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P10869 (AK_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aspartokinase

EC=2.7.2.4
Alternative name(s):
Aspartate kinase
Gene names
Name:HOM3
Ordered Locus Names:YER052C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length527 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

Binary interactions

With

Entry

#Exp.

IntAct

Notes

FPR1P200815EBI-2430,EBI-6961

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 527527Aspartokinase
PRO_0000066690

Regions

Domain367 – 44074ACT 1
Domain442 – 52786ACT 2

Amino acid modifications

Modified residue3331Phosphothreonine Ref.6

Sequences

Sequence LengthMass (Da)Tools
P10869 [UniParc].

Last modified August 1, 1990. Version 2.
Checksum: D4D28FB8D4374898

FASTA52758,110
        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 

« Hide

References

« Hide 'large scale' references
[1]"Structure of the yeast HOM3 gene which encodes aspartokinase."
Rafalski J.A., Falco S.C.
J. Biol. Chem. 263:2146-2151(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Structure of the yeast HOM3 gene which encodes aspartokinase."
Rafalski J.A., Falco S.C.
J. Biol. Chem. 265:15346-15346(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome V."
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. expand/collapse author list , 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.
Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-333, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[7]"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
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.
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03526 Genomic DNA. Translation: AAA34681.1.
U18796 Genomic DNA. Translation: AAB64587.1.
BK006939 Genomic DNA. Translation: DAA07708.1.
PIRKIBYD. A35888.
RefSeqNP_010972.1. NM_001178943.1.

3D structure databases

ProteinModelPortalP10869.
SMRP10869. Positions 16-501.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36791. 157 interactions.
DIPDIP-1319N.
IntActP10869. 8 interactions.
MINTMINT-392511.
STRING4932.YER052C.

Proteomic databases

PaxDbP10869.
PeptideAtlasP10869.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYER052C; YER052C; YER052C.
GeneID856778.
KEGGsce:YER052C.

Organism-specific databases

CYGDYER052c.
SGDS000000854. HOM3.

Phylogenomic databases

eggNOGCOG0527.
HOGENOMHOG000293094.
KOK00928.
OMAGANIKMI.
OrthoDBEOG7NPG3J.

Enzyme and pathway databases

BioCycYEAST:YER052C-MONOMER.
BRENDA2.7.2.4. 984.
SABIO-RKP10869.
UniPathwayUPA00034; UER00015.
UPA00050; UER00461.
UPA00051; UER00462.

Gene expression databases

GenevestigatorP10869.

Family and domain databases

Gene3D3.40.1160.10. 2 hits.
InterProIPR002912. ACT_dom.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR001341. Asp_kinase_dom.
IPR018042. Aspartate_kinase_CS.
IPR027795. GATS-like_ACT_dom.
[Graphical view]
PfamPF00696. AA_kinase. 1 hit.
PF13840. ACT_7. 1 hit.
[Graphical view]
SUPFAMSSF53633. SSF53633. 1 hit.
TIGRFAMsTIGR00657. asp_kinases. 1 hit.
PROSITEPS51671. ACT. 1 hit.
PS00324. ASPARTOKINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio982982.
PROP10869.

Entry information

Entry nameAK_YEAST
AccessionPrimary (citable) accession number: P10869
Secondary accession number(s): D3DLV4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: August 1, 1990
Last modified: March 19, 2014
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome V

Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways