CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008108
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Asparagine synthetase [glutamine-hydrolyzing] 2 
Protein Synonyms/Alias
 Glutamine-dependent asparagine synthetase 2 
Gene Name
 ASN2 
Gene Synonyms/Alias
 YGR124W; G6358 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
17HEDIHNFKPKALQLSacetylation[1]
91REMCSDYKFQTFSDCubiquitination[2]
253IAARETEKANADANEubiquitination[2]
455IEKYILRKAFDTTDEubiquitination[2]
529EAYWYRLKFDAWFPQubiquitination[2]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301] 
Functional Description
  
Sequence Annotation
 DOMAIN 2 186 Glutamine amidotransferase type-2.
 DOMAIN 194 545 Asparagine synthetase.
 NP_BIND 365 366 ATP (By similarity).
 REGION 49 53 Glutamine binding (By similarity).
 REGION 74 76 Glutamine binding (By similarity).
 ACT_SITE 2 2 For GATase activity (By similarity).
 BINDING 97 97 Glutamine (By similarity).
 BINDING 233 233 ATP; via carbonyl oxygen (By similarity).
 BINDING 291 291 ATP; via amide nitrogen and carbonyl  
Keyword
 Amino-acid biosynthesis; Asparagine biosynthesis; ATP-binding; Complete proteome; Glutamine amidotransferase; Ligase; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 572 AA 
Protein Sequence
MCGIFAAFKH EDIHNFKPKA LQLSKKIRHR GPDWSGNAVM NSTIFVHERL AIVGLDSGAQ 60
PITSADGEYM LGVNGEIYNH IQLREMCSDY KFQTFSDCEP IIPLYLEHDI DAPKYLDGMF 120
AFCLYDSKKD RIVAARDPIG VVTLYMGRSS QSPETVYFAS ELKCLTDVCD SIISFPPGHV 180
YDSETDKITR YFTPDWLDEK RIPSTPVDYH AIRHSLEKAV RKRLMAEVPY GVLLSGGLDS 240
SLIAAIAARE TEKANADANE DNNVDEKQLA GIDDQGHLHT SGWSRLHSFA IGLPNAPDLQ 300
AARKVAKFIG SIHHEHTFTL QEGLDALDDV IYHLETYDVT TIRASTPMFL LSRKIKAQGV 360
KMVLSGEGSD EIFGGYLYFA QAPSAAEFHT ESVQRVKNLH LADCLRANKS TMAWGLEARV 420
PFLDKDFLQL CMNIDPNEKM IKPKEGRIEK YILRKAFDTT DEPDVKPYLP EEILWRQKEQ 480
FSDGVGYSWI DGLRDTAERA ISDAMFANPK ADWGDDIPTT KEAYWYRLKF DAWFPQKTAA 540
DTVMRWIPKA DWGCAEDPSG RYAKIHEKHV SA 572 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:SGD.
 GO:0004066; F:asparagine synthase (glutamine-hydrolyzing) activity; IDA:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0006529; P:asparagine biosynthetic process; IGI:SGD.
 GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
 GO:0070981; P:L-asparagine biosynthetic process; IEA:UniProtKB-UniPathway. 
Interpro
 IPR006426; Asn_synth_AEB.
 IPR001962; Asn_synthase.
 IPR017932; GATase_2_dom.
 IPR000583; GATase_dom.
 IPR014729; Rossmann-like_a/b/a_fold. 
Pfam
 PF00733; Asn_synthase
 PF13537; GATase_7 
SMART
  
PROSITE
 PS51278; GATASE_TYPE_2 
PRINTS