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Reviewed, UniProtKB/Swiss-Prot P32288 (GLNA_YEAST)

Last modified June 16, 2009. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glutamine synthetase
      Short name=GS
    EC=6.3.1.2
Alternative name(s):
    Glutamate--ammonia ligase
Gene names
Name: GLN1
Ordered Locus Names: YPR035W
ORF Names: YP3085.01, YP9367.15
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length370 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine.

Subunit structure

Homooctamer.

Subcellular location

Cytoplasm.

Miscellaneous

Present with 346000 molecules/cell in log phase SD medium. Ref.5

Sequence similarities

Belongs to the glutamine synthetase family.

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

P538391EBI-7665,EBI-28263
ACB1P317871EBI-7665,EBI-2060
ADE16P541131EBI-7665,EBI-14213
ADE17P380091EBI-7665,EBI-14223
ADE4P040461EBI-7665,EBI-14238
ALO1P547831EBI-7665,EBI-2519
ARC18Q059331EBI-7665,EBI-2764
ARO7P321781EBI-7665,EBI-4613
ARP2P323811EBI-7665,EBI-2927
CAF20P129621EBI-7665,EBI-9010
CAP2P135171EBI-7665,EBI-4013
CPR6P536911EBI-7665,EBI-5429
CUE5Q084121EBI-7665,EBI-37580
DNM1P548611EBI-7665,EBI-6002
DOS2P548581EBI-7665,EBI-6042
DPH5P324691EBI-7665,EBI-6095
DYS1P387911EBI-7665,EBI-5871
EFT1P323241EBI-7665,EBI-6333
FAT2P381371EBI-7665,EBI-6831
FES1P382601EBI-7665,EBI-21563
GCD7P325021EBI-7665,EBI-6260
GCN1P338921EBI-7665,EBI-7442
GDH2P333271EBI-7665,EBI-5815
GLO2Q055841EBI-7665,EBI-7672
GRE3P387151EBI-7665,EBI-7884
GSY2P274721EBI-7665,EBI-8036
HCH1P538341EBI-7665,EBI-28288
HSP30P256191EBI-7665,EBI-8563
HUG1Q6Q5K61EBI-7665,EBI-392766
HYR1P405811EBI-7665,EBI-7869
IDI1P154961EBI-7665,EBI-8902
INO1P119861EBI-7665,EBI-9257
LIA1P471201EBI-7665,EBI-25526
MET3P085361EBI-7665,EBI-10753
MPG1P419401EBI-7665,EBI-11191
MTD1Q020461EBI-7665,EBI-2045181
NAP1P252931EBI-7665,EBI-11850
PEX11Q124621EBI-7665,EBI-13198
PEX14P531121EBI-7665,EBI-13212
PGM2P370121EBI-7665,EBI-13296
PHO13P198811EBI-7665,EBI-35376
PLM2Q043831EBI-7665,EBI-2079237
PRE10P212421EBI-7665,EBI-13963
PRE8P236391EBI-7665,EBI-13959
PRO2P548851EBI-7665,EBI-13872
PRO3P322631EBI-7665,EBI-13885
PST2Q123351EBI-7665,EBI-14064
PUP2P323791EBI-7665,EBI-13971
RAD25Q005781EBI-7665,EBI-14683
RAD51P254541EBI-7665,EBI-14709
RAS2P011201EBI-7665,EBI-14838
RIB1P380661EBI-7665,EBI-7436
SCL1P212431EBI-7665,EBI-13975
SDH4P372981EBI-7665,EBI-16796
SIS1P252941EBI-7665,EBI-17244
SLA2P333381EBI-7665,EBI-17323
SMI1P325661EBI-7665,EBI-17452
SNA3P143591EBI-7665,EBI-26122
SNC2P333281EBI-7665,EBI-17512
SRV2P175551EBI-7665,EBI-4024
SSD1P242761EBI-7665,EBI-18153
SSM4P403181EBI-7665,EBI-18208
STI1P157051EBI-7665,EBI-18418
TPD3P313831EBI-7665,EBI-1936
TRP2P008991EBI-7665,EBI-19575
TRP4P072851EBI-7665,EBI-2096870
URA7P282741EBI-7665,EBI-20128
VMA7P391111EBI-7665,EBI-20272
YNK1P360101EBI-7665,EBI-11968
YNL247WP538521EBI-7665,EBI-29230
YOP1Q124021EBI-7665,EBI-37092
YPR1Q124581EBI-7665,EBI-29490
YRF1-4O135591EBI-7665,EBI-29562

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 370369Glutamine synthetase
PRO_0000153166

Amino acid modifications

Modified residue21N-acetylalanine Ref.4
Cross-link324Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.6 Ref.7

Experimental info

Sequence conflict1651G → D AA sequence Ref.3
Sequence conflict1721M → V AA sequence Ref.3
Sequence conflict2511T → A in CAA92141. Ref.2
Sequence conflict2511T → A in CAA94985. Ref.2
Sequence conflict2641M → T in CAA92141. Ref.2
Sequence conflict2641M → T in CAA94985. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P32288-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 43139C40E97DB34D

FASTA37041,766
        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 

« Hide

References

« Hide 'large scale' references
[1]"Sequence of the GLN1 gene of Saccharomyces cerevisiae: role of the upstream region in regulation of glutamine synthetase expression."
Minehart P.L., Magasanik B.
J. Bacteriol. 174:1828-1836(1992) [PubMed: 1347768] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
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. expand/collapse author list , 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.
Nature 387:103-105(1997) [PubMed: 9169875] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[3]"Sequence of peptides from Saccharomyces cerevisiae glutamine synthetase. N-terminal peptide and ATP-binding domain."
Kim K.H., Rhee S.G.
J. Biol. Chem. 263:833-838(1988) [PubMed: 2891705] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-8; 149-166; 171-178; 220-224 AND 286-293.
[4]"Proteome studies of Saccharomyces cerevisiae: identification and characterization of abundant proteins."
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.
Electrophoresis 18:1347-1360(1997) [PubMed: 9298649] [Abstract]
Cited for: ACETYLATION AT ALA-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: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]"A proteomics approach to understanding protein ubiquitination."
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., Gygi S.P.
Nat. Biotechnol. 21:921-926(2003) [PubMed: 12872131] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-324, MASS SPECTROMETRY.
[7]"A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery."
Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.
Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003) [PubMed: 14557538] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-324, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

M65157 Genomic DNA. Translation: AAA34644.1. Sequence problems.
Z68111 Genomic DNA. Translation: CAA92141.1.
Z71255 Genomic DNA. Translation: CAA94985.1.
Z49274 Genomic DNA. Translation: CAA89289.1.
PIRS61058.

3D structure databases

HSSPHSSP built from PDB template 1LGR based on UniProtKB P06201.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:6699N.
IntActP32288. 105 interactions.

2-D gel databases

SWISS-2DPAGEP32288.

Proteomic databases

PeptideAtlasP32288.
PRIDEP32288.

Genome annotation databases

EnsemblYPR035W. Saccharomyces cerevisiae. [Contig view]
GenomeReviewsGene locus YPR035W in contig U00094_GR.
KEGGsce:YPR035W.

Organism-specific databases

CYGDYPR035w.
SGDS000006239. GLN1.
Yeast-GFPSearch...

Phylogenomic databases

HOGENOMP32288.

Enzyme and pathway databases

BioCycMetaCyc:MON-12439.
BRENDA6.3.1.2. 250.

Gene expression databases

ArrayExpressP32288.
GermOnlineYPR035W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR008147. Gln_synt_beta.
IPR014746. Gln_synth/guanido_kin_cat.
IPR008146. Gln_synth_cat.
[Graphical view]
Gene3DG3DSA:3.30.590.10. ATP-gua_Ptrans. 1 hit.
PfamPF00120. Gln-synt_C. 1 hit.
PF03951. Gln-synt_N. 1 hit.
[Graphical view]
ProDomPD001057. Gln_synt_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00180. GLNA_1. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLNA_YEAST
AccessionPrimary (citable) accession number: P32288
Secondary accession number(s): Q03959
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents