Reviewed, UniProtKB/Swiss-Prot P49090 (ASNS2_YEAST)

Names and origin

Protein names

Recommended name:
    Asparagine synthetase [glutamine-hydrolyzing] 2
    EC=6.3.5.4
Alternative name(s):
    Glutamine-dependent asparagine synthetase 2

Gene names

Name:	ASN2
Ordered Locus Names:	YGR124W
ORF Names:	G6358

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	572 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein 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.
Miscellaneous	Present with 58200 molecules/cell in log phase SD medium. Ref.3
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	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	asparagine biosynthetic process Inferred from genetic interaction. Source: SGD glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW asparagine synthase (glutamine-hydrolyzing) activity Inferred from direct assay. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ASN1	P49089	1	EBI-3048,EBI-3043

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 572	571	Asparagine synthetase [glutamine-hydrolyzing] 2		PRO_0000056918
Regions
	Domain	2 – 186	185	Glutamine amidotransferase type-2
	Domain	194 – 545	352	Asparagine synthetase
Sites
	Active site	2	1	For GATase activity By similarity
Amino acid modifications
	Modified residue	204	1	Phosphoserine Ref.4 Ref.5 Ref.6
	Modified residue	205	1	Phosphothreonine Ref.4 Ref.5 Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P49090-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 2809F3F0FEDE4183	FASTA	572	64,593
	10 20 30 40 50 60 MCGIFAAFKH EDIHNFKPKA LQLSKKIRHR GPDWSGNAVM NSTIFVHERL AIVGLDSGAQ 70 80 90 100 110 120 PITSADGEYM LGVNGEIYNH IQLREMCSDY KFQTFSDCEP IIPLYLEHDI DAPKYLDGMF 130 140 150 160 170 180 AFCLYDSKKD RIVAARDPIG VVTLYMGRSS QSPETVYFAS ELKCLTDVCD SIISFPPGHV 190 200 210 220 230 240 YDSETDKITR YFTPDWLDEK RIPSTPVDYH AIRHSLEKAV RKRLMAEVPY GVLLSGGLDS 250 260 270 280 290 300 SLIAAIAARE TEKANADANE DNNVDEKQLA GIDDQGHLHT SGWSRLHSFA IGLPNAPDLQ 310 320 330 340 350 360 AARKVAKFIG SIHHEHTFTL QEGLDALDDV IYHLETYDVT TIRASTPMFL LSRKIKAQGV 370 380 390 400 410 420 KMVLSGEGSD EIFGGYLYFA QAPSAAEFHT ESVQRVKNLH LADCLRANKS TMAWGLEARV 430 440 450 460 470 480 PFLDKDFLQL CMNIDPNEKM IKPKEGRIEK YILRKAFDTT DEPDVKPYLP EEILWRQKEQ 490 500 510 520 530 540 FSDGVGYSWI DGLRDTAERA ISDAMFANPK ADWGDDIPTT KEAYWYRLKF DAWFPQKTAA 550 560 570 DTVMRWIPKA DWGCAEDPSG RYAKIHEKHV SA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"An 18.3 kb DNA fragment from yeast chromosome VII carries four unknown open reading frames, the gene for an Asn synthase, remnants of Ty and three tRNA genes." van Dyck L., Tettelin H., Purnelle B., Goffeau A. Yeast 13:171-176(1997) [PubMed: 9046098] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K. Nature 387:81-84(1997) [PubMed: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[4]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204 AND THR-205, MASS SPECTROMETRY.
[5]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204 AND THR-205, MASS SPECTROMETRY.
[6]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204 AND THR-205, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X83099 Genomic DNA. Translation: CAA58159.1. Z72909 Genomic DNA. Translation: CAA97135.1.
PIR	S55982.
RefSeq	NP_011640.1.
3D structure databases
HSSP	HSSP built from PDB template 1CT9 based on UniProtKB P22106.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:5189N.
IntAct	P49090. 6 interactions.
STRING	P49090.
Protein family/group databases
MEROPS	C44.974.
Proteomic databases
PeptideAtlas	P49090.
PRIDE	P49090.
Genome annotation databases
Ensembl	YGR124W; YGR124W; YGR124W; Saccharomyces cerevisiae. [Genome view]
GeneID	853025.
GenomeReviews	Gene locus YGR124W in contig Y13135_GR.
KEGG	sce:YGR124W.
NMPDR	fig|4932.3.peg.2759.
Organism-specific databases
CYGD	YGR124w.
SGD	S000003356. ASN2.
Phylogenomic databases
HOGENOM	P49090.
OMA	NKSLAAW.
Enzyme and pathway databases
BRENDA	6.3.5.4. 250.
Gene expression databases
ArrayExpress	P49090.
Genevestigator	P49090.
GermOnline	YGR124W. Saccharomyces cerevisiae.
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	972902.

Entry information

Entry name

ASNS2_YEAST

Accession

Primary (citable) accession number: P49090

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 85 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)