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Protein

Guanylate kinase

Gene

GUK1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: 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 – 8248GMPAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • GMP metabolic process Source: SGD
  • nucleotide phosphorylation Source: GOC
  • 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.
BRENDAi2.7.4.8. 984.
ReactomeiREACT_275169. Abacavir metabolism.
REACT_275578. Synthesis and interconversion of nucleotide di- and triphosphates.

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 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR454C.
SGDiS000002862. GUK1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 187186Guanylate kinasePRO_0000170655Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei149 – 1491Phosphoserine4 Publications
Modified residuei157 – 1571Phosphotyrosine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP15454.
PaxDbiP15454.
PeptideAtlasiP15454.

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. 30 interactions.
DIPiDIP-6721N.
MINTiMINT-522729.
STRINGi4932.YDR454C.

Structurei

Secondary structure

1
187
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 84Combined sources
Helixi15 – 2511Combined sources
Turni27 – 293Combined sources
Beta strandi30 – 323Combined sources
Beta strandi35 – 373Combined sources
Turni47 – 493Combined sources
Beta strandi50 – 534Combined sources
Helixi56 – 649Combined sources
Beta strandi68 – 747Combined sources
Beta strandi77 – 826Combined sources
Helixi83 – 9210Combined sources
Beta strandi94 – 996Combined sources
Helixi102 – 1098Combined sources
Helixi112 – 1143Combined sources
Beta strandi117 – 1226Combined sources
Helixi126 – 13611Combined sources
Helixi141 – 15818Combined sources
Turni159 – 1613Combined sources
Beta strandi163 – 1686Combined sources
Helixi172 – 18312Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15454.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Belongs to the guanylate kinase family.Curated
Contains 1 guanylate kinase-like domain.Curated

Phylogenomic databases

eggNOGiCOG0194.
GeneTreeiENSGT00730000110700.
HOGENOMiHOG000037640.
InParanoidiP15454.
KOiK00942.
OMAiILLAEKC.
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

        10         20         30         40         50
MSRPIVISGP SGTGKSTLLK KLFAEYPDSF GFSVSSTTRT PRAGEVNGKD
60 70 80 90 100
YNFVSVDEFK SMIKNNEFIE WAQFSGNYYG STVASVKQVS KSGKTCILDI
110 120 130 140 150
DMQGVKSVKA IPELNARFLF IAPPSVEDLK KRLEGRGTET EESINKRLSA
160 170 180
AQAELAYAET GAHDKVIVND DLDKAYKELK DFIFAEK
Length:187
Mass (Da):20,637
Last modified:January 23, 2007 - v2
Checksum:i5DC4D2A22594BFB8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32509. 30 interactions.
DIPiDIP-6721N.
MINTiMINT-522729.
STRINGi4932.YDR454C.

Proteomic databases

MaxQBiP15454.
PaxDbiP15454.
PeptideAtlasiP15454.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YDR454C.
SGDiS000002862. GUK1.

Phylogenomic databases

eggNOGiCOG0194.
GeneTreeiENSGT00730000110700.
HOGENOMiHOG000037640.
InParanoidiP15454.
KOiK00942.
OMAiILLAEKC.
OrthoDBiEOG7TF7NW.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER3O-102.
YEAST:MONOMER3O-102.
BRENDAi2.7.4.8. 984.
ReactomeiREACT_275169. Abacavir metabolism.
REACT_275578. Synthesis and interconversion of nucleotide di- and triphosphates.

Miscellaneous databases

EvolutionaryTraceiP15454.
NextBioi970349.
PROiP15454.

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]
ProtoNetiSearch...

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: June 24, 2015
This is version 161 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.1 Publication

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

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.