Reviewed, UniProtKB/Swiss-Prot Q61024 (ASNS_MOUSE)

Names and origin

Protein names

Recommended name:
    Asparagine synthetase [glutamine-hydrolyzing]
    EC=6.3.5.4
Alternative name(s):
    Glutamine-dependent asparagine synthetase

Gene names

Name:

Asns

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	561 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
Sequence similarities	Contains 1 asparagine synthetase domain. Contains 1 glutamine amidotransferase type-2 domain.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Asparagine biosynthesis
Domain	Glutamine amidotransferase
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Acetylation Phosphoprotein
Gene Ontology (GO)
Biological process	asparagine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW asparagine synthase (glutamine-hydrolyzing) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 561	560	Asparagine synthetase [glutamine-hydrolyzing]		PRO_0000056912
Regions
	Domain	2 – 191	190	Glutamine amidotransferase type-2
	Domain	213 – 536	324	Asparagine synthetase
Sites
	Active site	2	1	For GATase activity By similarity
Amino acid modifications
	Modified residue	385	1	N6-acetyllysine By similarity
	Modified residue	471	1	Phosphoserine By similarity
Experimental info
	Sequence conflict	5	1	W → G in BAC36254. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q61024-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 1981956B69E1F9F1	FASTA	561	64,283
	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

References

	« Hide 'large scale' referencesShow '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. , 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: 16141072] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Mammary gland.
+	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.
IPI	IPI00116966.
RefSeq	NP_036185.1.
UniGene	Mm.2942
3D structure databases
SMR	Q61024. Positions 1-533.
ModBase	Search...
Protein-protein interaction databases
STRING	Q61024.
Protein family/group databases
MEROPS	C44.974.
PTM databases
PhosphoSite	Q61024.
Proteomic databases
PRIDE	Q61024.
Genome annotation databases
Ensembl	ENSMUST00000031766; ENSMUSP00000031766; ENSMUSG00000029752; Mus musculus. [Genome view] ENSMUST00000115542; ENSMUSP00000111204; ENSMUSG00000029752; Mus musculus. [Genome view]
GeneID	27053.
KEGG	mmu:27053.
NMPDR	fig|10090.3.peg.12931.
UCSC	uc009axf.1. mouse.
Organism-specific databases
CTD	27053.
MGI	MGI:1350929. Asns.
Phylogenomic databases
HOGENOM	HBG752912.
HOVERGEN	Q61024.
InParanoid	Q61024.
OMA	KVTDQQM.
OrthoDB	EOG95TG76.
PhylomeDB	Q61024.
Enzyme and pathway databases
BRENDA	6.3.5.4. 244.
Gene expression databases
ArrayExpress	Q61024.
Bgee	Q61024.
CleanEx	MM_ASNS.
Genevestigator	Q61024.
GermOnline	ENSMUSG00000029752. Mus musculus.
Family and domain databases
InterPro	IPR006426. Asn_synth_AEB. IPR001962. Asn_synthase. IPR000583. GATase_2. IPR017932. GATase_II. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
Gene3D	G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
Pfam	PF00733. Asn_synthase. 1 hit. PF00310. GATase_2. 1 hit. [Graphical view]
TIGRFAMs	TIGR01536. asn_synth_AEB. 1 hit.
PROSITE	PS51278. GATASE_TYPE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	304991.
SOURCE	Search...

Entry information

Entry name

ASNS_MOUSE

Accession

Primary (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:	February 9, 2010
This is version 78 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)