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P32288

- GLNA_YEAST

UniProt

P32288 - GLNA_YEAST

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
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 4 (21 Sep 2011)
      Previous versions | rss
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    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

    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-SubCell

    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. 39 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.
    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.

    P32288-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAEASIEKTQ ILQKYLELDQ RGRIIAEYVW IDGTGNLRSK GRTLKKRITS    50
    IDQLPEWNFD GSSTNQAPGH DSDIYLKPVA YYPDPFRRGD NIVVLAACYN 100
    NDGTPNKFNH RHEAAKLFAA HKDEEIWFGL EQEYTLFDMY DDVYGWPKGG 150
    YPAPQGPYYC GVGAGKVYAR DMIEAHYRAC LYAGLEISGI NAEVMPSQWE 200
    FQVGPCTGID MGDQLWMARY FLHRVAEEFG IKISFHPKPL KGDWNGAGCH 250
    TNVSTKEMRQ PGGMKYIEQA IEKLSKRHAE HIKLYGSDND MRLTGRHETA 300
    SMTAFSSGVA NRGSSIRIPR SVAKEGYGYF EDRRPASNID PYLVTGIMCE 350
    TVCGAIDNAD MTKEFERESS 370
    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. 39 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.
    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

    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 1, 2014
    This is version 134 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