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Q61024 (ASNS_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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.

Disruption phenotype

Mice carrying a gene trap insertion in the gene express 20% of the normal level of mRNA. The hypomorphic mutant displays a number of defects that mirror ASNSD syndrome, although the phenotype is milder. Mice have structural brain abnormalities, including reduced cortical thickness and enlarged ventricles. Mutant mice also show deficits in learning and memory. Mutant mice do not show abnormal motor activity or seizure activity. Ref.4

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

cellular response to glucose starvation

Inferred from electronic annotation. Source: Ensembl

cellular response to hormone stimulus

Inferred from electronic annotation. Source: Ensembl

glutamine metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

liver development

Inferred from electronic annotation. Source: Ensembl

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 electronic annotation. Source: Ensembl

response to follicle-stimulating hormone

Inferred from electronic annotation. Source: Ensembl

response to light stimulus

Inferred from electronic annotation. Source: Ensembl

response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

response to methotrexate

Inferred from electronic annotation. Source: Ensembl

response to toxic substance

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

asparagine synthase (glutamine-hydrolyzing) activity

Inferred from electronic annotation. Source: UniProtKB-EC

cofactor binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 561560Asparagine synthetase [glutamine-hydrolyzing]
PRO_0000056912

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 conflict51W → G in BAC36254. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q61024 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 1981956B69E1F9F1

FASTA56164,283
        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 GVRPLFKAMT EDGFLAVCSE AKGLVSLKHS TTPFLKVEPF 

       190        200        210        220        230        240 
LPGHYEVLDL KPNGKVASVE MVKYHHCTDE PLHAIYDSVE KLFPGFDLET VKNNLRILFD 

       250        260        270        280        290        300 
NAIKKRLMTD RRIGCLLSGG LDSSLVAASL 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 SLPPDMRIPK NGIEKHLLRE TFEDCNLLPK EILWRPKEAF SDGITSVKNS 

       490        500        510        520        530        540 
WFKILQDYVE HQVDDEMMSA ASQKFPFNTP KTKEGYFYRQ IFERHYPGRA DWLTHYWMPK 

       550        560 
WINATDPSAR TLTHYKSAAK A 

« Hide

References

« Hide 'large scale' references
[1]Goodwin L., Sellati L., Millan C., Guzowski D., Leeds N., Broome J., Pergolizzi R.
Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
Tissue: Liver.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Placenta.
[3]"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].
Strain: FVB/N.
Tissue: Mammary gland.
[4]"Deficiency of asparagine synthetase causes congenital microcephaly and a progressive form of encephalopathy."
Ruzzo E.K., Capo-Chichi J.M., Ben-Zeev B., Chitayat D., Mao H., Pappas A.L., Hitomi Y., Lu Y.F., Yao X., Hamdan F.F., Pelak K., Reznik-Wolf H., Bar-Joseph I., Oz-Levi D., Lev D., Lerman-Sagie T., Leshinsky-Silver E., Anikster Y. expand/collapse author list , Ben-Asher E., Olender T., Colleaux L., Decarie J.C., Blaser S., Banwell B., Joshi R.B., He X.P., Patry L., Silver R.J., Dobrzeniecka S., Islam M.S., Hasnat A., Samuels M.E., Aryal D.K., Rodriguiz R.M., Jiang Y.H., Wetsel W.C., McNamara J.O., Rouleau G.A., Silver D.L., Lancet D., Pras E., Mitchell G.A., Michaud J.L., Goldstein D.B.
Neuron 80:429-441(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U38940 mRNA. Translation: AAA85125.1.
AK076207 mRNA. Translation: BAC36254.1.
AK167524 mRNA. Translation: BAE39594.1.
BC005552 mRNA. Translation: AAH05552.1.
CCDSCCDS19907.1.
RefSeqNP_036185.1. NM_012055.3.
XP_006505155.1. XM_006505092.1.
XP_006505156.1. XM_006505093.1.
UniGeneMm.2942.

3D structure databases

ProteinModelPortalQ61024.
SMRQ61024. Positions 76-481.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid205108. 1 interaction.
IntActQ61024. 1 interaction.
MINTMINT-4088470.

Protein family/group databases

MEROPSC44.974.

PTM databases

PhosphoSiteQ61024.

Proteomic databases

MaxQBQ61024.
PaxDbQ61024.
PRIDEQ61024.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031766; ENSMUSP00000031766; ENSMUSG00000029752.
ENSMUST00000115542; ENSMUSP00000111204; ENSMUSG00000029752.
GeneID27053.
KEGGmmu:27053.
UCSCuc009axf.1. mouse.

Organism-specific databases

CTD440.
MGIMGI:1350929. Asns.

Phylogenomic databases

eggNOGCOG0367.
GeneTreeENSGT00390000001994.
HOGENOMHOG000027493.
HOVERGENHBG003103.
InParanoidQ61024.
KOK01953.
OMAWSGIYSS.
OrthoDBEOG75MVVS.
PhylomeDBQ61024.
TreeFamTF300603.

Enzyme and pathway databases

UniPathwayUPA00134; UER00195.

Gene expression databases

ArrayExpressQ61024.
BgeeQ61024.
CleanExMM_ASNS.
GenevestigatorQ61024.

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

NextBio304991.
PROQ61024.
SOURCESearch...

Entry information

Entry nameASNS_MOUSE
AccessionPrimary (citable) accession number: Q61024
Secondary accession number(s): Q3TJA1, Q8BPC8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 117 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot