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UniProtKB/Swiss-Prot entry P32288


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

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Entry information
Entry name GLNA_YEAST
Primary accession number P32288
Secondary accession number Q03959
Integrated into Swiss-Prot on October 1, 1993
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 83)
Name and origin of the protein
Protein name Glutamine synthetase
Synonyms GS
EC 6.3.1.2
Glutamate--ammonia ligase
Gene name
Name: GLN1
OrderedLocusNames: YPR035W
ORFNames: YP3085.01, YP9367.15
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].
PubMed=1347768 [NCBI, ExPASy, EBI, Israel, Japan]
Minehart P.L., Magasanik B.;
"Sequence of the GLN1 gene of Saccharomyces cerevisiae: role of the upstream region in regulation of glutamine synthetase expression.";
J. Bacteriol. 174:1828-1836(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=9169875 [NCBI, ExPASy, EBI, Israel, Japan]
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
Nature 387:103-105(1997).
[3]
PROTEIN SEQUENCE OF 2-8; 149-166; 171-178; 220-224 AND 286-293.
PubMed=2891705 [NCBI, ExPASy, EBI, Israel, Japan]
Kim K.H., Rhee S.G.;
"Sequence of peptides from Saccharomyces cerevisiae glutamine synthetase. N-terminal peptide and ATP-binding domain.";
J. Biol. Chem. 263:833-838(1988).
[4]
ACETYLATION AT ALA-2.
DOI=10.1002/elps.1150180810; PubMed=9298649 [NCBI, ExPASy, EBI, Israel, Japan]
Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I., Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R., Payne W.E.;
"Proteome studies of Saccharomyces cerevisiae: identification and characterization of abundant proteins.";
Electrophoresis 18:1347-1360(1997).
[5]
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).
[6]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-324, AND MASS SPECTROMETRY.
DOI=10.1038/nbt849; PubMed=12872131 [NCBI, ExPASy, EBI, Israel, Japan]
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., Gygi S.P.;
"A proteomics approach to understanding protein ubiquitination.";
Nat. Biotechnol. 21:921-926(2003).
[7]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-324, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.2135500100; PubMed=14557538 [NCBI, ExPASy, EBI, Israel, Japan]
Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
"A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery.";
Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(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
M65157; AAA34644.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z68111; CAA92141.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z71255; CAA94985.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z49274; CAA89289.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S61058; S61058.
3D structure databases
HSSP P06201; 1LGR. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
ModBase P32288.
Protein-protein interaction databases
DIP DIP:6699N; -.
IntAct P32288; -.
Enzyme and pathway databases
BioCyc MetaCyc:MON-12439; -.
2D gel databases
SWISS-2DPAGE P32288; -.
Organism-specific databases
CYGD YPR035w; -.
SGD S000006239; GLN1.
Yeast-GFP YPR035W.
Gene expression databases
ArrayExpress P32288; -.
GermOnline YPR035W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from SGD).
GO:0004356; Molecular function: glutamate-ammonia ligase activity (inferred from mutant phenotype from SGD).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006807; Biological process: nitrogen compound metabolic process (inferred from expression pattern from SGD).
QuickGo view.
Family and domain databases
InterPro IPR008147; Gln_synt_beta.
IPR014746; Gln_synth/guanido_kin_cat.
IPR008146; Gln_synth_cat.
Graphical view of domain structure.
Gene3D G3DSA:3.30.590.10; ATP-gua_Ptrans; 1.
Pfam PF00120; Gln-synt_C; 1.
PF03951; Gln-synt_N; 1.
Pfam graphical view of domain structure.
ProDom PD001057; Gln_synt_C; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00180; GLNA_1; 1.
PS00181; GLNA_ATP; 1.
BLOCKS P32288.
Proteomic databases
PeptideAtlas P32288; -.
Genome annotation databases
Ensembl YPR035W; Saccharomyces cerevisiae. [Contig view]
GenomeReviews U00094_GR; YPR035W.
Phylogenomic databases
HOGENOM P32288; -.
Other
LinkHub P32288; -.
ProtoNet P32288.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Ligase; Ubl conjugation.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   370  369     Glutamine synthetase. PRO_0000153166
MOD_RES   2     2        N-acetylalanine. 
CROSSLNK   324   324        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin). 
CONFLICT   165   165        G -> D (in Ref. 3; AA sequence). 
CONFLICT   172   172        M -> V (in Ref. 3; AA sequence). 
CONFLICT   251   251        T -> A (in Ref. 2; CAA92141/CAA94985). 
CONFLICT   264   264        M -> T (in Ref. 2; CAA92141/CAA94985). 
Sequence information
Length: 370 AA [This is the length of the unprocessed precursor] Molecular weight: 41766 Da [This is the MW of the unprocessed precursor] CRC64: 43139C40E97DB34D [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAEASIEKTQ ILQKYLELDQ RGRIIAEYVW IDGTGNLRSK GRTLKKRITS IDQLPEWNFD 

        70         80         90        100        110        120 
GSSTNQAPGH DSDIYLKPVA YYPDPFRRGD NIVVLAACYN NDGTPNKFNH RHEAAKLFAA 

       130        140        150        160        170        180 
HKDEEIWFGL EQEYTLFDMY DDVYGWPKGG YPAPQGPYYC GVGAGKVYAR DMIEAHYRAC 

       190        200        210        220        230        240 
LYAGLEISGI NAEVMPSQWE FQVGPCTGID MGDQLWMARY FLHRVAEEFG IKISFHPKPL 

       250        260        270        280        290        300 
KGDWNGAGCH TNVSTKEMRQ PGGMKYIEQA IEKLSKRHAE HIKLYGSDND MRLTGRHETA 

       310        320        330        340        350        360 
SMTAFSSGVA NRGSSIRIPR SVAKEGYGYF EDRRPASNID PYLVTGIMCE TVCGAIDNAD 

       370 
MTKEFERESS 

P32288 in FASTA format

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