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UniProtKB/Swiss-Prot entry P04802


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

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Entry information
Entry name SYDC_YEAST
Primary accession number P04802
Secondary accession numbers None
Integrated into Swiss-Prot on August 13, 1987
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    November 4, 2008 (Entry version 106)
Name and origin of the protein
Protein name Aspartyl-tRNA synthetase, cytoplasmic
Synonyms EC 6.1.1.12
Aspartate--tRNA ligase
AspRS
Gene name
Name: DPS1
Synonyms: APS, APS1
OrderedLocusNames: YLL018C
ORFNames: L1295
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].
STRAIN=ATCC 204508 / S288c;
DOI=10.1093/nar/16.3.1212; PubMed=3278298 [NCBI, ExPASy, EBI, Israel, Japan]
Reid G.A.;
"Sequence polymorphisms in the yeast gene encoding aspartyl tRNA synthase.";
Nucleic Acids Res. 16:1212-1212(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1093/nar/14.4.1657; PubMed=3513127 [NCBI, ExPASy, EBI, Israel, Japan]
Sellami M., Fasiolo F., Dirheimer G., Ebel J.-P., Gangloff J.;
"Nucleotide sequence of the gene coding for yeast cytoplasmic aspartyl-tRNA synthetase (APS); mapping of the 5' and 3' termini of AspRS mRNA.";
Nucleic Acids Res. 14:1657-1666(1986).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1002/(SICI)1097-0061(199702)13:2<183::AID-YEA65>3.3.CO;2-M; PubMed=9046100 [NCBI, ExPASy, EBI, Israel, Japan]
Purnelle B., Goffeau A.;
"The sequence of 32kb on the left arm of yeast chromosome XII reveals six known genes, a new member of the seripauperins family and a new ABC transporter homologous to the human multidrug resistance protein.";
Yeast 13:183-188(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=9169871 [NCBI, ExPASy, EBI, Israel, Japan]
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
Nature 387:87-90(1997).
[5]
PROTEIN SEQUENCE OF 2-557.
DOI=10.1016/S0300-9084(85)80200-5; PubMed=3902099 [NCBI, ExPASy, EBI, Israel, Japan]
Amiri I., Mejdoub H., Hounwanou N., Boulanger Y., Reinbolt J.;
"The complete amino acid sequence of cytoplasmic aspartyl-tRNA synthetase from Saccharomyces cerevisiae.";
Biochimie 67:607-613(1985).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-81.
STRAIN=ATCC 90840 / EAY235 / FY23;
DOI=10.1002/(SICI)1097-0061(19960615)12:7<693::AID-YEA956>3.3.CO;2-7; PubMed=8810043 [NCBI, ExPASy, EBI, Israel, Japan]
Miosga T., Zimmermann F.K.;
"Sequence analysis of the CEN12 region of Saccharomyces cerevisiae on a 43.7 kb fragment of chromosome XII including an open reading frame homologous to the human cystic fibrosis transmembrane conductance regulator protein CFTR.";
Yeast 12:693-708(1996).
[7]
PARTIAL PROTEIN SEQUENCE, AND MUTAGENESIS.
DOI=10.1021/bi00231a026; PubMed=2021621 [NCBI, ExPASy, EBI, Israel, Japan]
Gasparini S., Vincendon P., Eriani G., Gangloff J., Boulanger Y., Reinbolt J., Kern D.;
"Identification of structurally and functionally important histidine residues in cytoplasmic aspartyl-tRNA synthetase from Saccharomyces cerevisiae.";
Biochemistry 30:4284-4289(1991).
[8]
MUTAGENESIS OF PRO-273.
PubMed=8248175 [NCBI, ExPASy, EBI, Israel, Japan]
Eriani G., Cavarelli J., Martin F., Dirheimer G., Moras D., Gangloff J.;
"Role of dimerization in yeast aspartyl-tRNA synthetase and importance of the class II invariant proline.";
Proc. Natl. Acad. Sci. U.S.A. 90:10816-10820(1993).
[9]
ACETYLATION AT SER-2.
DOI=10.1002/elps.1150180810; PubMed=9298649 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[10]
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).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M400219-MCP200; PubMed=15665377 [NCBI, ExPASy, EBI, Israel, Japan]
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.;
"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway.";
Mol. Cell. Proteomics 4:310-327(2005).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301, 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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-546, 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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, 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).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; THR-243; SER-301; SER-502 AND SER-546, 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).
[16]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
PubMed=2047877 [NCBI, ExPASy, EBI, Israel, Japan]
Ruff M., Krishnaswamy S., Boeglin M., Poterszman A., Mitschler A., Podjarny A., Rees B., Thierry J.-C., Moras D.;
"Class II aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA(Asp).";
Science 252:1682-1689(1991).
[17]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), AND MUTAGENESIS.
PubMed=8313877 [NCBI, ExPASy, EBI, Israel, Japan]
Cavarelli J., Eriani G., Rees B., Ruff M., Boeglin M., Mitschler A., Martin F., Gangloff J., Thierry J.-C., Moras D.;
"The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation reaction.";
EMBO J. 13:327-337(1994).
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
X03606; CAA27269.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X06665; CAA29865.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X97560; CAA66172.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z73123; CAA97464.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z73122; CAA97463.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X91488; CAA62772.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A23508; SYBYDC.
RefSeq NP_013083.1; -.
3D structure databases
PDB
1ASY; X-ray; 2.90 A; A/B=68-557.[ExPASy / RCSB / EBI]
1ASZ; X-ray; 3.00 A; A/B=68-557.[ExPASy / RCSB / EBI]
1EOV; X-ray; 2.30 A; A=71-557.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1ASY; -.
1ASZ; -.
1EOV; -.
ModBase P04802.
Protein-protein interaction databases
DIP DIP:4093N; -.
IntAct P04802; -.
Organism-specific databases
CYGD YLL018c; -.
SGD S000003941; DPS1.
Yeast-GFP YLL018C.
Gene expression databases
ArrayExpress P04802; -.
GermOnline YLL018C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0004815; Molecular function: aspartate-tRNA ligase activity (inferred from direct assay from SGD).
GO:0042802; Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0003723; Molecular function: RNA binding (inferred from direct assay from SGD).
QuickGo view.
Family and domain databases
InterPro IPR004364; aa-tRNA-synt_II.
IPR006195; aa-tRNA-synth_II.
IPR002312; Asp-tRNA-synth_IIb.
IPR004523; Asp-tRNA-synth_IIb_arc/euk.
IPR012340; NA-bd_OB-fold.
IPR004365; NA_bd_OB_tRNA-helicase.
Graphical view of domain structure.
Gene3D G3DSA:2.40.50.140; OB_NA_bd_sub; 1.
PANTHER PTHR22594; aa-tRNA-synt_II; 1.
Pfam PF00152; tRNA-synt_2; 1.
PF01336; tRNA_anti; 1.
Pfam graphical view of domain structure.
PRINTS PR01042; TRNASYNTHASP.
TIGRFAMs TIGR00458; aspS_arch; 1.
PROSITE PS50862; AA_TRNA_LIGASE_II; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P04802.
ProtoNet P04802.
Genome annotation databases
Ensembl YLL018C; Saccharomyces cerevisiae. [Contig view]
GeneID 850643; -.
GenomeReviews Y13138_GR; YLL018C.
KEGG sce:YLL018C; -.
NMPDR fig|4932.3.peg.4075; -.
Phylogenomic databases
HOGENOM P04802; -.
Other
LinkHub P04802; -.
NextBio 966579; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Ligase; Nucleotide-binding; Phosphoprotein; Protein biosynthesis.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   557  556     Aspartyl-tRNA synthetase, cytoplasmic. PRO_0000111014
MOD_RES   2     2        N-acetylserine. 
MOD_RES   14    14        Phosphoserine. 
MOD_RES   243   243        Phosphothreonine. 
MOD_RES   301   301        Phosphoserine. 
MOD_RES   502   502        Phosphoserine. 
MOD_RES   546   546        Phosphoserine. 
MUTAGEN   273   273        P->G: Loss of activity; important for dimerization. 
STRAND   73    77  5      
HELIX   85    87  3      
HELIX   96    98  3      
TURN   101   106  6      
STRAND   108   120  13      
STRAND   122   132  11      
STRAND   135   142  8      
STRAND   145   149  5      
HELIX   151   157  7      
STRAND   165   174  10      
STRAND   182   198  17      
HELIX   208   211  4      
HELIX   215   220  6      
HELIX   228   233  6      
HELIX   235   238  4      
HELIX   242   264  23      
STRAND   274   278  5      
STRAND   280   284  5      
STRAND   288   291  4      
STRAND   294   298  5      
HELIX   303   311  9      
STRAND   316   324  9      
STRAND   336   346  11      
HELIX   352   372  21      
HELIX   374   383  10      
STRAND   398   401  4      
HELIX   402   411  10      
HELIX   424   437  14      
STRAND   441   446  6      
HELIX   450   452  3      
STRAND   466   474  9      
STRAND   477   485  9      
HELIX   489   498  10      
TURN   506   508  3      
HELIX   509   515  7      
STRAND   522   528  7      
HELIX   529   536  8      
HELIX   542   545  4      
Sequence information
Length: 557 AA [This is the length of the unprocessed precursor] Molecular weight: 63516 Da [This is the MW of the unprocessed precursor] CRC64: 6656279B3E9011A5 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSQDENIVKA VEESAEPAQV ILGEDGKPLS KKALKKLQKE QEKQRKKEER ALQLEAEREA 

        70         80         90        100        110        120 
REKKAAAEDT AKDNYGKLPL IQSRDSDRTG QKRVKFVDLD EAKDSDKEVL FRARVHNTRQ 

       130        140        150        160        170        180 
QGATLAFLTL RQQASLIQGL VKANKEGTIS KNMVKWAGSL NLESIVLVRG IVKKVDEPIK 

       190        200        210        220        230        240 
SATVQNLEIH ITKIYTISET PEALPILLED ASRSEAEAEA AGLPVVNLDT RLDYRVIDLR 

       250        260        270        280        290        300 
TVTNQAIFRI QAGVCELFRE YLATKKFTEV HTPKLLGAPS EGGSSVFEVT YFKGKAYLAQ 

       310        320        330        340        350        360 
SPQFNKQQLI VADFERVYEI GPVFRAENSN THRHMTEFTG LDMEMAFEEH YHEVLDTLSE 

       370        380        390        400        410        420 
LFVFIFSELP KRFAHEIELV RKQYPVEEFK LPKDGKMVRL TYKEGIEMLR AAGKEIGDFE 

       430        440        450        460        470        480 
DLSTENEKFL GKLVRDKYDT DFYILDKFPL EIRPFYTMPD PANPKYSNSY DFFMRGEEIL 

       490        500        510        520        530        540 
SGAQRIHDHA LLQERMKAHG LSPEDPGLKD YCDGFSYGCP PHAGGGIGLE RVVMFYLDLK 

       550 
NIRRASLFPR DPKRLRP 

P04802 in FASTA format

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