CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006737
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Low specificity L-threonine aldolase 
Protein Synonyms/Alias
 Low specificity L-TA; TA 
Gene Name
 GLY1 
Gene Synonyms/Alias
 YEL046C; SYGP-ORF34 
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
62TVARMAGKEAGLFCVubiquitination[1]
228SVLVGNLKFVKKATHacetylation[2]
228SVLVGNLKFVKKATHubiquitination[1, 3, 4, 5, 6, 7, 8, 9, 10]
301NFVFINLKAARMDPDubiquitination[1]
312MDPDVLVKKGLKYNVacetylation[2]
312MDPDVLVKKGLKYNVubiquitination[1]
320KGLKYNVKLMGGRVSubiquitination[1]
383GNAIREIKTYKY***ubiquitination[1]
Reference
 [1] 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]
 [2] 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]
 [3] A proteomics approach to understanding protein ubiquitination.
 Peng J, Schwartz D, Elias JE, Thoreen CC, Cheng D, Marsischky G, Roelofs J, Finley D, Gygi SP.
 Nat Biotechnol. 2003 Aug;21(8):921-6. [PMID: 12872131]
 [4] A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery.
 Hitchcock AL, Auld K, Gygi SP, Silver PA.
 Proc Natl Acad Sci U S A. 2003 Oct 28;100(22):12735-40. [PMID: 14557538]
 [5] A tandem affinity tag for two-step purification under fully denaturing conditions: application in ubiquitin profiling and protein complex identification combined with in vivocross-linking.
 Tagwerker C, Flick K, Cui M, Guerrero C, Dou Y, Auer B, Baldi P, Huang L, Kaiser P.
 Mol Cell Proteomics. 2006 Apr;5(4):737-48. [PMID: 16432255]
 [6] Systematic approach for validating the ubiquitinated proteome.
 Seyfried NT, Xu P, Duong DM, Cheng D, Hanfelt J, Peng J.
 Anal Chem. 2008 Jun 1;80(11):4161-9. [PMID: 18433149]
 [7] Computational identification of ubiquitylation sites from protein sequences.
 Tung CW, Ho SY.
 BMC Bioinformatics. 2008 Jul 15;9:310. [PMID: 18625080]
 [8] Identification, analysis, and prediction of protein ubiquitination sites.
 Radivojac P, Vacic V, Haynes C, Cocklin RR, Mohan A, Heyen JW, Goebl MG, Iakoucheva LM.
 Proteins. 2010 Feb 1;78(2):365-80. [PMID: 19722269]
 [9] A perturbed ubiquitin landscape distinguishes between ubiquitin in trafficking and in proteolysis.
 Ziv I, Matiuhin Y, Kirkpatrick DS, Erpapazoglou Z, Leon S, Pantazopoulou M, Kim W, Gygi SP, Haguenauer-Tsapis R, Reis N, Glickman MH, Kleifeld O.
 Mol Cell Proteomics. 2011 May;10(5):M111.009753. [PMID: 21427232]
 [10] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047
Functional Description
 Catalyzes the cleavage of L-allo-threonine and L- threonine to glycine and acetaldehyde. 
Sequence Annotation
 MOD_RES 213 213 N6-(pyridoxal phosphate)lysine (By
 MOD_RES 367 367 Phosphoserine.
 MOD_RES 369 369 Phosphoserine.
 MOD_RES 370 370 Phosphothreonine.
 CROSSLNK 228 228 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Complete proteome; Isopeptide bond; Lyase; Phosphoprotein; Pyridoxal phosphate; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 387 AA 
Protein Sequence
MTEFELPPKY ITAANDLRSD TFTTPTAEMM EAALEASIGD AVYGEDVDTV RLEQTVARMA 60
GKEAGLFCVS GTLSNQIAIR THLMQPPYSI LCDYRAHVYT HEAAGLAILS QAMVVPVVPS 120
NGDYLTLEDI KSHYVPDDGD IHGAPTRLIS LENTLHGIVY PLEELVRIKA WCMENGLKLH 180
CDGARIWNAA AQSGVPLKQY GEIFDSISIC LSKSMGAPIG SVLVGNLKFV KKATHFRKQQ 240
GGGIRQSGMM ARMALVNINN DWKSQLLYSH SLAHELAEYC EAKGIPLESP ADTNFVFINL 300
KAARMDPDVL VKKGLKYNVK LMGGRVSFHY QVTRDTLEKV KLAISEAFDY AKEHPFDCNG 360
PTQIYRSEST EVDVDGNAIR EIKTYKY 387 
Gene Ontology
 GO:0005829; C:cytosol; IDA:SGD.
 GO:0008732; F:L-allo-threonine aldolase activity; IDA:SGD.
 GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
 GO:0006545; P:glycine biosynthetic process; IDA:SGD.
 GO:0006567; P:threonine catabolic process; IDA:SGD. 
Interpro
 IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
 IPR015424; PyrdxlP-dep_Trfase.
 IPR015421; PyrdxlP-dep_Trfase_major_sub1.
 IPR015422; PyrdxlP-dep_Trfase_major_sub2.
 IPR023603; Threonine_aldolase. 
Pfam
 PF01212; Beta_elim_lyase 
SMART
  
PROSITE
  
PRINTS