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   27-MAR-2024, entry version 194.
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; 356.
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; 4932-YAR014C; -.
DR   PeptideAtlas; P27637; -.
DR   EnsemblFungi; YAR014C_mRNA; YAR014C; YAR014C.
DR   GeneID; 851271; -.
DR   KEGG; sce:YAR014C; -.
DR   AGR; SGD:S000000069; -.
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   OrthoDB; 1334285at2759; -.
DR   BioCyc; YEAST:G3O-28873-MONOMER; -.
DR   BioGRID-ORCS; 851271; 5 hits in 10 CRISPR screens.
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; NAS: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; NAS:ComplexPortal.
DR   GO; GO:0008360; P:regulation of cell shape; IGI:SGD.
DR   GO; GO:0032465; P:regulation of cytokinesis; IGI:SGD.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IDA: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:0060627; P:regulation of vesicle-mediated transport; IMP:SGD.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR47775; BUD SITE SELECTION PROTEIN 14; 1.
DR   PANTHER; PTHR47775:SF1; BUD SITE SELECTION PROTEIN 14; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3-domain; 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
//