BUD14_YEAST
ID BUD14_YEAST Reviewed; 709 AA.
AC P27637; D6VPM3;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Bud site selection protein 14;
GN Name=BUD14; OrderedLocusNames=YAR014C; ORFNames=FUN2;
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].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=7941740; DOI=10.1002/yea.320100413;
RA Clark M.W., Keng T., Storms R.K., Zhong W.-W., Fortin N., Zeng B.,
RA Delaney S., Ouellette B.F.F., Barton A.B., Kaback D.B., Bussey H.;
RT "Sequencing of chromosome I of Saccharomyces cerevisiae: analysis of the 42
RT kbp SPO7-CENI-CDC15 region.";
RL Yeast 10:535-541(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA Storms R.K.;
RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN [3]
RP SEQUENCE REVISION TO C-TERMINUS.
RA Fisk D., Cherry J.M.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 439; 573-595 AND 609.
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-142.
RX PubMed=1658741; DOI=10.1093/nar/19.20.5731;
RA Davies C.J., Hutchison C.A. III;
RT "A directed DNA sequencing strategy based upon Tn3 transposon mutagenesis:
RT application to the ADE1 locus on Saccharomyces cerevisiae chromosome I.";
RL Nucleic Acids Res. 19:5731-5738(1991).
RN [6]
RP FUNCTION.
RX PubMed=11452010; DOI=10.1091/mbc.12.7.2147;
RA Ni L., Snyder M.;
RT "A genomic study of the bipolar bud site selection pattern in Saccharomyces
RT cerevisiae.";
RL Mol. Biol. Cell 12:2147-2170(2001).
RN [7]
RP INTERACTION WITH GLC7.
RX PubMed=12477789; DOI=10.1128/ec.1.6.884-894.2002;
RA Cullen P.J., Sprague G.F. Jr.;
RT "The Glc7p-interacting protein Bud14p attenuates polarized growth,
RT pheromone response, and filamentous growth in Saccharomyces cerevisiae.";
RL Eukaryot. Cell 1:884-894(2002).
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 FUNCTION, INTERACTION WITH GLC7, AND FUNCTION OF THE BUD14-GLC7 COMPLEX.
RX PubMed=16107882; DOI=10.1038/sj.emboj.7600783;
RA Knaus M., Cameroni E., Pedruzzi I., Tatchell K., De Virgilio C., Peter M.;
RT "The Bud14p-Glc7p complex functions as a cortical regulator of dynein in
RT budding yeast.";
RL EMBO J. 24:3000-3011(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212; SER-222 AND SER-658, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160; SER-376 AND SER-378, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-159; SER-160; SER-162;
RP THR-177; SER-212; SER-222; SER-376; SER-378; SER-401; SER-507; SER-655;
RP SER-658 AND SER-670, 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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Important for bud site selection. Seems to be a regulatory
CC subunit of the BUD14-GLC7 type-I phosphatase complex. The BUD14-GLC7
CC complex is necessary to regulate microtubule dynamics at the cortex and
CC may function as a specific activator of the dynein complex.
CC {ECO:0000269|PubMed:11452010, ECO:0000269|PubMed:16107882}.
CC -!- SUBUNIT: Interacts with GLC7. {ECO:0000269|PubMed:12477789,
CC ECO:0000269|PubMed:16107882}.
CC -!- INTERACTION:
CC P27637; P39960: BEM2; NbExp=3; IntAct=EBI-20747, EBI-3517;
CC P27637; P32598: GLC7; NbExp=7; IntAct=EBI-20747, EBI-13715;
CC P27637; P13186: KIN2; NbExp=4; IntAct=EBI-20747, EBI-9723;
CC -!- MISCELLANEOUS: Present with 538 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; L22015; AAC04962.2; -; Genomic_DNA.
DR EMBL; M67445; AAA34397.1; -; Genomic_DNA.
DR EMBL; BK006935; DAA06993.2; -; Genomic_DNA.
DR PIR; S40904; S40904.
DR RefSeq; NP_009408.3; NM_001178215.2.
DR AlphaFoldDB; P27637; -.
DR SMR; P27637; -.
DR BioGRID; 31798; 349.
DR ComplexPortal; CPX-1705; BUD14-GLC7 phosphatase complex.
DR ComplexPortal; CPX-36; Kelch-containing Formin Regulatory Complex.
DR DIP; DIP-1756N; -.
DR IntAct; P27637; 100.
DR MINT; P27637; -.
DR STRING; 4932.YAR014C; -.
DR iPTMnet; P27637; -.
DR MaxQB; P27637; -.
DR PaxDb; P27637; -.
DR PRIDE; P27637; -.
DR EnsemblFungi; YAR014C_mRNA; YAR014C; YAR014C.
DR GeneID; 851271; -.
DR KEGG; sce:YAR014C; -.
DR SGD; S000000069; BUD14.
DR VEuPathDB; FungiDB:YAR014C; -.
DR eggNOG; ENOG502R17J; Eukaryota.
DR GeneTree; ENSGT00390000015725; -.
DR HOGENOM; CLU_024078_0_0_1; -.
DR InParanoid; P27637; -.
DR OMA; NCWKNEN; -.
DR BioCyc; YEAST:G3O-28873-MON; -.
DR PRO; PR:P27637; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P27637; 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; HDA:SGD.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:1990615; C:Kelch-containing formin regulatory complex; IDA:SGD.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0000164; C:protein phosphatase type 1 complex; IPI:ComplexPortal.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IDA:SGD.
DR GO; GO:0000282; P:cellular bud site selection; IC:ComplexPortal.
DR GO; GO:0007010; P:cytoskeleton organization; IMP:SGD.
DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IBA:GO_Central.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; IDA:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; IGI:SGD.
DR GO; GO:0032465; P:regulation of cytokinesis; IGI:SGD.
DR GO; GO:0090337; P:regulation of formin-nucleated actin cable assembly; IGI:SGD.
DR GO; GO:0032880; P:regulation of protein localization; IDA:SGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:SGD.
DR GO; GO:0060627; P:regulation of vesicle-mediated transport; IMP:SGD.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cell division; Phosphoprotein; Reference proteome;
KW SH3 domain.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..707
FT /note="Bud site selection protein 14"
FT /id="PRO_0000065012"
FT DOMAIN 259..320
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 61..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..510
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..650
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..680
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 159
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 177
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 401
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 507
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 658
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 670
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 439
FT /note="G -> A (in Ref. 1; no nucleotide entry and 2;
FT AAC04962)"
FT /evidence="ECO:0000305"
FT CONFLICT 573..595
FT /note="KDISQYIHAKSKIEETTNVENTE -> RTFTYIMQNRKLRDNKRGKHR (in
FT Ref. 1; no nucleotide entry and 2; AAC04962)"
FT /evidence="ECO:0000305"
FT CONFLICT 609
FT /note="A -> P (in Ref. 1; no nucleotide entry and 2;
FT AAC04962)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 709 AA; 78981 MW; F123511A4C592EB4 CRC64;
MSNKEEHVDE TSASGVKEVS SIAARHDNGY APSLITSTSG MDSFQSHALL NDPTLIEDYS
DIINNRPTSG SKLTLGNEDS ESMGGSVVVT PTSNKSSPFN SKLNILSNAA EKGHDVLRNR
DDDKELEEEN VEKHMHSNSK RDQRHYKENS SELPDSYDYS DSEFEDNLER RLQEIETDSV
DSADKDEVHF SVNNTMNPDV DDFSDGLKYA ISEDEDEEEN YSDDDDFDRK FQDSGFQGEK
DDLEEENDDY QPLSPPRELD PDKLYALYAF NGHDSSHCQL GQDEPCILLN DQDAYWWLVK
RITDGKIGFA PAEILETFPE RLARLNCWKN ENMSSQSVAS SDSKDDSISS GNKNQSDAES
IIPTPALNGY GKGNKSVSFN DVVGYADRFI DDAIEDTSLD SNDDGGEGNG QSYDDDVDND
KETKVTHRDE YTEAKLNFGK FQDDDTSDVV SDVSFSTSLN TPLNVKKVRR QDNKNESEPK
TSSSKDREDD YNANRYVGQE KSEPVDSDYD TDLKKVFEAP RMPFANGMAK SDSQNSLSTI
GEFSPSSSEW TNESPSTPIV EESSSIPSSR AIKDISQYIH AKSKIEETTN VENTEGQIQA
SLGSSGGMAN QTDAEQPKEE LEKHHSTPEE EKQSTLSLHS SSEEDFYMDE QRAVSSASIN
SSLSGSRALS NTNMSDPASK PNSLVQHLYA PVFDRMDVLM KQLDEIIRK
