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P15454

- KGUA_YEAST

UniProt

P15454 - KGUA_YEAST

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Protein
Guanylate kinase
Gene
GUK1, YDR454C, D9461.39
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Essential for recycling GMP and indirectly, cGMP.

Catalytic activityi

ATP + GMP = ADP + GDP.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi9 – 168ATP
Nucleotide bindingi35 – 8248GMP
Add
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. guanylate kinase activity Source: UniProtKB

GO - Biological processi

  1. GMP metabolic process Source: SGD
  2. nucleotide phosphorylation Source: GOC
  3. purine nucleotide metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER3O-102.
YEAST:MONOMER3O-102.
ReactomeiREACT_188930. Abacavir metabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanylate kinase (EC:2.7.4.8)
Alternative name(s):
GMP kinase
Gene namesi
Name:GUK1
Ordered Locus Names:YDR454C
ORF Names:D9461.39
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

SGDiS000002862. GUK1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 187186Guanylate kinase
PRO_0000170655Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei149 – 1491Phosphoserine
Modified residuei157 – 1571Phosphotyrosine

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP15454.
PaxDbiP15454.
PeptideAtlasiP15454.

Expressioni

Gene expression databases

GenevestigatoriP15454.

Interactioni

Subunit structurei

Monomer.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself1EBI-9672,EBI-9672
ACF2Q121681EBI-9672,EBI-32973
UBX2Q042281EBI-9672,EBI-27730

Protein-protein interaction databases

BioGridi32509. 29 interactions.
DIPiDIP-6721N.
MINTiMINT-522729.
STRINGi4932.YDR454C.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 84
Helixi15 – 2511
Turni27 – 293
Beta strandi30 – 323
Beta strandi35 – 373
Turni47 – 493
Beta strandi50 – 534
Helixi56 – 649
Beta strandi68 – 747
Beta strandi77 – 826
Helixi83 – 9210
Beta strandi94 – 996
Helixi102 – 1098
Helixi112 – 1143
Beta strandi117 – 1226
Helixi126 – 13611
Helixi141 – 15818
Turni159 – 1613
Beta strandi163 – 1686
Helixi172 – 18312

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EX6X-ray2.30A/B2-187[»]
1EX7X-ray1.90A2-187[»]
1GKYX-ray2.00A2-187[»]
4F4JX-ray2.45A/B1-187[»]
ProteinModelPortaliP15454.
SMRiP15454. Positions 2-187.

Miscellaneous databases

EvolutionaryTraceiP15454.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 184183Guanylate kinase-like
Add
BLAST

Sequence similaritiesi

Belongs to the guanylate kinase family.

Phylogenomic databases

eggNOGiCOG0194.
GeneTreeiENSGT00730000110700.
HOGENOMiHOG000037640.
KOiK00942.
OMAiDAVFSIS.
OrthoDBiEOG7TF7NW.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
HAMAPiMF_00328. Guanylate_kinase.
InterProiIPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like.
IPR017665. Guanylate_kinase.
IPR020590. Guanylate_kinase_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00625. Guanylate_kin. 1 hit.
[Graphical view]
SMARTiSM00072. GuKc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR03263. guanyl_kin. 1 hit.
PROSITEiPS00856. GUANYLATE_KINASE_1. 1 hit.
PS50052. GUANYLATE_KINASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P15454-1 [UniParc]FASTAAdd to Basket

« Hide

MSRPIVISGP SGTGKSTLLK KLFAEYPDSF GFSVSSTTRT PRAGEVNGKD    50
YNFVSVDEFK SMIKNNEFIE WAQFSGNYYG STVASVKQVS KSGKTCILDI 100
DMQGVKSVKA IPELNARFLF IAPPSVEDLK KRLEGRGTET EESINKRLSA 150
AQAELAYAET GAHDKVIVND DLDKAYKELK DFIFAEK 187
Length:187
Mass (Da):20,637
Last modified:January 23, 2007 - v2
Checksum:i5DC4D2A22594BFB8
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L04683 Genomic DNA. Translation: AAA34657.1.
U33007 Genomic DNA. Translation: AAB64881.1.
BK006938 Genomic DNA. Translation: DAA12289.1.
PIRiA45097. KIBYGU.
RefSeqiNP_010742.1. NM_001180762.1.

Genome annotation databases

EnsemblFungiiYDR454C; YDR454C; YDR454C.
GeneIDi852065.
KEGGisce:YDR454C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L04683 Genomic DNA. Translation: AAA34657.1 .
U33007 Genomic DNA. Translation: AAB64881.1 .
BK006938 Genomic DNA. Translation: DAA12289.1 .
PIRi A45097. KIBYGU.
RefSeqi NP_010742.1. NM_001180762.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EX6 X-ray 2.30 A/B 2-187 [» ]
1EX7 X-ray 1.90 A 2-187 [» ]
1GKY X-ray 2.00 A 2-187 [» ]
4F4J X-ray 2.45 A/B 1-187 [» ]
ProteinModelPortali P15454.
SMRi P15454. Positions 2-187.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32509. 29 interactions.
DIPi DIP-6721N.
MINTi MINT-522729.
STRINGi 4932.YDR454C.

Proteomic databases

MaxQBi P15454.
PaxDbi P15454.
PeptideAtlasi P15454.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YDR454C ; YDR454C ; YDR454C .
GeneIDi 852065.
KEGGi sce:YDR454C.

Organism-specific databases

SGDi S000002862. GUK1.

Phylogenomic databases

eggNOGi COG0194.
GeneTreei ENSGT00730000110700.
HOGENOMi HOG000037640.
KOi K00942.
OMAi DAVFSIS.
OrthoDBi EOG7TF7NW.

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER3O-102.
YEAST:MONOMER3O-102.
Reactomei REACT_188930. Abacavir metabolism.

Miscellaneous databases

EvolutionaryTracei P15454.
NextBioi 970349.
PROi P15454.

Gene expression databases

Genevestigatori P15454.

Family and domain databases

Gene3Di 3.40.50.300. 3 hits.
HAMAPi MF_00328. Guanylate_kinase.
InterProi IPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like.
IPR017665. Guanylate_kinase.
IPR020590. Guanylate_kinase_CS.
IPR027417. P-loop_NTPase.
[Graphical view ]
Pfami PF00625. Guanylate_kin. 1 hit.
[Graphical view ]
SMARTi SM00072. GuKc. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR03263. guanyl_kin. 1 hit.
PROSITEi PS00856. GUANYLATE_KINASE_1. 1 hit.
PS50052. GUANYLATE_KINASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of the essential gene for guanylate kinase from yeast."
    Konrad M.
    J. Biol. Chem. 267:25652-25655(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Guanylate kinase from Saccharomyces cerevisiae. Isolation and characterization, crystallization and preliminary X-ray analysis, amino acid sequence and comparison with adenylate kinases."
    Berger A., Schiltz E., Schulz G.E.
    Eur. J. Biochem. 184:433-443(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-187, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2.
  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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, 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-149, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, 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-149 AND TYR-157, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Three-dimensional structure of the complex of guanylate kinase from yeast with its substrate GMP."
    Stehle T., Schulz G.E.
    J. Mol. Biol. 211:249-254(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
  11. "Refined structure of the complex between guanylate kinase and its substrate GMP at 2.0-A resolution."
    Stehle T., Schulz G.E.
    J. Mol. Biol. 224:1127-1141(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Entry informationi

Entry nameiKGUA_YEAST
AccessioniPrimary (citable) accession number: P15454
Secondary accession number(s): D6VT79
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 154 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 20500 molecules/cell in log phase SD medium.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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 IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3

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