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Q61024

- ASNS_MOUSE

UniProt

Q61024 - ASNS_MOUSE

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Protein

Asparagine synthetase [glutamine-hydrolyzing]

Gene

Asns

Organism
Mus musculus (Mouse)
Status
Reviewed - 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: UniProtKB-EC
  2. ATP binding Source: UniProtKB-KW
  3. cofactor binding Source: Ensembl

GO - Biological processi

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

ReactomeiREACT_90370. ATF4 activates genes.
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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 6

Organism-specific databases

MGIiMGI:1350929. Asns.

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 561560Asparagine synthetase [glutamine-hydrolyzing]PRO_0000056912Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ61024.
PaxDbiQ61024.
PRIDEiQ61024.

PTM databases

PhosphoSiteiQ61024.

Expressioni

Gene expression databases

BgeeiQ61024.
CleanExiMM_ASNS.
ExpressionAtlasiQ61024. baseline and differential.
GenevestigatoriQ61024.

Interactioni

Protein-protein interaction databases

BioGridi205108. 1 interaction.
IntActiQ61024. 1 interaction.
MINTiMINT-4088470.

Structurei

3D structure databases

ProteinModelPortaliQ61024.
SMRiQ61024. Positions 76-481.
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.
InParanoidiQ61024.
KOiK01953.
OMAiWSGIYSS.
OrthoDBiEOG75MVVS.
PhylomeDBiQ61024.
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]
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.

Q61024-1 [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 GVRPLFKAMT
160 170 180 190 200
EDGFLAVCSE AKGLVSLKHS TTPFLKVEPF LPGHYEVLDL KPNGKVASVE
210 220 230 240 250
MVKYHHCTDE PLHAIYDSVE KLFPGFDLET VKNNLRILFD NAIKKRLMTD
260 270 280 290 300
RRIGCLLSGG LDSSLVAASL 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 SLPPDMRIPK NGIEKHLLRE
460 470 480 490 500
TFEDCNLLPK EILWRPKEAF SDGITSVKNS WFKILQDYVE HQVDDEMMSA
510 520 530 540 550
ASQKFPFNTP KTKEGYFYRQ IFERHYPGRA DWLTHYWMPK WINATDPSAR
560
TLTHYKSAAK A
Length:561
Mass (Da):64,283
Last modified:January 23, 2007 - v3
Checksum:i1981956B69E1F9F1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51W → G in BAC36254. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U38940 mRNA. Translation: AAA85125.1.
AK076207 mRNA. Translation: BAC36254.1.
AK167524 mRNA. Translation: BAE39594.1.
BC005552 mRNA. Translation: AAH05552.1.
CCDSiCCDS19907.1.
RefSeqiNP_036185.1. NM_012055.3.
XP_006505155.1. XM_006505092.1.
XP_006505156.1. XM_006505093.1.
UniGeneiMm.2942.

Genome annotation databases

EnsembliENSMUST00000031766; ENSMUSP00000031766; ENSMUSG00000029752.
ENSMUST00000115542; ENSMUSP00000111204; ENSMUSG00000029752.
GeneIDi27053.
KEGGimmu:27053.
UCSCiuc009axf.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U38940 mRNA. Translation: AAA85125.1 .
AK076207 mRNA. Translation: BAC36254.1 .
AK167524 mRNA. Translation: BAE39594.1 .
BC005552 mRNA. Translation: AAH05552.1 .
CCDSi CCDS19907.1.
RefSeqi NP_036185.1. NM_012055.3.
XP_006505155.1. XM_006505092.1.
XP_006505156.1. XM_006505093.1.
UniGenei Mm.2942.

3D structure databases

ProteinModelPortali Q61024.
SMRi Q61024. Positions 76-481.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 205108. 1 interaction.
IntActi Q61024. 1 interaction.
MINTi MINT-4088470.

PTM databases

PhosphoSitei Q61024.

Proteomic databases

MaxQBi Q61024.
PaxDbi Q61024.
PRIDEi Q61024.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000031766 ; ENSMUSP00000031766 ; ENSMUSG00000029752 .
ENSMUST00000115542 ; ENSMUSP00000111204 ; ENSMUSG00000029752 .
GeneIDi 27053.
KEGGi mmu:27053.
UCSCi uc009axf.1. mouse.

Organism-specific databases

CTDi 440.
MGIi MGI:1350929. Asns.

Phylogenomic databases

eggNOGi COG0367.
GeneTreei ENSGT00390000001994.
HOGENOMi HOG000027493.
HOVERGENi HBG003103.
InParanoidi Q61024.
KOi K01953.
OMAi WSGIYSS.
OrthoDBi EOG75MVVS.
PhylomeDBi Q61024.
TreeFami TF300603.

Enzyme and pathway databases

UniPathwayi UPA00134 ; UER00195 .
Reactomei REACT_90370. ATF4 activates genes.

Miscellaneous databases

NextBioi 304991.
PROi Q61024.
SOURCEi Search...

Gene expression databases

Bgeei Q61024.
CleanExi MM_ASNS.
ExpressionAtlasi Q61024. baseline and differential.
Genevestigatori Q61024.

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

« Hide 'large scale' publications
  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.
    , 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. Cited for: DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiASNS_MOUSE
AccessioniPrimary (citable) accession number: Q61024
Secondary accession number(s): Q3TJA1, Q8BPC8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 120 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3