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P49088

- ASNS_RAT

UniProt

P49088 - ASNS_RAT

Protein

Asparagine synthetase [glutamine-hydrolyzing]

Gene

Asns

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei2 – 21For GATase activityBy similarity
    Binding sitei97 – 971GlutamineBy similarity
    Binding sitei256 – 2561ATP; via carbonyl oxygenBy similarity
    Binding sitei288 – 2881ATP; via amide nitrogen and carbonyl oxygenBy similarity
    Sitei365 – 3651Important for beta-aspartyl-AMP intermediate formationBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi363 – 3642ATPBy similarity

    GO - Molecular functioni

    1. asparagine synthase (glutamine-hydrolyzing) activity Source: RGD
    2. ATP binding Source: UniProtKB-KW
    3. cofactor binding Source: RGD
    4. protein homodimerization activity Source: RGD

    GO - Biological processi

    1. asparagine biosynthetic process Source: RGD
    2. cellular amino acid metabolic process Source: RGD
    3. cellular response to glucose starvation Source: RGD
    4. cellular response to hormone stimulus Source: RGD
    5. glutamine metabolic process Source: UniProtKB-KW
    6. L-asparagine biosynthetic process Source: UniProtKB-UniPathway
    7. liver development Source: RGD
    8. negative regulation of apoptotic process Source: Ensembl
    9. positive regulation of mitotic cell cycle Source: Ensembl
    10. response to amino acid Source: RGD
    11. response to follicle-stimulating hormone Source: RGD
    12. response to light stimulus Source: RGD
    13. response to mechanical stimulus Source: RGD
    14. response to methotrexate Source: RGD
    15. response to nutrient levels Source: RGD
    16. response to toxic substance Source: RGD

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Amino-acid biosynthesis, Asparagine biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-13063.
    ReactomeiREACT_100810. ATF4 activates genes.
    REACT_214662. Amino acid synthesis and interconversion (transamination).
    UniPathwayiUPA00134; UER00195.

    Protein family/group databases

    MEROPSiC44.974.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Asparagine synthetase [glutamine-hydrolyzing] (EC:6.3.5.4)
    Alternative name(s):
    Glutamine-dependent asparagine synthetase
    Gene namesi
    Name:Asns
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 4

    Organism-specific databases

    RGDi2162. Asns.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 561560Asparagine synthetase [glutamine-hydrolyzing]PRO_0000056914Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei385 – 3851N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP49088.
    PRIDEiP49088.

    Expressioni

    Gene expression databases

    GenevestigatoriP49088.

    Interactioni

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000010079.

    Structurei

    3D structure databases

    ProteinModelPortaliP49088.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 191190Glutamine amidotransferase type-2PROSITE-ProRule annotationAdd
    BLAST
    Domaini213 – 536324Asparagine synthetaseAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni49 – 535Glutamine bindingBy similarity
    Regioni75 – 773Glutamine bindingBy similarity

    Sequence similaritiesi

    Contains 1 asparagine synthetase domain.Curated
    Contains 1 glutamine amidotransferase type-2 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Glutamine amidotransferase

    Phylogenomic databases

    eggNOGiCOG0367.
    GeneTreeiENSGT00390000001994.
    HOGENOMiHOG000027493.
    HOVERGENiHBG003103.
    InParanoidiP49088.
    KOiK01953.
    OMAiWMPRWIE.
    OrthoDBiEOG75MVVS.
    PhylomeDBiP49088.
    TreeFamiTF300603.

    Family and domain databases

    Gene3Di3.40.50.620. 1 hit.
    3.60.20.10. 1 hit.
    InterProiIPR006426. Asn_synth_AEB.
    IPR001962. Asn_synthase.
    IPR017932. GATase_2_dom.
    IPR000583. GATase_dom.
    IPR029055. Ntn_hydrolases_N.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view]
    PfamiPF00733. Asn_synthase. 1 hit.
    PF13537. GATase_7. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001589. Asn_synthetase_glu-h. 1 hit.
    SUPFAMiSSF56235. SSF56235. 1 hit.
    TIGRFAMsiTIGR01536. asn_synth_AEB. 1 hit.
    PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P49088-1 [UniParc]FASTAAdd to Basket

    « Hide

    MCGIWALFGS DDCLSVQCLS AMKIAHRGPD AFRFENVNGY TNCCFGFHRL    50
    AVVDPLFGMQ PIRVRKYPYL WLCYNGEIYN HKALQQRFEF EYQTNVDGEI 100
    ILHLYDKGGI EKTICMLDGV FAFILLDTAN KKVFLGRDTY GVRPLFKALT 150
    EDGFLAVCSE AKGLVSLKHS TTPFLKVEPF LPGHYEVLDL KPNGKVASVE 200
    MVKYHHCTDE PLHAIYDSVE KLFPGFEIET VKNNLRILFN NAIKKRLMTD 250
    RRIGCLLSGG LDSSLVAASL LKQLKEAQVP YALQTFAIGM EDSPDLLAAR 300
    KVANYIGSEH HEVLFNSEEG IQSLDEVIFS LETYDITTVR ASVGMYLISK 350
    YIRKNTDSVV IFSGEGSDEL TQGYIYFHKA PSPEKAEEES ERLLKELYLF 400
    DVLRADRTTA AHGLELRVPF LDHRFSSYYL SLPPEMRIPK DGIEKHLLRE 450
    TFEDSNLLPK EILWRPKEAF SDGITSVKNS WFKILQDFVE HQVDDAMMSE 500
    ASQKFPFNTP QTKEGYYYRQ IFEHHYPGRA DWLTHYWMPK WINATDPSAR 550
    TLTHYKSTAK A 561
    Length:561
    Mass (Da):64,247
    Last modified:January 23, 2007 - v3
    Checksum:i6C8C6438F424326F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti330 – 3301S → P in AAA77672. (PubMed:7818476)Curated
    Sequence conflicti330 – 3301S → P in AAA77671. (PubMed:7818476)Curated
    Sequence conflicti491 – 4911H → Y in AAA77672. (PubMed:7818476)Curated
    Sequence conflicti491 – 4911H → Y in AAA77671. (PubMed:7818476)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U07202 mRNA. Translation: AAA77672.1.
    U07201 mRNA. Translation: AAA77671.1.
    BC081719 mRNA. Translation: AAH81719.1.
    PIRiS53447.
    RefSeqiNP_037211.2. NM_013079.2.
    XP_006236151.1. XM_006236089.1.
    UniGeneiRn.11172.

    Genome annotation databases

    EnsembliENSRNOT00000010079; ENSRNOP00000010079; ENSRNOG00000007546.
    GeneIDi25612.
    KEGGirno:25612.
    UCSCiRGD:2162. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U07202 mRNA. Translation: AAA77672.1 .
    U07201 mRNA. Translation: AAA77671.1 .
    BC081719 mRNA. Translation: AAH81719.1 .
    PIRi S53447.
    RefSeqi NP_037211.2. NM_013079.2.
    XP_006236151.1. XM_006236089.1.
    UniGenei Rn.11172.

    3D structure databases

    ProteinModelPortali P49088.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000010079.

    Chemistry

    ChEMBLi CHEMBL2303.

    Protein family/group databases

    MEROPSi C44.974.

    Proteomic databases

    PaxDbi P49088.
    PRIDEi P49088.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000010079 ; ENSRNOP00000010079 ; ENSRNOG00000007546 .
    GeneIDi 25612.
    KEGGi rno:25612.
    UCSCi RGD:2162. rat.

    Organism-specific databases

    CTDi 440.
    RGDi 2162. Asns.

    Phylogenomic databases

    eggNOGi COG0367.
    GeneTreei ENSGT00390000001994.
    HOGENOMi HOG000027493.
    HOVERGENi HBG003103.
    InParanoidi P49088.
    KOi K01953.
    OMAi WMPRWIE.
    OrthoDBi EOG75MVVS.
    PhylomeDBi P49088.
    TreeFami TF300603.

    Enzyme and pathway databases

    UniPathwayi UPA00134 ; UER00195 .
    BioCyci MetaCyc:MONOMER-13063.
    Reactomei REACT_100810. ATF4 activates genes.
    REACT_214662. Amino acid synthesis and interconversion (transamination).

    Miscellaneous databases

    NextBioi 607355.
    PROi P49088.

    Gene expression databases

    Genevestigatori P49088.

    Family and domain databases

    Gene3Di 3.40.50.620. 1 hit.
    3.60.20.10. 1 hit.
    InterProi IPR006426. Asn_synth_AEB.
    IPR001962. Asn_synthase.
    IPR017932. GATase_2_dom.
    IPR000583. GATase_dom.
    IPR029055. Ntn_hydrolases_N.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view ]
    Pfami PF00733. Asn_synthase. 1 hit.
    PF13537. GATase_7. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001589. Asn_synthetase_glu-h. 1 hit.
    SUPFAMi SSF56235. SSF56235. 1 hit.
    TIGRFAMsi TIGR01536. asn_synth_AEB. 1 hit.
    PROSITEi PS51278. GATASE_TYPE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of rat asparagine synthetase and specificity of the amino acid-dependent control of its mRNA content."
      Hutson R.G., Kilberg M.S.
      Biochem. J. 304:745-750(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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: Testis.

    Entry informationi

    Entry nameiASNS_RAT
    AccessioniPrimary (citable) accession number: P49088
    Secondary accession number(s): Q66HR8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 114 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3