P49090 (ASNS2_YEAST) Reviewed, UniProtKB/Swiss-Prot

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 (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [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.5
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 Reference 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
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 – 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.6 Ref.7 Ref.8
	Modified residue	205	1	Phosphothreonine Ref.6 Ref.7 Ref.8
Experimental info
	Sequence conflict	560	1	G → S in AAT92877. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P49090 [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]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"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].
[6]	"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.
[7]	"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.
[8]	"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
EMBL GenBank DDBJ	X83099 Genomic DNA. Translation: CAA58159.1. Z72909 Genomic DNA. Translation: CAA97135.1. AY692858 Genomic DNA. Translation: AAT92877.1. BK006941 Genomic DNA. Translation: DAA08217.1.
PIR	S55982.
RefSeq	NP_011640.1. NM_001181253.1.
3D structure databases
ProteinModelPortal	P49090.
SMR	P49090. Positions 2-544.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-5189N.
IntAct	P49090. 4 interactions.
MINT	MINT-501384.
STRING	P49090.
Protein family/group databases
MEROPS	C44.974.
2D gel databases
UCD-2DPAGE	P49090.
Proteomic databases
PeptideAtlas	P49090.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YGR124W; YGR124W; YGR124W.
GeneID	853025.
KEGG	sce:YGR124W.
NMPDR	fig|4932.3.peg.2759.
Organism-specific databases
SGD	S000003356. ASN2.
Phylogenomic databases
eggNOG	fuNOG04663.
HOGENOM	HBG752912.
OMA	NYYVASE.
OrthoDB	EOG4XKZG7.
Gene expression databases
ArrayExpress	P49090.
Genevestigator	P49090.
GermOnline	YGR124W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR006426. Asn_synth_AEB. IPR001962. Asn_synthase. IPR017932. GATase_II. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
Gene3D	G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits.
KO	K01953.
Pfam	PF00733. Asn_synthase. 1 hit. [Graphical view]
PIRSF	PIRSF001589. Asn_synthetase_glu-h. 1 hit.
TIGRFAMs	TIGR01536. Asn_synth_AEB. 1 hit.
PROSITE	PS51278. GATASE_TYPE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	972902.

Entry information

Entry name

ASNS2_YEAST

Accession

Primary (citable) accession number: P49090
Secondary accession number(s): D6VUQ6, E9P8Y0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	January 23, 2007
Last modified:	December 14, 2011
This is version 106 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program