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BUD9_YEAST
ID   BUD9_YEAST              Reviewed;         547 AA.
AC   P53226; D6VUH9; Q9HFS8;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=Bud site selection protein 9;
GN   Name=BUD9; OrderedLocusNames=YGR041W; ORFNames=G4152;
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 [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=11514631; DOI=10.1091/mbc.12.8.2497;
RA   Harkins H.A., Page N., Schenkman L.R., De Virgilio C., Shaw S., Bussey H.,
RA   Pringle J.R.;
RT   "Bud8p and Bud9p, proteins that may mark the sites for bipolar budding in
RT   yeast.";
RL   Mol. Biol. Cell 12:2497-2518(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9290212;
RX   DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA   Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT   "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT   chromosome VII.";
RL   Yeast 13:1077-1090(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [4]
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   [5]
RP   CHARACTERIZATION.
RX   PubMed=8657162; DOI=10.1128/mcb.16.4.1857;
RA   Zahner J.E., Harkins H.A., Pringle J.R.;
RT   "Genetic analysis of the bipolar pattern of bud site selection in the yeast
RT   Saccharomyces cerevisiae.";
RL   Mol. Cell. Biol. 16:1857-1870(1996).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [7]
RP   TOPOLOGY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 208353 / W303-1A;
RX   PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA   Kim H., Melen K., Oesterberg M., von Heijne G.;
RT   "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN   [8]
RP   IDENTIFICATION BY 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 SER-112 AND SER-189, AND
RP   IDENTIFICATION BY 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: May be involved in positioning the proximal bud pole signal.
CC       {ECO:0000269|PubMed:11514631}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11514631};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:11514631}. Note=Found
CC       at the necks of large-budded cells and the proximal poles of daughter
CC       cells.
CC   -!- PTM: N- and O-glycosylated.
CC   -!- MISCELLANEOUS: Present with 952 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: To yeast BUD8. {ECO:0000305}.
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DR   EMBL; AF302239; AAG17454.1; -; Genomic_DNA.
DR   EMBL; Z72826; CAA97039.1; -; Genomic_DNA.
DR   EMBL; Z72827; CAA97041.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08140.1; -; Genomic_DNA.
DR   PIR; S64332; S64332.
DR   RefSeq; NP_011555.3; NM_001181170.3.
DR   AlphaFoldDB; P53226; -.
DR   BioGRID; 33288; 108.
DR   DIP; DIP-5513N; -.
DR   IntAct; P53226; 4.
DR   MINT; P53226; -.
DR   STRING; 4932.YGR041W; -.
DR   iPTMnet; P53226; -.
DR   MaxQB; P53226; -.
DR   PaxDb; P53226; -.
DR   PRIDE; P53226; -.
DR   EnsemblFungi; YGR041W_mRNA; YGR041W; YGR041W.
DR   GeneID; 852932; -.
DR   KEGG; sce:YGR041W; -.
DR   SGD; S000003273; BUD9.
DR   VEuPathDB; FungiDB:YGR041W; -.
DR   eggNOG; ENOG502S1HD; Eukaryota.
DR   HOGENOM; CLU_037885_0_0_1; -.
DR   InParanoid; P53226; -.
DR   OMA; ITTLCIC; -.
DR   BioCyc; YEAST:G3O-30761-MON; -.
DR   PRO; PR:P53226; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P53226; protein.
DR   GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IMP:SGD.
DR   GO; GO:0000282; P:cellular bud site selection; IMP:SGD.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell membrane; Glycoprotein; Membrane; Phosphoprotein;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..547
FT                   /note="Bud site selection protein 9"
FT                   /id="PRO_0000065021"
FT   TOPO_DOM        1..460
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        461..481
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        482..521
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        522..542
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        543..547
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          123..160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          194..232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          326..358
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..160
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        214..232
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        326..351
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         112
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         189
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   CARBOHYD        83
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        139
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        142
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        221
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        259
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        263
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        289
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        299
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        340
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        16
FT                   /note="K -> T (in Ref. 1; AAG17454)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        27
FT                   /note="A -> T (in Ref. 1; AAG17454)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        132
FT                   /note="N -> S (in Ref. 1; AAG17454)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        249
FT                   /note="A -> T (in Ref. 1; AAG17454)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        260
FT                   /note="S -> N (in Ref. 1; AAG17454)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        298
FT                   /note="R -> K (in Ref. 1; AAG17454)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        321
FT                   /note="S -> N (in Ref. 1; AAG17454)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        345
FT                   /note="T -> N (in Ref. 1; AAG17454)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        406
FT                   /note="S -> G (in Ref. 1; AAG17454)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        451
FT                   /note="G -> D (in Ref. 1; AAG17454)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        480
FT                   /note="I -> V (in Ref. 1; AAG17454)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        545
FT                   /note="I -> T (in Ref. 1; AAG17454)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   547 AA;  60751 MW;  913D622DAD52C103 CRC64;
     MTKITRDVSI TTENSKSTSG SATASSASLP ENDHPIFHQP RARIRSGSLF IEGSDSFPSS
     EVKSYNVYID DSKYSEILKG DTNSSSTDGK QVFEDARDDN FHQESHRDLE DSILDLVRRD
     PEVAAFPLPP PNSNERNRNS SNGSSAETNL NGHSSSGTIS TSVLLNMGSA EKHAGTTRGD
     HMESSSMKSF EKLGTRPSSL FYPPPEGTAP YQGPRATVSG NKSTRQTQGT YSFPSMRYGV
     DLVSPVEGAV DVAKSRVPNS TLNGTFPDKA FIPHEFQIPK KAWNRIPANK STSLKTPRNH
     SLLIDILKPF EAADLANDQR SSSAVLKNTV HSNGQYNPTN ETSGTRMQDQ RQKNTNEIDL
     EKIPNPQVPL GIAMDTMRSP NQLHEKEYES NIEAGLASGV GKGDNSIKQH QYKKIPQEID
     RDQQLSFQME TMPIQRIDSS SIRSFDSRIY GFSEIYSIPR VITTLCICLF VPPLFFFFSI
     NGNNGVSNYR LMRMIMNYEH RIGLLKGFEW DIDVQWFRTL CFVLGCIEML AIFASIGIGF
     GVGIIRE
 
 
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