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UniProtKB/Swiss-Prot entry P14540


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ALF_YEAST
Primary accession number P14540
Secondary accession numbers None
Integrated into Swiss-Prot on January 1, 1990
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    November 4, 2008 (Entry version 89)
Name and origin of the protein
Protein name Fructose-bisphosphate aldolase
Synonym EC 4.1.2.13
Gene name
Name: FBA1
OrderedLocusNames: YKL060C
ORFNames: YKL320
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1111/j.1432-1033.1989.tb14648.x; PubMed=2647491 [NCBI, ExPASy, EBI, Israel, Japan]
Schwelberger H.G., Kohlwein S.D., Paltauf F.;
"Molecular cloning, primary structure and disruption of the structural gene of aldolase from Saccharomyces cerevisiae.";
Eur. J. Biochem. 180:301-308(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1038/369371a0; PubMed=8196765 [NCBI, ExPASy, EBI, Israel, Japan]
Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.;
"Complete DNA sequence of yeast chromosome XI.";
Nature 369:371-378(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1002/yea.320100008; PubMed=8091862 [NCBI, ExPASy, EBI, Israel, Japan]
Rasmussen S.W.;
"Sequence of a 28.6 kb region of yeast chromosome XI includes the FBA1 and TOA2 genes, an open reading frame (ORF) similar to a translationally controlled tumour protein, one ORF containing motifs also found in plant storage proteins and 13 ORFs with weak or no homology to known proteins.";
Yeast 10:S63-S68(1994).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-96.
DOI=10.1016/0378-1119(90)90159-O; PubMed=1698168 [NCBI, ExPASy, EBI, Israel, Japan]
Gatignol A., Dassain M., Tiraby G.;
"Cloning of Saccharomyces cerevisiae promoters using a probe vector based on phleomycin resistance.";
Gene 91:35-41(1990).
[5]
PRELIMINARY PROTEIN SEQUENCE OF 2-40.
Jack R.S.;
Thesis (1973), University of Cambridge, United Kingdom.
[6]
PROTEIN SEQUENCE OF 333-339.
STRAIN=ATCC 204508 / S288c;
DOI=10.1002/elps.11501501210; PubMed=7895733 [NCBI, ExPASy, EBI, Israel, Japan]
Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B., Volpe T., Warner J.R., McLaughlin C.S.;
"Protein identifications for a Saccharomyces cerevisiae protein database.";
Electrophoresis 15:1466-1486(1994).
[7]
PROTEIN SEQUENCE OF 2-21.
STRAIN=ATCC 38531 / Y41;
DOI=10.1016/0378-1097(96)00006-7; PubMed=8935650 [NCBI, ExPASy, EBI, Israel, Japan]
Norbeck J., Blomberg A.;
"Protein expression during exponential growth in 0.7 M NaCl medium of Saccharomyces cerevisiae.";
FEMS Microbiol. Lett. 137:1-8(1996).
[8]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-11; THR-150; TYR-310 AND SER-313, AND MASS SPECTROMETRY.
DOI=10.1021/pr060559j; PubMed=17330950 [NCBI, ExPASy, EBI, Israel, Japan]
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-11; THR-24; SER-147; THR-179; SER-268; SER-270; THR-271 AND THR-277, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0607084104; PubMed=17287358 [NCBI, ExPASy, EBI, Israel, Japan]
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56 AND SER-313, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0701622104; PubMed=17563356 [NCBI, ExPASy, EBI, Israel, Japan]
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases.";
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40; SER-41; SER-42; THR-43; SER-54; SER-56; THR-62; SER-63; SER-76; SER-96; SER-147; THR-150; SER-156; THR-157; SER-214; SER-268; THR-290; TYR-294 AND SER-313, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X15003; CAA33111.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z28060; CAA81897.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X75781; CAA53412.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M32026; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
PIR S07855; ADBY2.
RefSeq NP_012863.1; -.
3D structure databases
HSSP P11604; 1GYN. [HSSP ENTRY / PDB]
ModBase P14540.
Protein-protein interaction databases
DIP DIP:4702N; -.
IntAct P14540; -.
2D gel databases
SWISS-2DPAGE P14540; -.
COMPLUYEAST-2DPAGE P14540; -.
Organism-specific databases
CYGD YKL060c; -.
SGD S000001543; FBA1.
Yeast-GFP YKL060C.
Gene expression databases
GermOnline YKL060C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from SGD).
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from SGD).
GO:0004332; Molecular function: fructose-bisphosphate aldolase activity (inferred from direct assay from SGD).
GO:0006094; Biological process: gluconeogenesis (inferred from mutant phenotype from SGD).
GO:0006096; Biological process: glycolysis (inferred from mutant phenotype from SGD).
QuickGo view.
Family and domain databases
InterPro IPR013785; Aldolase_TIM.
IPR006411; Fruct_bisP_bact.
IPR000771; K_bP_aldolase.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.70; Aldolase_TIM; 1.
Pfam PF01116; F_bP_aldolase; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001359; F_bP_aldolase_II; 1.
ProDom PD002376; K_bP_aldolase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR00167; cbbA; 1.
TIGR01520; FruBisAldo_II_A; 1.
PROSITE PS00602; ALDOLASE_CLASS_II_1; 1.
PS00806; ALDOLASE_CLASS_II_2; 1.
BLOCKS P14540.
ProtoNet P14540.
Proteomic databases
PeptideAtlas P14540; -.
Genome annotation databases
Ensembl YKL060C; Saccharomyces cerevisiae. [Contig view]
GeneID 853805; -.
GenomeReviews Y13137_GR; YKL060C.
KEGG sce:YKL060C; -.
NMPDR fig|4932.3.peg.3848; -.
Phylogenomic databases
HOGENOM P14540; -.
Other
LinkHub P14540; -.
NextBio 974960; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Direct protein sequencing; Glycolysis; Lyase; Metal-binding; Phosphoprotein; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   359  358     Fructose-bisphosphate aldolase. PRO_0000178762
METAL   108   108        Zinc (By similarity). 
METAL   111   111        Zinc (By similarity). 
MOD_RES   11    11        Phosphothreonine. 
MOD_RES   24    24        Phosphothreonine. 
MOD_RES   40    40        Phosphoserine. 
MOD_RES   41    41        Phosphoserine. 
MOD_RES   42    42        Phosphoserine. 
MOD_RES   43    43        Phosphothreonine. 
MOD_RES   54    54        Phosphoserine. 
MOD_RES   56    56        Phosphoserine. 
MOD_RES   62    62        Phosphothreonine. 
MOD_RES   63    63        Phosphoserine. 
MOD_RES   76    76        Phosphoserine. 
MOD_RES   96    96        Phosphoserine. 
MOD_RES   147   147        Phosphoserine. 
MOD_RES   150   150        Phosphothreonine. 
MOD_RES   156   156        Phosphoserine. 
MOD_RES   157   157        Phosphothreonine. 
MOD_RES   179   179        Phosphothreonine. 
MOD_RES   214   214        Phosphoserine. 
MOD_RES   268   268        Phosphoserine. 
MOD_RES   270   270        Phosphoserine. 
MOD_RES   271   271        Phosphothreonine. 
MOD_RES   277   277        Phosphothreonine. 
MOD_RES   290   290        Phosphothreonine. 
MOD_RES   294   294        Phosphotyrosine. 
MOD_RES   310   310        Phosphotyrosine. 
MOD_RES   313   313        Phosphoserine. 
Sequence information
Length: 359 AA [This is the length of the unprocessed precursor] Molecular weight: 39621 Da [This is the MW of the unprocessed precursor] CRC64: C67E61BA5C7E8E4C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGVEQILKRK TGVIVGEDVH NLFTYAKEHK FAIPAINVTS SSTAVAALEA ARDSKSPIIL 

        70         80         90        100        110        120 
QTSNGGAAYF AGKGISNEGQ NASIKGAIAA AHYIRSIAPA YGIPVVLHSD HCAKKLLPWF 

       130        140        150        160        170        180 
DGMLEADEAY FKEHGEPLFS SHMLDLSEET DEENISTCVK YFKRMAAMDQ WLEMEIGITG 

       190        200        210        220        230        240 
GEEDGVNNEN ADKEDLYTKP EQVYNVYKAL HPISPNFSIA AAFGNCHGLY AGDIALRPEI 

       250        260        270        280        290        300 
LAEHQKYTRE QVGCKEEKPL FLVFHGGSGS TVQEFHTGID NGVVKVNLDT DCQYAYLTGI 

       310        320        330        340        350 
RDYVLNKKDY IMSPVGNPEG PEKPNKKFFD PRVWVREGEK TMGAKITKSL ETFRTTNTL 

P14540 in FASTA format

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