Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Aspartokinase

Gene

HOM3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + L-aspartate = ADP + 4-phospho-L-aspartate.

Pathwayi

GO - Molecular functioni

  1. amino acid binding Source: InterPro
  2. aspartate kinase activity Source: SGD
  3. ATP binding Source: UniProtKB-KW

GO - Biological processi

  1. homoserine biosynthetic process Source: SGD
  2. lysine biosynthetic process via diaminopimelate Source: UniProtKB-UniPathway
  3. methionine biosynthetic process Source: SGD
  4. threonine biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Threonine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:YER052C-MONOMER.
BRENDAi2.7.2.4. 984.
SABIO-RKP10869.
UniPathwayiUPA00034; UER00015.
UPA00050; UER00461.
UPA00051; UER00462.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartokinase (EC:2.7.2.4)
Alternative name(s):
Aspartate kinase
Gene namesi
Name:HOM3
Ordered Locus Names:YER052C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome V

Organism-specific databases

CYGDiYER052c.
SGDiS000000854. HOM3.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 527527AspartokinasePRO_0000066690Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei333 – 3331Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP10869.
PaxDbiP10869.
PeptideAtlasiP10869.

Expressioni

Gene expression databases

GenevestigatoriP10869.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
FPR1P200815EBI-2430,EBI-6961

Protein-protein interaction databases

BioGridi36791. 160 interactions.
DIPiDIP-1319N.
IntActiP10869. 8 interactions.
MINTiMINT-392511.
STRINGi4932.YER052C.

Structurei

3D structure databases

ProteinModelPortaliP10869.
SMRiP10869. Positions 16-501.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini367 – 44074ACT 1PROSITE-ProRule annotationAdd
BLAST
Domaini442 – 52786ACT 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the aspartokinase family.Curated
Contains 2 ACT domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0527.
HOGENOMiHOG000293094.
InParanoidiP10869.
KOiK00928.
OMAiIRSHIPI.
OrthoDBiEOG7NPG3J.

Family and domain databases

Gene3Di3.40.1160.10. 2 hits.
InterProiIPR002912. ACT_dom.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR001341. Asp_kinase_dom.
IPR018042. Aspartate_kinase_CS.
IPR027795. GATS-like_ACT_dom.
[Graphical view]
PfamiPF00696. AA_kinase. 1 hit.
PF13840. ACT_7. 1 hit.
[Graphical view]
SUPFAMiSSF53633. SSF53633. 1 hit.
TIGRFAMsiTIGR00657. asp_kinases. 1 hit.
PROSITEiPS51671. ACT. 1 hit.
PS00324. ASPARTOKINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P10869-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPMDFQPTSS HSNWVVQKFG GTSVGKFPVQ IVDDIVKHYS KPDGPNNNVA
60 70 80 90 100
VVCSARSSYT KAEGTTSRLL KCCDLASQES EFQDIIEVIR QDHIDNADRF
110 120 130 140 150
ILNPALQAKL VDDTNKELEL VKKYLNASKV LGEVSSRTVD LVMSCGEKLS
160 170 180 190 200
CLFMTALCND RGCKAKYVDL SHIVPSDFSA SALDNSFYTF LVQALKEKLA
210 220 230 240 250
PFVSAKERIV PVFTGFFGLV PTGLLNGVGR GYTDLCAALI AVAVNADELQ
260 270 280 290 300
VWKEVDGIFT ADPRKVPEAR LLDSVTPEEA SELTYYGSEV IHPFTMEQVI
310 320 330 340 350
RAKIPIRIKN VQNPLGNGTI IYPDNVAKKG ESTPPHPPEN LSSSFYEKRK
360 370 380 390 400
RGATAITTKN DIFVINIHSN KKTLSHGFLA QIFTILDKYK LVVDLISTSE
410 420 430 440 450
VHVSMALPIP DADSLKSLRQ AEEKLRILGS VDITKKLSIV SLVGKHMKQY
460 470 480 490 500
IGIAGTMFTT LAEEGINIEM ISQGANEINI SCVINESDSI KALQCIHAKL
510 520
LSERTNTSNQ FEHAIDERLE QLKRLGI
Length:527
Mass (Da):58,110
Last modified:August 1, 1990 - v2
Checksum:iD4D28FB8D4374898
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03526 Genomic DNA. Translation: AAA34681.1.
U18796 Genomic DNA. Translation: AAB64587.1.
BK006939 Genomic DNA. Translation: DAA07708.1.
PIRiA35888. KIBYD.
RefSeqiNP_010972.1. NM_001178943.1.

Genome annotation databases

EnsemblFungiiYER052C; YER052C; YER052C.
GeneIDi856778.
KEGGisce:YER052C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03526 Genomic DNA. Translation: AAA34681.1.
U18796 Genomic DNA. Translation: AAB64587.1.
BK006939 Genomic DNA. Translation: DAA07708.1.
PIRiA35888. KIBYD.
RefSeqiNP_010972.1. NM_001178943.1.

3D structure databases

ProteinModelPortaliP10869.
SMRiP10869. Positions 16-501.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36791. 160 interactions.
DIPiDIP-1319N.
IntActiP10869. 8 interactions.
MINTiMINT-392511.
STRINGi4932.YER052C.

Proteomic databases

MaxQBiP10869.
PaxDbiP10869.
PeptideAtlasiP10869.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYER052C; YER052C; YER052C.
GeneIDi856778.
KEGGisce:YER052C.

Organism-specific databases

CYGDiYER052c.
SGDiS000000854. HOM3.

Phylogenomic databases

eggNOGiCOG0527.
HOGENOMiHOG000293094.
InParanoidiP10869.
KOiK00928.
OMAiIRSHIPI.
OrthoDBiEOG7NPG3J.

Enzyme and pathway databases

UniPathwayiUPA00034; UER00015.
UPA00050; UER00461.
UPA00051; UER00462.
BioCyciYEAST:YER052C-MONOMER.
BRENDAi2.7.2.4. 984.
SABIO-RKP10869.

Miscellaneous databases

NextBioi982982.
PROiP10869.

Gene expression databases

GenevestigatoriP10869.

Family and domain databases

Gene3Di3.40.1160.10. 2 hits.
InterProiIPR002912. ACT_dom.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR001341. Asp_kinase_dom.
IPR018042. Aspartate_kinase_CS.
IPR027795. GATS-like_ACT_dom.
[Graphical view]
PfamiPF00696. AA_kinase. 1 hit.
PF13840. ACT_7. 1 hit.
[Graphical view]
SUPFAMiSSF53633. SSF53633. 1 hit.
TIGRFAMsiTIGR00657. asp_kinases. 1 hit.
PROSITEiPS51671. ACT. 1 hit.
PS00324. ASPARTOKINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure of the yeast HOM3 gene which encodes aspartokinase."
    Rafalski J.A., Falco S.C.
    J. Biol. Chem. 263:2146-2151(1987) [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(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. 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(2006) [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(2006) [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(2007) [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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiAK_YEAST
AccessioniPrimary (citable) accession number: P10869
Secondary accession number(s): D3DLV4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: August 1, 1990
Last modified: March 4, 2015
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 48100 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome V
    Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.