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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.
28-MAR-2018, entry version 170.
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:
P48361:ASK10; NbExp=3; IntAct=EBI-3672, EBI-2993;
Q12527:ATG11; NbExp=2; IntAct=EBI-3672, EBI-31977;
P29311:BMH1; NbExp=8; IntAct=EBI-3672, EBI-3661;
Q05050:EIS1; NbExp=3; IntAct=EBI-3672, EBI-28061;
Q03898:FIN1; NbExp=4; IntAct=EBI-3672, EBI-32941;
P53739:FPK1; NbExp=5; IntAct=EBI-3672, EBI-9813;
P32598:GLC7; NbExp=5; IntAct=EBI-3672, EBI-13715;
Q12494:KCS1; NbExp=4; IntAct=EBI-3672, EBI-37528;
P32356:NTH1; NbExp=15; IntAct=EBI-3672, EBI-19509;
P39104:PIK1; NbExp=4; IntAct=EBI-3672, EBI-13423;
P40494:PRK1; NbExp=2; IntAct=EBI-3672, EBI-9703;
P22216:RAD53; NbExp=2; IntAct=EBI-3672, EBI-17843;
Q00816:REG1; NbExp=2; IntAct=EBI-3672, EBI-8270;
P32608:RTG2; NbExp=4; IntAct=EBI-3672, EBI-16322;
P50278:SOL1; NbExp=2; IntAct=EBI-3672, EBI-17675;
Q03497:STE20; NbExp=2; IntAct=EBI-3672, EBI-18285;
P53719:YNR014W; NbExp=2; IntAct=EBI-3672, EBI-28456;
-!- 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}.
-----------------------------------------------------------------------
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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; 244.
DIP; DIP-1212N; -.
IntAct; P34730; 115.
MINT; P34730; -.
STRING; 4932.YDR099W; -.
iPTMnet; P34730; -.
SWISS-2DPAGE; P34730; -.
MaxQB; P34730; -.
PaxDb; P34730; -.
PRIDE; P34730; -.
TopDownProteomics; P34730; -.
EnsemblFungi; YDR099W; YDR099W; YDR099W.
GeneID; 851676; -.
KEGG; sce:YDR099W; -.
EuPathDB; FungiDB:YDR099W; -.
SGD; S000002506; BMH2.
GeneTree; ENSGT00760000119116; -.
HOGENOM; HOG000240379; -.
InParanoid; P34730; -.
KO; K06630; -.
OMA; IPCATTG; -.
OrthoDB; EOG092C46UY; -.
BioCyc; YEAST:G3O-29702-MONOMER; -.
Reactome; R-SCE-1445148; Translocation of 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.
PRO; PR:P34730; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0005634; C:nucleus; IDA: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:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; 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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