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P32288

- GLNA_YEAST

UniProt

P32288 - GLNA_YEAST

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Protein

Glutamine synthetase

Gene

GLN1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. glutamate-ammonia ligase activity Source: SGD

GO - Biological processi

  1. glutamine biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12439.
YEAST:YPR035W-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamine synthetase (EC:6.3.1.2)
Short name:
GS
Alternative name(s):
Glutamate--ammonia ligase
Gene namesi
Name:GLN1
Ordered Locus Names:YPR035W
ORF Names:YP3085.01, YP9367.15
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XVI

Organism-specific databases

SGDiS000006239. GLN1.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed4 Publications
Chaini2 – 370369Glutamine synthetasePRO_0000153166Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei5 – 51Phosphoserine1 Publication
Cross-linki324 – 324Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP32288.
PaxDbiP32288.
PeptideAtlasiP32288.

2D gel databases

SWISS-2DPAGEP32288.

Expressioni

Gene expression databases

GenevestigatoriP32288.

Interactioni

Subunit structurei

Homooctamer.

Protein-protein interaction databases

BioGridi36213. 40 interactions.
DIPiDIP-6699N.
IntActiP32288. 8 interactions.
MINTiMINT-658171.
STRINGi4932.YPR035W.

Structurei

Secondary structure

1
370
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi24 – 318
Beta strandi33 – 353
Beta strandi37 – 4610
Helixi51 – 533
Beta strandi57 – 593
Turni61 – 655
Beta strandi74 – 8310
Turni85 – 873
Beta strandi92 – 998
Beta strandi103 – 1053
Helixi111 – 12010
Helixi122 – 1243
Beta strandi127 – 13711
Beta strandi141 – 1433
Beta strandi155 – 1573
Turni164 – 1663
Helixi170 – 18314
Beta strandi187 – 1926
Beta strandi198 – 20710
Helixi209 – 22719
Turni228 – 2303
Beta strandi232 – 2343
Beta strandi239 – 2446
Beta strandi248 – 2547
Helixi256 – 2594
Beta strandi260 – 2623
Helixi264 – 27613
Helixi278 – 2836
Helixi289 – 2913
Beta strandi307 – 3104
Beta strandi314 – 3185
Helixi320 – 3256
Beta strandi330 – 3323
Helixi341 – 35313
Turni361 – 3633

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3FKYX-ray2.95A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T1-370[»]
ProteinModelPortaliP32288.
SMRiP32288. Positions 21-366.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32288.

Family & Domainsi

Sequence similaritiesi

Belongs to the glutamine synthetase family.Curated

Phylogenomic databases

eggNOGiCOG0174.
GeneTreeiENSGT00390000010047.
HOGENOMiHOG000061500.
InParanoidiP32288.
KOiK01915.
OMAiDDFPEWS.
OrthoDBiEOG7GTTD8.

Family and domain databases

Gene3Di3.30.590.10. 1 hit.
InterProiIPR008147. Gln_synt_beta.
IPR014746. Gln_synth/guanido_kin_cat_dom.
IPR008146. Gln_synth_cat_dom.
IPR027303. Gln_synth_gly_rich_site.
IPR027302. Gln_synth_N_conserv_site.
[Graphical view]
PfamiPF00120. Gln-synt_C. 1 hit.
PF03951. Gln-synt_N. 1 hit.
[Graphical view]
SUPFAMiSSF54368. SSF54368. 1 hit.
PROSITEiPS00180. GLNA_1. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P32288 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAEASIEKTQ ILQKYLELDQ RGRIIAEYVW IDGTGNLRSK GRTLKKRITS
60 70 80 90 100
IDQLPEWNFD GSSTNQAPGH DSDIYLKPVA YYPDPFRRGD NIVVLAACYN
110 120 130 140 150
NDGTPNKFNH RHEAAKLFAA HKDEEIWFGL EQEYTLFDMY DDVYGWPKGG
160 170 180 190 200
YPAPQGPYYC GVGAGKVYAR DMIEAHYRAC LYAGLEISGI NAEVMPSQWE
210 220 230 240 250
FQVGPCTGID MGDQLWMARY FLHRVAEEFG IKISFHPKPL KGDWNGAGCH
260 270 280 290 300
TNVSTKEMRQ PGGMKYIEQA IEKLSKRHAE HIKLYGSDND MRLTGRHETA
310 320 330 340 350
SMTAFSSGVA NRGSSIRIPR SVAKEGYGYF EDRRPASNID PYLVTGIMCE
360 370
TVCGAIDNAD MTKEFERESS
Length:370
Mass (Da):41,766
Last modified:September 21, 2011 - v4
Checksum:i43139C40E97DB34D
GO

Sequence cautioni

The sequence AAA34644.1 differs from that shown. Reason: The submitted sequence does not correspond to the sequence published in the paper.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti165 – 1651G → D AA sequence (PubMed:2891705)Curated
Sequence conflicti172 – 1721M → V AA sequence (PubMed:2891705)Curated
Sequence conflicti251 – 2511T → A in CAA92141. (PubMed:9169875)Curated
Sequence conflicti251 – 2511T → A in CAA94985. (PubMed:9169875)Curated
Sequence conflicti264 – 2641M → T in CAA92141. (PubMed:9169875)Curated
Sequence conflicti264 – 2641M → T in CAA94985. (PubMed:9169875)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
BK006949 Genomic DNA. Translation: DAA11461.2.
PIRiS61058.
RefSeqiNP_015360.2. NM_001184132.2.

Genome annotation databases

EnsemblFungiiYPR035W; YPR035W; YPR035W.
GeneIDi856147.
KEGGisce:YPR035W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
BK006949 Genomic DNA. Translation: DAA11461.2 .
PIRi S61058.
RefSeqi NP_015360.2. NM_001184132.2.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3FKY X-ray 2.95 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T 1-370 [» ]
ProteinModelPortali P32288.
SMRi P32288. Positions 21-366.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 36213. 40 interactions.
DIPi DIP-6699N.
IntActi P32288. 8 interactions.
MINTi MINT-658171.
STRINGi 4932.YPR035W.

2D gel databases

SWISS-2DPAGE P32288.

Proteomic databases

MaxQBi P32288.
PaxDbi P32288.
PeptideAtlasi P32288.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YPR035W ; YPR035W ; YPR035W .
GeneIDi 856147.
KEGGi sce:YPR035W.

Organism-specific databases

SGDi S000006239. GLN1.

Phylogenomic databases

eggNOGi COG0174.
GeneTreei ENSGT00390000010047.
HOGENOMi HOG000061500.
InParanoidi P32288.
KOi K01915.
OMAi DDFPEWS.
OrthoDBi EOG7GTTD8.

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-12439.
YEAST:YPR035W-MONOMER.

Miscellaneous databases

EvolutionaryTracei P32288.
NextBioi 981271.
PROi P32288.

Gene expression databases

Genevestigatori P32288.

Family and domain databases

Gene3Di 3.30.590.10. 1 hit.
InterProi IPR008147. Gln_synt_beta.
IPR014746. Gln_synth/guanido_kin_cat_dom.
IPR008146. Gln_synth_cat_dom.
IPR027303. Gln_synth_gly_rich_site.
IPR027302. Gln_synth_N_conserv_site.
[Graphical view ]
Pfami PF00120. Gln-synt_C. 1 hit.
PF03951. Gln-synt_N. 1 hit.
[Graphical view ]
SUPFAMi SSF54368. SSF54368. 1 hit.
PROSITEi PS00180. GLNA_1. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 251 AND 264.
    Strain: ATCC 204508 / S288c.
  4. "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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-8; 149-166; 171-178; 220-224 AND 286-293.
  5. "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] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT ALA-2.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-324.
    Strain: SUB592.
  9. "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] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-324.
  10. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
    Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
    Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: YAL6B.
  11. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGLNA_YEAST
AccessioniPrimary (citable) accession number: P32288
Secondary accession number(s): D6W445, Q03959
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: September 21, 2011
Last modified: October 29, 2014
This is version 135 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 346000 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 XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

External Data

Dasty 3