BUD2_YEAST
ID BUD2_YEAST Reviewed; 1104 AA.
AC P33314; D6VXJ6;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Inhibitory regulator protein BUD2/CLA2;
DE AltName: Full=Bud site selection protein 2;
GN Name=BUD2; Synonyms=CLA2, ERC25; OrderedLocusNames=YKL092C;
GN ORFNames=YKL424;
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=8262070; DOI=10.1002/j.1460-2075.1993.tb06223.x;
RA Cvrckova F., Nasmyth K.;
RT "Yeast G1 cyclins CLN1 and CLN2 and a GAP-like protein have a role in bud
RT formation.";
RL EMBO J. 12:5277-5286(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8371782; DOI=10.1038/365269a0;
RA Park H.-O., Chant J., Herskowitz I.;
RT "BUD2 encodes a GTPase-activating protein for Bud1/Rsr1 necessary for
RT proper bud-site selection in yeast.";
RL Nature 365:269-274(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 237-1104.
RX PubMed=8203166; DOI=10.1002/yea.320100212;
RA James C.M., Gent M.E., Oliver S.G.;
RT "Sequence analysis of a 3.5 Kb EcoRI fragment from the left arm of
RT Saccharomyces cerevisiae chromosome XI reveals the location of the MBR1
RT gene and a sequence related to a GTPase-activating protein.";
RL Yeast 10:257-264(1994).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-854, AND IDENTIFICATION BY
RP 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-854, AND IDENTIFICATION BY
RP 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 [9]
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: Stimulates the GTPase activity of BUD1/RSR1. Participates in
CC the regulation of bud-site selection.
CC -!- MISCELLANEOUS: Present with 1230 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X74130; CAA52228.1; -; Genomic_DNA.
DR EMBL; L19162; AAA34461.1; -; Genomic_DNA.
DR EMBL; X75561; CAA53241.1; -; Genomic_DNA.
DR EMBL; Z28092; CAA81930.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09066.1; -; Genomic_DNA.
DR PIR; S36773; S36773.
DR RefSeq; NP_012831.1; NM_001179658.1.
DR AlphaFoldDB; P33314; -.
DR BioGRID; 34041; 95.
DR DIP; DIP-2689N; -.
DR IntAct; P33314; 9.
DR MINT; P33314; -.
DR STRING; 4932.YKL092C; -.
DR iPTMnet; P33314; -.
DR MaxQB; P33314; -.
DR PaxDb; P33314; -.
DR PRIDE; P33314; -.
DR EnsemblFungi; YKL092C_mRNA; YKL092C; YKL092C.
DR GeneID; 853770; -.
DR KEGG; sce:YKL092C; -.
DR SGD; S000001575; BUD2.
DR VEuPathDB; FungiDB:YKL092C; -.
DR eggNOG; KOG3508; Eukaryota.
DR GeneTree; ENSGT00550000074797; -.
DR HOGENOM; CLU_002973_0_0_1; -.
DR InParanoid; P33314; -.
DR OMA; WFVGLNY; -.
DR BioCyc; YEAST:G3O-31883-MON; -.
DR PRO; PR:P33314; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P33314; protein.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0005628; C:prospore membrane; HDA:SGD.
DR GO; GO:0005096; F:GTPase activator activity; IDA:SGD.
DR GO; GO:0007120; P:axial cellular bud site selection; IMP:SGD.
DR GO; GO:0007121; P:bipolar cellular bud site selection; IMP:SGD.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:SGD.
DR GO; GO:0030447; P:filamentous growth; IMP:SGD.
DR GO; GO:0036267; P:invasive filamentous growth; IMP:SGD.
DR GO; GO:0031578; P:mitotic spindle orientation checkpoint signaling; IMP:SGD.
DR GO; GO:0043087; P:regulation of GTPase activity; IEA:InterPro.
DR Gene3D; 1.10.506.10; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR039360; Ras_GTPase.
DR InterPro; IPR023152; RasGAP_CS.
DR InterPro; IPR001936; RasGAP_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR PANTHER; PTHR10194; PTHR10194; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00616; RasGAP; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00323; RasGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; GTPase activation; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..1104
FT /note="Inhibitory regulator protein BUD2/CLA2"
FT /id="PRO_0000056656"
FT DOMAIN 316..444
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 505..721
FT /note="Ras-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00167"
FT REGION 1027..1104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1027..1067
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 854
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
FT CONFLICT 437
FT /note="N -> Y (in Ref. 1; CAA52228)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1104 AA; 126663 MW; 451AFC3A78384760 CRC64;
MSSNNEPAQS RTSYFKLNEF LSNVKHYKNT FKGEIQWCNN LSLNDWKTHY LQITSTGALT
HSIDELTADS TNIQPIIKHL QQCRIEIIKD KHSSFKDINA NCNFIIQVNT SGKDNKVYLR
VKSWSDFKKL LTCLIWWSSM KTNGIFNKFQ VSRPLEFKSK KMAKPESLLV YKLNVFGPIV
KNIVLPPATN ILESPDIINN DDNSVGWFSA MGVLKSNGML DLLLQSDGSL IYSLNISQLL
RSEIRILDSS VLQSENSLFL GELPLLRSQL GLEKFRIENI ASAATNSSDI SQEIIVEFPL
RIDLEDCFIA LQSFARSEYL SITGSDKSND MKISNSFKIS ILEANFQSIN LNDKNNTPWS
IFTDITAWGH TWARTSMVSN SSNPFWREEF QFNELLRLTN SYLEIKQLFH DLNNKKRLRL
IGKIKITQEI INDTRYNKET RLPIMDVDNK NFQIGTICIK ISSNLNFILP STNFVKLEKL
LMNANLSMVS NLIYKSSSSM ENDNKLTQTS IIFLDIFQSL SRIEEWFHVL IDKELAKIDG
TVSRINQKNL DSKHVFNSLF RGNSILTKSI EQYFFRVGNE YLSKALSAIL KEIIESNKSC
ELDPARVKEK DEVKKRKIIA DNYKRLYSWV TKIWKRLYAT SNDLPIEIRN VLKIFRQKLE
IICIDDTLQI ILNGISGLLF LRFFCPVILN PKLFKYVSQN LNETARRNLT LISKVLLNLS
TLTQFANKEP WLMKMNNFID KRHNDLLDYI DKMTQKKLDF NSKILNLSST ISRPKLAIEQ
TMLDDLPQIP YLLDKNLRET EFVNLIVNFS QEDMTKMEKY NHMDNGGKGE LIEEEGLLSG
SSLNLSVDKK DLDSPIEVKP EIGELEFEKI TENNTEIFGD DLMNLLKSDD VGSRSRDLDN
GANSGIKFNS IIPKAEEEKH AMKELEQESC LLYNRINHIR KRLSGYECAS STLFEDKKYS
ISLSHKIFYE EIKEGKEIVL KLLNKPTNEN SSARLQKFFT KGVSSKSNNT VGDSYCKFLT
IDVSDENPKS SNKTSVHGTS SENGAKDDYL TLPNSQGKGN LGNRFSPTKL SRIMRKPPNA
DVPKEQNSRK LTRWFKKKKE TGGS
