CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018926
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Transaldolase 
Protein Synonyms/Alias
  
Gene Name
 Taldo1 
Gene Synonyms/Alias
 Tal; Taldo 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
71EAIAYGKKLGGPQEEubiquitination[1]
81GPQEEQIKNAIDKLFubiquitination[1]
86QIKNAIDKLFVLFGAacetylation[2]
115DARLSFDKDAMVARAacetylation[2, 3]
115DARLSFDKDAMVARAubiquitination[1]
130RRLIELYKEAGVGKDacetylation[2]
130RRLIELYKEAGVGKDubiquitination[1]
142GKDRILIKLSSTWEGacetylation[2]
203WHVANTDKKSYEPQEubiquitination[1]
204HVANTDKKSYEPQEDacetylation[2]
204HVANTDKKSYEPQEDubiquitination[1]
215PQEDPGVKSVTKIYNubiquitination[1, 4]
219PGVKSVTKIYNYYKKacetylation[2]
219PGVKSVTKIYNYYKKubiquitination[1]
225TKIYNYYKKFGYKTIacetylation[2]
230YYKKFGYKTIVMGASacetylation[2]
245FRNTGEIKALAGCDFacetylation[2]
258DFLTISPKLLGELLKacetylation[2, 5]
258DFLTISPKLLGELLKubiquitination[1, 4]
265KLLGELLKDNSKLAPacetylation[2]
265KLLGELLKDNSKLAPubiquitination[1]
269ELLKDNSKLAPALSVacetylation[6]
269ELLKDNSKLAPALSVubiquitination[1]
277LAPALSVKAAQTSDSubiquitination[1]
286AQTSDSEKIHLDEKAacetylation[2, 3]
286AQTSDSEKIHLDEKAubiquitination[1]
292EKIHLDEKAFRWLHNacetylation[2]
292EKIHLDEKAFRWLHNubiquitination[1]
307EDQMAVEKLSDGIRKacetylation[6]
307EDQMAVEKLSDGIRKubiquitination[1]
314KLSDGIRKFAADAIKphosphoglycerylation[7]
314KLSDGIRKFAADAIKubiquitination[1]
321KFAADAIKLERMLTEacetylation[2, 3, 5, 8]
321KFAADAIKLERMLTEubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [4] BTB-ZF factors recruit the E3 ligase cullin 3 to regulate lymphoid effector programs.
 Mathew R, Seiler MP, Scanlon ST, Mao AP, Constantinides MG, Bertozzi-Villa C, Singer JD, Bendelac A.
 Nature. 2012 Nov 22;491(7425):618-21. [PMID: 23086144]
 [5] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [6] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [7] Functional lysine modification by an intrinsically reactive primary glycolytic metabolite.
 Moellering RE, Cravatt BF.
 Science. 2013 Aug 2;341(6145):549-53. [PMID: 23908237]
 [8] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
 Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
 J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379] 
Functional Description
 Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway (By similarity). 
Sequence Annotation
 ACT_SITE 142 142 Schiff-base intermediate with substrate
 MOD_RES 219 219 N6-acetyllysine (By similarity).
 MOD_RES 269 269 N6-acetyllysine (By similarity).
 MOD_RES 286 286 N6-acetyllysine (By similarity).
 MOD_RES 321 321 N6-acetyllysine (By similarity).  
Keyword
 3D-structure; Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Pentose shunt; Reference proteome; Schiff base; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 337 AA 
Protein Sequence
MSGSPVKRQR MESALDQLKQ FTTVVADTGD FNAIDEYKPQ DATTNPSLIL AAAQMPAYQE 60
LVEEAIAYGK KLGGPQEEQI KNAIDKLFVL FGAEILKKIP GRVSTEVDAR LSFDKDAMVA 120
RARRLIELYK EAGVGKDRIL IKLSSTWEGI QAGKELEEQH GIHCNMTLLF SFAQAVACAE 180
AGVTLISPFV GRILDWHVAN TDKKSYEPQE DPGVKSVTKI YNYYKKFGYK TIVMGASFRN 240
TGEIKALAGC DFLTISPKLL GELLKDNSKL APALSVKAAQ TSDSEKIHLD EKAFRWLHNE 300
DQMAVEKLSD GIRKFAADAI KLERMLTERM FSAENGK 337 
Gene Ontology
 GO:0005829; C:cytosol; IEA:Compara.
 GO:0043231; C:intracellular membrane-bounded organelle; IEA:Compara.
 GO:0048029; F:monosaccharide binding; IEA:Compara.
 GO:0004801; F:sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase activity; IEA:EC.
 GO:0006002; P:fructose 6-phosphate metabolic process; IEA:Compara.
 GO:0019682; P:glyceraldehyde-3-phosphate metabolic process; IEA:Compara.
 GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IEA:Compara. 
Interpro
 IPR013785; Aldolase_TIM.
 IPR001585; Transaldolase.
 IPR004730; Transaldolase_1.
 IPR018225; Transaldolase_AS. 
Pfam
 PF00923; Transaldolase 
SMART
  
PROSITE
 PS01054; TRANSALDOLASE_1
 PS00958; TRANSALDOLASE_2 
PRINTS