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P17714

- ASNS_MESAU

UniProt

P17714 - ASNS_MESAU

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Protein
Asparagine synthetase [glutamine-hydrolyzing]
Gene
ASNS
Organism
Mesocricetus auratus (Golden hamster)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

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 activity By similarity
Binding sitei97 – 971Glutamine By similarity
Binding sitei256 – 2561ATP; via carbonyl oxygen By similarity
Binding sitei288 – 2881ATP; via amide nitrogen and carbonyl oxygen By similarity
Sitei365 – 3651Important for beta-aspartyl-AMP intermediate formation By similarity

Regions

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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. asparagine synthase (glutamine-hydrolyzing) activity Source: UniProtKB-EC

GO - Biological processi

  1. L-asparagine biosynthetic process Source: UniProtKB-UniPathway
  2. glutamine metabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Amino-acid biosynthesis, Asparagine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

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
OrganismiMesocricetus auratus (Golden hamster)
Taxonomic identifieri10036 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi414 – 4141L → 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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 561560Asparagine synthetase [glutamine-hydrolyzing]
PRO_0000056911Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Structurei

3D structure databases

ProteinModelPortaliP17714.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 191190Glutamine amidotransferase type-2
Add
BLAST
Domaini213 – 536324Asparagine synthetase
Add
BLAST

Region

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

Sequence similaritiesi

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

HOVERGENiHBG003103.

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.

P17714-1 [UniParc]FASTAAdd to Basket

« Hide

MCGIWALFGS DDCLSVQCLS AMKIAHRGPD AFRFENVNGY TNCCFGFHRL    50
AVVDPLFGMQ PIRVKKYPYL WLCYNGEIYN HKALQQRFEF EYQTNVDGEI 100
ILHLYDKGGI EQTICMLDGV FAFILLDTAN KKVFLGRDTY GVRPLFKAMT 150
EDGFLAVCSE AKGLVSLKHS TTPFLKVEPF LPGHYEVLDL KPNGKVASVE 200
MVKYHHCRDE PLHALYDSVE KLFPGFELET VKSNLRILFD NAVRKRLMTD 250
RRIVCLLSGG LDSSLVASSL LKQLKEAQVQ YPLQTFAIGM EDSPDLLAAR 300
KVANYIGSEH HEVLFNSEEG IQALDEVIFS LETYDITTVR ASVGMYLISK 350
YIRKNTDSVV IFSGEGSDEL TQGYIYFHKA PSPEKAEEES ERLLKELYLF 400
DVLRADRTTA AHGLELRVPF LDHRFSSYYL SLPPEMRVPK NGIEKHLLRE 450
TFEDSNLLPK EILWRPKEAF SDGITSVKNS WFKILQDYVE HQVDDAMMAT 500
AAQKFPFNTP KTKEGYFYRQ IFEHHYPGRA DWLTHYWMPK WINATDPSAR 550
TLTHYKSAAK A 561
Length:561
Mass (Da):64,274
Last modified:January 23, 2007 - v3
Checksum:i69DF791ED0FA0EF0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X52130 mRNA. Translation: CAA36375.1.
PIRiS12740. AJHYNG.
RefSeqiNP_001268543.1. NM_001281614.1.

Genome annotation databases

GeneIDi101836926.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X52130 mRNA. Translation: CAA36375.1 .
PIRi S12740. AJHYNG.
RefSeqi NP_001268543.1. NM_001281614.1.

3D structure databases

ProteinModelPortali P17714.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi C44.974.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 101836926.

Organism-specific databases

CTDi 440.

Phylogenomic databases

HOVERGENi HBG003103.

Enzyme and pathway databases

UniPathwayi UPA00134 ; UER00195 .

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. "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.

Entry informationi

Entry nameiASNS_MESAU
AccessioniPrimary (citable) accession number: P17714
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Documents

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

External Data

Dasty 3

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