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P15454 (KGUA_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 151. 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:
Guanylate kinase

EC=2.7.4.8
Alternative name(s):
GMP kinase
Gene names
Name:GUK1
Ordered Locus Names:YDR454C
ORF Names:D9461.39
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length187 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential for recycling GMP and indirectly, cGMP. HAMAP-Rule MF_00328

Catalytic activity

ATP + GMP = ADP + GDP. HAMAP-Rule MF_00328

Subunit structure

Monomer.

Miscellaneous

Present with 20500 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the guanylate kinase family.

Contains 1 guanylate kinase-like domain.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 187186Guanylate kinase HAMAP-Rule MF_00328
PRO_0000170655

Regions

Domain2 – 184183Guanylate kinase-like
Nucleotide binding9 – 168ATP HAMAP-Rule MF_00328
Nucleotide binding35 – 8248GMP HAMAP-Rule MF_00328

Amino acid modifications

Modified residue21N-acetylserine Ref.4
Modified residue1491Phosphoserine Ref.6 Ref.7 Ref.8 Ref.9
Modified residue1571Phosphotyrosine Ref.9

Secondary structure

..................................... 187
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P15454 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 5DC4D2A22594BFB8

FASTA18720,637
        10         20         30         40         50         60 
MSRPIVISGP SGTGKSTLLK KLFAEYPDSF GFSVSSTTRT PRAGEVNGKD YNFVSVDEFK 

        70         80         90        100        110        120 
SMIKNNEFIE WAQFSGNYYG STVASVKQVS KSGKTCILDI DMQGVKSVKA IPELNARFLF 

       130        140        150        160        170        180 
IAPPSVEDLK KRLEGRGTET EESINKRLSA AQAELAYAET GAHDKVIVND DLDKAYKELK 


DFIFAEK 

« Hide

References

« Hide 'large scale' references
[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. 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]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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]"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 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).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L04683 Genomic DNA. Translation: AAA34657.1.
U33007 Genomic DNA. Translation: AAB64881.1.
BK006938 Genomic DNA. Translation: DAA12289.1.
PIRKIBYGU. A45097.
RefSeqNP_010742.1. NM_001180762.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EX6X-ray2.30A/B2-186[»]
1EX7X-ray1.90A2-186[»]
1GKYX-ray2.00A2-187[»]
4F4JX-ray2.45A/B1-187[»]
ProteinModelPortalP15454.
SMRP15454. Positions 2-187.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32509. 29 interactions.
DIPDIP-6721N.
MINTMINT-522729.
STRING4932.YDR454C.

Proteomic databases

PaxDbP15454.
PeptideAtlasP15454.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR454C; YDR454C; YDR454C.
GeneID852065.
KEGGsce:YDR454C.

Organism-specific databases

SGDS000002862. GUK1.

Phylogenomic databases

eggNOGCOG0194.
GeneTreeENSGT00730000110700.
HOGENOMHOG000037640.
KOK00942.
OMARCILDIE.
OrthoDBEOG7TF7NW.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER3O-102.
YEAST:MONOMER3O-102.

Gene expression databases

GenevestigatorP15454.

Family and domain databases

Gene3D3.40.50.300. 3 hits.
HAMAPMF_00328. Guanylate_kinase.
InterProIPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like.
IPR017665. Guanylate_kinase.
IPR020590. Guanylate_kinase_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00625. Guanylate_kin. 1 hit.
[Graphical view]
SMARTSM00072. GuKc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR03263. guanyl_kin. 1 hit.
PROSITEPS00856. GUANYLATE_KINASE_1. 1 hit.
PS50052. GUANYLATE_KINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP15454.
NextBio970349.
PROP15454.

Entry information

Entry nameKGUA_YEAST
AccessionPrimary (citable) accession number: P15454
Secondary accession number(s): D6VT79
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 151 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 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references