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P49088 (ASNS_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processL-asparagine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

asparagine biosynthetic process

Inferred from direct assay PubMed 2887559. Source: RGD

cellular amino acid metabolic process

Inferred from expression pattern Ref.1. Source: RGD

cellular response to glucose starvation

Inferred from expression pattern PubMed 10085239. Source: RGD

cellular response to hormone stimulus

Inferred from expression pattern PubMed 1543496. Source: RGD

glutamine metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

liver development

Inferred from expression pattern PubMed 237754. Source: RGD

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

response to amino acid

Inferred from expression pattern PubMed 9176161. Source: RGD

response to follicle-stimulating hormone

Inferred from expression pattern PubMed 7915898. Source: RGD

response to light stimulus

Inferred from expression pattern PubMed 16885923. Source: RGD

response to mechanical stimulus

Inferred from expression pattern PubMed 16864689. Source: RGD

response to methotrexate

Inferred from expression pattern PubMed 6122150. Source: RGD

response to nutrient levels

Inferred from expression pattern PubMed 6104809. Source: RGD

response to toxic substance

Inferred from expression pattern PubMed 18164361. Source: RGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

asparagine synthase (glutamine-hydrolyzing) activity

Inferred from direct assay PubMed 6132621. Source: RGD

cofactor binding

Inferred from direct assay PubMed 2859838. Source: RGD

protein homodimerization activity

Inferred from direct assay PubMed 6132621. 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
Nucleotide binding363 – 3642ATP By similarity
Region49 – 535Glutamine binding By similarity
Region75 – 773Glutamine binding By similarity

Sites

Active site21For GATase activity By similarity
Binding site971Glutamine By similarity
Binding site2561ATP; via carbonyl oxygen By similarity
Binding site2881ATP; via amide nitrogen and carbonyl oxygen By similarity
Site3651Important for beta-aspartyl-AMP intermediate formation By similarity

Amino acid modifications

Modified residue3851N6-acetyllysine 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] [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.
+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.
PIRS53447.
RefSeqNP_037211.2. NM_013079.2.
XP_006236151.1. XM_006236089.1.
UniGeneRn.11172.

3D structure databases

ProteinModelPortalP49088.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000010079.

Chemistry

ChEMBLCHEMBL2303.

Protein family/group databases

MEROPSC44.974.

Proteomic databases

PaxDbP49088.
PRIDEP49088.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000010079; ENSRNOP00000010079; ENSRNOG00000007546.
GeneID25612.
KEGGrno:25612.
UCSCRGD:2162. rat.

Organism-specific databases

CTD440.
RGD2162. Asns.

Phylogenomic databases

eggNOGCOG0367.
GeneTreeENSGT00390000001994.
HOGENOMHOG000027493.
HOVERGENHBG003103.
InParanoidP49088.
KOK01953.
OMAWMPRWIE.
OrthoDBEOG75MVVS.
PhylomeDBP49088.
TreeFamTF300603.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13063.
UniPathwayUPA00134; UER00195.

Gene expression databases

GenevestigatorP49088.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
3.60.20.10. 1 hit.
InterProIPR006426. 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]
PfamPF00733. Asn_synthase. 1 hit.
PF13537. GATase_7. 1 hit.
[Graphical view]
PIRSFPIRSF001589. Asn_synthetase_glu-h. 1 hit.
SUPFAMSSF56235. SSF56235. 1 hit.
TIGRFAMsTIGR01536. asn_synth_AEB. 1 hit.
PROSITEPS51278. GATASE_TYPE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio607355.
PROP49088.

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: June 11, 2014
This is version 112 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways