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 27-MAR-2024, entry version 180.
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; 95.
DR DIP; DIP-4971N; -.
DR IntAct; P47136; 14.
DR MINT; P47136; -.
DR STRING; 4932.YJR092W; -.
DR iPTMnet; P47136; -.
DR MaxQB; P47136; -.
DR PaxDb; 4932-YJR092W; -.
DR PeptideAtlas; P47136; -.
DR EnsemblFungi; YJR092W_mRNA; YJR092W; YJR092W.
DR GeneID; 853554; -.
DR KEGG; sce:YJR092W; -.
DR AGR; SGD:S000003852; -.
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 OrthoDB; 2788168at2759; -.
DR BioCyc; YEAST:G3O-31719-MONOMER; -.
DR BioGRID-ORCS; 853554; 4 hits in 10 CRISPR screens.
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 CDD; cd13278; PH_Bud4; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR36100; BUD SITE SELECTION PROTEIN 4; 1.
DR PANTHER; PTHR36100:SF1; BUD SITE SELECTION PROTEIN 4; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF50729; PH domain-like; 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
//
