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UniProtKB/Swiss-Prot entry Q12326


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

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Entry information
Entry name PMG3_YEAST
Primary accession number Q12326
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on November 1, 1997 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 76)
Name and origin of the protein
Protein name Phosphoglycerate mutase 3
Synonyms PGAM 3
EC 5.4.2.1
Phosphoglyceromutase 3
MPGM 3
BPG-dependent PGAM 3
Gene name
Name: GPM3
OrderedLocusNames: YOL056W
ORFNames: O1236
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 [GENOMIC DNA].
STRAIN=ATCC 90843 / S288c / FY73;
DOI=10.1002/(SICI)1097-0061(199601)12:1<67::AID-YEA884>3.0.CO;2-F; PubMed=8789261 [NCBI, ExPASy, EBI, Israel, Japan]
Mannhaupt G., Vetter I., Schwarzlose C., Mitzel S., Feldmann H.;
"Analysis of a 26 kb region on the left arm of yeast chromosome XV.";
Yeast 12:67-76(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=9169874 [NCBI, ExPASy, EBI, Israel, Japan]
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
Nature 387:98-102(1997).
[3]
CHARACTERIZATION.
DOI=10.1002/(SICI)1097-0061(199802)14:3<203::AID-YEA205>3.3.CO;2-#; PubMed=9544241 [NCBI, ExPASy, EBI, Israel, Japan]
Heinisch J.J., Mueller S., Schlueter E., Jacoby J., Rodicio R.;
"Investigation of two yeast genes encoding putative isoenzymes of phosphoglycerate mutase.";
Yeast 14:203-213(1998).
[4]
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).
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
X91067; CAA62530.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z74798; CAA99064.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S61723; S61723.
RefSeq NP_014585.1; -.
3D structure databases
HSSP P00950; 1QHF. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
ModBase Q12326.
Protein-protein interaction databases
DIP DIP:4234N; -.
IntAct Q12326; -.
Organism-specific databases
CYGD YOL056w; -.
SGD S000005417; GPM3.
Yeast-GFP YOL056W.
Gene expression databases
GermOnline YOL056W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0004619; Molecular function: phosphoglycerate mutase activity (inferred from electronic annotation from EC).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006096; Biological process: glycolysis (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR001345; PG/BPGM_mutase.
IPR013078; PG_mutase.
IPR005952; Phosphogly_mut1.
Graphical view of domain structure.
PANTHER PTHR11931; Phosphogly_mut1; 1.
Pfam PF00300; PGAM; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR01258; pgm_1; 1.
PROSITE PS00175; PG_MUTASE; 1.
ProtoNet Q12326.
Proteomic databases
PeptideAtlas Q12326; -.
Genome annotation databases
Ensembl YOL056W; Saccharomyces cerevisiae. [Contig view]
GeneID 854098; -.
GenomeReviews Y13140_GR; YOL056W.
KEGG sce:YOL056W; -.
NMPDR fig|4932.3.peg.5677; -.
Phylogenomic databases
HOGENOM Q12326; -.
Other
LinkHub Q12326; -.
NextBio 975767; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Glycolysis; Isomerase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   303  303     Phosphoglycerate mutase 3. PRO_0000179841
ACT_SITE   14    14        Tele-phosphohistidine intermediate (By similarity). 
ACT_SITE   235   235        By similarity. 
SITE   70    70  1     Interaction with carboxyl group of phosphoglycerates (By similarity). 
Sequence information
Length: 303 AA [This is the length of the unprocessed precursor] Molecular weight: 34863 Da [This is the MW of the unprocessed precursor] CRC64: 29C3FF3D28560914 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTVTDTFKLF ILRHGQSELN SENIFCGWID AQLTEKGKSQ ARHSAKLIKQ FCDSNNISLP 

        70         80         90        100        110        120 
QIGYTSRLIR TQQTMDVILE ELGLKHTNYV ITTNTNIKEE LQDTRFEGSM PVLQTWRLNE 

       130        140        150        160        170        180 
RHYGAWQGQR KPDILKEYGK EKYMYIRRDY NGKPPKVNLN LEMVQEENDQ GSSTGYDFKE 

       190        200        210        220        230        240 
PNRHLKYGPE EKANERLPES ESLCEVVVRL KPFLNNVVLS TANKISQESC VIVGHGSSVR 

       250        260        270        280        290        300 
SLLKVLEGIS DEDIKDVDIP NGIPLVIELD RDNYSFVRKF YLDPESAKVN AQMVRDEGFE 


KNP 

Q12326 in FASTA format

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