Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P04773

- GLNA_CRIGR

UniProt

P04773 - GLNA_CRIGR

Protein

Glutamine synthetase

Gene

GLUL

Organism
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

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

    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: UniProtKB-EC
    3. glutamate decarboxylase activity Source: UniProtKB-EC

    GO - Biological processi

    1. glutamine biosynthetic process Source: InterPro

    Keywords - Molecular functioni

    Ligase, Lyase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    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
    OrganismiCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
    Taxonomic identifieri10029 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

    Subcellular locationi

    Cytoplasm By similarity. Mitochondrion By similarity

    GO - Cellular componenti

    1. mitochondrion Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 373372Glutamine synthetasePRO_0000153138Add
    BLAST

    Amino acid modifications

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

    Post-translational modificationi

    Ubiquitinated by ZNRF1.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliP04773.
    SMRiP04773. Positions 3-372.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glutamine synthetase family.Curated

    Phylogenomic databases

    HOVERGENiHBG005847.
    KOiK01915.

    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.

    P04773-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATSASSHLN KGIKQMYMSL PQGEKVQAMY IWVDGTGEGL RCKTRTLDCE    50
    PKCVEELPEW NFDGSSTFQS ESSNSDMYLS PVAMFRDPFR KEPNKLVFCE 100
    VFKYNQKPAE TNLRHTCKRI MDMVSNQHPW FGMEQEYTLL GTDGHPFGWP 150
    SDGFPGPQGL YYCGVGADKA YRRDIMEAHY RACLYAGVKI TGTYAEVKHA 200
    QWEFQIGPCE GIRMGDHLWV ARFILHRVCK DFGVIATFDS KPIPGNWNGA 250
    GCHTNFSTKT MREENGLKHI KEAIEKLSKR HRYHIRAYDP KGGLDNARRL 300
    TGFHKTSNIN DFSAGVADRS ASIRIPRTVG QEKKGYFEAR CPSANCDPFA 350
    VTEAIVRTCL LNETGDQPFQ YKN 373
    Length:373
    Mass (Da):42,320
    Last modified:January 23, 2007 - v4
    Checksum:i611D58CE20FB16CF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti12 – 121G → N in CAA27211. 1 PublicationCurated
    Sequence conflicti18 – 192MS → LC in CAA27211. 1 PublicationCurated
    Sequence conflicti72 – 721S → G in CAA27211. 1 PublicationCurated
    Sequence conflicti91 – 922KE → RD in CAA27211. 1 PublicationCurated
    Sequence conflicti106 – 1061Q → R in CAA27211. 1 PublicationCurated
    Sequence conflicti116 – 1161T → S in CAA27211. 1 PublicationCurated
    Sequence conflicti140 – 1401L → M in CAA27211. 1 PublicationCurated
    Sequence conflicti152 – 1521D → N in CAA27211. 1 PublicationCurated
    Sequence conflicti160 – 1601L → P in CAA27211. 1 PublicationCurated
    Sequence conflicti172 – 1721R → G in CAA27211. 1 PublicationCurated
    Sequence conflicti176 – 1761M → V in CAA27211. 1 PublicationCurated
    Sequence conflicti194 – 1941Y → N in CAA27211. 1 PublicationCurated
    Sequence conflicti198 – 1992KH → MP in CAA27211. 1 PublicationCurated
    Sequence conflicti230 – 2301K → E in CAA27211. 1 PublicationCurated
    Sequence conflicti240 – 2401S → P in CAA27211. 1 PublicationCurated
    Sequence conflicti260 – 2601T → A in CAA27211. 1 PublicationCurated
    Sequence conflicti271 – 2711K → E in CAA27211. 1 PublicationCurated
    Sequence conflicti299 – 2991R → G in CAA27211. 1 PublicationCurated
    Sequence conflicti305 – 3051K → E in CAA27211. 1 PublicationCurated
    Sequence conflicti318 – 3181D → N in CAA27211. 1 PublicationCurated
    Sequence conflicti339 – 3413ARC → DRR in CAA27211. 1 PublicationCurated
    Sequence conflicti367 – 3671Q → E in CAA27211. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03495 mRNA. Translation: CAA27211.1.
    AF150961 mRNA. Translation: AAG43362.1.
    RefSeqiNP_001233699.1. NM_001246770.1.

    Genome annotation databases

    GeneIDi100689337.
    KEGGicge:100689337.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03495 mRNA. Translation: CAA27211.1 .
    AF150961 mRNA. Translation: AAG43362.1 .
    RefSeqi NP_001233699.1. NM_001246770.1.

    3D structure databases

    ProteinModelPortali P04773.
    SMRi P04773. Positions 3-372.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100689337.
    KEGGi cge:100689337.

    Organism-specific databases

    CTDi 2752.

    Phylogenomic databases

    HOVERGENi HBG005847.
    KOi K01915.

    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. "The cloning and nucleotide sequence of cDNA for an amplified glutamine synthetase gene from the Chinese hamster."
      Hayward B.E., Hussain A., Wilson R.H., Lyons A., Woodcock V., McIntosh B., Harris T.J.R.
      Nucleic Acids Res. 14:999-1008(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Ovary.
    2. Tong Y., Wang H.
      Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiGLNA_CRIGR
    AccessioniPrimary (citable) accession number: P04773
    Secondary accession number(s): Q9EQP8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 88 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3