CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-043398
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Fructose-bisphosphate aldolase A 
Protein Synonyms/Alias
  
Gene Name
 ALDOA 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
82HRIVAPGKGILAADEubiquitination[1, 2, 3, 4, 5, 6, 7, 8]
96ESTGSIAKRLQSIGTacetylation[8, 9, 10, 11]
96ESTGSIAKRLQSIGTubiquitination[2, 3, 4, 5, 6, 7, 8, 12]
207AKWRCVLKIGEHTPSacetylation[8, 11]
207AKWRCVLKIGEHTPSubiquitination[2, 4, 6, 7, 8, 12]
254PDGDHDLKRCQYVTEacetylation[11]
254PDGDHDLKRCQYVTEubiquitination[3, 4, 6, 7, 8, 12]
262RCQYVTEKVLAAVYKubiquitination[2, 3, 4, 6, 7, 8]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [7] 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]
 [8] 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]
 [9] Monoclonal antibody cocktail as an enrichment tool for acetylome analysis.
 Shaw PG, Chaerkady R, Zhang Z, Davidson NE, Pandey A.
 Anal Chem. 2011 May 15;83(10):3623-6. [PMID: 21466224]
 [10] 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]
 [11] 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]
 [12] 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
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 278 AA 
Protein Sequence
MARRKPEGSS FNMTHLSMAM AFSFPPVASG QLHPQLGNTQ HQTELGKELA TTSTMPYQYP 60
ALTPEQKKEL SDIAHRIVAP GKGILAADES TGSIAKRLQS IGTENTEENR RFYRQLLLTA 120
DDRVNPCIGG VILFHETLYQ KADDGRPFPQ VIKSKGGVVG IKVDKGVVPL AGTNGETTTQ 180
GLDGLSERCA QYKKDGADFA KWRCVLKIGE HTPSALAIME NANVLARYAS ICQQNGIVPI 240
VEPEILPDGD HDLKRCQYVT EKVLAAVYKA LSDHHIYL 278 
Gene Ontology
 GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:InterPro.
 GO:0006096; P:glycolysis; IEA:InterPro. 
Interpro
 IPR000741; Aldolase_I.
 IPR013785; Aldolase_TIM. 
Pfam
 PF00274; Glycolytic 
SMART
  
PROSITE
  
PRINTS