BMH1_YEAST
ID BMH1_YEAST Reviewed; 267 AA.
AC P29311; D3DM86; Q06854;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Protein BMH1;
GN Name=BMH1; OrderedLocusNames=YER177W;
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 26109 / X2180;
RX PubMed=1378790; DOI=10.1016/0014-5793(92)80426-h;
RA van Heusden G.P., Wenzel T.J., Lagendijk E.L., de Steensma H.Y.,
RA van den Berg J.A.;
RT "Characterization of the yeast BMH1 gene encoding a putative protein
RT homologous to mammalian protein kinase II activators and protein kinase C
RT inhibitors.";
RL FEBS Lett. 302:145-150(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Mulligan J.T., Dietrich F.S., Hennessey K.M., Sehl P., Komp C., Wei Y.,
RA Taylor P., Nakahara K., Roberts D., Davis R.W.;
RL Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(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 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 [6]
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 [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89, 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 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).
RN [10]
RP SUBUNIT, AND 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).
RN [11]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-76, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [12] {ECO:0007744|PDB:5N6N}
RP X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF 1-236 IN COMPLEX WITH NTH1,
RP SUBUNIT, AND INTERACTION WITH NTH1.
RX PubMed=29087344; DOI=10.1073/pnas.1714491114;
RA Alblova M., Smidova A., Docekal V., Vesely J., Herman P., Obsilova V.,
RA Obsil T.;
RT "Molecular basis of the 14-3-3 protein-dependent activation of yeast
RT neutral trehalase Nth1.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E9811-E9820(2017).
CC -!- FUNCTION: Involved in growth regulation.
CC -!- SUBUNIT: Homodimer (PubMed:29087344). Interacts with NTH1 (via N-
CC terminus when phosphorylated by PKA); the interaction is direct and
CC activates NTH1 (PubMed:29087344, PubMed:22320399). Interacts with FIN1
CC (PubMed:12551942). {ECO:0000269|PubMed:12551942,
CC ECO:0000269|PubMed:22320399, ECO:0000269|PubMed:29087344}.
CC -!- INTERACTION:
CC P29311; P34730: BMH2; NbExp=7; IntAct=EBI-3661, EBI-3672;
CC P29311; P32356: NTH1; NbExp=7; IntAct=EBI-3661, EBI-19509;
CC P29311; Q96B36: AKT1S1; Xeno; NbExp=3; IntAct=EBI-3661, EBI-720593;
CC -!- MISCELLANEOUS: Present with 158000 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; X71664; CAA50656.1; -; Genomic_DNA.
DR EMBL; X66206; CAA46959.1; -; Genomic_DNA.
DR EMBL; U18922; AAB64704.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07840.1; -; Genomic_DNA.
DR PIR; S30863; S30863.
DR RefSeq; NP_011104.3; NM_001179067.3.
DR PDB; 5N6N; X-ray; 2.29 A; A/B=1-236.
DR PDB; 6QK8; X-ray; 2.92 A; A/B/C/D=1-236.
DR PDBsum; 5N6N; -.
DR PDBsum; 6QK8; -.
DR AlphaFoldDB; P29311; -.
DR SMR; P29311; -.
DR BioGRID; 36930; 699.
DR DIP; DIP-4313N; -.
DR IntAct; P29311; 141.
DR MINT; P29311; -.
DR STRING; 4932.YER177W; -.
DR iPTMnet; P29311; -.
DR COMPLUYEAST-2DPAGE; P29311; -.
DR SWISS-2DPAGE; P29311; -.
DR MaxQB; P29311; -.
DR PaxDb; P29311; -.
DR PRIDE; P29311; -.
DR TopDownProteomics; P29311; -.
DR EnsemblFungi; YER177W_mRNA; YER177W; YER177W.
DR GeneID; 856924; -.
DR KEGG; sce:YER177W; -.
DR SGD; S000000979; BMH1.
DR VEuPathDB; FungiDB:YER177W; -.
DR eggNOG; KOG0841; Eukaryota.
DR GeneTree; ENSGT01050000244964; -.
DR HOGENOM; CLU_058290_0_0_1; -.
DR InParanoid; P29311; -.
DR OMA; ICSYRSK; -.
DR BioCyc; YEAST:G3O-30336-MON; -.
DR PRO; PR:P29311; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P29311; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; HDA: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:0008047; F:enzyme activator activity; IDA:UniProtKB.
DR GO; GO:0050815; F:phosphoserine residue binding; IMP:SGD.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IDA:SGD.
DR GO; GO:0070842; P:aggresome assembly; 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:0034221; P:fungal-type cell wall chitin biosynthetic process; IGI:SGD.
DR GO; GO:0031578; P:mitotic spindle orientation checkpoint signaling; IGI:SGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:SGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:1904667; P:negative regulation of ubiquitin protein ligase activity; IPI: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 3D-structure; Acetylation; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298649"
FT CHAIN 2..267
FT /note="Protein BMH1"
FT /id="PRO_0000058715"
FT REGION 236..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 136
FT /note="NTH1 binding"
FT /evidence="ECO:0000269|PubMed:29087344,
FT ECO:0007744|PDB:5N6N"
FT SITE 185
FT /note="NTH1 binding"
FT /evidence="ECO:0000269|PubMed:29087344,
FT ECO:0007744|PDB:5N6N"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:9298649"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT CROSSLNK 76
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 197
FT /note="A -> R (in Ref. 1; CAA50656 and 2; CAA46959)"
FT /evidence="ECO:0000305"
FT CONFLICT 263..267
FT /note="GEAPK -> VKHQSKYSDKSKEKLLKKRKKKERGCNNL (in Ref. 1;
FT CAA50656)"
FT /evidence="ECO:0000305"
FT HELIX 6..18
FT /evidence="ECO:0007829|PDB:5N6N"
FT HELIX 21..33
FT /evidence="ECO:0007829|PDB:5N6N"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:5N6N"
FT HELIX 40..72
FT /evidence="ECO:0007829|PDB:5N6N"
FT HELIX 78..108
FT /evidence="ECO:0007829|PDB:5N6N"
FT HELIX 110..113
FT /evidence="ECO:0007829|PDB:5N6N"
FT HELIX 117..137
FT /evidence="ECO:0007829|PDB:5N6N"
FT HELIX 140..164
FT /evidence="ECO:0007829|PDB:5N6N"
FT HELIX 170..185
FT /evidence="ECO:0007829|PDB:5N6N"
FT HELIX 190..203
FT /evidence="ECO:0007829|PDB:5N6N"
FT TURN 204..207
FT /evidence="ECO:0007829|PDB:5N6N"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:5N6N"
FT HELIX 213..233
FT /evidence="ECO:0007829|PDB:5N6N"
SQ SEQUENCE 267 AA; 30091 MW; 0A234167E313688B CRC64;
MSTSREDSVY LAKLAEQAER YEEMVENMKT VASSGQELSV EERNLLSVAY KNVIGARRAS
WRIVSSIEQK EESKEKSEHQ VELICSYRSK IETELTKISD DILSVLDSHL IPSATTGESK
VFYYKMKGDY HRYLAEFSSG DAREKATNAS LEAYKTASEI ATTELPPTHP IRLGLALNFS
VFYYEIQNSP DKACHLAKQA FDDAIAELDT LSEESYKDST LIMQLLRDNL TLWTSDMSES
GQAEDQQQQQ QHQQQQPPAA AEGEAPK
