RAT:GLNA

Species (Taxon ID)	Rattus norvegicus (Rat). (10116)
Gene Name(s)	Glul (synonyms: Glns)
Protein Name(s)	Glutamine synthetase GS Glutamate decarboxylase Glutamate--ammonia ligase
External Links
UniProt	P09606
EMBL	X07921 M29599 M29595 M29596 M29597 M29598 M29579 M91652 BC061559 BC072694
PIR	S01242
RefSeq	NP_058769.4
UniGene	Rn.2204
ProteinModelPortal	P09606
SMR	P09606
BioGrid	247058
IntAct	P09606
MINT	MINT-4578083
PhosphoSite	P09606
World-2DPAGE	0004:P09606
PRIDE	P09606
Ensembl	ENSRNOT00000075480
GeneID	24957
KEGG	rno:24957
CTD	2752
RGD	2710
GeneTree	ENSGT00390000010047
HOVERGEN	HBG005847
InParanoid	P09606
KO	K01915
OMA	RIPRNVG
OrthoDB	EOG7CZK5G
PhylomeDB	P09606
Reactome	REACT_214662 REACT_219617
NextBio	604985
PRO	PR:P09606
Proteomes	UP000002494
Genevestigator	P09606
GO	GO:0043679 GO:0042995 GO:0005737 GO:0070062 GO:0097386 GO:0043231 GO:0005739 GO:0043005 GO:0005634 GO:0043204 GO:0043234 GO:0005791 GO:0005524 GO:0045503 GO:0016595 GO:0004351 GO:0004356 GO:0000287 GO:0030145 GO:0019676 GO:0008283 GO:0009267 GO:0006536 GO:0006542 GO:0042133 GO:0050679 GO:0032024 GO:0051968 GO:0051260 GO:0009749
Gene3D	3.30.590.10
InterPro	IPR008147 IPR014746 IPR008146 IPR027303 IPR027302
Pfam	PF00120 PF03951
SUPFAM	SSF54368
PROSITE	PS00180 PS00181

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
part_of	GO:0005886	plasma membrane	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P15104	C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P15104	C		Seeded From UniProt	complete
enables	GO:0019706	protein-cysteine S-palmitoyltransferase activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P15104	F		Seeded From UniProt	complete
involved_in	GO:1903670	regulation of sprouting angiogenesis	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P15104	P		Seeded From UniProt	complete
involved_in	GO:0018345	protein palmitoylation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P15104	P		Seeded From UniProt	complete
involved_in	GO:0010594	regulation of endothelial cell migration	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P15104	P		Seeded From UniProt	complete
part_of	GO:0043209	myelin sheath	PMID:17960831^[1]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000128)	Seeded From UniProt	complete
involved_in	GO:0051968	positive regulation of synaptic transmission, glutamatergic	PMID:10696145^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051260	protein homooligomerization	PMID:4403443^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051260	protein homooligomerization	PMID:28323^[4]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0050679	positive regulation of epithelial cell proliferation	PMID:9915876^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0045503	dynein light chain binding	PMID:14760703^[6]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:619866	F		Seeded From UniProt	complete
part_of	GO:0043679	axon terminus	PMID:6105901^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
NOT\|part_of	GO:0043679	axon terminus	PMID:31966^[8]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0043231	intracellular membrane-bounded organelle	PMID:37288^[9]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0043231	intracellular membrane-bounded organelle	PMID:28323^[4]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0043204	perikaryon	PMID:31966^[8]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0043204	perikaryon	PMID:1363168^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0043005	neuron projection	PMID:6105901^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0043005	neuron projection	PMID:37288^[9]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
NOT\|part_of	GO:0043005	neuron projection	PMID:31966^[8]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0042995	cell projection	PMID:31966^[8]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:4403443^[3]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:28323^[4]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0032024	positive regulation of insulin secretion	PMID:12575909^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0030145	manganese ion binding	PMID:4403443^[3]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0030145	manganese ion binding	PMID:28323^[4]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0019676	ammonia assimilation cycle	PMID:28323^[4]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0016595	glutamate binding	PMID:4403443^[3]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0016595	glutamate binding	PMID:28323^[4]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0006542	glutamine biosynthetic process	PMID:4403443^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006542	glutamine biosynthetic process	PMID:28323^[4]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006536	glutamate metabolic process	PMID:4403443^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005791	rough endoplasmic reticulum	PMID:31966^[8]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005791	rough endoplasmic reticulum	PMID:1363168^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:9219972^[12]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:4403443^[3]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:28323^[4]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004356	glutamate-ammonia ligase activity	PMID:4403443^[3]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004356	glutamate-ammonia ligase activity	PMID:28323^[4]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0000287	magnesium ion binding	PMID:4403443^[3]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0000287	magnesium ion binding	PMID:28323^[4]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A8YXX4 ensembl:ENSP00000307900	C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A8YXX4 ensembl:ENSP00000307900	C		Seeded From UniProt	complete
involved_in	GO:1903670	regulation of sprouting angiogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P15104 ensembl:ENSP00000307900	P		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P15104 ensembl:ENSP00000307900	F		Seeded From UniProt	complete
enables	GO:0019706	protein-cysteine S-palmitoyltransferase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P15104 ensembl:ENSP00000307900	F		Seeded From UniProt	complete
involved_in	GO:0018345	protein palmitoylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P15104 ensembl:ENSP00000307900	P		Seeded From UniProt	complete
involved_in	GO:0010594	regulation of endothelial cell migration	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P15104 ensembl:ENSP00000307900	P		Seeded From UniProt	complete
involved_in	GO:0008283	cell population proliferation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P15104 ensembl:ENSP00000307900	P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P15104 ensembl:ENSP00000307900	C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P15104 ensembl:ENSP00000307900	C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P15104 ensembl:ENSP00000307900	C		Seeded From UniProt	complete
enables	GO:0004356	glutamate-ammonia ligase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P15104 ensembl:ENSP00000307900	F		Seeded From UniProt	complete
involved_in	GO:1903670	regulation of sprouting angiogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P15105 ensembl:ENSMUSP00000083375	P		Seeded From UniProt	complete
part_of	GO:0097386	glial cell projection	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P15105 ensembl:ENSMUSP00000083375	C		Seeded From UniProt	complete
part_of	GO:0044297	cell body	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P15105 ensembl:ENSMUSP00000083375	C		Seeded From UniProt	complete
involved_in	GO:0010594	regulation of endothelial cell migration	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P15105 ensembl:ENSMUSP00000083375	P		Seeded From UniProt	complete
involved_in	GO:0009749	response to glucose	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P15105 ensembl:ENSMUSP00000083375	P		Seeded From UniProt	complete
involved_in	GO:0009267	cellular response to starvation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P15105 ensembl:ENSMUSP00000083375	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P15105 ensembl:ENSMUSP00000083375	C		Seeded From UniProt	complete
enables	GO:0003824	catalytic activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR014746	F		Seeded From UniProt	complete
enables	GO:0004356	glutamate-ammonia ligase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR008146 InterPro:IPR008147 InterPro:IPR036651	F		Seeded From UniProt	complete
involved_in	GO:0006542	glutamine biosynthetic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR008147 InterPro:IPR036651	P		Seeded From UniProt	complete
involved_in	GO:0006807	nitrogen compound metabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR008146 InterPro:IPR008147 InterPro:IPR036651	P		Seeded From UniProt	complete
enables	GO:0004356	glutamate-ammonia ligase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:6.3.1.2	F		Seeded From UniProt	complete
enables	GO:0019706	protein-cysteine S-palmitoyltransferase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.3.1.225	F		Seeded From UniProt	complete
involved_in	GO:0042133	neurotransmitter metabolic process	PMID:1674354^[13]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0019676	ammonia assimilation cycle	PMID:1674354^[13]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0004356	glutamate-ammonia ligase activity	PMID:1674354^[13]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0256	C		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C		Seeded From UniProt	complete
part_of	GO:0043231	intracellular membrane-bounded organelle	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0492 UniProtKB-SubCell:SL-0166	C		Seeded From UniProt	complete
enables	GO:0016874	ligase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0436	F		Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1003 UniProtKB-SubCell:SL-0039	C		Seeded From UniProt	complete
involved_in	GO:0001525	angiogenesis	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0037	P		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0496 UniProtKB-SubCell:SL-0173	C		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963	C		Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0091	C		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Yamaguchi, Y et al. (2008) Two-dimensional electrophoresis with cationic detergents: a powerful tool for the proteomic analysis of myelin proteins. Part 2: analytical aspects. J. Neurosci. Res. 86 766-75 PubMed GONUTS page
↑ Barnett, NL et al. (2000) Inhibition of Müller cell glutamine synthetase rapidly impairs the retinal response to light. Glia 30 64-73 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 ^3.6 ^3.7 ^3.8 Tate, SS et al. (1972) Rat liver glutamine synthetase. Preparation, properties, and mechanism of inhibition by carbamyl phosphate. J. Biol. Chem. 247 5312-21 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 ^4.3 ^4.4 ^4.5 ^4.6 ^4.7 ^4.8 ^4.9 Deuel, TF et al. (1978) Glutamine synthetase from rat liver. Purification, properties, and preparation of specific antisera. J. Biol. Chem. 253 6111-8 PubMed GONUTS page
↑ DeMarco, V et al. (1999) Inhibition of glutamine synthetase decreases proliferation of cultured rat intestinal epithelial cells. J. Nutr. 129 57-62 PubMed GONUTS page
↑ Navarro-Lérida, I et al. (2004) Proteomic identification of brain proteins that interact with dynein light chain LC8. Proteomics 4 339-46 PubMed GONUTS page
↑ ^7.0 ^7.1 Dennis, SC et al. (1980) The distribution of glutamine synthetase in subcellular fractions of rat brain. Brain Res. 197 469-75 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 ^8.3 ^8.4 Norenberg, MD & Martinez-Hernandez, A (1979) Fine structural localization of glutamine synthetase in astrocytes of rat brain. Brain Res. 161 303-10 PubMed GONUTS page
↑ ^9.0 ^9.1 Ward, HK & Bradford, HF (1979) Relative activities of glutamine synthetase and glutaminase in mammalian synaptosomes. J. Neurochem. 33 339-42 PubMed GONUTS page
↑ ^10.0 ^10.1 Krstić, R & Nicolas, D (1992) Light and electron microscopic immunocytochemical localization of glutamine synthetase in the superficial pineal gland of the rat. Acta Histochem. 93 382-7 PubMed GONUTS page
↑ Schneid, C et al. (2003) Effects of ornithine alpha-ketoglutarate on insulin secretion in rat pancreatic islets: implication of nitric oxide synthase and glutamine synthetase pathways. Br. J. Nutr. 89 249-57 PubMed GONUTS page
↑ Takumi, Y et al. (1997) Discrete cellular and subcellular localization of glutamine synthetase and the glutamate transporter GLAST in the rat vestibular end organ. Neuroscience 79 1137-44 PubMed GONUTS page
↑ ^13.0 ^13.1 ^13.2 Mill, JF et al. (1991) Cloning and functional characterization of the rat glutamine synthetase gene. Brain Res. Mol. Brain Res. 9 197-207 PubMed GONUTS page

[PMID:17960831-1] Yamaguchi, Y et al. (2008) Two-dimensional electrophoresis with cationic detergents: a powerful tool for the proteomic analysis of myelin proteins. Part 2: analytical aspects. J. Neurosci. Res. 86 766-75 PubMed GONUTS page

[PMID:10696145-2] Barnett, NL et al. (2000) Inhibition of Müller cell glutamine synthetase rapidly impairs the retinal response to light. Glia 30 64-73 PubMed GONUTS page

[PMID:4403443-3] 3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 ^3.6 ^3.7 ^3.8 Tate, SS et al. (1972) Rat liver glutamine synthetase. Preparation, properties, and mechanism of inhibition by carbamyl phosphate. J. Biol. Chem. 247 5312-21 PubMed GONUTS page

[PMID:28323-4] 4.0 ^4.1 ^4.2 ^4.3 ^4.4 ^4.5 ^4.6 ^4.7 ^4.8 ^4.9 Deuel, TF et al. (1978) Glutamine synthetase from rat liver. Purification, properties, and preparation of specific antisera. J. Biol. Chem. 253 6111-8 PubMed GONUTS page

[PMID:9915876-5] DeMarco, V et al. (1999) Inhibition of glutamine synthetase decreases proliferation of cultured rat intestinal epithelial cells. J. Nutr. 129 57-62 PubMed GONUTS page

[PMID:14760703-6] Navarro-Lérida, I et al. (2004) Proteomic identification of brain proteins that interact with dynein light chain LC8. Proteomics 4 339-46 PubMed GONUTS page

[PMID:6105901-7] 7.0 ^7.1 Dennis, SC et al. (1980) The distribution of glutamine synthetase in subcellular fractions of rat brain. Brain Res. 197 469-75 PubMed GONUTS page

[PMID:31966-8] 8.0 ^8.1 ^8.2 ^8.3 ^8.4 Norenberg, MD & Martinez-Hernandez, A (1979) Fine structural localization of glutamine synthetase in astrocytes of rat brain. Brain Res. 161 303-10 PubMed GONUTS page

[PMID:37288-9] 9.0 ^9.1 Ward, HK & Bradford, HF (1979) Relative activities of glutamine synthetase and glutaminase in mammalian synaptosomes. J. Neurochem. 33 339-42 PubMed GONUTS page

[PMID:1363168-10] 10.0 ^10.1 Krstić, R & Nicolas, D (1992) Light and electron microscopic immunocytochemical localization of glutamine synthetase in the superficial pineal gland of the rat. Acta Histochem. 93 382-7 PubMed GONUTS page

[PMID:12575909-11] Schneid, C et al. (2003) Effects of ornithine alpha-ketoglutarate on insulin secretion in rat pancreatic islets: implication of nitric oxide synthase and glutamine synthetase pathways. Br. J. Nutr. 89 249-57 PubMed GONUTS page

[PMID:9219972-12] Takumi, Y et al. (1997) Discrete cellular and subcellular localization of glutamine synthetase and the glutamate transporter GLAST in the rat vestibular end organ. Neuroscience 79 1137-44 PubMed GONUTS page

[PMID:1674354-13] 13.0 ^13.1 ^13.2 Mill, JF et al. (1991) Cloning and functional characterization of the rat glutamine synthetase gene. Brain Res. Mol. Brain Res. 9 197-207 PubMed GONUTS page

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RAT:GLNA

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