BUD3_YEAST
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 03-AUG-2022, entry version 169.
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 -!- SIMILARITY: Belongs to the BUD3 family. {ECO:0000305}.
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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; 120.
DR DIP; DIP-4969N; -.
DR IntAct; P25558; 11.
DR MINT; P25558; -.
DR STRING; 4932.YCL014W; -.
DR iPTMnet; P25558; -.
DR MaxQB; P25558; -.
DR PaxDb; P25558; -.
DR PRIDE; P25558; -.
DR EnsemblFungi; YCL014W_mRNA; YCL014W; YCL014W.
DR GeneID; 850345; -.
DR KEGG; sce:YCL014W; -.
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 BioCyc; YEAST:G3O-29281-MON; -.
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 GO; GO:0043547; P:positive regulation of GTPase activity; IDA:SGD.
DR InterPro; IPR021895; Bud3_N.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR Pfam; PF12015; DUF3507; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; SSF48065; 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 789..806
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..847
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..927
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..980
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1044..1060
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1164..1179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1338..1352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1440..1465
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
