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P15105

- GLNA_MOUSE

UniProt

P15105 - GLNA_MOUSE

Protein

Glutamine synthetase

Gene

Glul

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 6 (17 Apr 2007)
      Previous versions | rss
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    Functioni

    Essential for proliferation of fetal skin fibroblasts. This enzyme has 2 functions: it catalyzes the production of glutamine and 4-aminobutanoate (gamma-aminobutyric acid, GABA), the latter in a pyridoxal phosphate-independent manner By similarity.By similarity

    Catalytic activityi

    ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine.
    L-glutamate = 4-aminobutanoate + CO2.

    Cofactori

    Biotin.By similarity
    Magnesium or manganese.By similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. glutamate-ammonia ligase activity Source: UniProtKB-EC
    3. glutamate binding Source: Ensembl
    4. glutamate decarboxylase activity Source: UniProtKB-EC
    5. magnesium ion binding Source: Ensembl
    6. manganese ion binding Source: Ensembl
    7. protein binding Source: UniProtKB

    GO - Biological processi

    1. cell proliferation Source: Ensembl
    2. cellular response to starvation Source: MGI
    3. glutamate metabolic process Source: Ensembl
    4. glutamine biosynthetic process Source: Ensembl
    5. positive regulation of epithelial cell proliferation Source: Ensembl
    6. positive regulation of insulin secretion Source: Ensembl
    7. positive regulation of synaptic transmission, glutamatergic Source: Ensembl
    8. protein homooligomerization Source: Ensembl
    9. response to glucose Source: MGI

    Keywords - Molecular functioni

    Ligase, Lyase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamine synthetase (EC:6.3.1.2)
    Short name:
    GS
    Alternative name(s):
    Glutamate decarboxylase (EC:4.1.1.15)
    Glutamate--ammonia ligase
    Gene namesi
    Name:Glul
    Synonyms:Glns
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:95739. Glul.

    Subcellular locationi

    Cytoplasm. Mitochondrion By similarity

    GO - Cellular componenti

    1. axon terminus Source: Ensembl
    2. cell body Source: MGI
    3. cytoplasm Source: MGI
    4. glial cell projection Source: MGI
    5. mitochondrion Source: MGI
    6. perikaryon Source: Ensembl
    7. protein complex Source: Ensembl
    8. rough endoplasmic reticulum Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 373372Glutamine synthetasePRO_0000153141Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei104 – 1041Phosphotyrosine1 Publication

    Post-translational modificationi

    Ubiquitinated by ZNRF1.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP15105.
    PaxDbiP15105.
    PRIDEiP15105.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00626790.
    P15105.
    SWISS-2DPAGEP15105.
    UCD-2DPAGEP15105.

    PTM databases

    PhosphoSiteiP15105.

    Expressioni

    Gene expression databases

    ArrayExpressiP15105.
    BgeeiP15105.
    CleanExiMM_GLUL.
    GenevestigatoriP15105.

    Interactioni

    Subunit structurei

    Homooctamer and homotetramer. Interacts with PALMD.1 Publication

    Protein-protein interaction databases

    BioGridi199947. 1 interaction.
    IntActiP15105. 10 interactions.
    MINTiMINT-1549397.

    Structurei

    3D structure databases

    ProteinModelPortaliP15105.
    SMRiP15105. Positions 10-365.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glutamine synthetase family.Curated

    Phylogenomic databases

    eggNOGiCOG0174.
    GeneTreeiENSGT00390000010047.
    HOGENOMiHOG000061500.
    HOVERGENiHBG005847.
    InParanoidiP15105.
    KOiK01915.
    OMAiRIPRNVG.
    OrthoDBiEOG7CZK5G.
    PhylomeDBiP15105.
    TreeFamiTF300491.

    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.

    P15105-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATSASSHLN KGIKQMYMSL PQGEKVQAMY IWVDGTGEGL RCKTRTLDCE    50
    PKCVEELPEW NFDGSSTFQS EGSNSDMYLH PVAMFRDPFR KDPNKLVLCE 100
    VFKYNRKPAE TNLRHICKRI MDMVSNQHPW FGMEQEYTLM GTDGHPFGWP 150
    SNGFPGPQGP YYCGVGADKA YGRDIVEAHY RACLYAGVKI TGTNAEVMPA 200
    QWEFQIGPCE GIRMGDHLWI ARFILHRVCE DFGVIATFDP KPIPGNWNGA 250
    GCHTNFSTKA MREENGLKCI EEAIDKLSKR HQYHIRAYDP KGGLDNARRL 300
    TGFHETSNIN DFSAGVANRG ASIRIPRTVG QEKKGYFEDR RPSANCDPYA 350
    VTEAIVRTCL LNETGDEPFQ YKN 373
    Length:373
    Mass (Da):42,120
    Last modified:April 17, 2007 - v6
    Checksum:i1EC9CDC5D81DE63F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti91 – 911K → R in CAA34381. (PubMed:2475638)Curated
    Sequence conflicti111 – 1111T → S in AAA17989. 1 PublicationCurated
    Sequence conflicti133 – 1331M → L in BAE37022. (PubMed:16141072)Curated
    Sequence conflicti249 – 2491G → V in CAA34381. (PubMed:2475638)Curated
    Sequence conflicti269 – 2691C → W in AAA17989. 1 PublicationCurated
    Sequence conflicti299 – 2991R → A in CAA34381. (PubMed:2475638)Curated
    Sequence conflicti342 – 3432PS → LR in CAA34381. (PubMed:2475638)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16314 mRNA. Translation: CAA34381.1.
    U09114 mRNA. Translation: AAA17989.1.
    AY044241 mRNA. Translation: AAK95328.1.
    AK159106 mRNA. Translation: BAE34822.1.
    AK160670 mRNA. Translation: BAE35950.1.
    AK162685 mRNA. Translation: BAE37022.1.
    AK168493 mRNA. Translation: BAE40380.1.
    BC015086 mRNA. Translation: AAH15086.1.
    CCDSiCCDS15381.1.
    PIRiS04991. AJMSQ.
    RefSeqiNP_032157.2. NM_008131.4.
    UniGeneiMm.210745.

    Genome annotation databases

    EnsembliENSMUST00000086199; ENSMUSP00000083375; ENSMUSG00000026473.
    GeneIDi14645.
    KEGGimmu:14645.
    UCSCiuc007daq.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16314 mRNA. Translation: CAA34381.1 .
    U09114 mRNA. Translation: AAA17989.1 .
    AY044241 mRNA. Translation: AAK95328.1 .
    AK159106 mRNA. Translation: BAE34822.1 .
    AK160670 mRNA. Translation: BAE35950.1 .
    AK162685 mRNA. Translation: BAE37022.1 .
    AK168493 mRNA. Translation: BAE40380.1 .
    BC015086 mRNA. Translation: AAH15086.1 .
    CCDSi CCDS15381.1.
    PIRi S04991. AJMSQ.
    RefSeqi NP_032157.2. NM_008131.4.
    UniGenei Mm.210745.

    3D structure databases

    ProteinModelPortali P15105.
    SMRi P15105. Positions 10-365.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199947. 1 interaction.
    IntActi P15105. 10 interactions.
    MINTi MINT-1549397.

    PTM databases

    PhosphoSitei P15105.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00626790.
    P15105.
    SWISS-2DPAGE P15105.
    UCD-2DPAGE P15105.

    Proteomic databases

    MaxQBi P15105.
    PaxDbi P15105.
    PRIDEi P15105.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000086199 ; ENSMUSP00000083375 ; ENSMUSG00000026473 .
    GeneIDi 14645.
    KEGGi mmu:14645.
    UCSCi uc007daq.1. mouse.

    Organism-specific databases

    CTDi 2752.
    MGIi MGI:95739. Glul.

    Phylogenomic databases

    eggNOGi COG0174.
    GeneTreei ENSGT00390000010047.
    HOGENOMi HOG000061500.
    HOVERGENi HBG005847.
    InParanoidi P15105.
    KOi K01915.
    OMAi RIPRNVG.
    OrthoDBi EOG7CZK5G.
    PhylomeDBi P15105.
    TreeFami TF300491.

    Miscellaneous databases

    NextBioi 286500.
    PROi P15105.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P15105.
    Bgeei P15105.
    CleanExi MM_GLUL.
    Genevestigatori P15105.

    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. "Mouse glutamine synthetase is encoded by a single gene that can be expressed in a localized fashion."
      Kuo C.F., Darnell J.E. Jr.
      J. Mol. Biol. 208:45-56(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Sequence of a mouse glutamine synthetase cDNA."
      Lindemann A.E., Tempest P.R.
      Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Thymus.
    3. "Glutamine synthetase mRNA in rodents."
      Labruyere W.T., van Hemert F.J., Lamers W.H.
      Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: FVB.
      Tissue: Liver.
    4. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Amnion, Hippocampus and Vagina.
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: FVB/N.
      Tissue: Colon.
    6. Bienvenut W.V.
      Submitted (JUL-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-11; 15-25; 96-103; 174-181; 292-298 AND 341-357, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Liver.
    7. "Molecular characterization and immunohistochemical localization of palmdelphin, a cytosolic isoform of the paralemmin protein family implicated in membrane dynamics."
      Hu B., Petrasch-Parwez E., Laue M.M., Kilimann M.W.
      Eur. J. Cell Biol. 84:853-866(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PALMD.
    8. Lubec G., Kang S.U., Klug S., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 26-41; 46-52; 174-222 AND 341-357, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6 and OF1.
      Tissue: Brain and Hippocampus.
    9. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
      Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
      J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-104, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    10. "Proteasomal degradation of glutamine synthetase regulates schwann cell differentiation."
      Saitoh F., Araki T.
      J. Neurosci. 30:1204-1212(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION.

    Entry informationi

    Entry nameiGLNA_MOUSE
    AccessioniPrimary (citable) accession number: P15105
    Secondary accession number(s): Q3TRK7, Q64432, Q91VC6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 17, 2007
    Last modified: October 1, 2014
    This is version 132 of the entry and version 6 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3