BMH2_YEAST
ID BMH2_YEAST Reviewed; 273 AA.
AC P34730; A2TBP2; D6VS86; Q06HN5;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Protein BMH2;
GN Name=BMH2; OrderedLocusNames=YDR099W; ORFNames=YD8557.08;
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=7744048; DOI=10.1111/j.1432-1033.1995.0045l.x;
RA van Heusden G.P.H., Griffith D.J.F., Ford J.C., Chin-A-Woeng T.F.C.,
RA Schrader P.A.T., Carr A.M., Steensma H.Y.;
RT "The 14-3-3 proteins encoded by the BMH1 and BMH2 genes are essential in
RT the yeast Saccharomyces cerevisiae and can be replaced by a plant
RT homologue.";
RL Eur. J. Biochem. 229:45-53(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8524799; DOI=10.1073/pnas.92.25.11539;
RA Gelperin D., Weigle J., Nelson K.K., Roseboom P., Irie K., Matsumoto K.,
RA Lemmon S.K.;
RT "14-3-3 proteins: potential roles in vesicular transport and Ras signaling
RT in Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:11539-11543(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
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 [MRNA] OF 1-143.
RC STRAIN=ATCC 201390 / BY4743;
RX PubMed=17351133; DOI=10.1101/gr.6049107;
RA Zhang Z., Hesselberth J.R., Fields S.;
RT "Genome-wide identification of spliced introns using a tiling microarray.";
RL Genome Res. 17:503-509(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-116.
RC STRAIN=ATCC 201390 / BY4743;
RX PubMed=17244705; DOI=10.1073/pnas.0610354104;
RA Juneau K., Palm C., Miranda M., Davis R.W.;
RT "High-density yeast-tiling array reveals previously undiscovered introns
RT and extensive regulation of meiotic splicing.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1522-1527(2007).
RN [7]
RP ACETYLATION AT SER-2.
RX PubMed=9298649; DOI=10.1002/elps.1150180810;
RA Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I.,
RA Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R.,
RA Payne W.E.;
RT "Proteome studies of Saccharomyces cerevisiae: identification and
RT characterization of abundant proteins.";
RL Electrophoresis 18:1347-1360(1997).
RN [8]
RP INTERACTION WITH FIN1.
RX PubMed=12551942; DOI=10.1074/jbc.m212495200;
RA van Hemert M.J., Deelder A.M., Molenaar C., Steensma H.Y.,
RA van Heusden G.P.H.;
RT "Self-association of the spindle pole body-related intermediate filament
RT protein Fin1p and its phosphorylation-dependent interaction with 14-3-3
RT proteins in yeast.";
RL J. Biol. Chem. 278:15049-15055(2003).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [10]
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 [11]
RP INTERACTION WITH NTH1.
RX PubMed=22320399; DOI=10.1042/bj20111615;
RA Veisova D., Macakova E., Rezabkova L., Sulc M., Vacha P., Sychrova H.,
RA Obsil T., Obsilova V.;
RT "Role of individual phosphorylation sites for the 14-3-3-protein-dependent
RT activation of yeast neutral trehalase Nth1.";
RL Biochem. J. 443:663-670(2012).
CC -!- SUBUNIT: Interacts with NTH1 (via N-terminus when phosphorylated by
CC PKA); the interaction is direct and activates NTH1 (PubMed:22320399).
CC Interacts with FIN1 (PubMed:12551942). {ECO:0000269|PubMed:12551942,
CC ECO:0000269|PubMed:22320399}.
CC -!- INTERACTION:
CC P34730; P29311: BMH1; NbExp=7; IntAct=EBI-3672, EBI-3661;
CC P34730; P32356: NTH1; NbExp=8; IntAct=EBI-3672, EBI-19509;
CC P34730; P22216: RAD53; NbExp=2; IntAct=EBI-3672, EBI-17843;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 47600 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
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DR EMBL; X84817; CAA59275.1; -; Genomic_DNA.
DR EMBL; U01883; AAA03336.1; -; Unassigned_DNA.
DR EMBL; Z47746; CAA87675.1; -; Genomic_DNA.
DR EMBL; DQ881448; ABI95875.1; -; mRNA.
DR EMBL; EF123145; ABM97489.1; -; mRNA.
DR EMBL; BK006938; DAA11946.1; -; Genomic_DNA.
DR PIR; S51250; S51250.
DR RefSeq; NP_010384.3; NM_001180407.3.
DR AlphaFoldDB; P34730; -.
DR SMR; P34730; -.
DR BioGRID; 32157; 443.
DR DIP; DIP-1212N; -.
DR IntAct; P34730; 83.
DR MINT; P34730; -.
DR STRING; 4932.YDR099W; -.
DR iPTMnet; P34730; -.
DR SWISS-2DPAGE; P34730; -.
DR MaxQB; P34730; -.
DR PaxDb; P34730; -.
DR PRIDE; P34730; -.
DR TopDownProteomics; P34730; -.
DR EnsemblFungi; YDR099W_mRNA; YDR099W; YDR099W.
DR GeneID; 851676; -.
DR KEGG; sce:YDR099W; -.
DR SGD; S000002506; BMH2.
DR VEuPathDB; FungiDB:YDR099W; -.
DR eggNOG; KOG0841; Eukaryota.
DR GeneTree; ENSGT01050000244964; -.
DR HOGENOM; CLU_058290_0_0_1; -.
DR InParanoid; P34730; -.
DR OMA; IPCATTG; -.
DR BioCyc; YEAST:G3O-29702-MON; -.
DR PRO; PR:P34730; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P34730; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR GO; GO:0003688; F:DNA replication origin binding; IDA:SGD.
DR GO; GO:0050815; F:phosphoserine residue binding; IMP:SGD.
DR GO; GO:0030437; P:ascospore formation; IGI:SGD.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IMP:SGD.
DR GO; GO:0006270; P:DNA replication initiation; IGI:SGD.
DR GO; GO:0034221; P:fungal-type cell wall chitin biosynthetic process; IGI:SGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:SGD.
DR GO; GO:1904667; P:negative regulation of ubiquitin protein ligase activity; IPI:SGD.
DR GO; GO:0006267; P:pre-replicative complex assembly involved in nuclear cell cycle DNA replication; IGI:SGD.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0007124; P:pseudohyphal growth; IGI:SGD.
DR GO; GO:0007265; P:Ras protein signal transduction; IGI:SGD.
DR GO; GO:0070873; P:regulation of glycogen metabolic process; IGI:SGD.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0001402; P:signal transduction involved in filamentous growth; IGI:SGD.
DR Gene3D; 1.20.190.20; -; 1.
DR InterPro; IPR000308; 14-3-3.
DR InterPro; IPR023409; 14-3-3_CS.
DR InterPro; IPR036815; 14-3-3_dom_sf.
DR InterPro; IPR023410; 14-3-3_domain.
DR PANTHER; PTHR18860; PTHR18860; 1.
DR Pfam; PF00244; 14-3-3; 1.
DR PIRSF; PIRSF000868; 14-3-3; 1.
DR PRINTS; PR00305; 1433ZETA.
DR SMART; SM00101; 14_3_3; 1.
DR SUPFAM; SSF48445; SSF48445; 1.
DR PROSITE; PS00796; 1433_1; 1.
DR PROSITE; PS00797; 1433_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Nucleus; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298649"
FT CHAIN 2..273
FT /note="Protein BMH2"
FT /id="PRO_0000058716"
FT REGION 236..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:9298649"
FT CONFLICT 119
FT /note="S -> C (in Ref. 1; CAA59275)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="G -> F (in Ref. 1; CAA59275)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 273 AA; 31061 MW; 74788A9103F129FB CRC64;
MSQTREDSVY LAKLAEQAER YEEMVENMKA VASSGQELSV EERNLLSVAY KNVIGARRAS
WRIVSSIEQK EESKEKSEHQ VELIRSYRSK IETELTKISD DILSVLDSHL IPSATTGESK
VFYYKMKGDY HRYLAEFSSG DAREKATNSS LEAYKTASEI ATTELPPTHP IRLGLALNFS
VFYYEIQNSP DKACHLAKQA FDDAIAELDT LSEESYKDST LIMQLLRDNL TLWTSDISES
GQEDQQQQQQ QQQQQQQQQQ QAPAEQTQGE PTK
