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TIP41_YEAST
ID   TIP41_YEAST             Reviewed;         356 AA.
AC   Q12199; D6W449;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 154.
DE   RecName: Full=Type 2A phosphatase activator TIP41;
DE   AltName: Full=PP2A phosphatase activator TIP41;
DE   AltName: Full=TAP42-interacting protein 1;
GN   Name=TIP41; OrderedLocusNames=YPR040W; ORFNames=YP3085.04;
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=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA   Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA   Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA   DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA   Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA   Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA   Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA   Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA   Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA   Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA   Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(1997).
RN   [2]
RP   GENOME REANNOTATION.
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   REVISION OF GENE MODEL.
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   PubMed=8972573;
RX   DOI=10.1002/(sici)1097-0061(199612)12:15<1501::aid-yea40>3.0.co;2-h;
RA   Lisowsky T.;
RT   "Removal of an intron with unique 3' branch site creates an amino-terminal
RT   protein sequence directing the scERV1 gene product to mitochondria.";
RL   Yeast 12:1501-1510(1996).
RN   [4]
RP   FUNCTION, INTERACTION WITH TAP42 AND NPR1, AND PHOSPHORYLATION.
RX   PubMed=11741537; DOI=10.1016/s1097-2765(01)00386-0;
RA   Jacinto E., Guo B., Arndt K.T., Schmelzle T., Hall M.N.;
RT   "TIP41 interacts with TAP42 and negatively regulates the TOR signaling
RT   pathway.";
RL   Mol. Cell 8:1017-1026(2001).
RN   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=14504216; DOI=10.1093/genetics/165.1.35;
RA   Dunn C.D., Jensen R.E.;
RT   "Suppression of a defect in mitochondrial protein import identifies
RT   cytosolic proteins required for viability of yeast cells lacking
RT   mitochondrial DNA.";
RL   Genetics 165:35-45(2003).
RN   [6]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [7]
RP   FUNCTION.
RX   PubMed=15470255; DOI=10.1128/ec.3.5.1261-1271.2004;
RA   Santhanam A., Hartley A., Duevel K., Broach J.R., Garrett S.;
RT   "PP2A phosphatase activity is required for stress and Tor kinase regulation
RT   of yeast stress response factor Msn2p.";
RL   Eukaryot. Cell 3:1261-1271(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-55, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-55, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: Involved in negative regulation of the TOR signaling pathway
CC       in response to type of available nitrogen source. Indirectly activates
CC       the PP2A phosphatase SIT4 via interaction with its suppressor TAP42.
CC       This interaction is enhanced under nitrogen limitation conditions. Also
CC       has a role in regulation of NPR1 in response to nitrogen limitation.
CC       {ECO:0000269|PubMed:11741537, ECO:0000269|PubMed:15470255}.
CC   -!- SUBUNIT: Interacts with TAP42 and NPR1. {ECO:0000269|PubMed:11741537}.
CC   -!- INTERACTION:
CC       Q12199; P43612: SAP155; NbExp=3; IntAct=EBI-38123, EBI-16370;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- PTM: Phosphorylation. Dephosphorylated by SIT4.
CC       {ECO:0000269|PubMed:11741537}.
CC   -!- SIMILARITY: Belongs to the TIP41 family. {ECO:0000305}.
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DR   EMBL; Z71255; CAA94988.1; -; Genomic_DNA.
DR   EMBL; Z68111; CAA92144.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11465.1; -; Genomic_DNA.
DR   PIR; S61061; S61061.
DR   RefSeq; NP_015365.1; NM_001184137.1.
DR   AlphaFoldDB; Q12199; -.
DR   SMR; Q12199; -.
DR   BioGRID; 36217; 95.
DR   DIP; DIP-1609N; -.
DR   IntAct; Q12199; 18.
DR   MINT; Q12199; -.
DR   STRING; 4932.YPR040W; -.
DR   iPTMnet; Q12199; -.
DR   MaxQB; Q12199; -.
DR   PaxDb; Q12199; -.
DR   PRIDE; Q12199; -.
DR   EnsemblFungi; YPR040W_mRNA; YPR040W; YPR040W.
DR   GeneID; 856153; -.
DR   KEGG; sce:YPR040W; -.
DR   SGD; S000006244; TIP41.
DR   VEuPathDB; FungiDB:YPR040W; -.
DR   eggNOG; KOG3224; Eukaryota.
DR   GeneTree; ENSGT00390000006659; -.
DR   HOGENOM; CLU_039187_0_2_1; -.
DR   InParanoid; Q12199; -.
DR   OMA; GIPIPEM; -.
DR   BioCyc; YEAST:G3O-34196-MON; -.
DR   PRO; PR:Q12199; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; Q12199; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR   GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; IBA:GO_Central.
DR   GO; GO:0031929; P:TOR signaling; IBA:GO_Central.
DR   InterPro; IPR007303; TIP41-like.
DR   PANTHER; PTHR21021:SF16; PTHR21021:SF16; 1.
DR   Pfam; PF04176; TIP41; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW   Signal transduction inhibitor.
FT   CHAIN           1..356
FT                   /note="Type 2A phosphatase activator TIP41"
FT                   /id="PRO_0000247903"
FT   REGION          36..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         55
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   356 AA;  41020 MW;  7E5E31189983EE9F CRC64;
     MSKRNTPPLR SSGINTIQIN AAREMHAQTV RARRMPMPTS GITTPSVQPT AAPATPPRHI
     CNNPNNPQCL HCGSVIIPSP RATLPLEDNP SISINDWTIS SRKKPILNSQ ELDIWENEKL
     KGLTLPEMIF GNNYIRIENS KQHWSIEFNA LDALKEVQLQ DSGIRVAYSN DWINSKKRQN
     STNGAQRFTN DVNDDSLNII HKYDWTYTTR YKGTESSPES KFRLDNDQKL PLDKLAVHDK
     ILFYDDMILF EDELADNGIS ILNVKIRVMN ERLLLLSRFF LRVDDVLVRV YDTRIYVEFD
     ENVVIRESKE FEGKYQDVLA KHRLSQSHDP KAALRDSNWV AQNTPMIKRQ CEIIQF
 
 
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