ID   BUD3_YEAST              Reviewed;        1636 AA.
AC   P25558; D6VQZ9; P25556; P25557; P87007;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   02-SEP-2026, entry version 185.
DE   RecName: Full=Bud site selection protein 3;
GN   Name=BUD3; OrderedLocusNames=YCL014W;
GN   ORFNames=YCL012W, YCL013W, YCL12W, YCL13W, YCL14W;
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].
RX   PubMed=7730410; DOI=10.1083/jcb.129.3.767;
RA   Chant J., Mischke M., Mitchell E., Herskowitz I., Pringle J.R.;
RT   "Role of Bud3p in producing the axial budding pattern of yeast.";
RL   J. Cell Biol. 129:767-778(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=1574125; DOI=10.1038/357038a0;
RA   Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA   Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA   Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA   Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA   Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA   Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA   Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA   Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA   Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA   Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA   Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA   Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA   Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA   Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA   Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA   Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA   Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA   Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA   Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA   Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA   Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA   Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA   Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA   Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA   Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA   Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA   Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA   Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA   Sgouros J.G.;
RT   "The complete DNA sequence of yeast chromosome III.";
RL   Nature 357:38-46(1992).
RN   [3]
RP   SEQUENCE REVISION.
RA   Gromadka R.;
RL   Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   SEQUENCE REVISION.
RA   Valles G., Volckaerts G.;
RL   Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1075 AND SER-1614, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [7]
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   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1063; SER-1075; SER-1134;
RP   SER-1149; THR-1157; SER-1160; SER-1254; SER-1257; SER-1412; THR-1440;
RP   SER-1443 AND SER-1614, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-766; THR-1045; SER-1063;
RP   SER-1075; SER-1134; THR-1157; SER-1160; SER-1228; SER-1254; SER-1257;
RP   SER-1390; SER-1412; THR-1429; THR-1440; SER-1443; SER-1501; SER-1549;
RP   SER-1589 AND SER-1614, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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).
RN   [11]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-792 AND LYS-963, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22106047; DOI=10.1002/pmic.201100166;
RA   Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT   "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL   Proteomics 12:236-240(2012).
CC   -!- FUNCTION: Co-assembles with BUD4 at bud sites. BUD4 and BUD3 may
CC       cooperate to recognize a spatial landmark (the neck filaments) during
CC       mitosis and they subsequently become a landmark for establishing the
CC       axial budding pattern in G1.
CC   -!- SUBUNIT: Interacts with AXL2. {ECO:0000269|PubMed:17460121}.
CC   -!- INTERACTION:
CC       P25558; P38928: AXL2; NbExp=2; IntAct=EBI-3840, EBI-3397;
CC       P25558; P47136: BUD4; NbExp=2; IntAct=EBI-3840, EBI-3848;
CC   -!- SIMILARITY: Belongs to the BUD3 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U17580; AAA86315.1; -; Genomic_DNA.
DR   EMBL; X59720; CAA42346.2; -; Genomic_DNA.
DR   EMBL; BK006937; DAA07468.1; -; Genomic_DNA.
DR   PIR; S74285; S74285.
DR   PIR; S74286; S74286.
DR   RefSeq; NP_009914.2; NM_001178662.1.
DR   AlphaFoldDB; P25558; -.
DR   BioGRID; 30969; 127.
DR   DIP; DIP-4969N; -.
DR   FunCoup; P25558; 194.
DR   IntAct; P25558; 12.
DR   MINT; P25558; -.
DR   STRING; 4932.YCL014W; -.
DR   GlyGen; P25558; 3 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; P25558; -.
DR   PaxDb; 4932-YCL014W; -.
DR   PeptideAtlas; P25558; -.
DR   EnsemblFungi; YCL014W_mRNA; YCL014W; YCL014W.
DR   GeneID; 850345; -.
DR   KEGG; sce:YCL014W; -.
DR   AGR; SGD:S000000520; -.
DR   SGD; S000000520; BUD3.
DR   VEuPathDB; FungiDB:YCL014W; -.
DR   eggNOG; ENOG502QSNK; Eukaryota.
DR   HOGENOM; CLU_001458_0_0_1; -.
DR   InParanoid; P25558; -.
DR   OMA; VELQYKW; -.
DR   OrthoDB; 4066896at2759; -.
DR   BioCyc; YEAST:G3O-29281-MONOMER; -.
DR   BioGRID-ORCS; 850345; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P25558; -.
DR   Proteomes; UP000002311; Chromosome III.
DR   RNAct; P25558; 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:0005085; F:guanyl-nucleotide exchange factor activity; IDA:SGD.
DR   GO; GO:0007120; P:axial cellular bud site selection; IMP:SGD.
DR   GO; GO:0000755; P:cytogamy; IMP:SGD.
DR   InterPro; IPR057454; Bud3_C.
DR   InterPro; IPR021895; Bud3_N.
DR   InterPro; IPR035899; DBL_dom_sf.
DR   InterPro; IPR000219; DH_dom.
DR   Pfam; PF12015; Bud3_N; 1.
DR   Pfam; PF25351; PH_BUD3_C; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Isopeptide bond; Phosphoprotein; Reference proteome;
KW   Ubl conjugation.
FT   CHAIN           1..1636
FT                   /note="Bud site selection protein 3"
FT                   /id="PRO_0000065016"
FT   REGION          789..998
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1025..1063
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1107..1130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1152..1179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1331..1354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1435..1465
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        872..885
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        912..921
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        965..980
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        981..991
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1044..1063
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1161..1179
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1342..1351
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1440..1452
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         766
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         1045
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         1063
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         1075
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MOD_RES         1134
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         1149
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         1157
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         1160
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         1228
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         1254
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         1257
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         1390
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         1412
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         1429
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         1440
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         1443
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         1501
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         1549
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         1589
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         1614
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   CROSSLNK        792
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
FT   CROSSLNK        963
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
SQ   SEQUENCE   1636 AA;  184719 MW;  9E4E46BA5C3A3F69 CRC64;
     MEKDLSSLYS EKKDKENDET LFNIKLSKSV VETTPLNGHS LFDDDKSLSD WTDNVFTQSV
     FYHGSDDLIW GKFFVCVYKS PNSNKLNAII FDKLGTSCFE SVDISSNSQY YPAIENLSPS
     DQESNVKKCI AVILLQRYPL LSPSDLSQIL SNKSENCDYD PPYAGDLASS CQLITAVPPE
     DLGKRFFTSG LLQNRFVSST LLDVIYENNE STIELNNRLV FHLGEQLEQL FNPVTEYSPE
     QTEYGYKAPE DELPTESDDD LVKAICNELL QLQTNFTFNL VEFLQKFLIA LRVRVLNEEI
     NGLSTTKLNR LFPPTIDEVT RINCIFLDSL KTAIPYGSLE VLKACSITIP YFYKAYTRHE
     AATKNFSKDI KLFIRHFSNV IPEREVYTEM KIESIIKGPQ EKLLKLKLII ERLWKSKKWR
     PKNQEMAKKC YNNIIDVIDS FGKLDSPLHS YSTRVFTPSG KILTELAKCW PVELQYKWLK
     RRVVGVYDVV DLNDENKRNL LVIFSDYVVF INILEAESYY TSDGSNRPLI SDILMNSLIN
     EVPLPSKIPK LKVERHCYID EVLVSILDKS TLRFDRLKGK DSFSMVCKLS SAFISSSSVA
     DLITKARILE KDTAFHLFKA SRSHFTLYST AHELCAYDSE KIKSKFALFL NIPPSKEILE
     VNNLHLAFFA RFCSNDGRDN IVILDVLTKH DDKHIEVTSD NIVFTIINQL AIEIPICFSS
     LNSSMAKDLL CVNENLIKNL EHQLEEVKHP STDEHRAVNS KLSGASDFDA THEKKRSYGT
     ITTFRSYTSD LKDSPSGDNS NVTKETKEIL PVKPTKKSSK KPREIQKKTK TNASKAEHIE
     KKKPNKGKGF FGVLKNVFGS KSKSKPSPVQ RVPKKISQRH PKSPVKKPMT SEKKSSPKRA
     VVSSPKIKKK STSFSTKESQ TAKSSLRAVE FKSDDLIGKP PDVGNGAHPQ ENTRISSVVR
     DTKYVSYNPS QPVTENTSNE KNVEPKADQS TKQDNISNFA DVEVSASSYP EKLDAETDDQ
     IIGKATNSSS VHGNKELPDL AEVTTANRVS TTSAGDQRID TQSEFLRAAD VENLSDDDEH
     RQNESRVFND DLFGDFIPKH YRNKQENINS SSNLFPEGKV PQEKGVSNEN TNISLKTNED
     ASTLTQKLSP QASKVLTENS NELKDTNNEG KDAKDIKLGD DYSDKETAKE ITKPKNFVEG
     ITERKEIFPT IPRLAPPASK INFQRSPSYI ELFQGMRVVL DKHDAHYNWK RLASQVSLSE
     GLKVNTEEDA AIINKSQDDA KAERMTQISE VIEYEMQQPI PTYLPKAHLD DSGIEKSDDK
     FFEIEEELKE ELKGSKTGNE DVGNNNPSNS IPKIEKPPAF KVIRTSPVRI IGRTFEDTRK
     YENGSPSDIS FTYDTHNNDE PDKRLMELKF PSQDEIPDDR FYTPAEEPTA EFPVEELPNT
     PRSINVTTSN NKSTDDKLSS GNIDQKPTEL LDDLEFSSFN IAFGNTSMST DNMKISSDLS
     SNKTVLGNAQ KVQESPSGPL IYVLPQSSTK HEKEGFLRKK QKDEPIWVSP SKIDFADLSR
     RTKALTPERN TVPLKNNDSR KYKYTGEGSI GNMTNMLLTK DASYAYLKDF VALSDDEDED
     GKQNCAVGGP EKLKFY
//