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P17714 (ASNS_MESAU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 89. 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
OrganismMesocricetus auratus (Golden hamster)
Taxonomic identifier10036 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

Protein attributes

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

Miscellaneous

The temperature-sensitive mutation affecting G1 progression results from a single amino acid substitution.

Sequence similarities

Contains 1 asparagine synthetase domain.

Contains 1 glutamine amidotransferase type-2 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 561560Asparagine synthetase [glutamine-hydrolyzing]
PRO_0000056911

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

Mutagenesis4141L → F in ts11; temperature-sensitive. Blocked in the G1 phase of the cell cycle at the non-permissive temperature (39.5 degrees Celsius). Heat labile.

Sequences

Sequence LengthMass (Da)Tools
P17714 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 69DF791ED0FA0EF0

FASTA56164,274
        10         20         30         40         50         60 
MCGIWALFGS DDCLSVQCLS AMKIAHRGPD AFRFENVNGY TNCCFGFHRL AVVDPLFGMQ 

        70         80         90        100        110        120 
PIRVKKYPYL WLCYNGEIYN HKALQQRFEF EYQTNVDGEI ILHLYDKGGI EQTICMLDGV 

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

       190        200        210        220        230        240 
LPGHYEVLDL KPNGKVASVE MVKYHHCRDE PLHALYDSVE KLFPGFELET VKSNLRILFD 

       250        260        270        280        290        300 
NAVRKRLMTD RRIVCLLSGG LDSSLVASSL LKQLKEAQVQ YPLQTFAIGM EDSPDLLAAR 

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

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

       430        440        450        460        470        480 
LDHRFSSYYL SLPPEMRVPK NGIEKHLLRE TFEDSNLLPK EILWRPKEAF SDGITSVKNS 

       490        500        510        520        530        540 
WFKILQDYVE HQVDDAMMAT AAQKFPFNTP KTKEGYFYRQ IFEHHYPGRA DWLTHYWMPK 

       550        560 
WINATDPSAR TLTHYKSAAK A 

« Hide

References

[1]"A mammalian temperature-sensitive mutation affecting G1 progression results from a single amino acid substitution in asparagine synthetase."
Gong S.S., Basilico C.
Nucleic Acids Res. 18:3509-3513(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTANTS TS11.
Strain: Syrian.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X52130 mRNA. Translation: CAA36375.1.
PIRAJHYNG. S12740.
RefSeqNP_001268543.1. NM_001281614.1.

3D structure databases

ProteinModelPortalP17714.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSC44.974.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID101836926.

Organism-specific databases

CTD440.

Phylogenomic databases

HOVERGENHBG003103.

Enzyme and pathway databases

UniPathwayUPA00134; UER00195.

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...

Entry information

Entry nameASNS_MESAU
AccessionPrimary (citable) accession number: P17714
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 89 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