CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001838
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tryptophan synthase 
Protein Synonyms/Alias
  
Gene Name
 TRP5 
Gene Synonyms/Alias
 YGL026C 
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
206SRVRKYTKDTPLAVGacetylation[1]
249CGDAPEGKRYDVAKEubiquitination[2]
272AKHKVLSKDEFFAFQacetylation[1]
280DEFFAFQKESLKSANacetylation[1]
301DEFDENHKHPIRFGDacetylation[1]
396LAQVLLAKRLGKKNVubiquitination[2]
461IAVTNGTKTLRDATSubiquitination[2]
507TFQSVIGKETKEQFAacetylation[1]
510SVIGKETKEQFAAMNubiquitination[2]
563GGDGVDTKFHSATLTacetylation[1]
690SVAEVLPKLGPKIGWacetylation[1]
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, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301
Functional Description
  
Sequence Annotation
 REGION 1 297 Tryptophan synthase alpha chain.
 REGION 298 707 Tryptophan synthase beta chain.
 ACT_SITE 50 50 Proton acceptor (By similarity).
 ACT_SITE 61 61 Proton acceptor (By similarity).
 MOD_RES 384 384 N6-(pyridoxal phosphate)lysine (By
 MOD_RES 540 540 Phosphoserine.
 MOD_RES 683 683 Phosphoserine.  
Keyword
 Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Complete proteome; Lyase; Phosphoprotein; Pyridoxal phosphate; Reference proteome; Tryptophan biosynthesis. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 707 AA 
Protein Sequence
MSEQLRQTFA NAKKENRNAL VTFMTAGYPT VKDTVPILKG FQDGGVDIIE LGMPFSDPIA 60
DGPTIQLSNT VALQNGVTLP QTLEMVSQAR NEGVTVPIIL MGYYNPILNY GEERFIQDAA 120
KAGANGFIIV DLPPEEALKV RNYINDNGLS LIPLVAPSTT DERLELLSHI ADSFVYVVSR 180
MGTTGVQSSV ASDLDELISR VRKYTKDTPL AVGFGVSTRE HFQSVGSVAD GVVIGSKIVT 240
LCGDAPEGKR YDVAKEYVQG ILNGAKHKVL SKDEFFAFQK ESLKSANVKK EILDEFDENH 300
KHPIRFGDFG GQYVPEALHA CLRELEKGFD EAVADPTFWE DFKSLYSYIG RPSSLHKAER 360
LTEHCQGAQI WLKREDLNHT GSHKINNALA QVLLAKRLGK KNVIAETGAG QHGVATATAC 420
AKFGLTCTVF MGAEDVRRQA LNVFRMRILG AKVIAVTNGT KTLRDATSEA FRFWVTNLKT 480
TYYVVGSAIG PHPYPTLVRT FQSVIGKETK EQFAAMNNGK LPDAVVACVG GGSNSTGMFS 540
PFEHDTSVKL LGVEAGGDGV DTKFHSATLT AGRPGVFHGV KTYVLQDSDG QVHDTHSVSA 600
GLDYPGVGPE LAYWKSTGRA QFIAATDAQA LLGFKLLSQL EGIIPALESS HAVYGACELA 660
KTMKPDQHLV INISGRGDKD VQSVAEVLPK LGPKIGWDLR FEEDPSA 707 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:SGD.
 GO:0005634; C:nucleus; IDA:SGD.
 GO:0004834; F:tryptophan synthase activity; IDA:SGD. 
Interpro
 IPR013785; Aldolase_TIM.
 IPR011060; RibuloseP-bd_barrel.
 IPR001926; Trp_syn_b_sub_like_PLP_eny_SF.
 IPR006653; Trp_synth_b_CS.
 IPR006654; Trp_synth_beta.
 IPR023026; Trp_synth_beta/beta-like.
 IPR018204; Trp_synthase_alpha_AS.
 IPR002028; Trp_synthase_suA. 
Pfam
 PF00291; PALP
 PF00290; Trp_syntA 
SMART
  
PROSITE
 PS00167; TRP_SYNTHASE_ALPHA
 PS00168; TRP_SYNTHASE_BETA 
PRINTS