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BIT2_YEAST
ID   BIT2_YEAST              Reviewed;         545 AA.
AC   P38346; D6VQR6;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Probable target of rapamycin complex 2 subunit BIT2;
DE            Short=TORC2 subunit BIT2;
DE   AltName: Full=Binding partner of TOR2 protein 2;
GN   Name=BIT2; OrderedLocusNames=YBR270C; ORFNames=YBR1738;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 152-152.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   INTERACTION WITH SLM1; SLM2 AND TSC11.
RX   PubMed=11283351; DOI=10.1073/pnas.061034498;
RA   Ito T., Chiba T., Ozawa R., Yoshida M., Hattori M., Sakaki Y.;
RT   "A comprehensive two-hybrid analysis to explore the yeast protein
RT   interactome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4569-4574(2001).
RN   [4]
RP   INTERACTION WITH SLM1 AND SLM2.
RX   PubMed=15689497; DOI=10.1091/mbc.e04-07-0564;
RA   Fadri M., Daquinag A., Wang S., Xue T., Kunz J.;
RT   "The pleckstrin homology domain proteins Slm1 and Slm2 are required for
RT   actin cytoskeleton organization in yeast and bind phosphatidylinositol-4,5-
RT   bisphosphate and TORC2.";
RL   Mol. Biol. Cell 16:1883-1900(2005).
CC   -!- SUBUNIT: Interacts with the target of rapamycin complex 2 (TORC2)
CC       subunit TSC11 and the TORC2 effectors SLM1 and SLM2.
CC       {ECO:0000269|PubMed:11283351, ECO:0000269|PubMed:15689497}.
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DR   EMBL; Z36139; CAA85233.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07386.2; -; Genomic_DNA.
DR   PIR; S46151; S46151.
DR   RefSeq; NP_009829.2; NM_001178618.2.
DR   AlphaFoldDB; P38346; -.
DR   BioGRID; 32965; 94.
DR   DIP; DIP-1443N; -.
DR   IntAct; P38346; 20.
DR   MINT; P38346; -.
DR   STRING; 4932.YBR270C; -.
DR   iPTMnet; P38346; -.
DR   MaxQB; P38346; -.
DR   PaxDb; P38346; -.
DR   PRIDE; P38346; -.
DR   EnsemblFungi; YBR270C_mRNA; YBR270C; YBR270C.
DR   GeneID; 852573; -.
DR   KEGG; sce:YBR270C; -.
DR   SGD; S000000474; BIT2.
DR   VEuPathDB; FungiDB:YBR270C; -.
DR   eggNOG; ENOG502RZ40; Eukaryota.
DR   GeneTree; ENSGT00940000176511; -.
DR   HOGENOM; CLU_037144_0_0_1; -.
DR   InParanoid; P38346; -.
DR   OMA; WSQVGFQ; -.
DR   BioCyc; YEAST:G3O-29191-MON; -.
DR   Reactome; R-SCE-1257604; PIP3 activates AKT signaling.
DR   Reactome; R-SCE-389357; CD28 dependent PI3K/Akt signaling.
DR   Reactome; R-SCE-5218920; VEGFR2 mediated vascular permeability.
DR   Reactome; R-SCE-6804757; Regulation of TP53 Degradation.
DR   PRO; PR:P38346; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P38346; protein.
DR   GO; GO:0031932; C:TORC2 complex; IDA:SGD.
DR   GO; GO:0038203; P:TORC2 signaling; IBA:GO_Central.
DR   InterPro; IPR013745; Bit61/PRR5.
DR   PANTHER; PTHR32428; PTHR32428; 1.
DR   Pfam; PF08539; HbrB; 1.
PE   1: Evidence at protein level;
KW   Reference proteome.
FT   CHAIN           1..545
FT                   /note="Probable target of rapamycin complex 2 subunit BIT2"
FT                   /id="PRO_0000202530"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          78..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..166
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        152..153
FT                   /note="SG -> RA (in Ref. 1; CAA85233)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   545 AA;  61219 MW;  84215A8C09614321 CRC64;
     MATDLNRKRS ATSGSLSVTN PNIKATNRKP ARVYSVSSDI VPQALTHPDE DVHLKTSKSP
     HDAAPRWSQV GFQSIFHDGS NARRSTDSIE EEYSQGTENN DGHSEIGSSS SNRMEGNTTS
     NDSLFSSNSR GNKRRLSIFT NSKDNMRNRS RSGSKNYGTV ITGTSSNNIS RSGSKLFHTK
     SNMSVNSLQS SLSTGHSHSN KGSNVFSKMA KKLLPYKPHN SIGKDDVEPV VPSPFSKFLH
     SSYGKHRSPV QFIHTSTGGL IDSGKSVYSF NPSINNNPND TALSLIQDDA FDATNVSLLH
     DLLKNLPSLI ANYKSFTVQE LFVLEGNIWG IYCSIVVELF KNKRVWQLPA KIEDIDRLLE
     FYITLKTQTK AAVTHSRFLA EIEEFITTSL YILENQIVFN YANEDTVNTA LKRVGIIWKV
     FYQQVYYDMM AVLLPFEKSF QKNSNYWLDG YLSEPSRYAP SIDVLLLKCF RDSIILPYYE
     SFLHTNDGAS KSFQRYIFSE EEQNGVTEED KLTLLQCFGI LNTIKGNSRN QRIIGELLEG
     IRMSI
 
 
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