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Protein

Glutamine synthetase

Gene

Glul

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Protein has several cofactor binding sites:

GO - Molecular functioni

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

GO - Biological processi

  1. cell proliferation Source: MGI
  2. cellular response to starvation Source: MGI
  3. glutamate metabolic process Source: Ensembl
  4. glutamine biosynthetic process Source: InterPro
  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
Complete GO annotation...

Keywords - Molecular functioni

Ligase, Lyase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi6.3.1.2. 3474.
ReactomeiREACT_298432. Astrocytic Glutamate-Glutamine Uptake And Metabolism.
REACT_309077. Amino acid synthesis and interconversion (transamination).

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 Componenti: 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. extracellular vesicular exosome Source: MGI
  5. glial cell projection Source: MGI
  6. mitochondrion Source: MGI
  7. myelin sheath Source: UniProtKB
  8. nucleus Source: MGI
  9. perikaryon Source: Ensembl
  10. protein complex Source: Ensembl
  11. rough endoplasmic reticulum Source: Ensembl
Complete GO annotation...

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
Modified residuei343 – 3431PhosphoserineBy similarity

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

BgeeiP15105.
CleanExiMM_GLUL.
ExpressionAtlasiP15105. baseline and differential.
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

        10         20         30         40         50
MATSASSHLN KGIKQMYMSL PQGEKVQAMY IWVDGTGEGL RCKTRTLDCE
60 70 80 90 100
PKCVEELPEW NFDGSSTFQS EGSNSDMYLH PVAMFRDPFR KDPNKLVLCE
110 120 130 140 150
VFKYNRKPAE TNLRHICKRI MDMVSNQHPW FGMEQEYTLM GTDGHPFGWP
160 170 180 190 200
SNGFPGPQGP YYCGVGADKA YGRDIVEAHY RACLYAGVKI TGTNAEVMPA
210 220 230 240 250
QWEFQIGPCE GIRMGDHLWI ARFILHRVCE DFGVIATFDP KPIPGNWNGA
260 270 280 290 300
GCHTNFSTKA MREENGLKCI EEAIDKLSKR HQYHIRAYDP KGGLDNARRL
310 320 330 340 350
TGFHETSNIN DFSAGVANRG ASIRIPRTVG QEKKGYFEDR RPSANCDPYA
360 370
VTEAIVRTCL LNETGDEPFQ YKN
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 (Ref. 2) Curated
Sequence conflicti133 – 1331M → L in BAE37022 (PubMed:16141072).Curated
Sequence conflicti249 – 2491G → V in CAA34381 (PubMed:2475638).Curated
Sequence conflicti269 – 2691C → W in AAA17989 (Ref. 2) Curated
Sequence conflicti299 – 2991R → A in CAA34381 (PubMed:2475638).Curated
Sequence conflicti342 – 3432PS → LR in CAA34381 (PubMed:2475638).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

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

PTM databases

PhosphoSiteiP15105.

2D gel databases

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

Proteomic databases

MaxQBiP15105.
PaxDbiP15105.
PRIDEiP15105.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi2752.
MGIiMGI:95739. Glul.

Phylogenomic databases

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

Enzyme and pathway databases

BRENDAi6.3.1.2. 3474.
ReactomeiREACT_298432. Astrocytic Glutamate-Glutamine Uptake And Metabolism.
REACT_309077. Amino acid synthesis and interconversion (transamination).

Miscellaneous databases

NextBioi286500.
PROiP15105.
SOURCEiSearch...

Gene expression databases

BgeeiP15105.
CleanExiMM_GLUL.
ExpressionAtlasiP15105. baseline and differential.
GenevestigatoriP15105.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Sequence of a mouse glutamine synthetase cDNA."
    Lindemann A.E., Tempest P.R.
    Submitted (MAR-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 (JUN-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(2004) [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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Colon.
  6. Bienvenut W.V.
    Submitted (JUN-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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PALMD.
  8. Lubec G., Kang S.U., Klug S., Sunyer B., Chen W.-Q.
    Submitted (DEC-2008) 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(2007) [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(2009) [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: April 1, 2015
This is version 138 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.