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BUD4_YEAST
ID   BUD4_YEAST              Reviewed;        1447 AA.
AC   P47136; D6VWR0;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   03-AUG-2022, entry version 175.
DE   RecName: Full=Bud site selection protein 4;
GN   Name=BUD4; OrderedLocusNames=YJR092W; ORFNames=J1905;
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, SUBCELLULAR LOCATION, AND
RP   INDUCTION.
RX   PubMed=8707826; DOI=10.1083/jcb.134.2.413;
RA   Sanders S.L., Herskowitz I.;
RT   "The BUD4 protein of yeast, required for axial budding, is localized to the
RT   mother/BUD neck in a cell cycle-dependent manner.";
RL   J. Cell Biol. 134:413-427(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
RN   [3]
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   [4]
RP   INTERACTION WITH AXL1.
RX   PubMed=12176366; DOI=10.1016/s0960-9822(02)01042-4;
RA   Lord M., Inose F., Hiroko T., Hata T., Fujita A., Chant J.;
RT   "Subcellular localization of Axl1, the cell type-specific regulator of
RT   polarity.";
RL   Curr. Biol. 12:1347-1352(2002).
RN   [5]
RP   INTERACTION WITH IQG1 AND SEC3.
RX   PubMed=12446742; DOI=10.1083/jcb.200205084;
RA   Osman M.A., Konopka J.B., Cerione R.A.;
RT   "Iqg1p links spatial and secretion landmarks to polarity and cytokinesis.";
RL   J. Cell Biol. 159:601-611(2002).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=12221111; DOI=10.1091/mbc.e02-03-0151;
RA   Cullen P.J., Sprague G.F. Jr.;
RT   "The roles of bud-site-selection proteins during haploid invasive growth in
RT   yeast.";
RL   Mol. Biol. Cell 13:2990-3004(2002).
RN   [7]
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   [8]
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   [9]
RP   PHOSPHORYLATION BY CDC28.
RX   PubMed=14574415; DOI=10.1038/nature02062;
RA   Ubersax J.A., Woodbury E.L., Quang P.N., Paraz M., Blethrow J.D., Shah K.,
RA   Shokat K.M., Morgan D.O.;
RT   "Targets of the cyclin-dependent kinase Cdk1.";
RL   Nature 425:859-864(2003).
RN   [10]
RP   FUNCTION.
RX   PubMed=15784684; DOI=10.1242/jcs.02286;
RA   Gladfelter A.S., Kozubowski L., Zyla T.R., Lew D.J.;
RT   "Interplay between septin organization, cell cycle and cell shape in
RT   yeast.";
RL   J. Cell Sci. 118:1617-1628(2005).
RN   [11]
RP   INTERACTION WITH AXL2.
RX   PubMed=17460121; DOI=10.1091/mbc.e06-09-0822;
RA   Gao X.D., Sperber L.M., Kane S.A., Tong Z., Tong A.H., Boone C., Bi E.;
RT   "Sequential and distinct roles of the cadherin domain-containing protein
RT   Axl2p in cell polarization in yeast cell cycle.";
RL   Mol. Biol. Cell 18:2542-2560(2007).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-78; SER-81; SER-91
RP   AND SER-96, AND 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   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167; THR-365; SER-367;
RP   SER-511; SER-616; SER-805 AND SER-811, AND IDENTIFICATION BY MASS
RP   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: Required for establishment of the axial budding pattern in
CC       haploid cells. Cooperates with other bud site selection proteins to
CC       recognize a spatial landmark during mitosis and they subsequently
CC       become a landmark for downstream polarity establishment factors that
CC       coordinate axial budding and cytokinesis. Involved in the septin
CC       organization at the bud neck. {ECO:0000269|PubMed:15784684,
CC       ECO:0000269|PubMed:8707826}.
CC   -!- SUBUNIT: Interacts with AXL1, AXL2, IQG1 and SEC3.
CC       {ECO:0000269|PubMed:12176366, ECO:0000269|PubMed:12446742,
CC       ECO:0000269|PubMed:17460121}.
CC   -!- INTERACTION:
CC       P47136; P38928: AXL2; NbExp=2; IntAct=EBI-3848, EBI-3397;
CC       P47136; P25342: CDC10; NbExp=2; IntAct=EBI-3848, EBI-4174;
CC       P47136; Q12280: IQG1; NbExp=4; IntAct=EBI-3848, EBI-35351;
CC   -!- SUBCELLULAR LOCATION: Bud neck {ECO:0000269|PubMed:12221111,
CC       ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:8707826}.
CC       Note=Localizes to two distinct rings on either side of the mother-bud
CC       neck. The rings stay present in cells after cytokinesis and disappear
CC       before the next bud emergence. Requires IQG1 for proper localization.
CC   -!- INDUCTION: Cell cycle-dependent with low levels at START and a peak in
CC       mitosis (at protein level). {ECO:0000269|PubMed:8707826}.
CC   -!- PTM: Phosphorylated by CDC28. {ECO:0000269|PubMed:14574415}.
CC   -!- MISCELLANEOUS: Present with 1600 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA89620.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U41641; AAB17116.1; -; Genomic_DNA.
DR   EMBL; Z49592; CAA89620.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; Z49591; CAA89619.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08876.1; -; Genomic_DNA.
DR   PIR; S57113; S57113.
DR   RefSeq; NP_012625.5; NM_001181749.3.
DR   AlphaFoldDB; P47136; -.
DR   BioGRID; 33846; 90.
DR   DIP; DIP-4971N; -.
DR   IntAct; P47136; 14.
DR   MINT; P47136; -.
DR   STRING; 4932.YJR092W; -.
DR   iPTMnet; P47136; -.
DR   MaxQB; P47136; -.
DR   PaxDb; P47136; -.
DR   PRIDE; P47136; -.
DR   EnsemblFungi; YJR092W_mRNA; YJR092W; YJR092W.
DR   GeneID; 853554; -.
DR   KEGG; sce:YJR092W; -.
DR   SGD; S000003852; BUD4.
DR   VEuPathDB; FungiDB:YJR092W; -.
DR   eggNOG; ENOG502REBM; Eukaryota.
DR   HOGENOM; CLU_004727_0_0_1; -.
DR   InParanoid; P47136; -.
DR   OMA; MLVKHNT; -.
DR   BioCyc; YEAST:G3O-31719-MON; -.
DR   PRO; PR:P47136; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P47136; protein.
DR   GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR   GO; GO:0000142; C:cellular bud neck contractile ring; IDA:SGD.
DR   GO; GO:0005621; C:cellular bud scar; IDA:SGD.
DR   GO; GO:0005525; F:GTP binding; IDA:SGD.
DR   GO; GO:0007120; P:axial cellular bud site selection; IMP:SGD.
DR   GO; GO:0097271; P:protein localization to bud neck; IMP:SGD.
DR   GO; GO:0031106; P:septin ring organization; IMP:SGD.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00233; PH; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Phosphoprotein; Reference proteome.
FT   CHAIN           1..1447
FT                   /note="Bud site selection protein 4"
FT                   /id="PRO_0000065017"
FT   DOMAIN          1302..1413
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          57..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          272..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          444..479
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          529..591
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          648..673
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          768..879
FT                   /note="Interaction with IQG1"
FT                   /evidence="ECO:0000269|PubMed:12446742"
FT   COMPBIAS        1..20
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        274..316
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        456..474
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        529..587
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        648..670
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         10
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         78
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         81
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         91
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         96
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         167
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         365
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         367
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         511
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         616
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         805
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         811
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   CONFLICT        340
FT                   /note="D -> E (in Ref. 2; CAA89620)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1447 AA;  164486 MW;  1D056B9FF1B7067B CRC64;
     MHDAESTVDS LLKEIDNEME QTKSNITQNG SEDTPHNWKL PLQEIGDDTM EMLVKHNTRS
     NATENSRGRS PSKMSTISNE SLNLGLLRVN SELEESPAAV HQERIKNSVA NGALGHANSP
     KVLNNLKNMA QDIDKLARDE EKPVKLSSSP LKFTLKSTQP LLSYPESPIH RSSIEIETNY
     DDEDEEEEDA YTCLTQSPQI LHSPSRIPIT NAVSINKLNL DFTLNPNESD KSLVSDTSVD
     STGRELDTKT IPELPFCMSS TPEMTPVDEK CNLPSKLLNT SNNSHSDSRS PTASVEDLNI
     STNLPGADSS QNNPVTTDAD ALIENDVVRD LQQNMEHIDD AFDEKKVLDE GCSNEPVTFL
     GENDTRSIVY SNKGTNANVQ EFSQEDSLAH SEPKFKDLNA TSDDVWNEDK ETDANISTST
     KSEESYIADY KVTRQEDWDT KKLHQESEHA NEQPAIIPQK DSSEETFTEL NNESEFQRNF
     KDGEEYRIVQ HEESLYGQRT KSPEENIING SEIGVDHGEA AEVNEPLAKT SAEEHDLSSS
     CEDQSVSEAR NKDRIEEKEV ETKDENIETE KDESEYHKVE ENEEPEHVPL LPPLPRWEEI
     QFNEPFIDEN DTSNDSIDLT RSMKPSDYIS IWHIQEEEIK SNSPESIANS QFSQQSSITT
     ASTVDSKKDN GSTSFKFKPR IVSRSRIYNP KSRVSSLNYY DNEDYILSNS EWNALDPMRR
     NTLISKRIQD NIRTQKGHAP LIRPSIMKLN GEDSGFQNHF LEVEQPQEHE NIPLSTHLSE
     QDITTNVGLD EQKLPTNTQD EAEISIREIE SAGDITFNRG DLLSLSFDEE LGQDFANFLD
     ALDHDSTSFN HGPDDSSSFQ RDSSKKSFNS LWESSYELKP PPSIRKQPIA PDVLQKLLES
     DTKDDADLEK IREERITEPR TGLGIGMLKT PVKDVSIALA ASIKGYEASF SDTDSRPEGM
     NNSDAITLNM FDDFEEDKMT PSTPVRSISP IKRHVSSPFK VVKAGNKQEN NEINIKAEEE
     IEPMTQQETD GLKQDIPPLL AQTKDNVEAK EETITQLEEP QDVEQEFPDM GTLYLSIKAI
     STLALYGTKS HRATYAIVFD NGENVVQTPW ESLPYDGNIR INKEFELPID FKGKAETSSA
     SSERDSYKKC VITLKCKYEK PRHELVEIVD KVPVGKSFFG KTKYKFEKKY VQKKPKQDEW
     DYLFAQDGSF ARCEIEINEE FLKNVAFNTS HMHYNMINKW SRIADKIHGS KRLYELPRKA
     PHKVASLDVE ACFLERTSAF EQFPKQFSLV NKIVSKYKLQ QNIYKEGYLL QDGGDLKGKI
     ENRFFKLHGS QLSGYHEISR KAKIDINLLK VTKVLRNEDI QADNGGQRNF TDWVLFNECF
     QLVFDDGERI TFNAECSNEE KSDWYNKLQE VVELNVFHQP WVKKYCEKLA EEEKTRTTGH
     NLKQDFN
 
 
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