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Protein

Asparagine synthetase [glutamine-hydrolyzing]

Gene

Asns

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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: RGD
  2. ATP binding Source: UniProtKB-KW
  3. cofactor binding Source: RGD
  4. protein homodimerization activity Source: RGD

GO - Biological processi

  1. asparagine biosynthetic process Source: RGD
  2. cellular amino acid metabolic process Source: RGD
  3. cellular response to glucose starvation Source: RGD
  4. cellular response to hormone stimulus Source: RGD
  5. glutamine metabolic process Source: UniProtKB-KW
  6. L-asparagine biosynthetic process Source: UniProtKB-UniPathway
  7. liver development Source: RGD
  8. negative regulation of apoptotic process Source: Ensembl
  9. positive regulation of mitotic cell cycle Source: Ensembl
  10. response to amino acid Source: RGD
  11. response to follicle-stimulating hormone Source: RGD
  12. response to light stimulus Source: RGD
  13. response to mechanical stimulus Source: RGD
  14. response to methotrexate Source: RGD
  15. response to nutrient levels Source: RGD
  16. response to toxic substance Source: RGD
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

BioCyciMetaCyc:MONOMER-13063.
ReactomeiREACT_292751. Amino acid synthesis and interconversion (transamination).
UniPathwayiUPA00134; UER00195.

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 4

Organism-specific databases

RGDi2162. Asns.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 561560Asparagine synthetase [glutamine-hydrolyzing]PRO_0000056914Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP49088.
PRIDEiP49088.

Expressioni

Gene expression databases

GenevestigatoriP49088.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000010079.

Structurei

3D structure databases

ProteinModelPortaliP49088.
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

eggNOGiCOG0367.
GeneTreeiENSGT00390000001994.
HOGENOMiHOG000027493.
HOVERGENiHBG003103.
InParanoidiP49088.
KOiK01953.
OMAiDWSGIYS.
OrthoDBiEOG75MVVS.
PhylomeDBiP49088.
TreeFamiTF300603.

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]
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.

P49088-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCGIWALFGS DDCLSVQCLS AMKIAHRGPD AFRFENVNGY TNCCFGFHRL
60 70 80 90 100
AVVDPLFGMQ PIRVRKYPYL WLCYNGEIYN HKALQQRFEF EYQTNVDGEI
110 120 130 140 150
ILHLYDKGGI EKTICMLDGV FAFILLDTAN KKVFLGRDTY GVRPLFKALT
160 170 180 190 200
EDGFLAVCSE AKGLVSLKHS TTPFLKVEPF LPGHYEVLDL KPNGKVASVE
210 220 230 240 250
MVKYHHCTDE PLHAIYDSVE KLFPGFEIET VKNNLRILFN NAIKKRLMTD
260 270 280 290 300
RRIGCLLSGG LDSSLVAASL LKQLKEAQVP YALQTFAIGM EDSPDLLAAR
310 320 330 340 350
KVANYIGSEH HEVLFNSEEG IQSLDEVIFS LETYDITTVR ASVGMYLISK
360 370 380 390 400
YIRKNTDSVV IFSGEGSDEL TQGYIYFHKA PSPEKAEEES ERLLKELYLF
410 420 430 440 450
DVLRADRTTA AHGLELRVPF LDHRFSSYYL SLPPEMRIPK DGIEKHLLRE
460 470 480 490 500
TFEDSNLLPK EILWRPKEAF SDGITSVKNS WFKILQDFVE HQVDDAMMSE
510 520 530 540 550
ASQKFPFNTP QTKEGYYYRQ IFEHHYPGRA DWLTHYWMPK WINATDPSAR
560
TLTHYKSTAK A
Length:561
Mass (Da):64,247
Last modified:January 23, 2007 - v3
Checksum:i6C8C6438F424326F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti330 – 3301S → P in AAA77672 (PubMed:7818476).Curated
Sequence conflicti330 – 3301S → P in AAA77671 (PubMed:7818476).Curated
Sequence conflicti491 – 4911H → Y in AAA77672 (PubMed:7818476).Curated
Sequence conflicti491 – 4911H → Y in AAA77671 (PubMed:7818476).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07202 mRNA. Translation: AAA77672.1.
U07201 mRNA. Translation: AAA77671.1.
BC081719 mRNA. Translation: AAH81719.1.
PIRiS53447.
RefSeqiNP_037211.2. NM_013079.2.
XP_006236151.1. XM_006236089.2.
UniGeneiRn.11172.

Genome annotation databases

EnsembliENSRNOT00000010079; ENSRNOP00000010079; ENSRNOG00000007546.
GeneIDi25612.
KEGGirno:25612.
UCSCiRGD:2162. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07202 mRNA. Translation: AAA77672.1.
U07201 mRNA. Translation: AAA77671.1.
BC081719 mRNA. Translation: AAH81719.1.
PIRiS53447.
RefSeqiNP_037211.2. NM_013079.2.
XP_006236151.1. XM_006236089.2.
UniGeneiRn.11172.

3D structure databases

ProteinModelPortaliP49088.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000010079.

Chemistry

ChEMBLiCHEMBL2303.

Proteomic databases

PaxDbiP49088.
PRIDEiP49088.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000010079; ENSRNOP00000010079; ENSRNOG00000007546.
GeneIDi25612.
KEGGirno:25612.
UCSCiRGD:2162. rat.

Organism-specific databases

CTDi440.
RGDi2162. Asns.

Phylogenomic databases

eggNOGiCOG0367.
GeneTreeiENSGT00390000001994.
HOGENOMiHOG000027493.
HOVERGENiHBG003103.
InParanoidiP49088.
KOiK01953.
OMAiDWSGIYS.
OrthoDBiEOG75MVVS.
PhylomeDBiP49088.
TreeFamiTF300603.

Enzyme and pathway databases

UniPathwayiUPA00134; UER00195.
BioCyciMetaCyc:MONOMER-13063.
ReactomeiREACT_292751. Amino acid synthesis and interconversion (transamination).

Miscellaneous databases

NextBioi607355.
PROiP49088.

Gene expression databases

GenevestigatoriP49088.

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]
SUPFAMiSSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR01536. asn_synth_AEB. 1 hit.
PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1993) [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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.

Entry informationi

Entry nameiASNS_RAT
AccessioniPrimary (citable) accession number: P49088
Secondary accession number(s): Q66HR8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: April 1, 2015
This is version 118 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.