ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P51601


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name GCH1_YEAST
Primary accession number P51601
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on October 1, 1996 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 75)
Name and origin of the protein
Protein name GTP cyclohydrolase 1
Synonyms EC 3.5.4.16
GTP cyclohydrolase I
GTP-CH-I
Gene name
Name: FOL2
OrderedLocusNames: YGR267C
ORFNames: G9349
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE.
STRAIN=C836;
Witter K., Guetlich M., Stucka R., Ziegler I., Bacher A.;
Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
DOI=10.1006/bbrc.1996.0048; PubMed=8573145 [NCBI, ExPASy, EBI, Israel, Japan]
Nardese V., Gutlich M., Brambilla A., Agostoni Carbone M.L.;
"Disruption of the GTP-cyclohydrolase I gene in Saccharomyces cerevisiae.";
Biochem. Biophys. Res. Commun. 218:273-279(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
DOI=10.1002/(SICI)1097-0061(19980430)14:6<587::AID-YEA268>3.0.CO;2-I; PubMed=9605509 [NCBI, ExPASy, EBI, Israel, Japan]
Agostoni Carbone M.L., Lucchini G., Melchioretto P., Nardese V., Vanoni M., Panzeri L.;
"A 9359 bp fragment from the right arm of Saccharomyces cerevisiae chromosome VII includes the FOL2 and YTA7 genes and three unknown open reading frames.";
Yeast 14:587-591(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=9169869 [NCBI, ExPASy, EBI, Israel, Japan]
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
Nature 387:81-84(1997).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1101/gr.6037607; PubMed=17322287 [NCBI, ExPASy, EBI, Israel, Japan]
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 115-208.
STRAIN=ATCC 204508 / S288c;
DOI=10.1006/bbrc.1995.2026; PubMed=7542887 [NCBI, ExPASy, EBI, Israel, Japan]
Maier J., Witter K., Guetlich M., Ziegler I., Werner T., Ninnemann H.;
"Homology cloning of GTP-cyclohydrolase I from various unrelated eukaryotes by reverse-transcription polymerase chain reaction using a general set of degenerate primers.";
Biochem. Biophys. Res. Commun. 212:705-711(1995).
[7]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-15 AND SER-23, AND MASS SPECTROMETRY.
DOI=10.1021/pr060559j; PubMed=17330950 [NCBI, ExPASy, EBI, Israel, Japan]
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-15; THR-22 AND SER-23, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0701622104; PubMed=17563356 [NCBI, ExPASy, EBI, Israel, Japan]
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases.";
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-15; THR-22; SER-23 AND TYR-25, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Z47201; CAA87397.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X94314; CAA63975.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y07893; CAA69198.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z73052; CAA97297.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY692993; AAT93012.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z49756; CAA89826.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JC4585; JC4585.
RefSeq NP_011783.1; -.
3D structure databases
HSSP P22288; 1IS8. [HSSP ENTRY / PDB]
ModBase P51601.
Protein-protein interaction databases
DIP DIP:1318N; -.
IntAct P51601; 13.
Organism-specific databases
CYGD YGR267c; -.
SGD S000003499; FOL2.
Yeast-GFP YGR267C.
Gene expression databases
GermOnline YGR267C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0005634; Cellular component: nucleus (inferred from direct assay from SGD).
GO:0003934; Molecular function: GTP cyclohydrolase I activity (inferred from electronic annotation from InterPro).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009396; Biological process: folic acid and derivative biosynthetic process (inferred from mutant phenotype from SGD).
GO:0006729; Biological process: tetrahydrobiopterin biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001474; GTP_CycOHase_I.
Graphical view of domain structure.
PANTHER PTHR11109; GTP_cyclohydro_I; 1.
Pfam PF01227; GTP_cyclohydroI; 1.
Pfam graphical view of domain structure.
ProDom PD003330; GTP_cyclohydroI; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR00063; folE; 1.
PROSITE PS00859; GTP_CYCLOHYDROL_1_1; 1.
PS00860; GTP_CYCLOHYDROL_1_2; 1.
Proteomic databases
PeptideAtlas P51601; -.
Proteomics databases
PRIDE P51601; -.
Genome annotation databases
Ensembl YGR267C; Saccharomyces cerevisiae. [Contig view]
GeneID 853183; -.
GenomeReviews Y13135_GR; YGR267C.
KEGG sce:YGR267C; -.
NMPDR fig|4932.3.peg.2912; -.
Phylogenomic databases
HOGENOM P51601; -.
Other
LinkHub P51601; -.
NextBio 973323; -.
ProtoNet P51601.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Allosteric enzyme; Complete proteome; Hydrolase; Metal-binding; Phosphoprotein; Tetrahydrobiopterin biosynthesis; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   243  243     GTP cyclohydrolase 1. PRO_0000119489
METAL   132   132        Zinc (By similarity). 
METAL   135   135        Zinc (By similarity). 
METAL   203   203        Zinc (By similarity). 
MOD_RES   15    15        Phosphothreonine. 
MOD_RES   22    22        Phosphothreonine. 
MOD_RES   23    23        Phosphoserine. 
MOD_RES   25    25        Phosphotyrosine. 
CONFLICT   159   160        LA -> QG (in Ref. 6; CAA89826). 
CONFLICT   206   206        S -> M (in Ref. 6; CAA89826). 
CONFLICT   217   217        V -> A (in Ref. 1; CAA87397). 
Sequence information
Length: 243 AA [This is the length of the unprocessed precursor] Molecular weight: 27769 Da [This is the MW of the unprocessed precursor] CRC64: A71AB8750AECD3F6 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MHNIQLVQEI ERHETPLNIR PTSPYTLNPP VERDGFSWPS VGTRQRAEET EEEEKERIQR 

        70         80         90        100        110        120 
ISGAIKTILT ELGEDVNREG LLDTPQRYAK AMLYFTKGYQ TNIMDDVIKN AVFEEDHDEM 

       130        140        150        160        170        180 
VIVRDIEIYS LCEHHLVPFF GKVHIGYIPN KKVIGLSKLA RLAEMYARRL QVQERLTKQI 

       190        200        210        220        230        240 
AMALSDILKP LGVAVVMEAS HMCMVSRGIQ KTGSSTVTSC MLGGFRAHKT REEFLTLLGR 


RSI 

P51601 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!