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P00549

- KPYK1_YEAST

UniProt

P00549 - KPYK1_YEAST

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Protein

Pyruvate kinase 1

Gene

CDC19

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

Functioni

Catalytic activityi

ATP + pyruvate = ADP + phosphoenolpyruvate.

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

The activity is regulated by glucose levels. Activated by fructose-1,6-bisphosphate.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei49 – 491SubstrateBy similarity
Metal bindingi51 – 511PotassiumBy similarity
Metal bindingi53 – 531PotassiumBy similarity
Metal bindingi84 – 841PotassiumBy similarity
Metal bindingi85 – 851Potassium; via carbonyl oxygenBy similarity
Sitei240 – 2401Transition state stabilizerBy similarity
Metal bindingi242 – 2421MagnesiumSequence Analysis
Binding sitei265 – 2651Substrate; via amide nitrogenBy similarity
Metal bindingi266 – 2661MagnesiumBy similarity
Binding sitei266 – 2661Substrate; via amide nitrogenBy similarity
Binding sitei298 – 2981SubstrateBy similarity
Binding sitei337 – 3371ADPSequence Analysis

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. magnesium ion binding Source: InterPro
  3. potassium ion binding Source: InterPro
  4. pyruvate kinase activity Source: SGD

GO - Biological processi

  1. glycolytic process Source: SGD
  2. pyruvate metabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium, Pyruvate

Enzyme and pathway databases

BioCyciYEAST:YAL038W-MONOMER.
ReactomeiREACT_229625. Glycolysis.
REACT_237953. Regulation of gene expression in beta cells.
REACT_241476. ChREBP activates metabolic gene expression.
SABIO-RKP00549.
UniPathwayiUPA00109; UER00188.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate kinase 1 (EC:2.7.1.40)
Short name:
PK 1
Alternative name(s):
cell division cycle protein 19
Gene namesi
Name:CDC19
Synonyms:PYK1
Ordered Locus Names:YAL038W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome I

Organism-specific databases

CYGDiYAL038w.
SGDiS000000036. CDC19.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 500499Pyruvate kinase 1PRO_0000112121Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei9 – 91Phosphoserine2 Publications
Modified residuei16 – 161Phosphoserine2 Publications
Modified residuei31 – 311Phosphothreonine1 Publication
Modified residuei70 – 701Phosphoserine1 Publication
Modified residuei184 – 1841Phosphothreonine1 Publication
Modified residuei213 – 2131Phosphoserine1 Publication
Modified residuei316 – 3161Phosphoserine1 Publication
Modified residuei450 – 4501Phosphoserine1 Publication
Modified residuei478 – 4781Phosphothreonine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP00549.
PaxDbiP00549.
PeptideAtlasiP00549.

2D gel databases

COMPLUYEAST-2DPAGEP00549.

Expressioni

Gene expression databases

GenevestigatoriP00549.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

BioGridi31727. 145 interactions.
DIPiDIP-4124N.
IntActiP00549. 182 interactions.
MINTiMINT-565419.
STRINGi4932.YAL038W.

Structurei

Secondary structure

1
500
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 86Combined sources
Beta strandi21 – 266Combined sources
Helixi29 – 313Combined sources
Helixi34 – 4310Combined sources
Beta strandi47 – 493Combined sources
Helixi57 – 7317Combined sources
Beta strandi82 – 843Combined sources
Beta strandi96 – 994Combined sources
Beta strandi108 – 1125Combined sources
Turni116 – 1205Combined sources
Beta strandi126 – 1294Combined sources
Helixi133 – 1364Combined sources
Beta strandi142 – 1454Combined sources
Turni146 – 1494Combined sources
Beta strandi150 – 1534Combined sources
Turni159 – 1613Combined sources
Beta strandi163 – 1675Combined sources
Beta strandi178 – 1803Combined sources
Helixi193 – 20513Combined sources
Beta strandi208 – 2125Combined sources
Helixi218 – 23215Combined sources
Beta strandi235 – 2417Combined sources
Helixi245 – 2484Combined sources
Helixi250 – 2567Combined sources
Beta strandi260 – 2623Combined sources
Helixi264 – 2707Combined sources
Helixi273 – 2753Combined sources
Helixi276 – 29015Combined sources
Beta strandi294 – 2963Combined sources
Helixi302 – 3054Combined sources
Helixi312 – 32413Combined sources
Beta strandi327 – 3293Combined sources
Turni333 – 3375Combined sources
Helixi341 – 35515Combined sources
Beta strandi357 – 3593Combined sources
Helixi361 – 3688Combined sources
Helixi378 – 39316Combined sources
Beta strandi398 – 4014Combined sources
Beta strandi403 – 4053Combined sources
Helixi406 – 4138Combined sources
Beta strandi420 – 4256Combined sources
Helixi429 – 4324Combined sources
Helixi433 – 4353Combined sources
Beta strandi439 – 4435Combined sources
Turni452 – 4543Combined sources
Helixi455 – 46915Combined sources
Beta strandi478 – 4836Combined sources
Turni487 – 4893Combined sources
Beta strandi494 – 4996Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A3WX-ray3.00A/B1-500[»]
1A3XX-ray3.00A/B1-500[»]
ProteinModelPortaliP00549.
SMRiP00549. Positions 2-500.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00549.

Family & Domainsi

Sequence similaritiesi

Belongs to the pyruvate kinase family.Curated

Phylogenomic databases

eggNOGiCOG0469.
GeneTreeiENSGT00390000008859.
HOGENOMiHOG000021559.
InParanoidiP00549.
KOiK00873.
OMAiHADHQRS.
OrthoDBiEOG7M6DJC.

Family and domain databases

Gene3Di2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
InterProiIPR001697. Pyr_Knase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
IPR011037. Pyrv_Knase-like_insert_dom.
IPR015794. Pyrv_Knase_a/b.
IPR018209. Pyrv_Knase_AS.
IPR015793. Pyrv_Knase_brl.
IPR015795. Pyrv_Knase_C.
IPR015806. Pyrv_Knase_insert_dom.
[Graphical view]
PANTHERiPTHR11817. PTHR11817. 1 hit.
PfamiPF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]
PRINTSiPR01050. PYRUVTKNASE.
SUPFAMiSSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52935. SSF52935. 1 hit.
TIGRFAMsiTIGR01064. pyruv_kin. 1 hit.
PROSITEiPS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00549-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSRLERLTSL NVVAGSDLRR TSIIGTIGPK TNNPETLVAL RKAGLNIVRM
60 70 80 90 100
NFSHGSYEYH KSVIDNARKS EELYPGRPLA IALDTKGPEI RTGTTTNDVD
110 120 130 140 150
YPIPPNHEMI FTTDDKYAKA CDDKIMYVDY KNITKVISAG RIIYVDDGVL
160 170 180 190 200
SFQVLEVVDD KTLKVKALNA GKICSHKGVN LPGTDVDLPA LSEKDKEDLR
210 220 230 240 250
FGVKNGVHMV FASFIRTAND VLTIREVLGE QGKDVKIIVK IENQQGVNNF
260 270 280 290 300
DEILKVTDGV MVARGDLGIE IPAPEVLAVQ KKLIAKSNLA GKPVICATQM
310 320 330 340 350
LESMTYNPRP TRAEVSDVGN AILDGADCVM LSGETAKGNY PINAVTTMAE
360 370 380 390 400
TAVIAEQAIA YLPNYDDMRN CTPKPTSTTE TVAASAVAAV FEQKAKAIIV
410 420 430 440 450
LSTSGTTPRL VSKYRPNCPI ILVTRCPRAA RFSHLYRGVF PFVFEKEPVS
460 470 480 490 500
DWTDDVEARI NFGIEKAKEF GILKKGDTYV SIQGFKAGAG HSNTLQVSTV
Length:500
Mass (Da):54,545
Last modified:July 1, 1989 - v2
Checksum:i78D753FC410C5820
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti382 – 3865VAASA → SLPR in CAA24631. (PubMed:2653861)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01321 Genomic DNA. Translation: CAA24631.1.
X14400 Genomic DNA. Translation: CAA32573.1.
AY949862 Genomic DNA. Translation: AAY27264.1.
AY949863 Genomic DNA. Translation: AAY27265.1.
AY949864 Genomic DNA. Translation: AAY27266.1.
AY949865 Genomic DNA. Translation: AAY27267.1.
AY949866 Genomic DNA. Translation: AAY27268.1.
AY949867 Genomic DNA. Translation: AAY27269.1.
AY949868 Genomic DNA. Translation: AAY27270.1.
AY949869 Genomic DNA. Translation: AAY27271.1.
AY949870 Genomic DNA. Translation: AAY27272.1.
AY949871 Genomic DNA. Translation: AAY27273.1.
AY949872 Genomic DNA. Translation: AAY27274.1.
AY949873 Genomic DNA. Translation: AAY27275.1.
AY949874 Genomic DNA. Translation: AAY27276.1.
AY949875 Genomic DNA. Translation: AAY27277.1.
AY949876 Genomic DNA. Translation: AAY27278.1.
AY949877 Genomic DNA. Translation: AAY27279.1.
AY949878 Genomic DNA. Translation: AAY27280.1.
AY949879 Genomic DNA. Translation: AAY27281.1.
AY949880 Genomic DNA. Translation: AAY27282.1.
AY949881 Genomic DNA. Translation: AAY27283.1.
AY949882 Genomic DNA. Translation: AAY27284.1.
AY949883 Genomic DNA. Translation: AAY27285.1.
AY949884 Genomic DNA. Translation: AAY27286.1.
AY949885 Genomic DNA. Translation: AAY27287.1.
AY949886 Genomic DNA. Translation: AAY27288.1.
AY949887 Genomic DNA. Translation: AAY27289.1.
AY949888 Genomic DNA. Translation: AAY27290.1.
AY949889 Genomic DNA. Translation: AAY27291.1.
AY949890 Genomic DNA. Translation: AAY27292.1.
U12980 Genomic DNA. Translation: AAC04993.1.
AY693107 Genomic DNA. Translation: AAT93126.1.
BK006935 Genomic DNA. Translation: DAA06948.1.
PIRiS05764. KIBYP.
RefSeqiNP_009362.1. NM_001178183.1.

Genome annotation databases

EnsemblFungiiYAL038W; YAL038W; YAL038W.
GeneIDi851193.
KEGGisce:YAL038W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01321 Genomic DNA. Translation: CAA24631.1 .
X14400 Genomic DNA. Translation: CAA32573.1 .
AY949862 Genomic DNA. Translation: AAY27264.1 .
AY949863 Genomic DNA. Translation: AAY27265.1 .
AY949864 Genomic DNA. Translation: AAY27266.1 .
AY949865 Genomic DNA. Translation: AAY27267.1 .
AY949866 Genomic DNA. Translation: AAY27268.1 .
AY949867 Genomic DNA. Translation: AAY27269.1 .
AY949868 Genomic DNA. Translation: AAY27270.1 .
AY949869 Genomic DNA. Translation: AAY27271.1 .
AY949870 Genomic DNA. Translation: AAY27272.1 .
AY949871 Genomic DNA. Translation: AAY27273.1 .
AY949872 Genomic DNA. Translation: AAY27274.1 .
AY949873 Genomic DNA. Translation: AAY27275.1 .
AY949874 Genomic DNA. Translation: AAY27276.1 .
AY949875 Genomic DNA. Translation: AAY27277.1 .
AY949876 Genomic DNA. Translation: AAY27278.1 .
AY949877 Genomic DNA. Translation: AAY27279.1 .
AY949878 Genomic DNA. Translation: AAY27280.1 .
AY949879 Genomic DNA. Translation: AAY27281.1 .
AY949880 Genomic DNA. Translation: AAY27282.1 .
AY949881 Genomic DNA. Translation: AAY27283.1 .
AY949882 Genomic DNA. Translation: AAY27284.1 .
AY949883 Genomic DNA. Translation: AAY27285.1 .
AY949884 Genomic DNA. Translation: AAY27286.1 .
AY949885 Genomic DNA. Translation: AAY27287.1 .
AY949886 Genomic DNA. Translation: AAY27288.1 .
AY949887 Genomic DNA. Translation: AAY27289.1 .
AY949888 Genomic DNA. Translation: AAY27290.1 .
AY949889 Genomic DNA. Translation: AAY27291.1 .
AY949890 Genomic DNA. Translation: AAY27292.1 .
U12980 Genomic DNA. Translation: AAC04993.1 .
AY693107 Genomic DNA. Translation: AAT93126.1 .
BK006935 Genomic DNA. Translation: DAA06948.1 .
PIRi S05764. KIBYP.
RefSeqi NP_009362.1. NM_001178183.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A3W X-ray 3.00 A/B 1-500 [» ]
1A3X X-ray 3.00 A/B 1-500 [» ]
ProteinModelPortali P00549.
SMRi P00549. Positions 2-500.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 31727. 145 interactions.
DIPi DIP-4124N.
IntActi P00549. 182 interactions.
MINTi MINT-565419.
STRINGi 4932.YAL038W.

2D gel databases

COMPLUYEAST-2DPAGE P00549.

Proteomic databases

MaxQBi P00549.
PaxDbi P00549.
PeptideAtlasi P00549.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YAL038W ; YAL038W ; YAL038W .
GeneIDi 851193.
KEGGi sce:YAL038W.

Organism-specific databases

CYGDi YAL038w.
SGDi S000000036. CDC19.

Phylogenomic databases

eggNOGi COG0469.
GeneTreei ENSGT00390000008859.
HOGENOMi HOG000021559.
InParanoidi P00549.
KOi K00873.
OMAi HADHQRS.
OrthoDBi EOG7M6DJC.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00188 .
BioCyci YEAST:YAL038W-MONOMER.
Reactomei REACT_229625. Glycolysis.
REACT_237953. Regulation of gene expression in beta cells.
REACT_241476. ChREBP activates metabolic gene expression.
SABIO-RK P00549.

Miscellaneous databases

EvolutionaryTracei P00549.
NextBioi 968037.

Gene expression databases

Genevestigatori P00549.

Family and domain databases

Gene3Di 2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
InterProi IPR001697. Pyr_Knase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
IPR011037. Pyrv_Knase-like_insert_dom.
IPR015794. Pyrv_Knase_a/b.
IPR018209. Pyrv_Knase_AS.
IPR015793. Pyrv_Knase_brl.
IPR015795. Pyrv_Knase_C.
IPR015806. Pyrv_Knase_insert_dom.
[Graphical view ]
PANTHERi PTHR11817. PTHR11817. 1 hit.
Pfami PF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view ]
PRINTSi PR01050. PYRUVTKNASE.
SUPFAMi SSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52935. SSF52935. 1 hit.
TIGRFAMsi TIGR01064. pyruv_kin. 1 hit.
PROSITEi PS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The yeast pyruvate kinase gene does not contain a string of non-preferred codons: revised nucleotide sequence."
    McNally T., Purvis I.J., Fothergill-Gilmore L.A., Brown A.L.P.
    FEBS Lett. 247:312-316(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The isolation, characterization, and sequence of the pyruvate kinase gene of Saccharomyces cerevisiae."
    Burke R.L., Tekamp-Olson P., Najarian R.
    J. Biol. Chem. 258:2193-2201(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Population structure and gene evolution in Saccharomyces cerevisiae."
    Aa E., Townsend J.P., Adams R.I., Nielsen K.M., Taylor J.W.
    FEMS Yeast Res. 6:702-715(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 76625 / YPH499, Ba194, Bb32, Fy93, M1-2A, M2-8, M5-7A, M5-7B, M7-8D, MMR2-1, MMR2-3, MMR2-5, MMW1-12, MMW1-15, MMW1-15h2, MMW1-2, MMW1-2h2, ORM1-1, Sgu52E, Sgu52F, YPS396, YPS400, YPS598, YPS600, YPS602, YPS604, YPS606, YPS608 and YPS610.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
    Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
    Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: YAL6B.
  9. "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 SER-9 AND THR-478, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  10. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  11. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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-9; SER-16; THR-31; SER-70; THR-184; SER-316; SER-450 AND THR-478, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "The allosteric regulation of pyruvate kinase by fructose-1,6-bisphosphate."
    Jurica M.S., Mesecar A., Heath P.J., Shi W., Nowak T., Stoddard B.L.
    Structure 6:195-210(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).

Entry informationi

Entry nameiKPYK1_YEAST
AccessioniPrimary (citable) accession number: P00549
Secondary accession number(s): D6VPH8, Q2VQG5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 1, 1989
Last modified: November 26, 2014
This is version 155 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 291000 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3