CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-037132
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Glyceraldehyde-3-phosphate dehydrogenase 
Protein Synonyms/Alias
  
Gene Name
 GAPDH 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
9EEMRDPSKIKWGDAGubiquitination[1]
11MRDPSKIKWGDAGAEubiquitination[1, 2, 3, 4, 5, 6, 7, 8]
32GVFTTMEKAGAHLQGacetylation[8, 9]
32GVFTTMEKAGAHLQGphosphoglycerylation[10]
32GVFTTMEKAGAHLQGubiquitination[1, 3, 4, 6, 7, 8]
42AHLQGGAKRVIISAPacetylation[8]
42AHLQGGAKRVIISAPubiquitination[1, 3, 4, 5, 7]
64VMGVNHEKYDNSLKIacetylation[8, 9, 11, 12]
64VMGVNHEKYDNSLKIphosphoglycerylation[10]
64VMGVNHEKYDNSLKIubiquitination[1, 2, 3, 6, 7, 8]
70EKYDNSLKIISNASCacetylation[8]
70EKYDNSLKIISNASCphosphoglycerylation[10]
70EKYDNSLKIISNASCubiquitination[1, 2, 3, 4, 5, 6, 8]
87NCLAPLAKVIHDNFGphosphoglycerylation[10]
111HAITATQKTVDGPSGacetylation[8, 9, 12]
111HAITATQKTVDGPSGubiquitination[1, 3, 6, 7, 8, 13]
119TVDGPSGKLWRDGRGacetylation[8, 11, 12]
119TVDGPSGKLWRDGRGphosphoglycerylation[10]
119TVDGPSGKLWRDGRGubiquitination[1, 2, 3, 4, 6, 7, 8, 13]
140PASTGAAKAVGKVIPacetylation[8, 9]
140PASTGAAKAVGKVIPphosphoglycerylation[10]
140PASTGAAKAVGKVIPubiquitination[1, 2, 3, 4, 5, 6, 7, 8, 13]
144GAAKAVGKVIPELNGacetylation[8, 12]
144GAAKAVGKVIPELNGubiquitination[1, 2, 3, 6, 7, 8]
152VIPELNGKLTGMAFRacetylation[8, 12]
152VIPELNGKLTGMAFRubiquitination[1, 2, 3, 6, 7, 8]
176DLTCRLEKPAKYDDIubiquitination[1, 5, 6, 8]
179CRLEKPAKYDDIKKVacetylation[8, 9, 11, 12]
179CRLEKPAKYDDIKKVphosphoglycerylation[10]
179CRLEKPAKYDDIKKVubiquitination[1, 3, 5, 6, 7, 8]
184PAKYDDIKKVVKQASacetylation[9]
184PAKYDDIKKVVKQASubiquitination[1, 3, 5, 7]
185AKYDDIKKVVKQASEphosphoglycerylation[10]
185AKYDDIKKVVKQASEubiquitination[3, 6]
188DDIKKVVKQASEGPLacetylation[8, 11, 12]
188DDIKKVVKQASEGPLphosphoglycerylation[10]
188DDIKKVVKQASEGPLubiquitination[1, 2, 3, 4, 6, 7, 8, 13]
196QASEGPLKGILGYTEubiquitination[1, 3]
259LMAHMASKE******acetylation[8, 9, 12]
259LMAHMASKE******ubiquitination[1, 3, 5, 6, 7, 8]
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] 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] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [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] 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] 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]
 [10] Functional lysine modification by an intrinsically reactive primary glycolytic metabolite.
 Moellering RE, Cravatt BF.
 Science. 2013 Aug 2;341(6145):549-53. [PMID: 23908237]
 [11] 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]
 [12] 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]
 [13] 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
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Oxidoreductase; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 260 AA 
Protein Sequence
MEEMRDPSKI KWGDAGAEYV VESTGVFTTM EKAGAHLQGG AKRVIISAPS ADAPMFVMGV 60
NHEKYDNSLK IISNASCTTN CLAPLAKVIH DNFGIVEGLM TTVHAITATQ KTVDGPSGKL 120
WRDGRGALQN IIPASTGAAK AVGKVIPELN GKLTGMAFRV PTANVSVVDL TCRLEKPAKY 180
DDIKKVVKQA SEGPLKGILG YTEHQVVSSD FNSDTHSSTF DAGAGIALND HFVKLISWYD 240
NEFGYSNRVV DLMAHMASKE 260 
Gene Ontology
 GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:EC. 
Interpro
 IPR020831; GlycerAld/Erythrose_P_DH.
 IPR020830; GlycerAld_3-P_DH_AS.
 IPR020829; GlycerAld_3-P_DH_cat.
 IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
 IPR016040; NAD(P)-bd_dom. 
Pfam
 PF02800; Gp_dh_C
 PF00044; Gp_dh_N 
SMART
 SM00846; Gp_dh_N 
PROSITE
 PS00071; GAPDH 
PRINTS
 PR00078; G3PDHDRGNASE.