BUD6_YEAST
ID BUD6_YEAST Reviewed; 788 AA.
AC P41697; D6VYW2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Bud site selection protein 6;
DE AltName: Full=Actin-interacting protein 3;
GN Name=BUD6; Synonyms=AIP3; OrderedLocusNames=YLR319C; ORFNames=L8543.5;
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=9247651; DOI=10.1091/mbc.8.4.729;
RA Amberg D.C., Zahner J.E., Mulholland J.W., Pringle J.R., Botstein D.;
RT "Aip3p/Bud6p, a yeast actin-interacting protein that is involved in
RT morphogenesis and the selection of bipolar budding sites.";
RL Mol. Biol. Cell 8:729-753(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 359-788.
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 [5]
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233; SER-327 AND SER-342, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-342, AND IDENTIFICATION BY
RP 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-233; SER-327 AND SER-342, AND
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-12; SER-233 AND SER-327, 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: Not essential for mitotic growth but is necessary for normal
CC morphogenesis. Involved in the organization and/or function of the
CC actin cytoskeleton.
CC -!- MISCELLANEOUS: Present with 2610 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; L38903; AAB04948.1; -; Genomic_DNA.
DR EMBL; U35668; AAA79143.1; -; Genomic_DNA.
DR EMBL; U20618; AAB64514.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09628.1; -; Genomic_DNA.
DR PIR; S53397; S53397.
DR RefSeq; NP_013423.1; NM_001182208.1.
DR PDB; 3OKQ; X-ray; 2.04 A; A=549-688.
DR PDB; 3ONX; X-ray; 2.90 A; A/B=549-688.
DR PDB; 4WYB; X-ray; 3.49 A; B/D/F/H/J/L/N/P/R/T/V/Y=699-788.
DR PDBsum; 3OKQ; -.
DR PDBsum; 3ONX; -.
DR PDBsum; 4WYB; -.
DR AlphaFoldDB; P41697; -.
DR SMR; P41697; -.
DR BioGRID; 31583; 198.
DR ComplexPortal; CPX-3188; Polarisome.
DR DIP; DIP-880N; -.
DR IntAct; P41697; 7.
DR MINT; P41697; -.
DR STRING; 4932.YLR319C; -.
DR iPTMnet; P41697; -.
DR MaxQB; P41697; -.
DR PaxDb; P41697; -.
DR PRIDE; P41697; -.
DR EnsemblFungi; YLR319C_mRNA; YLR319C; YLR319C.
DR GeneID; 851029; -.
DR KEGG; sce:YLR319C; -.
DR SGD; S000004311; BUD6.
DR VEuPathDB; FungiDB:YLR319C; -.
DR eggNOG; ENOG502QS95; Eukaryota.
DR HOGENOM; CLU_005287_0_0_1; -.
DR InParanoid; P41697; -.
DR OMA; TQTFALV; -.
DR BioCyc; YEAST:G3O-32403-MON; -.
DR EvolutionaryTrace; P41697; -.
DR PRO; PR:P41697; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P41697; protein.
DR GO; GO:0051286; C:cell tip; IBA:GO_Central.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0043332; C:mating projection tip; IDA:SGD.
DR GO; GO:0000133; C:polarisome; IDA:SGD.
DR GO; GO:0005628; C:prospore membrane; HDA:SGD.
DR GO; GO:0099503; C:secretory vesicle; IDA:SGD.
DR GO; GO:0005816; C:spindle pole body; IDA:SGD.
DR GO; GO:0003779; F:actin binding; IDA:SGD.
DR GO; GO:0005519; F:cytoskeletal regulatory protein binding; IDA:SGD.
DR GO; GO:0008047; F:enzyme activator activity; IMP:SGD.
DR GO; GO:0051017; P:actin filament bundle assembly; IMP:SGD.
DR GO; GO:0030953; P:astral microtubule organization; IMP:SGD.
DR GO; GO:0007121; P:bipolar cellular bud site selection; IMP:SGD.
DR GO; GO:0007118; P:budding cell apical bud growth; IMP:SGD.
DR GO; GO:0030010; P:establishment of cell polarity; IMP:SGD.
DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IC:ComplexPortal.
DR GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IMP:SGD.
DR GO; GO:0051127; P:positive regulation of actin nucleation; IDA:SGD.
DR GO; GO:0090338; P:positive regulation of formin-nucleated actin cable assembly; IDA:SGD.
DR GO; GO:0007124; P:pseudohyphal growth; IMP:SGD.
DR GO; GO:0032880; P:regulation of protein localization; IMP:SGD.
DR GO; GO:0006903; P:vesicle targeting; IC:ComplexPortal.
DR InterPro; IPR022782; AIP3-like_C.
DR InterPro; IPR005613; AIP3_C.
DR Pfam; PF03915; AIP3; 1.
DR SMART; SM00806; AIP3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Phosphoprotein; Reference proteome.
FT CHAIN 1..788
FT /note="Bud site selection protein 6"
FT /id="PRO_0000065018"
FT REGION 140..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 573..628
FT /evidence="ECO:0000255"
FT COMPBIAS 147..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 12
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956"
FT CONFLICT 376
FT /note="Missing (in Ref. 1; AAB04948)"
FT /evidence="ECO:0000305"
FT CONFLICT 384..385
FT /note="NA -> KP (in Ref. 1; AAB04948)"
FT /evidence="ECO:0000305"
FT CONFLICT 434
FT /note="E -> A (in Ref. 1; AAB04948)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="P -> S (in Ref. 1; AAB04948)"
FT /evidence="ECO:0000305"
FT CONFLICT 454
FT /note="M -> I (in Ref. 1; AAB04948)"
FT /evidence="ECO:0000305"
FT CONFLICT 565..568
FT /note="ELGD -> SH (in Ref. 1; AAB04948)"
FT /evidence="ECO:0000305"
FT CONFLICT 742
FT /note="S -> T (in Ref. 1; AAB04948)"
FT /evidence="ECO:0000305"
FT CONFLICT 764..788
FT /note="FEEVERIRKQKDEANLRAYFGPGFT -> LKK (in Ref. 1;
FT AAB04948)"
FT /evidence="ECO:0000305"
FT HELIX 555..594
FT /evidence="ECO:0007829|PDB:3OKQ"
FT HELIX 600..676
FT /evidence="ECO:0007829|PDB:3OKQ"
FT HELIX 701..713
FT /evidence="ECO:0007829|PDB:4WYB"
FT HELIX 719..733
FT /evidence="ECO:0007829|PDB:4WYB"
FT TURN 734..737
FT /evidence="ECO:0007829|PDB:4WYB"
SQ SEQUENCE 788 AA; 88817 MW; 4BAE8F541B8BDF1F CRC64;
MKMAVDDPTY GTPKIKRTAS SSSSIETTVT KLLMSTKHLL QVLTQWSKGT TSGRLVSDAY
VQLGNDFKVV SKFFMHAKVD MSDVGDVPMA LRRVLEVTLR EPPSDETLNK HLPKIREIIV
TLLDKLKVKQ AILKNMQQEH RISVKSHHQQ NPSFTSNLSL GSEGTREGTP LSSRKSSIVR
DQRQSDSVEN SYGEKVNSTS TGTPSAQSAE ATLTKPRTNI KQNLKSNNAP NASDDDDALS
QLKKGTNLQR RASKRYSAYH MAKLTNQSTT EAAAAAGLMT TPSPSMLHLE ETVRKSKLYG
NNNNDDDRNI NSAENKGKSI DDVSKASPLA KTPLPIENVR ASPRRLSSVV TTSPDKAMNG
TCPVFLRIGD KTKKCHVQLP TTKNALRLLF IERFAYSPGA NSFPDIYIMD PQYGVFYELE
ELNLLDIKEG FVIELKLEEN PNNTIKEFID TVKMEISNSQ NDIIRHLKEM SFGSAISGKQ
TEVLPQPGLE ANKHDLVGQN KKDDDKTIKD IQYELGKIKQ VHNINRSNIN ETIFNILRKV
DNFKSLSFSA KNSSNRMYME KSQTELGDLS DTLLSKVDDL QDVIEIMRKD VAERRSQPAK
KKLETVSKDL ENAQADVLKL QEFIDTEKPH WKKTWEAELD KVCEEQQFLT LQEELILDLK
EDLGKALETF DLIKLCCEEQ EKNPSRSKSN PILPIMRPGT FNQVREQVMV AVQSLNPDHD
SRVEAIDKAE KMWEMERKLK ASNEFDDELE NFVGNSNLKK SGGFEEVERI RKQKDEANLR
AYFGPGFT
