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P48570 (HOSC_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 123. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Homocitrate synthase, cytosolic isozyme

EC=2.3.3.14
Gene names
Name:LYS20
Ordered Locus Names:YDL182W
ORF Names:D1298
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length428 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Acetyl-CoA + H2O + 2-oxoglutarate = (R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA.

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-alpha-aminoadipate from 2-oxoglutarate: step 1/5.

Subcellular location

Cytoplasm.

Miscellaneous

Present with 28100 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the alpha-IPM synthase/homocitrate synthase family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Lysine biosynthesis
   Cellular componentCytoplasm
   Molecular functionTransferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processlysine biosynthetic process via aminoadipic acid

Inferred from genetic interaction PubMed 18524920. Source: SGD

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay PubMed 9099739. Source: SGD

   Molecular_functionhomocitrate synthase activity

Inferred from direct assay PubMed 14984204. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 428428Homocitrate synthase, cytosolic isozyme
PRO_0000140454

Amino acid modifications

Modified residue3851Phosphoserine Ref.9
Modified residue3961Phosphothreonine Ref.6 Ref.9
Modified residue4011Phosphoserine Ref.7
Modified residue4101Phosphoserine Ref.9

Sequences

Sequence LengthMass (Da)Tools
P48570 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 8774FF56FA678E5E

FASTA42847,099
        10         20         30         40         50         60 
MTAAKPNPYA AKPGDYLSNV NNFQLIDSTL REGEQFANAF FDTEKKIEIA RALDDFGVDY 

        70         80         90        100        110        120 
IELTSPVASE QSRKDCEAIC KLGLKAKILT HIRCHMDDAK VAVETGVDGV DVVIGTSKFL 

       130        140        150        160        170        180 
RQYSHGKDMN YIAKSAVEVI EFVKSKGIEI RFSSEDSFRS DLVDLLNIYK TVDKIGVNRV 

       190        200        210        220        230        240 
GIADTVGCAN PRQVYELIRT LKSVVSCDIE CHFHNDTGCA IANAYTALEG GARLIDVSVL 

       250        260        270        280        290        300 
GIGERNGITP LGGLMARMIV AAPDYVKSKY KLHKIRDIEN LVADAVEVNI PFNNPITGFC 

       310        320        330        340        350        360 
AFTHKAGIHA KAILANPSTY EILDPHDFGM KRYIHFANRL TGWNAIKARV DQLNLNLTDD 

       370        380        390        400        410        420 
QIKEVTAKIK KLGDVRSLNI DDVDSIIKNF HAEVSTPQVL SAKKNKKNDS DVPELATIPA 


AKRTKPSA 

« Hide

References

« Hide 'large scale' references
[1]"New open reading frames, one of which is similar to the nifV gene of Azotobacter vinelandii, found on a 12.5 kbp fragment of chromosome IV of Saccharomyces cerevisiae."
Verhasselt P., Voet M., Volckaert G.
Yeast 11:961-966(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
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. expand/collapse author list , 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.
Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
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.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Identification of a gene encoding a homocitrate synthase isoenzyme of Saccharomyces cerevisiae."
Ramos F., Verhasselt P., Feller A., Peeters P., Wach A., Dubois E., Volckaert G.
Yeast 12:1315-1320(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[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-396, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385; THR-396 AND SER-410, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X83276 Genomic DNA. Translation: CAA58264.1.
Z67750 Genomic DNA. Translation: CAA91564.1.
Z74230 Genomic DNA. Translation: CAA98757.1.
Z74229 Genomic DNA. Translation: CAA98756.1.
BK006938 Genomic DNA. Translation: DAA11680.1.
PIRS58735.
RefSeqNP_010099.1. NM_001180242.1.

3D structure databases

ProteinModelPortalP48570.
SMRP48570. Positions 5-392.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31862. 90 interactions.
IntActP48570. 4 interactions.
MINTMINT-2780078.
STRING4932.YDL182W.

Proteomic databases

MaxQBP48570.
PeptideAtlasP48570.
PRIDEP48570.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDL182W; YDL182W; YDL182W.
GeneID851346.
KEGGsce:YDL182W.

Organism-specific databases

CYGDYDL182w.
SGDS000002341. LYS20.

Phylogenomic databases

GeneTreeENSGT00390000006101.
HOGENOMHOG000046858.
KOK01655.
OMAPICIHCH.
OrthoDBEOG76HQ9T.

Enzyme and pathway databases

BioCycYEAST:YDL182W-MONOMER.
SABIO-RKP48570.
UniPathwayUPA00033; UER00028.

Gene expression databases

GenevestigatorP48570.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR002034. AIPM/Hcit_synth_CS.
IPR013785. Aldolase_TIM.
IPR011872. Homocitrate_synth_fun/arc.
IPR000891. PYR_CT.
[Graphical view]
PfamPF00682. HMGL-like. 1 hit.
[Graphical view]
TIGRFAMsTIGR02146. LysS_fung_arch. 1 hit.
PROSITEPS00815. AIPM_HOMOCIT_SYNTH_1. 1 hit.
PS00816. AIPM_HOMOCIT_SYNTH_2. 1 hit.
PS50991. PYR_CT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio968429.

Entry information

Entry nameHOSC_YEAST
AccessionPrimary (citable) accession number: P48570
Secondary accession number(s): D6VRH0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: June 11, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: 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