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Protein

Glutamine synthetase

Gene

Glul

Organism
Mus musculus (Mouse)
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 (By similarity). 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 (PubMed:25870278). Essential for proliferation of fetal skin fibroblasts (By similarity). Independently of its glutamine synthetase activity, required for endothelial cell migration during vascular development (PubMed:30158707). Involved in angiogenesis by regulating membrane localization and activation of the GTPase RHOJ, possibly by promoting RHOJ palmitoylation (By similarity). May act as a palmitoyltransferase for RHOJ: able to autopalmitoylate and then transfer the palmitoyl group to RHOJ (By similarity).By similarity2 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+By similarity

<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).By similarity

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 1By similarity1
<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 sitei134ATPBy similarity1
Metal bindingi136Manganese 2By similarity1
Metal bindingi196Manganese 2By similarity1
Metal bindingi203Manganese 2By similarity1
Metal bindingi253Manganese 1; via pros nitrogenBy similarity1
Binding sitei319ATPBy similarity1
Binding sitei319L-glutamateBy similarity1
Binding sitei324ATPBy similarity1
Metal bindingi338Manganese 1By similarity1
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 – 208ATPBy similarity6
Nucleotide bindingi255 – 257ATPBy similarity3
Nucleotide bindingi336 – 338ADPBy similarity3

<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

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
6.3.1.2 3474

Reactome - a knowledgebase of biological pathways and processes

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

<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 synthetase1 Publication (EC:6.3.1.2By similarity)
Short name:
Alternative name(s):
Glutamate--ammonia ligaseCurated
Palmitoyltransferase GLULCurated (EC:2.3.1.225By similarity)
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:95739 Glul

<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 describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Embryonic lethality when embryos move from the uterine tube to the uterine environment (PubMed:17557305). Conditional deletion in the liver leads to a marked increase of plasma ammonia levels, causing increased locomotion, impaired fear memory and a slightly reduced life span (PubMed:25870278). Conditional deletion in endothelial cells impairs vessel sprouting during vascular development due to defects in endothelial cell migration (PubMed:30158707).3 Publications

<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 methionineiRemoved1 Publication
<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_00001531412 – 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-acetylalanine1 Publication1
Modified residuei104PhosphotyrosineCombined sources1
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.By similarity
Ubiquitinated by ZNRF1.1 Publication

Keywords - PTMi

Acetylation, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P15105

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P15105

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

More...
PaxDbi
P15105

PeptideAtlas

More...
PeptideAtlasi
P15105

PRoteomics IDEntifications database

More...
PRIDEi
P15105

2D gel databases

REPRODUCTION-2DPAGE

More...
REPRODUCTION-2DPAGEi
IPI00626790
P15105

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

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SWISS-2DPAGEi
P15105

University College Dublin 2-DE Proteome Database

More...
UCD-2DPAGEi
P15105

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P15105

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

More...
PhosphoSitePlusi
P15105

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P15105

<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 microvascular endothelial cells.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000026473 Expressed in 323 organ(s), highest expression level in efferent duct

CleanEx database of gene expression profiles

More...
CleanExi
MM_GLUL

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P15105 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P15105 MM

<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 (By similarity). Interacts with PALMD (PubMed:16323283). Interacrts with RHOJ (By similarity).By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
199947, 11 interactors

Protein interaction database and analysis system

More...
IntActi
P15105, 18 interactors

Molecular INTeraction database

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MINTi
P15105

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000083375

<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

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P15105

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

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SMRi
P15105

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...

<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

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eggNOGi
KOG0683 Eukaryota
COG0174 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000010047

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000061500

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG005847

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P15105

KEGG Orthology (KO)

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KOi
K01915

Identification of Orthologs from Complete Genome Data

More...
OMAi
MMPDGVT

Database of Orthologous Groups

More...
OrthoDBi
EOG091G07E9

Database for complete collections of gene phylogenies

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PhylomeDBi
P15105

TreeFam database of animal gene trees

More...
TreeFami
TF300491

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
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

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

Superfamily database of structural and functional annotation

More...
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 2 potential isoforms that are computationally mapped.Show allAlign All

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
<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:i1EC9CDC5D81DE63F
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 are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
D3Z121D3Z121_MOUSE
Glutamine synthetase
Glul
112Annotation 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>
D3YVK1D3YVK1_MOUSE
Glutamine synthetase
Glul
198Annotation 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 conflicti91K → R in CAA34381 (PubMed:2475638).Curated1
Sequence conflicti111T → S in AAA17989 (Ref. 2) Curated1
Sequence conflicti133M → L in BAE37022 (PubMed:16141072).Curated1
Sequence conflicti249G → V in CAA34381 (PubMed:2475638).Curated1
Sequence conflicti269C → W in AAA17989 (Ref. 2) Curated1
Sequence conflicti299R → A in CAA34381 (PubMed:2475638).Curated1
Sequence conflicti342 – 343PS → LR in CAA34381 (PubMed:2475638).Curated2

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

The Consensus CDS (CCDS) project

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CCDSi
CCDS15381.1

Protein sequence database of the Protein Information Resource

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PIRi
S04991 AJMSQ

NCBI Reference Sequences

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RefSeqi
NP_032157.2, NM_008131.4

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Mm.210745

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000086199; ENSMUSP00000083375; ENSMUSG00000026473

Database of genes from NCBI RefSeq genomes

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GeneIDi
14645

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:14645

UCSC genome browser

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UCSCi
uc007daq.2 mouse

<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

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
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199947, 11 interactors
IntActiP15105, 18 interactors
MINTiP15105
STRINGi10090.ENSMUSP00000083375

PTM databases

iPTMnetiP15105
PhosphoSitePlusiP15105
SwissPalmiP15105

2D gel databases

REPRODUCTION-2DPAGEiIPI00626790
P15105
SWISS-2DPAGEiP15105
UCD-2DPAGEiP15105

Proteomic databases

EPDiP15105
MaxQBiP15105
PaxDbiP15105
PeptideAtlasiP15105
PRIDEiP15105

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000086199; ENSMUSP00000083375; ENSMUSG00000026473
GeneIDi14645
KEGGimmu:14645
UCSCiuc007daq.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
2752
MGIiMGI:95739 Glul

Phylogenomic databases

eggNOGiKOG0683 Eukaryota
COG0174 LUCA
GeneTreeiENSGT00390000010047
HOGENOMiHOG000061500
HOVERGENiHBG005847
InParanoidiP15105
KOiK01915
OMAiMMPDGVT
OrthoDBiEOG091G07E9
PhylomeDBiP15105
TreeFamiTF300491

Enzyme and pathway databases

BRENDAi6.3.1.2 3474
ReactomeiR-MMU-210455 Astrocytic Glutamate-Glutamine Uptake And Metabolism
R-MMU-70614 Amino acid synthesis and interconversion (transamination)

Miscellaneous databases

Protein Ontology

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PROi
PR:P15105

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
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Gene expression databases

BgeeiENSMUSG00000026473 Expressed in 323 organ(s), highest expression level in efferent duct
CleanExiMM_GLUL
ExpressionAtlasiP15105 baseline and differential
GenevisibleiP15105 MM

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
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<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_MOUSE
<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: P15105
Secondary accession number(s): Q3TRK7, Q64432, Q91VC6
<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: April 17, 2007
Last modified: December 5, 2018
This is version 169 of the entry and version 6 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

<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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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