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O14356

- TOR1_SCHPO

UniProt

O14356 - TOR1_SCHPO

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
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    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 binding Source: IntAct
    5. 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. L-arginine import Source: PomBase
    8. phosphatidylinositol-mediated signaling Source: PomBase
    9. positive regulation of conjugation with cellular fusion Source: PomBase
    10. protein phosphorylation Source: GOC
    11. regulation of conjugation with cellular fusion Source: PomBase
    12. regulation of leucine import Source: PomBase
    13. response to temperature stimulus Source: PomBase
    14. TOR signaling Source: PomBase

    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

    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.
    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

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    MEYFSDLKNK NESIQLAAAD QLKEFVHSST KELSGESLAR FNNDINRRIF     50
    ELIHSHDSHE RFGGILAIGK LIEFESEGDV TNLSRYANYL RMTLPSTDWH 100
    SMELSAKVLG HLAASGGTLA AEFVEFEVQR AFEWLQGDRQ EQKRMAAILI 150
    IKALAQNSPT LVYLYISEIF QNLWTGLRDP KPLIRETAAD ALGASLDVVC 200
    QREAKVQLQC FNEVLLQAEH GLRQSSVEYL HGSLLAYKEL FEKSGSFIRE 250
    HYTEFCDLAL RLREHRDNSI RRCIVFLLPT LSEYNPKKFQ QRYLDSFMVY 300
    LLSHIRKDKE KSLAFEAIGR IAMAVNEAMI PYLQNILKVI RDTLTAKVRE 350
    KTQYEKPVFE CIGMLAAAVK LELLEDSRSL LGLIFSCELS VHLRQALVKM 400
    AENIPPLLAP IQERLLNMVS QILTGKNFEI RTNDTYTPSF TNIYSAREPD 450
    QRSKSTESII LALETLGTFN FTGYSLISFI QESVLSYLEN DNSEIRIAAA 500
    RTCCQVFARD PICRKTNPLA VESVAEVLEK LLTLGIADSD PKIRETVLSL 550
    LDERFDRHLA HPDNIRCLFI ALNDEVFSIR EIAIIIIGRL ALYNPAHVMP 600
    SLRKTIIQLL SDMEYSGNSR QKEESAQLLK LLVSKARTLI KPYIQSIIHV 650
    ILPKAADTSP GVSSAIISAL GELASVEGED MPVDVRGSFM KLILVNLQDQ 700
    SSTLKRLASL KCLRKLCGRS GYVIQPYLDY PPLLGALIGI LQSEQPTPIR 750
    REVLRTLGVL GALDPYTYLT TEEVSDDLQS SHNNAHGVPQ ISAAQYPSLE 800
    NYAMVAVVTL IGILKDSSLS MHHSSVVQAV MHICSQMGSK STVFLPQVVP 850
    TFLQVMQSLS ASSAEFYFQQ LTTLTSIIGP NIRDYVSDIF NLSKVFWEST 900
    TSLLLVILEL IDAIAIALQD EFKFYLPQIL SCMLKAFSLD NTSSRSVSYK 950
    VLQSFVIFGS NIEEYMHLVL PVIIRSFERD TIPLGFRKSA LKCIAQLFQS 1000
    VNFSDHASRI IHPLVRMLGK SNGDLRAVIM DTLCAIVSQL GYDYSIFIPM 1050
    VNKVLVSHKI SHPAYELLVS RLLKGEPLPK DVVVKEFKPR PSTKPFSTQD 1100
    EVLTKLPVDQ ASLKAAWESS QKLTRDDWQD WIRRISIELL KESPSSALRS 1150
    CSTLAGIYHP LARDLFNVSF LSCWDELTES NKKNLVKSIE LAMNAPNISV 1200
    EILQTLLNLA EYMEREDHTL PIPIKVISAH ASKCNVYAKA LHYTELQFVQ 1250
    ETKEEVSIST IESLITINNH LQQSDAAVGM LQYTKEHKQF SLKETWYEKL 1300
    HRWDDALAAY EHREREGDSS FEINIGKLRC YYALGDWDHL SELAQKAWVT 1350
    SEQEHREAIA PLAAAAAWGL GQWNLISEYV SAMDRDPQDK EFFSAISAVH 1400
    LGQYNKAYGH IERHRDILVN DLSSIIGESY NRAYGIMVKS QMLSELEEII 1450
    DYKKNMQYEN NLDSLKKTWR KRLEGCQKNV DVWHNTLRFR ALVLSPQDSP 1500
    EMWIKLADLC RRSDRLKLSN QCLTYLMGRD PSNAYPLDSL KLLNPHVVYT 1550
    YLKYLWATDQ KNIAVSELEE FTSYLSSKHG YKMGDSSKLV DILASSSVSS 1600
    EERSFLARCF HKLGKWKKSL QDSVNQESVR DILNCYFYAT LFDKSWYKAW 1650
    HSWALANFEV VGYYEQTEHG VTQDMYEQYI VPAIKGFFHS SVLNQKNSLQ 1700
    DILRLLNLWF KFGEHSDVAA AIVEGFSNVP MDTWLEVIPQ LIARIHTSSS 1750
    SVRASVHQLL SDIGRVHPQA LVYSLTVSSK STNPQQKHSA KSIMDSMLSH 1800
    SDTLVRQALL VSQELIRVAI LWHELWYEGL EEASQAYFSD HDISLMIDIV 1850
    KPLHETLEKG PSTLSEISFA QTFGYDLRKA RSYWQKFLQD GDPTELNQSW 1900
    DLYYQVFRRI QKQLPRIKHL ELQYVSPKLL DACDLELAVP GTYGHNKPVI 1950
    RISHFHHTFE VISSKQRPRR LTIHGSDGKD YQYVLKGHED LRQDERVMQL 2000
    FGLCNTLLTT DSETFKRRLN IERYTVIPLS PNSGLLGWVP HSDTLHFLIK 2050
    EFRSKRNILL NLEHRMMLQM APDCDSLTLL QKLEVFEYVM ANTDGYDLYH 2100
    VLWLKSRSSE AWLDRRTSYT QSLAVMSMVG YILGLGDRHP SNLMMDRYSG 2150
    KIIHIDFGDC FEVAMHREKF PEKIPFRLTR MLINAMEVSG IQGTYKITCE 2200
    LVMRVLRSNT ESLMAVLEAF VYDPLINWRL MTKSSFGAST TLRPTSSSVE 2250
    EKGRSYTHRA RHADYAALSE TNGVNAEGLN ERSIQVLKRV SNKLTGKDFD 2300
    LKEQLPVKAQ VEKLIQQATA PENLCRCYVG WCSFW 2335
    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.
    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

    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 1, 2014
    This is version 103 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