CPLM-002087

Genbank Nucleotide ID

Fructose-bisphosphate aldolase A

Protein Synonyms/Alias

Lung cancer antigen NY-LU-1; Muscle-type aldolase

Homo sapiens (Human)

Position	Peptide	Type	References
13	PALTPEQKKELSDIA	acetylation	[1, 2]
13	PALTPEQKKELSDIA	ubiquitination	[3, 4, 5]
14	ALTPEQKKELSDIAH	ubiquitination	[5, 6, 7]
28	HRIVAPGKGILAADE	ubiquitination	[4, 5, 6, 7, 8, 9, 10, 11, 12, 13]
42	ESTGSIAKRLQSIGT	acetylation	[1, 2, 14]
42	ESTGSIAKRLQSIGT	ubiquitination	[4, 5, 6, 7, 8, 10, 11, 12, 13]
99	RPFPQVIKSKGGVVG	ubiquitination	[5, 10, 13]
101	FPQVIKSKGGVVGIK	ubiquitination	[5, 10]
108	KGGVVGIKVDKGVVP	acetylation	[14]
108	KGGVVGIKVDKGVVP	ubiquitination	[4, 5, 6, 7, 10, 11, 12, 13]
111	VVGIKVDKGVVPLAG	malonylation	[15]
111	VVGIKVDKGVVPLAG	ubiquitination	[4, 5, 6, 7, 10, 12, 13]
140	ERCAQYKKDGADFAK	ubiquitination	[5, 10]
147	KDGADFAKWRCVLKI	acetylation	[1, 14]
147	KDGADFAKWRCVLKI	ubiquitination	[4, 5, 7, 10, 11, 12, 13]
153	AKWRCVLKIGEHTPS	ubiquitination	[4, 5, 6, 7, 13]
200	PDGDHDLKRCQYVTE	ubiquitination	[4, 5, 10, 13]
208	RCQYVTEKVLAAVYK	ubiquitination	[4, 5, 7, 10, 11]
215	KVLAAVYKALSDHHI	ubiquitination	[5]
230	YLEGTLLKPNMVTPG	acetylation	[14]
230	YLEGTLLKPNMVTPG	ubiquitination	[5, 10]
294	INKCPLLKPWALTFS	ubiquitination	[4, 5, 10, 11]
312	ALQASALKAWGGKKE	malonylation	[15]
312	ALQASALKAWGGKKE	ubiquitination	[5, 6, 7, 12]
317	ALKAWGGKKENLKAA	ubiquitination	[4, 5]
318	LKAWGGKKENLKAAQ	ubiquitination	[5, 10, 12, 13]
322	GGKKENLKAAQEEYV	ubiquitination	[4, 5, 6, 7, 9, 10, 12, 13]
330	AAQEEYVKRALANSL	acetylation	[14]
330	AAQEEYVKRALANSL	ubiquitination	[4, 5, 6, 7, 9, 10, 13]
342	NSLACQGKYTPSGQA	ubiquitination	[4, 5, 7]

[1] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
[2] Proteome-wide prediction of acetylation substrates.
Basu A, Rose KL, Zhang J, Beavis RC, Ueberheide B, Garcia BA, Chait B, Zhao Y, Hunt DF, Segal E, Allis CD, Hake SB.
Proc Natl Acad Sci U S A. 2009 Aug 18;106(33):13785-90. [PMID: 19666589]
[3] 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]
[4] 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]
[5] 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]
[6] 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]
[7] 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]
[8] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
Xu G, Paige JS, Jaffrey SR.
Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
[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] 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]
[11] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
[12] 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]
[13] 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]
[14] 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]
[15] The first identification of lysine malonylation substrates and its regulatory enzyme.
Peng C, Lu Z, Xie Z, Cheng Z, Chen Y, Tan M, Luo H, Zhang Y, He W, Yang K, Zwaans BM, Tishkoff D, Ho L, Lombard D, He TC, Dai J, Verdin E, Ye Y, Zhao Y.
Mol Cell Proteomics. 2011 Dec;10(12):M111.012658. [PMID: 21908771]

Functional Description

Plays a key role in glycolysis and gluconeogenesis. In addition, may also function as scaffolding protein (By similarity).

ACT_SITE 188 188 Proton acceptor (By similarity).
ACT_SITE 230 230 Schiff-base intermediate with
BINDING 56 56 Substrate.
BINDING 147 147 Substrate.
MOD_RES 36 36 Phosphoserine.
MOD_RES 39 39 Phosphoserine.
MOD_RES 42 42 N6-acetyllysine.
MOD_RES 46 46 Phosphoserine.
MOD_RES 108 108 N6-acetyllysine.
MOD_RES 111 111 N6-malonyllysine.
MOD_RES 174 174 Nitrated tyrosine (By similarity).
MOD_RES 312 312 N6-malonyllysine.
MOD_RES 330 330 N6-acetyllysine.

3D-structure; Acetylation; Alternative splicing; Complete proteome; Direct protein sequencing; Disease mutation; Glycogen storage disease; Glycolysis; Hereditary hemolytic anemia; Lyase; Nitration; Phosphoprotein; Polymorphism; Reference proteome; Schiff base.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0015629; C:actin cytoskeleton; IDA:BHF-UCL.
GO:0005829; C:cytosol; TAS:Reactome.
GO:0070062; C:extracellular vesicular exosome; IDA:BHF-UCL.
GO:0031674; C:I band; TAS:BHF-UCL.
GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
GO:0003779; F:actin binding; TAS:BHF-UCL.
GO:0070061; F:fructose binding; IDA:BHF-UCL.
GO:0004332; F:fructose-bisphosphate aldolase activity; IDA:BHF-UCL.
GO:0042802; F:identical protein binding; TAS:BHF-UCL.
GO:0015631; F:tubulin binding; TAS:BHF-UCL.
GO:0007015; P:actin filament organization; TAS:BHF-UCL.
GO:0006754; P:ATP biosynthetic process; IMP:BHF-UCL.
GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IDA:BHF-UCL.
GO:0006000; P:fructose metabolic process; IMP:BHF-UCL.
GO:0006094; P:gluconeogenesis; TAS:Reactome.
GO:0006096; P:glycolysis; IMP:BHF-UCL.
GO:0046716; P:muscle cell homeostasis; IMP:BHF-UCL.
GO:0030168; P:platelet activation; TAS:Reactome.
GO:0002576; P:platelet degranulation; TAS:Reactome.
GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
GO:0008360; P:regulation of cell shape; IDA:BHF-UCL.
GO:0006941; P:striated muscle contraction; IMP:BHF-UCL.

IPR000741; Aldolase_I.
IPR013785; Aldolase_TIM.

PS00158; ALDOLASE_CLASS_I