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P49088 (ASNS_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Asparagine synthetase [glutamine-hydrolyzing]
EC=6.3.5.4
Alternative name(s):
Glutamine-dependent asparagine synthetase
Gene names
Name:Asns
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length561 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

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

Pathway

Amino-acid biosynthesis; L-asparagine biosynthesis; L-asparagine from L-aspartate (L-Gln route): step 1/1.

Sequence similarities

Contains 1 asparagine synthetase domain.

Contains 1 glutamine amidotransferase type-2 domain.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Asparagine biosynthesis
   DomainGlutamine amidotransferase
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processasparagine biosynthetic process

Inferred from direct assay. Source: RGD

cellular response to glucose starvation

Inferred from expression pattern. Source: RGD

cellular response to hormone stimulus

Inferred from expression pattern. Source: RGD

glutamine metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

liver development

Inferred from expression pattern. Source: RGD

response to amino acid stimulus

Inferred from expression pattern. Source: RGD

response to follicle-stimulating hormone stimulus

Inferred from expression pattern. Source: RGD

response to light stimulus

Inferred from expression pattern. Source: RGD

response to mechanical stimulus

Inferred from expression pattern. Source: RGD

response to methotrexate

Inferred from expression pattern. Source: RGD

response to toxin

Inferred from expression pattern. Source: RGD

   Cellular componentsoluble fraction

Inferred from direct assay. Source: RGD

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

asparagine synthase (glutamine-hydrolyzing) activity

Inferred from direct assay. Source: RGD

cofactor binding

Inferred from direct assay. Source: RGD

protein homodimerization activity

Inferred from direct assay. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 561560Asparagine synthetase [glutamine-hydrolyzing]
PRO_0000056914

Regions

Domain2 – 191190Glutamine amidotransferase type-2
Domain213 – 536324Asparagine synthetase

Sites

Active site21For GATase activity By similarity

Amino acid modifications

Modified residue3851N6-acetyllysine By similarity
Modified residue4711Phosphoserine By similarity

Experimental info

Sequence conflict3301S → P in AAA77672. Ref.1
Sequence conflict3301S → P in AAA77671. Ref.1
Sequence conflict4911H → Y in AAA77672. Ref.1
Sequence conflict4911H → Y in AAA77671. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P49088 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 6C8C6438F424326F

FASTA56164,247
        10         20         30         40         50         60 
MCGIWALFGS DDCLSVQCLS AMKIAHRGPD AFRFENVNGY TNCCFGFHRL AVVDPLFGMQ 

        70         80         90        100        110        120 
PIRVRKYPYL WLCYNGEIYN HKALQQRFEF EYQTNVDGEI ILHLYDKGGI EKTICMLDGV 

       130        140        150        160        170        180 
FAFILLDTAN KKVFLGRDTY GVRPLFKALT EDGFLAVCSE AKGLVSLKHS TTPFLKVEPF 

       190        200        210        220        230        240 
LPGHYEVLDL KPNGKVASVE MVKYHHCTDE PLHAIYDSVE KLFPGFEIET VKNNLRILFN 

       250        260        270        280        290        300 
NAIKKRLMTD RRIGCLLSGG LDSSLVAASL LKQLKEAQVP YALQTFAIGM EDSPDLLAAR 

       310        320        330        340        350        360 
KVANYIGSEH HEVLFNSEEG IQSLDEVIFS LETYDITTVR ASVGMYLISK YIRKNTDSVV 

       370        380        390        400        410        420 
IFSGEGSDEL TQGYIYFHKA PSPEKAEEES ERLLKELYLF DVLRADRTTA AHGLELRVPF 

       430        440        450        460        470        480 
LDHRFSSYYL SLPPEMRIPK DGIEKHLLRE TFEDSNLLPK EILWRPKEAF SDGITSVKNS 

       490        500        510        520        530        540 
WFKILQDFVE HQVDDAMMSE ASQKFPFNTP QTKEGYYYRQ IFEHHYPGRA DWLTHYWMPK 

       550        560 
WINATDPSAR TLTHYKSTAK A

« Hide

References

« Hide 'large scale' references
[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: 7818476] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U07202 mRNA. Translation: AAA77672.1.
U07201 mRNA. Translation: AAA77671.1.
BC081719 mRNA. Translation: AAH81719.1.
IPIIPI00471908.
PIRS53447.
RefSeqNP_037211.2. NM_013079.2.
UniGeneRn.11172.

3D structure databases

ProteinModelPortalP49088.
ModBaseSearch...

Protein-protein interaction databases

STRINGP49088.

Protein family/group databases

MEROPSC44.974.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000010079; ENSRNOP00000010079; ENSRNOG00000007546.
GeneID25612.
KEGGrno:25612.
NMPDRfig|10116.3.peg.20825.
UCSCNM_013079. rat.

Organism-specific databases

CTD440.
RGD2162. Asns.

Phylogenomic databases

eggNOGroNOG12089.
GeneTreeENSGT00390000001994.
HOVERGENHBG003103.
InParanoidP49088.
OMANYYVASE.
OrthoDBEOG4RV2R2.
PhylomeDBP49088.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13063.

Gene expression databases

ArrayExpressP49088.
GenevestigatorP49088.
GermOnlineENSRNOG00000007546. Rattus norvegicus.

Family and domain databases

InterProIPR006426. Asn_synth_AEB.
IPR001962. Asn_synthase.
IPR000583. GATase_2.
IPR017932. GATase_II.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
KOK01953.
PfamPF00733. Asn_synthase. 1 hit.
PF00310. GATase_2. 1 hit.
[Graphical view]
PIRSFPIRSF001589. Asn_synthetase_glu-h. 1 hit.
TIGRFAMsTIGR01536. Asn_synth_AEB. 1 hit.
PROSITEPS51278. GATASE_TYPE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio607355.

Entry information

Entry nameASNS_RAT
AccessionPrimary (citable) accession number: P49088
Secondary accession number(s): Q66HR8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: November 16, 2011
This is version 88 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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