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P15104

- GLNA_HUMAN

UniProt

P15104 - GLNA_HUMAN

Protein

Glutamine synthetase

Gene

GLUL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 162 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    This enzyme has 2 functions: it catalyzes the production of glutamine and 4-aminobutanoate (gamma-aminobutyric acid, GABA), the latter in a pyridoxal phosphate-independent manner By similarity. Essential for proliferation of fetal skin fibroblasts.By similarity1 Publication

    Catalytic activityi

    ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine.
    L-glutamate = 4-aminobutanoate + CO2.

    Cofactori

    Biotin.By similarity
    Magnesium or manganese.By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. cell proliferation Source: UniProtKB
    2. cellular amino acid biosynthetic process Source: Reactome
    3. cellular nitrogen compound metabolic process Source: Reactome
    4. glutamate catabolic process Source: BHF-UCL
    5. glutamine biosynthetic process Source: BHF-UCL
    6. neurotransmitter uptake Source: Reactome
    7. positive regulation of epithelial cell proliferation Source: Ensembl
    8. positive regulation of insulin secretion Source: Ensembl
    9. positive regulation of synaptic transmission, glutamatergic Source: Ensembl
    10. protein homooligomerization Source: Ensembl
    11. response to glucose Source: Ensembl
    12. small molecule metabolic process Source: Reactome
    13. synaptic transmission Source: Reactome

    Keywords - Molecular functioni

    Ligase, Lyase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS06066-MONOMER.
    ReactomeiREACT_13639. Astrocytic Glutamate-Glutamine Uptake And Metabolism.
    REACT_238. Amino acid synthesis and interconversion (transamination).
    SABIO-RKP15104.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamine synthetase (EC:6.3.1.2)
    Short name:
    GS
    Alternative name(s):
    Glutamate decarboxylase (EC:4.1.1.15)
    Glutamate--ammonia ligase
    Gene namesi
    Name:GLUL
    Synonyms:GLNS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:4341. GLUL.

    Subcellular locationi

    Cytoplasm. Mitochondrion By similarity

    GO - Cellular componenti

    1. axon terminus Source: Ensembl
    2. cytoplasm Source: HPA
    3. cytosol Source: Reactome
    4. extracellular vesicular exosome Source: UniProt
    5. mitochondrion Source: UniProtKB-SubCell
    6. nucleus Source: UniProt
    7. perikaryon Source: Ensembl
    8. protein complex Source: Ensembl
    9. rough endoplasmic reticulum Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Congenital systemic glutamine deficiency (CSGD) [MIM:610015]: Rare 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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti324 – 3241R → C in CSGD; reduced glutamine synthetase activity. 1 Publication
    VAR_026560
    Natural varianti341 – 3411R → C in CSGD; suggests reduced glutamine synthetase activity. 1 Publication
    VAR_026561

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi610015. phenotype.
    Orphaneti71278. Congenital brain dysgenesis due to glutamine synthetase deficiency.
    PharmGKBiPA28743.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 373372Glutamine synthetasePRO_0000153139Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylthreonine1 Publication
    Modified residuei104 – 1041PhosphotyrosineBy similarity

    Post-translational modificationi

    Ubiquitinated by ZNRF1.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP15104.
    PaxDbiP15104.
    PeptideAtlasiP15104.
    PRIDEiP15104.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00010130.
    UCD-2DPAGEP15104.

    PTM databases

    PhosphoSiteiP15104.

    Expressioni

    Developmental stagei

    Expressed during early fetal stages.1 Publication

    Inductioni

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

    Gene expression databases

    ArrayExpressiP15104.
    BgeeiP15104.
    CleanExiHS_GLUL.
    GenevestigatoriP15104.

    Organism-specific databases

    HPAiCAB008636.
    HPA007316.
    HPA007571.

    Interactioni

    Subunit structurei

    Homooctamer and homotetramer. Interacts with PALMD By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-746653,EBI-746653

    Protein-protein interaction databases

    BioGridi109014. 20 interactions.
    DIPiDIP-308N.
    IntActiP15104. 18 interactions.
    MINTiMINT-1183856.
    STRINGi9606.ENSP00000307900.

    Structurei

    Secondary structure

    1
    373
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 84
    Helixi11 – 188
    Beta strandi26 – 338
    Beta strandi40 – 4910
    Helixi54 – 563
    Beta strandi60 – 634
    Turni64 – 685
    Beta strandi69 – 713
    Helixi72 – 743
    Beta strandi76 – 8611
    Turni88 – 903
    Beta strandi95 – 1028
    Beta strandi106 – 1083
    Helixi114 – 12310
    Helixi124 – 1274
    Beta strandi130 – 14011
    Beta strandi144 – 1463
    Beta strandi158 – 1603
    Turni167 – 1693
    Helixi173 – 18614
    Beta strandi190 – 1956
    Beta strandi201 – 21010
    Helixi213 – 23220
    Beta strandi235 – 2373
    Beta strandi245 – 2473
    Beta strandi251 – 2577
    Helixi259 – 2624
    Turni264 – 2663
    Helixi267 – 27812
    Helixi281 – 2877
    Turni290 – 2956
    Helixi296 – 2983
    Beta strandi314 – 3163
    Beta strandi321 – 3255
    Helixi327 – 3326
    Beta strandi337 – 3393
    Helixi348 – 35912

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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. Positions 10-365.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP15104.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glutamine synthetase family.Curated

    Phylogenomic databases

    eggNOGiCOG0174.
    HOGENOMiHOG000061500.
    HOVERGENiHBG005847.
    InParanoidiP15104.
    KOiK01915.
    OMAiRIPRNVG.
    OrthoDBiEOG7CZK5G.
    PhylomeDBiP15104.
    TreeFamiTF300491.

    Family and domain databases

    Gene3Di3.30.590.10. 1 hit.
    InterProiIPR008147. Gln_synt_beta.
    IPR014746. Gln_synth/guanido_kin_cat_dom.
    IPR008146. Gln_synth_cat_dom.
    IPR027303. Gln_synth_gly_rich_site.
    IPR027302. Gln_synth_N_conserv_site.
    [Graphical view]
    PfamiPF00120. Gln-synt_C. 1 hit.
    PF03951. Gln-synt_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF54368. SSF54368. 1 hit.
    PROSITEiPS00180. GLNA_1. 1 hit.
    PS00181. GLNA_ATP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P15104-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTTSASSHLN KGIKQVYMSL PQGEKVQAMY IWIDGTGEGL RCKTRTLDSE    50
    PKCVEELPEW NFDGSSTLQS EGSNSDMYLV PAAMFRDPFR KDPNKLVLCE 100
    VFKYNRRPAE TNLRHTCKRI MDMVSNQHPW FGMEQEYTLM GTDGHPFGWP 150
    SNGFPGPQGP YYCGVGADRA YGRDIVEAHY RACLYAGVKI AGTNAEVMPA 200
    QWEFQIGPCE GISMGDHLWV ARFILHRVCE DFGVIATFDP KPIPGNWNGA 250
    GCHTNFSTKA MREENGLKYI EEAIEKLSKR HQYHIRAYDP KGGLDNARRL 300
    TGFHETSNIN DFSAGVANRS ASIRIPRTVG QEKKGYFEDR RPSANCDPFS 350
    VTEALIRTCL LNETGDEPFQ YKN 373
    Length:373
    Mass (Da):42,064
    Last modified:January 23, 2007 - v4
    Checksum:i45390C100924FAF3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti7 – 71S → Y in AAH31964. (PubMed:15489334)Curated
    Sequence conflicti154 – 1541F → L in CAD97626. (PubMed:17974005)Curated
    Sequence conflicti155 – 1551P → T in AAH31964. (PubMed:15489334)Curated
    Sequence conflicti314 – 3141A → G in CAA68457. (PubMed:2888076)Curated
    Sequence conflicti322 – 3232SI → RL in CAA42495. (PubMed:1681907)Curated
    Sequence conflicti347 – 3471D → E in CAA42495. (PubMed:1681907)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti324 – 3241R → C in CSGD; reduced glutamine synthetase activity. 1 Publication
    VAR_026560
    Natural varianti341 – 3411R → C in CSGD; suggests reduced glutamine synthetase activity. 1 Publication
    VAR_026561

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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. Translation: CAI19842.1.
    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_001033044.2.
    NP_001028228.1. NM_001033056.2.
    NP_002056.2. NM_002065.5.
    XP_006711341.1. XM_006711278.1.
    UniGeneiHs.518525.

    Genome annotation databases

    EnsembliENST00000311223; ENSP00000307900; ENSG00000135821.
    ENST00000331872; ENSP00000356537; ENSG00000135821.
    ENST00000339526; ENSP00000344958; ENSG00000135821.
    ENST00000417584; ENSP00000398320; ENSG00000135821.
    GeneIDi2752.
    KEGGihsa:2752.
    UCSCiuc001gpa.2. human.

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Glutamine synthetase entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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. Translation: CAI19842.1 .
    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 .
    CCDSi CCDS1344.1.
    PIRi S18455. AJHUQ.
    RefSeqi NP_001028216.1. NM_001033044.2.
    NP_001028228.1. NM_001033056.2.
    NP_002056.2. NM_002065.5.
    XP_006711341.1. XM_006711278.1.
    UniGenei Hs.518525.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2OJW X-ray 2.05 A/B/C/D/E 5-365 [» ]
    2QC8 X-ray 2.60 A/B/C/D/E/F/G/H/I/J 5-365 [» ]
    ProteinModelPortali P15104.
    SMRi P15104. Positions 10-365.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109014. 20 interactions.
    DIPi DIP-308N.
    IntActi P15104. 18 interactions.
    MINTi MINT-1183856.
    STRINGi 9606.ENSP00000307900.

    Chemistry

    BindingDBi P15104.
    ChEMBLi CHEMBL4612.
    DrugBanki DB00023. Asparaginase.
    DB00142. L-Glutamic Acid.
    DB00130. L-Glutamine.
    DB00134. L-Methionine.

    PTM databases

    PhosphoSitei P15104.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00010130.
    UCD-2DPAGE P15104.

    Proteomic databases

    MaxQBi P15104.
    PaxDbi P15104.
    PeptideAtlasi P15104.
    PRIDEi P15104.

    Protocols and materials databases

    DNASUi 2752.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000311223 ; ENSP00000307900 ; ENSG00000135821 .
    ENST00000331872 ; ENSP00000356537 ; ENSG00000135821 .
    ENST00000339526 ; ENSP00000344958 ; ENSG00000135821 .
    ENST00000417584 ; ENSP00000398320 ; ENSG00000135821 .
    GeneIDi 2752.
    KEGGi hsa:2752.
    UCSCi uc001gpa.2. human.

    Organism-specific databases

    CTDi 2752.
    GeneCardsi GC01M182350.
    HGNCi HGNC:4341. GLUL.
    HPAi CAB008636.
    HPA007316.
    HPA007571.
    MIMi 138290. gene.
    610015. phenotype.
    neXtProti NX_P15104.
    Orphaneti 71278. Congenital brain dysgenesis due to glutamine synthetase deficiency.
    PharmGKBi PA28743.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0174.
    HOGENOMi HOG000061500.
    HOVERGENi HBG005847.
    InParanoidi P15104.
    KOi K01915.
    OMAi RIPRNVG.
    OrthoDBi EOG7CZK5G.
    PhylomeDBi P15104.
    TreeFami TF300491.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS06066-MONOMER.
    Reactomei REACT_13639. Astrocytic Glutamate-Glutamine Uptake And Metabolism.
    REACT_238. Amino acid synthesis and interconversion (transamination).
    SABIO-RK P15104.

    Miscellaneous databases

    ChiTaRSi GLUL. human.
    EvolutionaryTracei P15104.
    GenomeRNAii 2752.
    NextBioi 10840.
    PROi P15104.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P15104.
    Bgeei P15104.
    CleanExi HS_GLUL.
    Genevestigatori P15104.

    Family and domain databases

    Gene3Di 3.30.590.10. 1 hit.
    InterProi IPR008147. Gln_synt_beta.
    IPR014746. Gln_synth/guanido_kin_cat_dom.
    IPR008146. Gln_synth_cat_dom.
    IPR027303. Gln_synth_gly_rich_site.
    IPR027302. Gln_synth_N_conserv_site.
    [Graphical view ]
    Pfami PF00120. Gln-synt_C. 1 hit.
    PF03951. Gln-synt_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54368. SSF54368. 1 hit.
    PROSITEi PS00180. GLNA_1. 1 hit.
    PS00181. GLNA_ATP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    3. "Overexpression of glutamine synthetase in human primary liver cancer."
      Christa L., Simon M.T., Flinois J.P., Gebhardt R., Brechot C., Lasserre C.
      Gastroenterology 106:1312-1320(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    4. Haberle J., Koch H.G.
      Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Retina.
    6. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain, Colon, Eye, Muscle and Testis.
    8. "Glutamine synthetase isolated from human brain: octameric structure and homology of partial primary structure with human liver glutamine synthetase."
      Boksha I.S., Schonfeld H.J., Langen H., Muller F., Tereshkina E.B., Burbaeva G.S.H.
      Biochemistry (Mosc.) 67:1012-1020(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain.
    9. "Glutamine synthetase is essential for proliferation of fetal skin fibroblasts."
      Vermeulen T., Goerg B., Vogl T., Wolf M., Varga G., Toutain A., Paul R., Schliess F., Haeussinger D., Haeberle J.
      Arch. Biochem. Biophys. 478:96-102(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DEVELOPMENTAL STAGE.
    10. "Wnt and steroid pathways control glutamate signalling by regulating glutamine synthetase activity in osteoblastic cells."
      Olkku A., Mahonen A.
      Bone 43:483-493(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: VARIANTS CSGD CYS-324 AND CYS-341, CHARACTERIZATION OF VARIANTS CSGD CYS-324 AND CYS-341.

    Entry informationi

    Entry nameiGLNA_HUMAN
    AccessioniPrimary (citable) accession number: P15104
    Secondary accession number(s): Q499Y9
    , Q5T9Z1, Q7Z3W4, Q8IZ17
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 162 of the entry and version 4 of the sequence. [Complete history]
    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.

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

    External Data

    Dasty 3