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UniProtKB/Swiss-Prot entry P10869


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

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Entry information
Entry name AK_YEAST
Primary accession number P10869
Secondary accession numbers None
Integrated into Swiss-Prot on July 1, 1989
Sequence was last modified on August 1, 1990 (Sequence version 2)
Annotations were last modified on    December 16, 2008 (Entry version 79)
Name and origin of the protein
Protein name Aspartokinase
Synonyms EC 2.7.2.4
Aspartate kinase
Gene name
Name: HOM3
OrderedLocusNames: YER052C
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].
PubMed=2892836 [NCBI, ExPASy, EBI, Israel, Japan]
Rafalski J.A., Falco S.C.;
"Structure of the yeast HOM3 gene which encodes aspartokinase.";
J. Biol. Chem. 263:2146-2151(1988).
[2]
SEQUENCE REVISION.
PubMed=2168408 [NCBI, ExPASy, EBI, Israel, Japan]
Rafalski J.A., Falco S.C.;
"Structure of the yeast HOM3 gene which encodes aspartokinase.";
J. Biol. Chem. 265:15346-15346(1990).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=9169868 [NCBI, ExPASy, EBI, Israel, Japan]
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
Nature 387:78-81(1997).
[4]
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).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-333, 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).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-333, 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).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-333 AND SER-441, 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
J03526; AAA34681.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U18796; AAB64587.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A35888; KIBYD.
RefSeq NP_010972.1; -.
3D structure databases
ModBase P10869.
Protein-protein interaction databases
DIP DIP:1319N; -.
IntAct P10869; 14.
Organism-specific databases
CYGD YER052c; -.
SGD S000000854; HOM3.
Yeast-GFP YER052C.
Gene expression databases
ArrayExpress P10869; -.
GermOnline YER052C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from SGD).
GO:0016597; Molecular function: amino acid binding (inferred from electronic annotation from InterPro).
GO:0004072; Molecular function: aspartate kinase activity (inferred from electronic annotation from InterPro).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006555; Biological process: methionine metabolic process (traceable author statement from SGD).
GO:0042493; Biological process: response to drug (inferred from mutant phenotype from SGD).
GO:0009088; Biological process: threonine biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR002912; ACT_bd.
IPR001048; Asp/Glu/Uridylate_kinase.
IPR001341; Asp_kin_reg.
Graphical view of domain structure.
Gene3D G3DSA:3.40.1160.10; Aa_kinase; 1.
Pfam PF00696; AA_kinase; 1.
PF01842; ACT; 2.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00657; asp_kinases; 1.
PROSITE PS00324; ASPARTOKINASE; 1.
Proteomic databases
PeptideAtlas P10869; -.
Proteomics databases
PRIDE P10869; -.
Genome annotation databases
Ensembl YER052C; Saccharomyces cerevisiae. [Contig view]
GeneID 856778; -.
GenomeReviews U00092_GR; YER052C.
KEGG sce:YER052C; -.
NMPDR fig|4932.3.peg.2035; -.
Phylogenomic databases
HOGENOM P10869; -.
Other
LinkHub P10869; -.
NextBio 982982; -.
ProtoNet P10869.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Complete proteome; Kinase; Phosphoprotein; Repeat; Threonine biosynthesis; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   527  527     Aspartokinase. PRO_0000066690
DOMAIN   363   433  71     ACT 1. 
DOMAIN   438   506  69     ACT 2. 
MOD_RES   333   333        Phosphothreonine. 
MOD_RES   441   441        Phosphoserine. 
Sequence information
Length: 527 AA [This is the length of the unprocessed precursor] Molecular weight: 58110 Da [This is the MW of the unprocessed precursor] CRC64: D4D28FB8D4374898 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPMDFQPTSS HSNWVVQKFG GTSVGKFPVQ IVDDIVKHYS KPDGPNNNVA VVCSARSSYT 

        70         80         90        100        110        120 
KAEGTTSRLL KCCDLASQES EFQDIIEVIR QDHIDNADRF ILNPALQAKL VDDTNKELEL 

       130        140        150        160        170        180 
VKKYLNASKV LGEVSSRTVD LVMSCGEKLS CLFMTALCND RGCKAKYVDL SHIVPSDFSA 

       190        200        210        220        230        240 
SALDNSFYTF LVQALKEKLA PFVSAKERIV PVFTGFFGLV PTGLLNGVGR GYTDLCAALI 

       250        260        270        280        290        300 
AVAVNADELQ VWKEVDGIFT ADPRKVPEAR LLDSVTPEEA SELTYYGSEV IHPFTMEQVI 

       310        320        330        340        350        360 
RAKIPIRIKN VQNPLGNGTI IYPDNVAKKG ESTPPHPPEN LSSSFYEKRK RGATAITTKN 

       370        380        390        400        410        420 
DIFVINIHSN KKTLSHGFLA QIFTILDKYK LVVDLISTSE VHVSMALPIP DADSLKSLRQ 

       430        440        450        460        470        480 
AEEKLRILGS VDITKKLSIV SLVGKHMKQY IGIAGTMFTT LAEEGINIEM ISQGANEINI 

       490        500        510        520 
SCVINESDSI KALQCIHAKL LSERTNTSNQ FEHAIDERLE QLKRLGI 

P10869 in FASTA format

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