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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 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: UniProtKB-EC
  2. ATP binding Source: UniProtKB-KW

GO - Biological processi

  1. glutamine metabolic process Source: UniProtKB-KW
  2. L-asparagine biosynthetic process Source: UniProtKB-UniPathway
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 – 11RemovedBy similarity
Chaini2 – 561560Asparagine synthetase [glutamine-hydrolyzing]PRO_0000056911Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Structurei

3D structure databases

ProteinModelPortaliP17714.
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

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

        10         20         30         40         50
MCGIWALFGS DDCLSVQCLS AMKIAHRGPD AFRFENVNGY TNCCFGFHRL
60 70 80 90 100
AVVDPLFGMQ PIRVKKYPYL WLCYNGEIYN HKALQQRFEF EYQTNVDGEI
110 120 130 140 150
ILHLYDKGGI EQTICMLDGV FAFILLDTAN KKVFLGRDTY GVRPLFKAMT
160 170 180 190 200
EDGFLAVCSE AKGLVSLKHS TTPFLKVEPF LPGHYEVLDL KPNGKVASVE
210 220 230 240 250
MVKYHHCRDE PLHALYDSVE KLFPGFELET VKSNLRILFD NAVRKRLMTD
260 270 280 290 300
RRIVCLLSGG LDSSLVASSL LKQLKEAQVQ YPLQTFAIGM EDSPDLLAAR
310 320 330 340 350
KVANYIGSEH HEVLFNSEEG IQALDEVIFS LETYDITTVR ASVGMYLISK
360 370 380 390 400
YIRKNTDSVV IFSGEGSDEL TQGYIYFHKA PSPEKAEEES ERLLKELYLF
410 420 430 440 450
DVLRADRTTA AHGLELRVPF LDHRFSSYYL SLPPEMRVPK NGIEKHLLRE
460 470 480 490 500
TFEDSNLLPK EILWRPKEAF SDGITSVKNS WFKILQDYVE HQVDDAMMAT
510 520 530 540 550
AAQKFPFNTP KTKEGYFYRQ IFEHHYPGRA DWLTHYWMPK WINATDPSAR
560
TLTHYKSAAK A
Length:561
Mass (Da):64,274
Last modified:January 23, 2007 - v3
Checksum:i69DF791ED0FA0EF0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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: October 1, 2014
This is version 90 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