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ASP3-1/YLR155C Single Page Format

This page provides an alternative format to the SGD Locus Summary Page. Note that additional information may be available on or linked from the standard format SGD Locus Summary page.

Contents

Names and Identifiers GO Annotations Pathways Summary Paragraph Mutant Phenotypes Interactions Homologs Protein Info (physical properties, transcript info) PDB Homologs (protein structure info) Motifs Genome-wide Expression (and other large-scale analyses) Locus History (misc. notes) Sequence Retrieval and Analysis Map and Displays Localization Community Annotation Literature Guide

Sequence Coordinates   ChrXII: 470406 to 469318 CDS: 470406 - 469318 Click on map for expanded view SGD ORF map GBrowse

SGD Locus Page

Names and Identifiers [TOP] [NEXT]
Standard Name	Systematic Name	Alias	Feature Type	SGDID
ASP3-1	YLR155C	ASP3	ORF, Verified	S000004145
See Nomenclature Note.
Description
Cell-wall L-asparaginase II, involved in asparagine catabolism; expression is induced during nitrogen starvation; four copies of ASP3 are present in the genome reference strain S288C

GO Annotations [TOP] [NEXT]
Molecular Function Annotation(s) Reference(s) Evidence Assigned By asparaginase activity Kim KW, et al. (1988) Asparaginase II of Saccharomyces cerevisiae. Characterization of the ASP3 gene. J Biol Chem 263(24):11948-53      TAS : Traceable Author Statement Assigned on 2001-01-18 SGD DDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.      IEA : Inferred from Electronic Annotation with EBI:IPR004550 Assigned on 2007-05-23 UniProtKB GOA curators and MGI curators (2001) Gene Ontology annotation based on Enzyme Commission mapping.      IEA : Inferred from Electronic Annotation with IUBMB:3.5.1.1 Assigned on 2007-05-23 UniProtKB hydrolase activity GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0378 Assigned on 2007-05-23 UniProtKB
Biological Process Annotation(s) Reference(s) Evidence Assigned By asparagine catabolic process Cooper TG (1982) "Nitrogen metabolism in Saccharomyces cerevisiae." Pp. 39-99 in The Molecular Biology of the Yeast Saccharomyces: Metabolism and Gene Expression, edited by Strathern JN, Jones EW and Broach JR. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press    TAS : Traceable Author Statement Assigned on 2003-06-25 SGD asparagine metabolic process DDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.      IEA : Inferred from Electronic Annotation with EBI:IPR004550 Assigned on 2007-05-23 UniProtKB cellular amino acid metabolic process DDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.      IEA : Inferred from Electronic Annotation with EBI:IPR006034 , EBI:IPR020827 Assigned on 2007-05-23 UniProtKB cellular response to nitrogen starvation Bon EP, et al. (1997) Asparaginase II of Saccharomyces cerevisiae. GLN3/URE2 regulation of a periplasmic enzyme. Appl Biochem Biotechnol 63-65():203-12      TAS : Traceable Author Statement Assigned on 2001-01-18 SGD response to starvation Huttenhower C and Troyanskaya OG (2009) Prediction of Gene Ontology annotations by integrating high-throughput datasets    RCA : Reviewed Computational Analysis Assigned on 2009-08-06 bioPIXIE_MEFIT vacuolar protein catabolic process Huttenhower C and Troyanskaya OG (2009) Prediction of Gene Ontology annotations by integrating high-throughput datasets    RCA : Reviewed Computational Analysis Assigned on 2009-08-06 bioPIXIE_MEFIT
Cellular Component Annotation(s) Reference(s) Evidence Assigned By cell wall GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0134 Assigned on 2008-02-14 UniProtKB GOA curators and UniProt curators (2007) Gene Ontology annotation based on Swiss-Prot Subcellular Location vocabulary mapping.      IEA : Inferred from Electronic Annotation with EBI:SL-0041 Assigned on 2009-05-06 UniProtKB cell wall-bounded periplasmic space Bon EP, et al. (1997) Asparaginase II of Saccharomyces cerevisiae. GLN3/URE2 regulation of a periplasmic enzyme. Appl Biochem Biotechnol 63-65():203-12      TAS : Traceable Author Statement Assigned on 2001-09-24 SGD endoplasmic reticulum Kumar A, et al. (2002) Subcellular localization of the yeast proteome. Genes Dev 16(6):707-19              IDA : Inferred from Direct Assay Assigned on 2002-05-07 SGD extracellular region GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0964 Assigned on 2009-06-29 UniProtKB nuclear envelope Kumar A, et al. (2002) Subcellular localization of the yeast proteome. Genes Dev 16(6):707-19              IDA : Inferred from Direct Assay Assigned on 2002-05-07 SGD

Pathways [TOP] [NEXT]
asparagine degradation

Summary Paragraph [TOP] [NEXT]

SUMMARY PARAGRAPH for ASP3-1/YLR155C for ASP3-1 ASP3 encodes a nitrogen catabolite-regulated cell wall L-asparaginase II (1). It is one of two asparaginases in yeast, the other being the constitutive intracellular asparaginase I Asp1p, with which Asp3p shares 46% identity (2). Asp3p catalyzes the conversion of L-asparagine to aspartate and ammonia. Asp3p is secreted in response to nitrogen starvation and appears to be regulated by Gln3p/Ure2p (3). ASP3 is located at the junction on chromosome XII with the rRNA genes and is repeated at least four times, to create ASP3-1, ASP3-2, ASP3-3, ASP3-4. Last Updated: 1999-09-01

Basic References [TOP]

BASIC INFORMATION REFERENCES forASP3-1/YLR155C for ASP3-1 1) Kim KW, et al. (1988) Asparaginase II of Saccharomyces cerevisiae. Characterization of the ASP3 gene. J Biol Chem 263(24):11948-53      2) Sinclair K, et al. (1994) The ASP1 gene of Saccharomyces cerevisiae, encoding the intracellular isozyme of L-asparaginase. Gene 144(1):37-43      3) Bon EP, et al. (1997) Asparaginase II of Saccharomyces cerevisiae. GLN3/URE2 regulation of a periplasmic enzyme. Appl Biochem Biotechnol 63-65():203-12      4) Oliveira EM, et al. (2003) The role of the GATA factors Gln3p, Nil1p, Dal80p and the Ure2p on ASP3 regulation in Saccharomyces cerevisiae. Yeast 20(1):31-7

Mutant Phenotypes [TOP] [NEXT]
Phenotype page for ASP3-1/YLR155C

Interactions: genetic, physical, and other gene-gene links. [TOP] [NEXT]
Interaction page for ASP3-1/YLR155C

Homologs [TOP] [NEXT]
Comparison Resources PSI-BLAST Results Ashbya Homologs (AGD) BLASTN vs. fungi BLASTP at NCBI BLASTP vs. fungi Fungal Alignment Fungal Orthogroups Repository Ortholog Search (P-POD) PhylomeDB Synteny Viewer Yeast Gene Order Browser (YGOB) eukarYotic OrtholoGY (YOGY)

Physical Properties and Transcript Information: predicted from sequence [TOP] [NEXT]
Protein Sequence Calculations from Predicted Full length Translation N-term MRSLNTL C-term FSGVYGG Length(aa) 362 MW(Da) 38,686 pI 4.53 Amino Acid Composition (full length) GCG tools: PepPlot, Helical Wheel, PepStruct Transcript Translation Calculations Codon Bias 0.169   Codon Adaptation Index 0.166   Frequency of Optimal Codons 0.493   Hydropathicity of Protein -0.023   Aromaticity Score 0.091	10 20 30 40 50 | | | | | MRSLNTLLLSLFVAMSSGAPLLKIREEKNSSLPSIKIFGTGGTIASKGST SATTAGYSVGLTVNDLIEAVPSLAEKANLDYLQVSNVGSNSLNYTHLIPL YHGISEALASDDYAGAVVTHGTDTMEETAFFLDLTINSEKPVCIAGAMRP ATATSADGPMNLYQAVSIAASEKSLGRGTMITLNDRIASGFWTTKMNANS LDTFRADEQGYLGYFSNDDVEFYYPPVKPNGWQFFDISNLTDPSEIPEVI ILYSYQGLNPELIVKAVKDLGAKGIVLAGSGAGSWTATGSIVNEQLYEEY GIPIVHSRRTADGTVPPDDAPEYAIGSGYLNPQKSRILLQLCLYSGYGMD QIRSVFSGVYGG*

Protein Structures from PDB: proteins of known structure with sequence similarity to ASP3-1/YLR155C, based on Smith-Waterman analysis. [TOP] [NEXT]

PDB protein structure(s) homologous to ASP3-1 Homolog Source (per PDB) Protein Alignment: ASP3-1 vs. Homolog External Links P-Value %Identical %Similar Alignment 1hfw ( Chain: A, C, D, B) X-ray structure of the complex between erwinia chrysanthemi l-asparaginase and l-glutamate PDB_Info PDB_Structure Erwinia chrysanthemi Chain A = 1.4e-46 46 29 View alignment SCOP MMDB CATH Chain C = 1.4e-46 46 29 View alignment Chain D = 1.4e-46 46 29 View alignment Chain B = 1.4e-46 46 29 View alignment 1o7j ( Chain: A, C, B, D) Atomic resolution structure of erwinia chrysanthemi l-asparaginase PDB_Info PDB_Structure Erwinia chrysanthemi Chain A = 1.4e-46 46 29 View alignment SCOP MMDB CATH Chain C = 1.4e-46 46 29 View alignment Chain B = 1.4e-46 46 29 View alignment Chain D = 1.4e-46 46 29 View alignment 1hg1 ( Chain: A, B, D, C) X-ray structure of the complex between erwinia chrysanthemi l-asparaginase and d-aspartate PDB_Info PDB_Structure Erwinia chrysanthemi Chain A = 1.4e-46 46 29 View alignment SCOP MMDB CATH Chain B = 1.4e-46 46 29 View alignment Chain D = 1.4e-46 46 29 View alignment Chain C = 1.4e-46 46 29 View alignment 1jsl ( Chain: C, B, A, D) Crystal structure of erwinia chrysanthemi l-asparaginase complexed with 6-hydroxy-d-norleucine PDB_Info PDB_Structure Erwinia chrysanthemi Chain C = 1.4e-46 46 29 View alignment SCOP MMDB CATH Chain B = 1.4e-46 46 29 View alignment Chain A = 1.4e-46 46 29 View alignment Chain D = 1.4e-46 46 29 View alignment 1hg0 ( Chain: D, B, A, C) X-ray structure of the complex between erwinia chrysanthemi l-asparaginase and succinic acid PDB_Info PDB_Structure Erwinia chrysanthemi Chain D = 1.4e-46 46 29 View alignment SCOP MMDB CATH Chain B = 1.4e-46 46 29 View alignment Chain A = 1.4e-46 46 29 View alignment Chain C = 1.4e-46 46 29 View alignment 1hfj ( Chain: A, C) Asparaginase from erwinia chrysanthemi, hexagonal form with sulfate PDB_Info PDB_Structure Erwinia chrysanthemi Chain A = 1.4e-46 46 29 View alignment SCOP MMDB CATH Chain C = 1.4e-46 46 29 View alignment 1jsr ( Chain: A, B, C, D) Crystal structure of erwinia chrysanthemi l-asparaginase complexed with 6-hydroxy-l-norleucine PDB_Info PDB_Structure Erwinia chrysanthemi Chain A = 1.4e-46 46 29 View alignment SCOP MMDB CATH Chain B = 1.4e-46 46 29 View alignment Chain C = 1.4e-46 46 29 View alignment Chain D = 1.4e-46 46 29 View alignment 1hfk ( Chain: C, A) Asparaginase from erwinia chrysanthemi, hexagonal form with weak sulfate PDB_Info PDB_Structure Erwinia chrysanthemi Chain C = 1.4e-46 46 29 View alignment SCOP MMDB CATH Chain A = 1.4e-46 46 29 View alignment 2jk0 ( Chain: F, E, D, C, B, H, G, A) Structural and functional insights into erwinia carotovora l-asparaginase PDB_Info PDB_Structure Pectobacterium carotovorum Chain F = 2.0e-46 45 29 View alignment SCOP MMDB CATH Chain E = 2.0e-46 45 29 View alignment Chain D = 2.0e-46 45 29 View alignment Chain C = 2.0e-46 45 29 View alignment Chain B = 2.0e-46 45 29 View alignment Chain H = 2.0e-46 45 29 View alignment Chain G = 2.0e-46 45 29 View alignment Chain A = 2.0e-46 45 29 View alignment 2gvn ( Chain: C, B, A, H, F, G, D, E) L-asparaginase from erwinia carotovora in complex with aspartic acid PDB_Info PDB_Structure Pectobacterium atrosepticum Chain C = 2.0e-46 45 29 View alignment SCOP MMDB CATH Chain B = 2.0e-46 45 29 View alignment Chain A = 2.0e-46 45 29 View alignment Chain H = 2.0e-46 45 29 View alignment Chain F = 2.0e-46 45 29 View alignment Chain G = 2.0e-46 45 29 View alignment Chain D = 2.0e-46 45 29 View alignment Chain E = 2.0e-46 45 29 View alignment 1zcf ( Chain: H, C, D, E, B, A, F, G) L-asparaginase from erwinia carotovora PDB_Info PDB_Structure Pectobacterium atrosepticum SCRI1043 Chain H = 2.0e-46 45 29 View alignment SCOP MMDB CATH Chain C = 2.0e-46 45 29 View alignment Chain D = 2.0e-46 45 29 View alignment Chain E = 2.0e-46 45 29 View alignment Chain B = 2.0e-46 45 29 View alignment Chain A = 2.0e-46 45 29 View alignment Chain F = 2.0e-46 45 29 View alignment Chain G = 2.0e-46 45 29 View alignment 2hln ( Chain: H, C, E, L, K, I, A, B, D, J, G, F) L-asparaginase from erwinia carotovora in complex with glutamic acid PDB_Info PDB_Structure Pectobacterium atrosepticum Chain H = 2.0e-46 45 29 View alignment SCOP MMDB CATH Chain C = 2.0e-46 45 29 View alignment Chain E = 2.0e-46 45 29 View alignment Chain L = 2.0e-46 45 29 View alignment Chain K = 2.0e-46 45 29 View alignment Chain I = 2.0e-46 45 29 View alignment Chain A = 2.0e-46 45 29 View alignment Chain B = 2.0e-46 45 29 View alignment Chain D = 2.0e-46 45 29 View alignment Chain J = 2.0e-46 45 29 View alignment Chain G = 2.0e-46 45 29 View alignment Chain F = 2.0e-46 45 29 View alignment 3eca ( Chain: C, D, B, A) Crystal structure of escherichia coli l-asparaginase, an enzyme used in cancer therapy PDB_Info PDB_Structure Escherichia coli Chain C = 5.2e-41 41 29 View alignment SCOP MMDB CATH Chain D = 5.2e-41 41 29 View alignment Chain B = 5.2e-41 41 29 View alignment Chain A = 5.2e-41 41 29 View alignment 1nns ( Chain: B, A) L-asparaginase of e. coli in c2 space group and 1.95 a resolution PDB_Info PDB_Structure Escherichia coli Chain B = 5.2e-41 41 29 View alignment SCOP MMDB CATH Chain A = 5.2e-41 41 29 View alignment 1ho3 ( Chain: B, A) Crystal structure analysis of e. coli l-asparaginase ii (y25f mutant) PDB_Info PDB_Structure Escherichia coli Chain B = 9.6e-41 41 29 View alignment SCOP MMDB CATH Chain A = 9.6e-41 41 29 View alignment 1jja ( Chain: B, D, E, C, F, A) Crystal structure of orthorhombic form of d90e mutant of escherichia coli l-asparaginase ii PDB_Info PDB_Structure Escherichia coli Chain B = 1.3e-40 41 29 View alignment SCOP MMDB CATH Chain D = 1.3e-40 41 29 View alignment Chain E = 1.3e-40 41 29 View alignment Chain C = 1.3e-40 41 29 View alignment Chain F = 1.3e-40 41 29 View alignment Chain A = 1.3e-40 41 29 View alignment 1jaz ( Chain: A, B) Crystal structure of monoclinic form of d90e mutant of escherichia coli asparaginase ii PDB_Info PDB_Structure Escherichia coli Chain A = 1.3e-40 41 29 View alignment SCOP MMDB CATH Chain B = 1.3e-40 41 29 View alignment 1ihd ( Chain: A, C) Crystal structure of trigonal form of d90e mutant of escherichia coli asparaginase ii PDB_Info PDB_Structure Escherichia coli Chain A = 1.3e-40 41 29 View alignment SCOP MMDB CATH Chain C = 1.3e-40 41 29 View alignment 4eca ( Chain: B, D, A, C) Asparaginase from e. coli, mutant t89v with covalently bound aspartate PDB_Info PDB_Structure Escherichia coli k12 Chain B = 2.7e-40 41 28 View alignment SCOP MMDB CATH Chain D = 2.7e-40 41 28 View alignment Chain A = 2.7e-40 41 28 View alignment Chain C = 2.7e-40 41 28 View alignment 1wsa ( Chain: B, A) Structure of l-asparaginase ii precursor PDB_Info PDB_Structure Wolinella succinogenes Chain B = 2.3e-38 37 34 View alignment SCOP MMDB CATH Chain A = 2.3e-38 37 34 View alignment 3pga ( Chain: 2, 1, 4, 3) Structural characterization of pseudomonas 7a glutaminase- asparaginase PDB_Info PDB_Structure Pseudomonas sp. 7A Chain 2 = 3.8e-35 36 32 View alignment SCOP MMDB CATH Chain 1 = 3.8e-35 36 32 View alignment Chain 4 = 3.8e-35 36 32 View alignment Chain 3 = 3.8e-35 36 32 View alignment 4pga ( Chain: A, B) Glutaminase-asparaginase from pseudomonas 7a PDB_Info PDB_Structure Pseudomonas sp. 7A Chain A = 1.0e-33 35 33 View alignment SCOP MMDB CATH Chain B = 1.0e-33 35 33 View alignment 1agx ( Chain: A) Refined crystal structure of acinetobacter glutaminasificans glutaminase-asparaginase PDB_Info PDB_Structure Acinetobacter glutaminasificans 1.0e-33 36 33 View alignment SCOP MMDB CATH 1djo ( Chain: A, B) Crystal structure of pseudomonas 7a glutaminase- asparaginase with the inhibitor donv covalently bound in the active site PDB_Info PDB_Structure Pseudomonas sp. 7A Chain A = 2.7e-33 35 32 View alignment SCOP MMDB CATH Chain B = 2.7e-33 35 32 View alignment 1djp ( Chain: A, B) Crystal structure of pseudomonas 7a glutaminase- asparaginase with the inhibitor don covalently bound in the active site PDB_Info PDB_Structure Pseudomonas sp. 7A Chain A = 2.7e-33 35 32 View alignment SCOP MMDB CATH Chain B = 2.7e-33 35 32 View alignment 1zq1 ( Chain: B, A) Structure of gatde trna-dependent amidotransferase from pyrococcus abyssi PDB_Info PDB_Structure Pyrococcus abyssi Chain B = 1.7e-16 28 28 View alignment SCOP MMDB CATH Chain A = 1.7e-16 28 28 View alignment 2d6f ( Chain: A, B) Crystal structure of glu-trna(gln) amidotransferase in the complex with trna(gln) PDB_Info PDB_Structure Methanothermobacter thermautotrophicus Chain A = 1.9e-15 27 33 View alignment SCOP MMDB CATH Chain B = 1.9e-15 27 33 View alignment 1wls ( Chain: A, B) Crystal structure of l-asparaginase i homologue protein from pyrococcus horikoshii PDB_Info PDB_Structure Pyrococcus horikoshii Chain A = 2.9e-14 28 32 View alignment SCOP MMDB CATH Chain B = 2.9e-14 28 32 View alignment 1wnf ( Chain: B, A) Crystal structure of ph0066 from pyrococcus horikoshii PDB_Info PDB_Structure Pyrococcus horikoshii Chain B = 2.9e-14 28 32 View alignment SCOP MMDB CATH Chain A = 2.9e-14 28 32 View alignment 2p2d ( Chain: D, B, A, C) Crystal structure and allosteric regulation of the cytoplasmic escherichia coli l-asparaginase i PDB_Info PDB_Structure Escherichia coli Chain D = 1.7e-08 27 29 View alignment SCOP MMDB CATH Chain B = 1.7e-08 27 29 View alignment Chain A = 1.7e-08 27 29 View alignment Chain C = 1.7e-08 27 29 View alignment 2p2n ( Chain: C, B, A, D) Crystal structure and allosteric regulation of the cytoplasmic escherichia coli l-asparaginase i PDB_Info PDB_Structure Escherichia coli Chain C = 1.7e-08 27 29 View alignment SCOP MMDB CATH Chain B = 1.7e-08 27 29 View alignment Chain A = 1.7e-08 27 29 View alignment Chain D = 1.7e-08 27 29 View alignment 2him ( Chain: B, A, C, D) Crystal structure and allosteric regulation of the cytoplasmic escherichia coli l-asparaginase i PDB_Info PDB_Structure Escherichia coli Chain B = 3.7e-08 26 30 View alignment SCOP MMDB CATH Chain A = 3.7e-08 26 30 View alignment Chain C = 3.7e-08 26 30 View alignment Chain D = 3.7e-08 26 30 View alignment 2ocd ( Chain: A, D, C, B) Crystal structure of l-asparaginase i from vibrio cholerae o1 biovar eltor str. n16961 PDB_Info PDB_Structure Vibrio cholerae Chain A = 1.9e-05 24 31 View alignment SCOP MMDB CATH Chain D = 1.9e-05 24 31 View alignment Chain C = 1.9e-05 24 31 View alignment Chain B = 1.9e-05 24 31 View alignment

Genome-wide Expression and Other Large-Scale Analyses [TOP] [NEXT]
Functional Analysis Expression Connection Summary Cell cycle and metabolic oscillation Cell cycle transcript profile Cyclebase Genevestigator GermOnline SPELL Microarray Search YGAC Triples Yeast Microarray Global Viewer YeastFunc	You can also search multiple datasets simultaneously using Expression Connection for expression studies or Function Junction for other large scale analyses.

Locus History (misc. notes) [TOP] [NEXT]

Nomenclature History

Standard Name	Reference
ASP3-1	SGD (2007) Information without a citation in SGD

Mapping Notes

Date	Note
1998-11-10	Edition 15: ASP3 is located in a repeated region. SGD represents four repeats, ASP3-1, ASP3-2, ASP3-3 and ASP3-4. Cherry JM, et al. (1998) "Genetic and Physical Maps of Saccharomyces cerevisiae (Edition 15)". Pp. 414-420 in 1998 Yeast Genetics and Molecular Biology Meeting Program and Abstracts. Bethesda, MD: The Genetics Society of America

Sequence Retrieval [TOP] [NEXT]
Sequence Type	Output Format
Genomic DNA	GCG | FASTA | NoHeader
Genomic DNA with 1 kb up and downstream	GCG | FASTA | NoHeader
DNA coding sequence (without introns, without flanking regions)	GCG | FASTA | NoHeader
Protein Translation of ORF	GCG | FASTA | NoHeader
6-Frame Translation(with Restriction Map)	GCG
Restriction Fragment Sizes	GCG
Sequence Analysis Tools BLASTP BLASTN Design Primers FASTA aa FASTA nt Restriction Fragment Map Restriction Fragment Sizes Six-Frame Translation

Sequence from other databases
Sequence ID	Source
YLR155C	SGD Systematic Sequence
850850	NCBI: Gene ID
NP_013256.1	NCBI: RefSeq protein version ID
NP_013256.1	NCBI: RefSeq protein version ID
6323184	NCBI: NCBI protein GI

Map and Displays [TOP] [NEXT]
Physical, Genetic Maps:	Chromosomal Feature Map	GBrowse	Combined Physical and Genetic Map	Genetic Distance vs. Physical Distance Ratios
Similarity Viewers:	Synteny Viewer	Genomic Stripe View	SAGE Results Map

Localization [TOP] [NEXT]
Localization Resources Organelle DB (UMich) YGAC Triples YeastGFP DB (UCSF) at SGD

Community Annotation [TOP] [NEXT]

DNA & RNA Details Topic Research Highlight Reference Contributor Other DNA & RNA Details Description: ASP3 transcriptional start site is nitrogen regulated. Full length transcript is only produced during nitrogen starvation. otherTopic: Transcript length regulation Kim KW, et al. (1988) Asparaginase II of Saccharomyces cerevisiae. Characterization of the ASP3 gene. J Biol Chem 263(24):11948-53      Evan Hurowitz 2003-04-07

Literature Guide: papers categorized by topic. [TOP]
Topics	Reference	Other Genes Addressed
33 curated references; 0 references not yet curated
DNA/RNA Sequence Features	Argueso JL, et al. (2009) Genome structure of a Saccharomyces cerevisiae strain widely used in bioethanol production. Genome Res 19(12):2258-70	|ASP3-2 |ASP3-3 |ASP3-4 |ENA1 |ENA2 |ENA5 |END3 |FLO8 |HXT3 |HXT6 |HXT7 |HXT8 |MIP1 |MKT1 |MORE
DNA/RNA Sequence Features Fungal Related Genes/Proteins	Gordon JL, et al. (2009) Additions, losses, and rearrangements on the evolutionary route from a reconstructed ancestor to the modern Saccharomyces cerevisiae genome. PLoS Genet 5(5):e1000485	|ABM1 |ADH1 |ADH2 |ARI1 |ASP3-2 |ASP3-3 |ASP3-4 |AUS1 |AXL2 |AZR1 |CCT2 |DAL4 |DAL7 |DIA3 |MORE
Evolution Fungal Related Genes/Proteins	Katju V, et al. (2009) Variation in gene duplicates with low synonymous divergence in Saccharomyces cerevisiae relative to Caenorhabditis elegans. Genome Biol 10(7):R75	|AAD15 |AAD3 |ANB1 |ASP3-2 |ASP3-3 |ASP3-4 |BUD5 |COS1 |COS5 |CUP1-1 |CUP1-2 |DOG1 |DOG2 |DSF1 |MORE
Computational analysis	Biswas S, et al. (2008) Mapping gene expression quantitative trait loci by singular value decomposition and independent component analysis. BMC Bioinformatics 9:244	|ASP3-2 |ASP3-3 |ASP3-4 |ENA1 |ENA2 |ENA5 |YERCTy1-1 |ZAP1
Evolution Industrial Applications	Carreto L, et al. (2008) Comparative genomics of wild type yeast strains unveils important genome diversity. BMC Genomics 9524	|AAD10 |AAD3 |AAD6 |ADH7 |AGP3 |ARR3 |ASP3-2 |ASP3-3 |ASP3-4 |COG3 |CUP1-2 |DAK2 |DIP5 |ENA1 |MORE
Mutants/Phenotypes Strains/Constructs	Pope GA, et al. (2007) Metabolic footprinting as a tool for discriminating between brewing yeasts. Yeast 24(8):667-79	|AAD15 |AAD16 |AAD3 |ADH7 |ALD2 |ASP3-2 |ASP3-3 |ASP3-4 |GDB1 |GPH1 |HXT15 |HXT16 |MAL33
DNA/RNA Sequence Features	Steigele S, et al. (2007) Comparative analysis of structured RNAs in S. cerevisiae indicates a multitude of different functions. BMC Biol 5:25	|AIM5 |ALR1 |AMA1 |ARC40 |ARG1 |ASP3-2 |ASP3-3 |ASP3-4 |ASR1 |ATP2 |BMH1 |BMH2 |BRP1 |BUD20 |MORE
DNA/RNA Sequence Features RNA Levels and Processing Regulation of Transcription	Scherens B, et al. (2006) Identification of direct and indirect targets of the Gln3 and Gat1 activators by transcriptional profiling in response to nitrogen availability in the short and long term. FEMS Yeast Res 6(5):777-91	|ASP3-2 |ASP3-3 |ASP3-4 |AVT7 |BAP2 |BAT2 |CDC60 |DDR2 |FIS1 |GAP1 |GAT1 |GCN4 |GLN3 |GNP1 |MORE
Function/Process	Homann OR, et al. (2005) Harnessing natural diversity to probe metabolic pathways. PLoS Genet 1(6):e80	|ASP3-2 |ASP3-3 |ASP3-4 |CUP9 |DAL5 |PTR2
Regulation of Translational Regulation	Law GL, et al. (2005) The undertranslated transcriptome reveals widespread translational silencing by alternative 5' transcript leaders. Genome Biol 6(13):R111	|ALD3 |AMD2 |APA2 |AQY1 |ARG80 |ARO80 |ASP3-2 |ASP3-3 |ASP3-4 |ATG13 |ATG5 |BCK1 |CCZ1 |CRH1 |MORE
Regulation of Transcription	Oliveira EM, et al. (2003) The role of the GATA factors Gln3p, Nil1p, Dal80p and the Ure2p on ASP3 regulation in Saccharomyces cerevisiae. Yeast 20(1):31-7	|ASP3-2 |ASP3-3 |ASP3-4 |DAL80 |GAT1 |GLN3 |GZF3 |URE2
Regulation of	Bertram PG, et al. (2000) Tripartite regulation of Gln3p by TOR, Ure2p, and phosphatases. J Biol Chem 275(46):35727-33	|AGP1 |APE2 |ARG1 |ARG4 |ARO10 |ARO9 |ASP3-2 |ASP3-3 |ASP3-4 |BAT2 |CAN1 |CAR1 |CPS1 |DAL2 |MORE
Reviews	ter Schure EG, et al. (2000) The role of ammonia metabolism in nitrogen catabolite repression in Saccharomyces cerevisiae. FEMS Microbiol Rev 24(1):67-83	|ASP3-2 |ASP3-3 |ASP3-4 |BAS1 |CAN1 |CAR1 |DAL1 |DAL2 |DAL4 |DAL7 |DAL80 |DSD1 |FUR4 |GAP1 |MORE
Alias RNA Levels and Processing Regulation of	Jelinsky SA and Samson LD (1999) Global response of Saccharomyces cerevisiae to an alkylating agent. Proc Natl Acad Sci U S A 96(4):1486-91	|AAD14 |AAD16 |AAD4 |AAD6 |ABF1 |ADP1 |AGX1 |AMD2 |ARG1 |ARG3 |ARG4 |ARG5,6 |ARG7 |ARO1 |MORE
Function/Process Regulation of	Oliveira EM, et al. (1999) L-asparaginase II of saccharomyces cerevisiae. Activity profile during growth using an ure2 mutant P40-3C and a P40-3C + URE2p strain. Appl Biochem Biotechnol 77-79():311-6	|ASP3-2 |ASP3-3 |ASP3-4 |URE2
Mutants/Phenotypes Strains/Constructs	Winzeler EA, et al. (1999) Whole genome genetic-typing in yeast using high-density oligonucleotide arrays. Parasitology 118 Suppl:S73-80	|ARN2 |ASP3-2 |ASP3-3 |ASP3-4 |ATS1 |AYT1 |BDS1 |COS6 |COS7 |COS8 |FLO1 |FMP32 |HXT9 |MAL11 |MORE
Cellular Location Regulation of	Bon EP, et al. (1997) Asparaginase II of Saccharomyces cerevisiae. GLN3/URE2 regulation of a periplasmic enzyme. Appl Biochem Biotechnol 63-65():203-12	|ASP3-2 |ASP3-3 |ASP3-4 |GAP1 |GDH2 |GLN1 |GLN3 |PUT4 |URE2
Alias Cellular Location Function/Process Fungal Related Genes/Proteins Non-Fungal Related Genes/Proteins	Sinclair K, et al. (1994) The ASP1 gene of Saccharomyces cerevisiae, encoding the intracellular isozyme of L-asparaginase. Gene 144(1):37-43	|ASP1 |ASP3-2 |ASP3-3 |ASP3-4
DNA/RNA Sequence Features Protein Physical Properties Protein Sequence Features RNA Levels and Processing Regulation of Transcription	Kim KW, et al. (1988) Asparaginase II of Saccharomyces cerevisiae. Characterization of the ASP3 gene. J Biol Chem 263(24):11948-53	|ASP3-2 |ASP3-3 |ASP3-4
Regulation of	Kamerud JQ and Roon RJ (1986) Asparaginase II of Saccharomyces cerevisiae: selection of four mutations that cause derepressed enzyme synthesis. J Bacteriol 165(1):293-6	|ASP3-2 |ASP3-3 |ASP3-4
Function/Process Mapping Mutants/Phenotypes Strains/Constructs	Kim KW and Roon RJ (1984) Asparaginase II of Saccharomyces cerevisiae: positive selection of two mutations that prevent enzyme synthesis. J Bacteriol 157(3):958-61	|ASP3-2 |ASP3-3 |ASP3-4
Cell Cycle Phase Involved Cellular Location Protein Physical Properties Protein Processing/Modification/Regulation Regulation of	Kim KW and Roon RJ (1983) Asparaginase II of Saccharomyces cerevisiae: comparison of enzyme stability in vivo and in vitro. Biochemistry 22(11):2704-7	|ASP3-2 |ASP3-3 |ASP3-4
Function/Process Reviews	Cooper TG (1982) "Nitrogen metabolism in Saccharomyces cerevisiae." Pp. 39-99 in The Molecular Biology of the Yeast Saccharomyces: Metabolism and Gene Expression, edited by Strathern JN, Jones EW and Broach JR. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press	|ASP1 |ASP3-2 |ASP3-3 |ASP3-4
Function/Process Regulation of	Kim KW and Roon RJ (1982) Transport and metabolic effects of alpha-aminoisobutyric acid in Saccharomyces cerevisiae. Biochim Biophys Acta 719(2):356-62	|ASP3-2 |ASP3-3 |ASP3-4 |GAP1
Regulation of	Roon RJ, et al. (1982) Derepression of asparaginase II during exponential growth of Saccharomyces cerevisiae on ammonium ion. Arch Biochem Biophys 219(1):101-9	|ASP3-2 |ASP3-3 |ASP3-4
Function/Process Regulation of	Dunlop PC, et al. (1980) Nitrogen catabolite repression of asparaginase II in Saccharomyces cerevisiae. J Bacteriol 143(1):422-6	|ASP3-2 |ASP3-3 |ASP3-4 |GDH1
Function/Process Substrates/Ligands/Cofactors	Dunlop PC, et al. (1980) Reactions of asparaginase II of Saccharomyces cerevisiae. A mechanistic analysis of hydrolysis and hydroxylaminolysis. J Biol Chem 255(4):1542-6	|ASP3-2 |ASP3-3 |ASP3-4
Cell Cycle Phase Involved Regulation of	Pauling KD and Jones GE (1980) Asparaginase II of Saccharomyces cerevisiae: inactivation during the transition to stationary phase. Biochim Biophys Acta 616(2):271-82	|ASP3-2 |ASP3-3 |ASP3-4
Cellular Location Function/Process Protein Physical Properties Techniques and Reagents	Dunlop PC, et al. (1978) Characterization of two forms of asparaginase in Saccharomyces cerevisiae. J Biol Chem 253(4):1297-304	|ASP3-2 |ASP3-3 |ASP3-4
Function/Process Mapping Mutants/Phenotypes Strains/Constructs	Jones GE (1977) Genetic and physiological relationships between L-asparaginase I and asparaginase II in Saccharomyces cerevisiae. J Bacteriol 130(1):128-30	|ASP1 |ASP3-2 |ASP3-3 |ASP3-4
Function/Process Fungal Related Genes/Proteins Transcription	Jones GE (1977) Genetics of expression of asparaginase II activity in Saccharomyces cerevisiae. J Bacteriol 129(2):1165-7	|ASP3-2 |ASP3-3 |ASP3-4
Cellular Location Function/Process Substrates/Ligands/Cofactors	Dunlop PC, et al. (1976) Utilization of D-asparagine by Saccharomyces cerevisiae. J Bacteriol 125(3):999-1004	|ASP3-2 |ASP3-3 |ASP3-4
Cellular Location Function/Process	Dunlop PC and Roon RJ (1975) L-Asparaginase of Saccharomyces cerevisiae: an extracellular Enzyme. J Bacteriol 122(3):1017-24	|ASP3-2 |ASP3-3 |ASP3-4

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