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Protein

Glutamine synthetase

Gene

GLUL

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Glutamine synthetase that catalyzes the ATP-dependent conversion of glutamate and ammonia to glutamine (PubMed:30158707, PubMed:16267323). Its role depends on tissue localization: in the brain, it regulates the levels of toxic ammonia and converts neurotoxic glutamate to harmless glutamine, whereas in the liver, it is one of the enzymes responsible for the removal of ammonia (By similarity). Essential for proliferation of fetal skin fibroblasts (PubMed:18662667). Independently of its glutamine synthetase activity, required for endothelial cell migration during vascular development: acts by regulating membrane localization and activation of the GTPase RHOJ, possibly by promoting RHOJ palmitoylation (PubMed:30158707). May act as a palmitoyltransferase for RHOJ: able to autopalmitoylate and then transfer the palmitoyl group to RHOJ (PubMed:30158707).By similarity3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+By similarity, Mn2+1 Publication

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Glutamine synthetase activity is inhibited by methionine sulfoximine (MSO).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi134Manganese 1Combined sources1
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei134ATPCombined sources1
Metal bindingi136Manganese 2Combined sources1
Metal bindingi196Manganese 2Combined sources1
Metal bindingi203Manganese 2Combined sources1
Metal bindingi253Manganese 1; via pros nitrogenCombined sources1
Binding sitei319ATPCombined sources1
Binding sitei319L-glutamateBy similarity1
Binding sitei324ATPCombined sources1
Metal bindingi338Manganese 1Combined sources1
Binding sitei340L-glutamateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi203 – 208ATPCombined sources6
Nucleotide bindingi255 – 257ATPCombined sources3
Nucleotide bindingi336 – 338ADPCombined sources3

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionLigase, Transferase
Biological processAngiogenesis
LigandATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:HS06066-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
6.3.1.2 2681

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-210455 Astrocytic Glutamate-Glutamine Uptake And Metabolism
R-HSA-70614 Amino acid synthesis and interconversion (transamination)

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P15104

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Glutamine synthetase2 Publications (EC:6.3.1.21 Publication)
Short name:
GS2 Publications
Alternative name(s):
Glutamate--ammonia ligaseCurated
Palmitoyltransferase GLULCurated (EC:2.3.1.2251 Publication)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:GLUL1 PublicationImported
Synonyms:GLNS
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000135821.16

Human Gene Nomenclature Database

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HGNCi
HGNC:4341 GLUL

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
138290 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P15104

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Endoplasmic reticulum, Membrane, Microsome, Mitochondrion

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Congenital systemic glutamine deficiency (CSGD)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionRare developmental disorder with severe brain malformation resulting in multi-organ failure and neonatal death. Glutamine is largely absent from affected patients serum, urine and cerebrospinal fluid.
See also OMIM:610015
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_026560324R → C in CSGD; reduced glutamine synthetase activity. 1 PublicationCorresponds to variant dbSNP:rs80358214EnsemblClinVar.1
Natural variantiVAR_026561341R → C in CSGD; suggests reduced glutamine synthetase activity. 1 PublicationCorresponds to variant dbSNP:rs80358215EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi209C → A: Reduced ability to mediate autopalmitoylation. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...
DisGeNETi
2752

MalaCards human disease database

More...
MalaCardsi
GLUL
MIMi610015 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000135821

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
71278 Congenital brain dysgenesis due to glutamine synthetase deficiency

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA28743

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4612

Drug and drug target database

More...
DrugBanki
DB06774 Capsaicin
DB01212 Ceftriaxone
DB01119 Diazoxide
DB08794 Ethyl biscoumacetate
DB00142 L-Glutamic Acid
DB00130 L-Glutamine
DB00134 L-Methionine
DB00082 Pegvisomant
DB00466 Picrotoxin

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
GLUL

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001531392 – 373Glutamine synthetaseAdd BLAST372

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylthreonineCombined sources1
Modified residuei104PhosphotyrosineBy similarity1
Modified residuei343PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Palmitoylated; undergoes autopalmitoylation.1 Publication
Ubiquitinated by ZNRF1.By similarity

Keywords - PTMi

Acetylation, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P15104

MaxQB - The MaxQuant DataBase

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MaxQBi
P15104

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P15104

PeptideAtlas

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PeptideAtlasi
P15104

PRoteomics IDEntifications database

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PRIDEi
P15104

ProteomicsDB human proteome resource

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ProteomicsDBi
53107

2D gel databases

REPRODUCTION-2DPAGE

More...
REPRODUCTION-2DPAGEi
IPI00010130

University College Dublin 2-DE Proteome Database

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UCD-2DPAGEi
P15104

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P15104

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P15104

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in endothelial cells.1 Publication

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Expressed during early fetal stages.1 Publication

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By glucocorticoids. Vitamin D and the Wnt signaling pathway inhibit its expression and activity.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000135821 Expressed in 243 organ(s), highest expression level in medial globus pallidus

CleanEx database of gene expression profiles

More...
CleanExi
HS_GLUL

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P15104 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P15104 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB008636
HPA007316
HPA007571

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Decamer; composed of two pentamers (PubMed:18005987). Interacts with PALMD (By similarity). Interacrts with RHOJ (PubMed:30158707).By similarity2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
109014, 38 interactors

Database of interacting proteins

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DIPi
DIP-308N

Protein interaction database and analysis system

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IntActi
P15104, 25 interactors

Molecular INTeraction database

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MINTi
P15104

STRING: functional protein association networks

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STRINGi
9606.ENSP00000307900

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P15104

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1373
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P15104

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P15104

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P15104

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni246 – 247L-glutamate bindingBy similarity2

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the glutamine synthetase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0683 Eukaryota
COG0174 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00390000010047

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000061500

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG005847

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P15104

KEGG Orthology (KO)

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KOi
K01915

Identification of Orthologs from Complete Genome Data

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OMAi
MMPDGVT

Database of Orthologous Groups

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OrthoDBi
EOG091G07E9

Database for complete collections of gene phylogenies

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PhylomeDBi
P15104

TreeFam database of animal gene trees

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TreeFami
TF300491

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.10.20.70, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR008147 Gln_synt_b-grasp
IPR036651 Gln_synt_N
IPR014746 Gln_synth/guanido_kin_cat_dom
IPR008146 Gln_synth_cat_dom
IPR027303 Gln_synth_gly_rich_site
IPR027302 Gln_synth_N_conserv_site

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00120 Gln-synt_C, 1 hit
PF03951 Gln-synt_N, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01230 Gln-synt_C, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF54368 SSF54368, 1 hit
SSF55931 SSF55931, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00180 GLNA_1, 1 hit
PS00181 GLNA_ATP, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P15104-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTTSASSHLN KGIKQVYMSL PQGEKVQAMY IWIDGTGEGL RCKTRTLDSE
60 70 80 90 100
PKCVEELPEW NFDGSSTLQS EGSNSDMYLV PAAMFRDPFR KDPNKLVLCE
110 120 130 140 150
VFKYNRRPAE TNLRHTCKRI MDMVSNQHPW FGMEQEYTLM GTDGHPFGWP
160 170 180 190 200
SNGFPGPQGP YYCGVGADRA YGRDIVEAHY RACLYAGVKI AGTNAEVMPA
210 220 230 240 250
QWEFQIGPCE GISMGDHLWV ARFILHRVCE DFGVIATFDP KPIPGNWNGA
260 270 280 290 300
GCHTNFSTKA MREENGLKYI EEAIEKLSKR HQYHIRAYDP KGGLDNARRL
310 320 330 340 350
TGFHETSNIN DFSAGVANRS ASIRIPRTVG QEKKGYFEDR RPSANCDPFS
360 370
VTEALIRTCL LNETGDEPFQ YKN
Length:373
Mass (Da):42,064
Last modified:January 23, 2007 - v4
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i45390C100924FAF3
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A2R8YDT1A0A2R8YDT1_HUMAN
Glutamine synthetase
GLUL
507Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti7S → Y in AAH31964 (PubMed:15489334).Curated1
Sequence conflicti154F → L in CAD97626 (PubMed:17974005).Curated1
Sequence conflicti155P → T in AAH31964 (PubMed:15489334).Curated1
Sequence conflicti314A → G in CAA68457 (PubMed:2888076).Curated1
Sequence conflicti322 – 323SI → RL in CAA42495 (PubMed:1681907).Curated2
Sequence conflicti347D → E in CAA42495 (PubMed:1681907).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_026560324R → C in CSGD; reduced glutamine synthetase activity. 1 PublicationCorresponds to variant dbSNP:rs80358214EnsemblClinVar.1
Natural variantiVAR_026561341R → C in CSGD; suggests reduced glutamine synthetase activity. 1 PublicationCorresponds to variant dbSNP:rs80358215EnsemblClinVar.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
Y00387 mRNA Translation: CAA68457.1
X59834 mRNA Translation: CAA42495.1
S70290 mRNA Translation: AAB30693.1
AY486122 mRNA Translation: AAS57904.1
AY486123 Genomic DNA Translation: AAS57905.1
BX537384 mRNA Translation: CAD97626.1
AL139344 Genomic DNA No translation available.
BC010037 mRNA Translation: AAH10037.1
BC011700 mRNA Translation: AAH11700.1
BC011852 mRNA Translation: AAH11852.1
BC018992 mRNA Translation: AAH18992.1
BC031964 mRNA Translation: AAH31964.1
BC051726 mRNA Translation: AAH51726.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS1344.1

Protein sequence database of the Protein Information Resource

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PIRi
S18455 AJHUQ

NCBI Reference Sequences

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RefSeqi
NP_001028216.1, NM_001033044.3
NP_001028228.1, NM_001033056.3
NP_002056.2, NM_002065.6
XP_006711341.1, XM_006711278.1

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.132016
Hs.518525

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000311223; ENSP00000307900; ENSG00000135821
ENST00000331872; ENSP00000356537; ENSG00000135821
ENST00000339526; ENSP00000344958; ENSG00000135821
ENST00000417584; ENSP00000398320; ENSG00000135821

Database of genes from NCBI RefSeq genomes

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GeneIDi
2752

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:2752

UCSC genome browser

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UCSCi
uc001gpa.3 human

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Wikipedia

Glutamine synthetase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00387 mRNA Translation: CAA68457.1
X59834 mRNA Translation: CAA42495.1
S70290 mRNA Translation: AAB30693.1
AY486122 mRNA Translation: AAS57904.1
AY486123 Genomic DNA Translation: AAS57905.1
BX537384 mRNA Translation: CAD97626.1
AL139344 Genomic DNA No translation available.
BC010037 mRNA Translation: AAH10037.1
BC011700 mRNA Translation: AAH11700.1
BC011852 mRNA Translation: AAH11852.1
BC018992 mRNA Translation: AAH18992.1
BC031964 mRNA Translation: AAH31964.1
BC051726 mRNA Translation: AAH51726.1
CCDSiCCDS1344.1
PIRiS18455 AJHUQ
RefSeqiNP_001028216.1, NM_001033044.3
NP_001028228.1, NM_001033056.3
NP_002056.2, NM_002065.6
XP_006711341.1, XM_006711278.1
UniGeneiHs.132016
Hs.518525

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2OJWX-ray2.05A/B/C/D/E5-365[»]
2QC8X-ray2.60A/B/C/D/E/F/G/H/I/J5-365[»]
ProteinModelPortaliP15104
SMRiP15104
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109014, 38 interactors
DIPiDIP-308N
IntActiP15104, 25 interactors
MINTiP15104
STRINGi9606.ENSP00000307900

Chemistry databases

BindingDBiP15104
ChEMBLiCHEMBL4612
DrugBankiDB06774 Capsaicin
DB01212 Ceftriaxone
DB01119 Diazoxide
DB08794 Ethyl biscoumacetate
DB00142 L-Glutamic Acid
DB00130 L-Glutamine
DB00134 L-Methionine
DB00082 Pegvisomant
DB00466 Picrotoxin

PTM databases

iPTMnetiP15104
PhosphoSitePlusiP15104

Polymorphism and mutation databases

BioMutaiGLUL

2D gel databases

REPRODUCTION-2DPAGEiIPI00010130
UCD-2DPAGEiP15104

Proteomic databases

EPDiP15104
MaxQBiP15104
PaxDbiP15104
PeptideAtlasiP15104
PRIDEiP15104
ProteomicsDBi53107

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
2752
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000311223; ENSP00000307900; ENSG00000135821
ENST00000331872; ENSP00000356537; ENSG00000135821
ENST00000339526; ENSP00000344958; ENSG00000135821
ENST00000417584; ENSP00000398320; ENSG00000135821
GeneIDi2752
KEGGihsa:2752
UCSCiuc001gpa.3 human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
2752
DisGeNETi2752
EuPathDBiHostDB:ENSG00000135821.16

GeneCards: human genes, protein and diseases

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GeneCardsi
GLUL
HGNCiHGNC:4341 GLUL
HPAiCAB008636
HPA007316
HPA007571
MalaCardsiGLUL
MIMi138290 gene
610015 phenotype
neXtProtiNX_P15104
OpenTargetsiENSG00000135821
Orphaneti71278 Congenital brain dysgenesis due to glutamine synthetase deficiency
PharmGKBiPA28743

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0683 Eukaryota
COG0174 LUCA
GeneTreeiENSGT00390000010047
HOGENOMiHOG000061500
HOVERGENiHBG005847
InParanoidiP15104
KOiK01915
OMAiMMPDGVT
OrthoDBiEOG091G07E9
PhylomeDBiP15104
TreeFamiTF300491

Enzyme and pathway databases

BioCyciMetaCyc:HS06066-MONOMER
BRENDAi6.3.1.2 2681
ReactomeiR-HSA-210455 Astrocytic Glutamate-Glutamine Uptake And Metabolism
R-HSA-70614 Amino acid synthesis and interconversion (transamination)
SABIO-RKiP15104

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
GLUL human
EvolutionaryTraceiP15104

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
2752

Protein Ontology

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PROi
PR:P15104

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000135821 Expressed in 243 organ(s), highest expression level in medial globus pallidus
CleanExiHS_GLUL
ExpressionAtlasiP15104 baseline and differential
GenevisibleiP15104 HS

Family and domain databases

Gene3Di3.10.20.70, 1 hit
InterProiView protein in InterPro
IPR008147 Gln_synt_b-grasp
IPR036651 Gln_synt_N
IPR014746 Gln_synth/guanido_kin_cat_dom
IPR008146 Gln_synth_cat_dom
IPR027303 Gln_synth_gly_rich_site
IPR027302 Gln_synth_N_conserv_site
PfamiView protein in Pfam
PF00120 Gln-synt_C, 1 hit
PF03951 Gln-synt_N, 1 hit
SMARTiView protein in SMART
SM01230 Gln-synt_C, 1 hit
SUPFAMiSSF54368 SSF54368, 1 hit
SSF55931 SSF55931, 1 hit
PROSITEiView protein in PROSITE
PS00180 GLNA_1, 1 hit
PS00181 GLNA_ATP, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiGLNA_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P15104
Secondary accession number(s): Q499Y9
, Q5T9Z1, Q7Z3W4, Q8IZ17
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: December 5, 2018
This is version 203 of the entry and version 4 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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