CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006804
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Transaldolase 
Protein Synonyms/Alias
  
Gene Name
 TALDO1 
Gene Synonyms/Alias
 TAL; TALDO; TALDOR 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
71EAIAYGRKLGGSQEDubiquitination[1, 2, 3]
81GSQEDQIKNAIDKLFubiquitination[1]
115DARLSFDKDAMVARAubiquitination[1, 3, 4, 5, 6]
130RRLIELYKEAGISKDubiquitination[1, 4, 5, 6, 7]
203WHVANTDKKSYEPLEubiquitination[3]
204HVANTDKKSYEPLEDubiquitination[1, 3]
215PLEDPGVKSVTKIYNubiquitination[1, 3, 4, 5, 6, 7]
219PGVKSVTKIYNYYKKacetylation[8]
219PGVKSVTKIYNYYKKubiquitination[1, 3, 4, 5, 6, 7]
230YYKKFSYKTIVMGASubiquitination[4, 6]
258DFLTISPKLLGELLQubiquitination[1]
269ELLQDNAKLVPVLSAacetylation[8]
269ELLQDNAKLVPVLSAubiquitination[1, 3, 4, 5, 6, 7, 9, 10]
277LVPVLSAKAAQASDLubiquitination[1, 3, 4, 5, 6, 7, 9, 11]
286AQASDLEKIHLDEKSacetylation[8, 11, 12, 13, 14]
286AQASDLEKIHLDEKSubiquitination[3]
292EKIHLDEKSFRWLHNubiquitination[3]
307EDQMAVEKLSDGIRKacetylation[14]
307EDQMAVEKLSDGIRKubiquitination[1, 3, 4, 6, 11]
314KLSDGIRKFAADAVKubiquitination[3, 4, 6]
321KFAADAVKLERMLTEacetylation[8, 11, 13, 14]
321KFAADAVKLERMLTEubiquitination[3, 4, 5, 6]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [6] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [7] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [8] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [9] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [10] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [11] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [12] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [13] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [14] 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
Functional Description
 Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. 
Sequence Annotation
 ACT_SITE 142 142 Schiff-base intermediate with substrate.
 MOD_RES 219 219 N6-acetyllysine.
 MOD_RES 269 269 N6-acetyllysine.
 MOD_RES 286 286 N6-acetyllysine.
 MOD_RES 321 321 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Cytoplasm; Disease mutation; Pentose shunt; Reference proteome; Schiff base; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 337 AA 
Protein Sequence
MSSSPVKRQR MESALDQLKQ FTTVVADTGD FHAIDEYKPQ DATTNPSLIL AAAQMPAYQE 60
LVEEAIAYGR KLGGSQEDQI KNAIDKLFVL FGAEILKKIP GRVSTEVDAR LSFDKDAMVA 120
RARRLIELYK EAGISKDRIL IKLSSTWEGI QAGKELEEQH GIHCNMTLLF SFAQAVACAE 180
AGVTLISPFV GRILDWHVAN TDKKSYEPLE DPGVKSVTKI YNYYKKFSYK TIVMGASFRN 240
TGEIKALAGC DFLTISPKLL GELLQDNAKL VPVLSAKAAQ ASDLEKIHLD EKSFRWLHNE 300
DQMAVEKLSD GIRKFAADAV KLERMLTERM FNAENGK 337 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 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; TAS:ProtInc.
 GO:0006112; P:energy reserve metabolic process; TAS:Reactome.
 GO:0006002; P:fructose 6-phosphate metabolic process; IEA:Compara.
 GO:0019682; P:glyceraldehyde-3-phosphate metabolic process; IEA:Compara.
 GO:0006098; P:pentose-phosphate shunt; TAS:Reactome.
 GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IEA:Compara.
 GO:0005999; P:xylulose biosynthetic process; TAS:Reactome. 
Interpro
 IPR013785; Aldolase_TIM.
 IPR001585; Transaldolase.
 IPR004730; Transaldolase_1.
 IPR018225; Transaldolase_AS. 
Pfam
 PF00923; Transaldolase 
SMART
  
PROSITE
 PS01054; TRANSALDOLASE_1
 PS00958; TRANSALDOLASE_2 
PRINTS