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P15105 (GLNA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamine synthetase

Short name=GS
EC=6.3.1.2
Alternative name(s):
Glutamate decarboxylase
EC=4.1.1.15
Glutamate--ammonia ligase
Gene names
Name:Glul
Synonyms:Glns
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length373 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

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

L-glutamate = 4-aminobutanoate + CO2.

Cofactor

Biotin By similarity.

Magnesium or manganese By similarity.

Subunit structure

Homooctamer and homotetramer. Interacts with PALMD. Ref.7

Subcellular location

Cytoplasm. Mitochondrion By similarity.

Post-translational modification

Ubiquitinated by ZNRF1. Ref.10

Sequence similarities

Belongs to the glutamine synthetase family.

Ontologies

Keywords
   Cellular componentCytoplasm
Mitochondrion
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
Lyase
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell proliferation

Inferred from electronic annotation. Source: Ensembl

cellular response to starvation

Inferred from expression pattern PubMed 23260145. Source: MGI

glutamate metabolic process

Inferred from electronic annotation. Source: Ensembl

glutamine biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of epithelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of insulin secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of synaptic transmission, glutamatergic

Inferred from electronic annotation. Source: Ensembl

protein homooligomerization

Inferred from electronic annotation. Source: Ensembl

response to glucose

Inferred from mutant phenotype PubMed 17854388. Source: MGI

   Cellular_componentaxon terminus

Inferred from electronic annotation. Source: Ensembl

cell body

Inferred from direct assay PubMed 23386608. Source: MGI

cytoplasm

Inferred from direct assay PubMed 12923239. Source: MGI

glial cell projection

Inferred from direct assay PubMed 23386608. Source: MGI

mitochondrion

Inferred from direct assay PubMed 14651853. Source: MGI

perikaryon

Inferred from electronic annotation. Source: Ensembl

protein complex

Inferred from electronic annotation. Source: Ensembl

rough endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glutamate binding

Inferred from electronic annotation. Source: Ensembl

glutamate decarboxylase activity

Inferred from electronic annotation. Source: UniProtKB-EC

glutamate-ammonia ligase activity

Inferred from electronic annotation. Source: UniProtKB-EC

magnesium ion binding

Inferred from electronic annotation. Source: Ensembl

manganese ion binding

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction Ref.7. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 373372Glutamine synthetase
PRO_0000153141

Amino acid modifications

Modified residue21N-acetylalanine Ref.6
Modified residue1041Phosphotyrosine Ref.9

Experimental info

Sequence conflict911K → R in CAA34381. Ref.1
Sequence conflict1111T → S in AAA17989. Ref.2
Sequence conflict1331M → L in BAE37022. Ref.4
Sequence conflict2491G → V in CAA34381. Ref.1
Sequence conflict2691C → W in AAA17989. Ref.2
Sequence conflict2991R → A in CAA34381. Ref.1
Sequence conflict342 – 3432PS → LR in CAA34381. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P15105 [UniParc].

Last modified April 17, 2007. Version 6.
Checksum: 1EC9CDC5D81DE63F

FASTA37342,120
        10         20         30         40         50         60 
MATSASSHLN KGIKQMYMSL PQGEKVQAMY IWVDGTGEGL RCKTRTLDCE PKCVEELPEW 

        70         80         90        100        110        120 
NFDGSSTFQS EGSNSDMYLH PVAMFRDPFR KDPNKLVLCE VFKYNRKPAE TNLRHICKRI 

       130        140        150        160        170        180 
MDMVSNQHPW FGMEQEYTLM GTDGHPFGWP SNGFPGPQGP YYCGVGADKA YGRDIVEAHY 

       190        200        210        220        230        240 
RACLYAGVKI TGTNAEVMPA QWEFQIGPCE GIRMGDHLWI ARFILHRVCE DFGVIATFDP 

       250        260        270        280        290        300 
KPIPGNWNGA GCHTNFSTKA MREENGLKCI EEAIDKLSKR HQYHIRAYDP KGGLDNARRL 

       310        320        330        340        350        360 
TGFHETSNIN DFSAGVANRG ASIRIPRTVG QEKKGYFEDR RPSANCDPYA VTEAIVRTCL 

       370 
LNETGDEPFQ YKN 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS15381.1.
PIRAJMSQ. S04991.
RefSeqNP_032157.2. NM_008131.4.
UniGeneMm.210745.

3D structure databases

ProteinModelPortalP15105.
SMRP15105. Positions 10-365.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199947. 1 interaction.
IntActP15105. 10 interactions.
MINTMINT-1549397.

PTM databases

PhosphoSiteP15105.

2D gel databases

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

Proteomic databases

MaxQBP15105.
PaxDbP15105.
PRIDEP15105.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000086199; ENSMUSP00000083375; ENSMUSG00000026473.
GeneID14645.
KEGGmmu:14645.
UCSCuc007daq.1. mouse.

Organism-specific databases

CTD2752.
MGIMGI:95739. Glul.

Phylogenomic databases

eggNOGCOG0174.
GeneTreeENSGT00390000010047.
HOGENOMHOG000061500.
HOVERGENHBG005847.
InParanoidP15105.
KOK01915.
OMARIPRNVG.
OrthoDBEOG7CZK5G.
PhylomeDBP15105.
TreeFamTF300491.

Gene expression databases

ArrayExpressP15105.
BgeeP15105.
CleanExMM_GLUL.
GenevestigatorP15105.

Family and domain databases

Gene3D3.30.590.10. 1 hit.
InterProIPR008147. 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]
PfamPF00120. Gln-synt_C. 1 hit.
PF03951. Gln-synt_N. 1 hit.
[Graphical view]
SUPFAMSSF54368. SSF54368. 1 hit.
PROSITEPS00180. GLNA_1. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio286500.
PROP15105.
SOURCESearch...

Entry information

Entry nameGLNA_MOUSE
AccessionPrimary (citable) accession number: P15105
Secondary accession number(s): Q3TRK7, Q64432, Q91VC6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 17, 2007
Last modified: July 9, 2014
This is version 131 of the entry and version 6 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot