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Protein BMH2

 BMH2_YEAST              Reviewed;         273 AA.
P34730; A2TBP2; D6VS86; Q06HN5;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
13-FEB-2019, entry version 178.
RecName: Full=Protein BMH2;
Name=BMH2; OrderedLocusNames=YDR099W; ORFNames=YD8557.08;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7744048; DOI=10.1111/j.1432-1033.1995.0045l.x;
van Heusden G.P.H., Griffith D.J.F., Ford J.C., Chin-A-Woeng T.F.C.,
Schrader P.A.T., Carr A.M., Steensma H.Y.;
"The 14-3-3 proteins encoded by the BMH1 and BMH2 genes are essential
in the yeast Saccharomyces cerevisiae and can be replaced by a plant
homologue.";
Eur. J. Biochem. 229:45-53(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8524799; DOI=10.1073/pnas.92.25.11539;
Gelperin D., Weigle J., Nelson K.K., Roseboom P., Irie K.,
Matsumoto K., Lemmon S.K.;
"14-3-3 proteins: potential roles in vesicular transport and Ras
signaling in Saccharomyces cerevisiae.";
Proc. Natl. Acad. Sci. U.S.A. 92:11539-11543(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867;
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-143.
STRAIN=ATCC 201390 / BY4743;
PubMed=17351133; DOI=10.1101/gr.6049107;
Zhang Z., Hesselberth J.R., Fields S.;
"Genome-wide identification of spliced introns using a tiling
microarray.";
Genome Res. 17:503-509(2007).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-116.
STRAIN=ATCC 201390 / BY4743;
PubMed=17244705; DOI=10.1073/pnas.0610354104;
Juneau K., Palm C., Miranda M., Davis R.W.;
"High-density yeast-tiling array reveals previously undiscovered
introns and extensive regulation of meiotic splicing.";
Proc. Natl. Acad. Sci. U.S.A. 104:1522-1527(2007).
[7]
ACETYLATION AT SER-2.
PubMed=9298649; DOI=10.1002/elps.1150180810;
Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I.,
Kobayashi R., Schwender B., Volpe T., Anderson D.S.,
Mesquita-Fuentes R., Payne W.E.;
"Proteome studies of Saccharomyces cerevisiae: identification and
characterization of abundant proteins.";
Electrophoresis 18:1347-1360(1997).
[8]
INTERACTION WITH FIN1.
PubMed=12551942; DOI=10.1074/jbc.M212495200;
van Hemert M.J., Deelder A.M., Molenaar C., Steensma H.Y.,
van Heusden G.P.H.;
"Self-association of the spindle pole body-related intermediate
filament protein Fin1p and its phosphorylation-dependent interaction
with 14-3-3 proteins in yeast.";
J. Biol. Chem. 278:15049-15055(2003).
[9]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[10]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
-!- SUBUNIT: Interacts with FIN1. {ECO:0000269|PubMed:12551942}.
-!- INTERACTION:
P32356:NTH1; NbExp=8; IntAct=EBI-3672, EBI-19509;
P22216:RAD53; NbExp=2; IntAct=EBI-3672, EBI-17843;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
Nucleus {ECO:0000269|PubMed:14562095}.
-!- MISCELLANEOUS: Present with 47600 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
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EMBL; X84817; CAA59275.1; -; Genomic_DNA.
EMBL; U01883; AAA03336.1; -; Unassigned_DNA.
EMBL; Z47746; CAA87675.1; -; Genomic_DNA.
EMBL; DQ881448; ABI95875.1; -; mRNA.
EMBL; EF123145; ABM97489.1; -; mRNA.
EMBL; BK006938; DAA11946.1; -; Genomic_DNA.
PIR; S51250; S51250.
RefSeq; NP_010384.3; NM_001180407.3.
ProteinModelPortal; P34730; -.
SMR; P34730; -.
BioGrid; 32157; 251.
DIP; DIP-1212N; -.
IntAct; P34730; 83.
MINT; P34730; -.
STRING; 4932.YDR099W; -.
iPTMnet; P34730; -.
SWISS-2DPAGE; P34730; -.
MaxQB; P34730; -.
PaxDb; P34730; -.
PRIDE; P34730; -.
TopDownProteomics; P34730; -.
EnsemblFungi; YDR099W_mRNA; YDR099W_mRNA; YDR099W.
GeneID; 851676; -.
KEGG; sce:YDR099W; -.
EuPathDB; FungiDB:YDR099W; -.
SGD; S000002506; BMH2.
GeneTree; ENSGT00940000153953; -.
HOGENOM; HOG000240379; -.
InParanoid; P34730; -.
KO; K06630; -.
OMA; MKEHEKG; -.
BioCyc; YEAST:G3O-29702-MONOMER; -.
Reactome; R-SCE-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
Reactome; R-SCE-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-SCE-3371511; HSF1 activation.
Reactome; R-SCE-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
Reactome; R-SCE-5625740; RHO GTPases activate PKNs.
Reactome; R-SCE-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
Reactome; R-SCE-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
Reactome; R-SCE-9614399; Regulation of localization of FOXO transcription factors.
PRO; PR:P34730; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0005886; C:plasma membrane; HDA:SGD.
GO; GO:0003688; F:DNA replication origin binding; IDA:SGD.
GO; GO:0050815; F:phosphoserine residue binding; IMP:SGD.
GO; GO:0019904; F:protein domain specific binding; IEA:InterPro.
GO; GO:0030437; P:ascospore formation; IGI:SGD.
GO; GO:0000077; P:DNA damage checkpoint; IMP:SGD.
GO; GO:0006270; P:DNA replication initiation; IGI:SGD.
GO; GO:0034221; P:fungal-type cell wall chitin biosynthetic process; IGI:SGD.
GO; GO:0005977; P:glycogen metabolic process; IGI:SGD.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:SGD.
GO; GO:1904667; P:negative regulation of ubiquitin protein ligase activity; IPI:SGD.
GO; GO:0006267; P:pre-replicative complex assembly involved in nuclear cell cycle DNA replication; IGI:SGD.
GO; GO:0007124; P:pseudohyphal growth; IGI:SGD.
GO; GO:0007265; P:Ras protein signal transduction; IGI:SGD.
GO; GO:0001402; P:signal transduction involved in filamentous growth; IGI:SGD.
Gene3D; 1.20.190.20; -; 1.
InterPro; IPR000308; 14-3-3.
InterPro; IPR023409; 14-3-3_CS.
InterPro; IPR036815; 14-3-3_dom_sf.
InterPro; IPR023410; 14-3-3_domain.
PANTHER; PTHR18860; PTHR18860; 1.
Pfam; PF00244; 14-3-3; 1.
PIRSF; PIRSF000868; 14-3-3; 1.
PRINTS; PR00305; 1433ZETA.
SMART; SM00101; 14_3_3; 1.
SUPFAM; SSF48445; SSF48445; 1.
PROSITE; PS00796; 1433_1; 1.
PROSITE; PS00797; 1433_2; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Cytoplasm; Nucleus;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:9298649}.
CHAIN 2 273 Protein BMH2.
/FTId=PRO_0000058716.
COMPBIAS 245 261 Poly-Gln.
MOD_RES 2 2 N-acetylserine.
{ECO:0000269|PubMed:9298649}.
CONFLICT 119 119 S -> C (in Ref. 1; CAA59275).
{ECO:0000305}.
CONFLICT 174 174 G -> F (in Ref. 1; CAA59275).
{ECO:0000305}.
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


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Pathways :
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair
WP1673: Naphthalene and anthracene degradation
WP1675: Nitrogen metabolism
WP1676: Non-homologous end-joining
WP1678: Nucleotide excision repair

Related Genes :
[BMH2 YDR099W YD8557.08] Protein BMH2
[FIN1 YDR130C YD9302.05C] Filament protein FIN1 (Filaments in between nuclei protein 1)
[COI] Cytochrome c oxidase subunit 1 (EC 1.9.3.1) (Fragment)
[STE20 YHL007C] Serine/threonine-protein kinase STE20 (EC 2.7.11.1)
[RAD53 MEC2 SAD1 SPK1 YPL153C P2588] Serine/threonine-protein kinase RAD53 (EC 2.7.12.1) (CHEK2 homolog) (Serine-protein kinase 1)
[NTH1 NTH YDR001C YD8119.07C] Neutral trehalase (EC 3.2.1.28) (Alpha,alpha-trehalase) (Alpha,alpha-trehalose glucohydrolase)
[cytb] Cytochrome b (Fragment)
[] Cytochrome c oxidase subunit 1 (EC 1.9.3.1) (Fragment)
[ACM1 YPL267W] APC/C-CDH1 modulator 1
[YDR099W SKUD_180104] BMH2-like protein
[DI49_0295] BMH2-like protein
[KO01_00905] BMH2p 14-3-3 protein, minor isoform
[BMH2 AWJ20_738] 14-3-3 family protein BMH2
[BMH2 AWJ20_4346] 14-3-3 family protein BMH2
[BMH2 KLMA_20132] Protein BMH2
[K7_BMH2 SYK7_012581] K7_Bmh2p
[BMH2 C1Q_02600] Bmh2p
[ODF3B ODF3L3] Outer dense fiber protein 3B (Outer dense fiber protein 3-like protein 3)
[] Long wavelength rhodopsin (Fragment)
[BMH2 MSY001_0438 MSYG_2252] 14-3-3 protein, minor isoform
[BMH2 SCY_1001] 14-3-3 protein
[ZPAR0C06710_A BZL39_C06710] BMH2 (YDR099W) and BMH1 (YER177W)
[ZPAR0L03350_B BZL39_L03350] BMH2 (YDR099W) and BMH1 (YER177W)
[PGUG_04326] Protein BMH2
[LELG_01535] Protein BMH2
[CTRG_04785] Protein BMH2
[SPAPADRAFT_58080] Protein BMH2
[BMH2 TRFO_01329] Protein BMH2
[BMH2 Hypma_010234] Protein BMH2
[CNAG_05235] Protein BMH2

Bibliography :
[30373304] Efficient Heterologous Production of Lipase via Optimization of Multiple Expression-Related Helper Proteins.
[29556216] Arbuscular Mycorrhizal Fungal 14-3-3 Proteins Are Involved in Arbuscule Formation and Responses to Abiotic Stresses During AM Symbiosis.
[29391437] Differential abundance and transcription of 14-3-3 proteins during vegetative growth and sexual reproduction in budding yeast.
[28877665] Lack of 14-3-3 proteins in Saccharomyces cerevisiae results in cell-to-cell heterogeneity in the expression of Pho4-regulated genes SPL2 and PHO84.
[28468835] Multilevel regulation of an α-arrestin by glucose depletion controls hexose transporter endocytosis.
[27827352] Crystal structures of a yeast 14-3-3 protein from Lachancea thermotolerans in the unliganded form and bound to a human lipid kinase PI4KB-derived peptide reveal high evolutionary conservation.
[27558777] Quantitative proteomic comparison of stationary/G0 phase cells and tetrads in budding yeast.
[27261460] Regulation of the Yeast Hxt6 Hexose Transporter by the Rod1 α-Arrestin, the Snf1 Protein Kinase, and the Bmh2 14-3-3 Protein.
[26843527] The Rtr1p CTD phosphatase autoregulates its mRNA through a degradation pathway involving the REX exonucleases.
[26537993] Functional analysis of Paracoccidioides brasiliensis 14-3-3 adhesin expressed in Saccharomyces cerevisiae.
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