
Last modified:January 1, 1998 - v1
Checksum:i5DCF1CF4ABE8E9A4
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CU329671 Genomic DNA. Translation: CAB10805.1.
PIRiT40186.
RefSeqiNP_596275.1. NM_001022196.2.

Genome annotation databases

EnsemblFungiiSPBC30D10.10c.1; SPBC30D10.10c.1:pep; SPBC30D10.10c.
GeneIDi2540473.
KEGGispo:SPBC30D10.10c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CU329671 Genomic DNA. Translation: CAB10805.1 .
PIRi T40186.
RefSeqi NP_596275.1. NM_001022196.2.

3D structure databases

ProteinModelPortali O14356.
SMRi O14356. Positions 2303-2335.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 277001. 162 interactions.
IntActi O14356. 7 interactions.
MINTi MINT-4672581.
STRINGi 4896.SPBC30D10.10c-1.

Proteomic databases

MaxQBi O14356.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii SPBC30D10.10c.1 ; SPBC30D10.10c.1:pep ; SPBC30D10.10c .
GeneIDi 2540473.
KEGGi spo:SPBC30D10.10c.

Organism-specific databases

PomBasei SPBC30D10.10c.

Phylogenomic databases

eggNOGi COG5032.
HOGENOMi HOG000163215.
InParanoidi O14356.
KOi K07203.
OMAi NIYSARE.
OrthoDBi EOG7Z3FCR.
PhylomeDBi O14356.

Enzyme and pathway databases

BRENDAi 2.7.1.137. 5615.
Reactomei REACT_188268. CD28 dependent PI3K/Akt signaling.
REACT_188279. PIP3 activates AKT signaling.
REACT_207307. HSF1-dependent transactivation.
REACT_227968. Constitutive PI3K/AKT Signaling in Cancer.

Miscellaneous databases

NextBioi 20801600.

Family and domain databases

Gene3Di 1.10.1070.11. 3 hits.
1.25.10.10. 5 hits.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR024585. DUF3385_TOR.
IPR003152. FATC.
IPR011009. Kinase-like_dom.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR003151. PIK-rel_kinase_FAT.
IPR014009. PIK_FAT.
IPR009076. Rapamycin-bd_dom.
[Graphical view ]
Pfami PF11865. DUF3385. 1 hit.
PF02259. FAT. 1 hit.
PF02260. FATC. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
PF08771. Rapamycin_bind. 1 hit.
[Graphical view ]
SMARTi SM00146. PI3Kc. 1 hit.
[Graphical view ]
SUPFAMi SSF47212. SSF47212. 1 hit.
SSF48371. SSF48371. 4 hits.
SSF56112. SSF56112. 2 hits.
PROSITEi PS51189. FAT. 1 hit.
PS51190. FATC. 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 ]
ProtoNeti Search...

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, FUNCTION, INDUCTION.
  3. "Phosphorylation of the TOR ATP binding domain by AGC kinase constitutes a novel mode of TOR inhibition."
    Halova L., Du W., Kirkham S., Smith D.L., Petersen J.
    J. Cell Biol. 203:595-604(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-1972, MUTAGENESIS OF THR-1972.

Entry informationi

Entry nameiTOR1_SCHPO
AccessioniPrimary (citable) accession number: O14356
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: January 1, 1998
Last modified: October 29, 2014
This is version 104 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

External Data

Dasty 3