CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010686
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Fumarate hydratase, mitochondrial 
Protein Synonyms/Alias
 Fumarase; EF-3 
Gene Name
 Fh 
Gene Synonyms/Alias
 Fh1 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
58FDTFGELKVPTDKYYacetylation[1, 2, 3]
58FDTFGELKVPTDKYYsuccinylation[3]
58FDTFGELKVPTDKYYubiquitination[4]
63ELKVPTDKYYGAQTVacetylation[1, 2, 3, 5, 6, 7, 8, 9, 10, 11]
63ELKVPTDKYYGAQTVsuccinylation[3]
63ELKVPTDKYYGAQTVubiquitination[4]
77VRSTMNFKIGGATERacetylation[1, 2, 3, 6, 8, 10, 11]
77VRSTMNFKIGGATERsuccinylation[3]
77VRSTMNFKIGGATERubiquitination[4]
97IQAFGILKRAAAEVNacetylation[8]
97IQAFGILKRAAAEVNubiquitination[4]
112QEYGLDPKIASAIMKacetylation[1, 2, 3, 5, 6, 8, 9, 11]
112QEYGLDPKIASAIMKsuccinylation[3]
112QEYGLDPKIASAIMKubiquitination[4]
119KIASAIMKAADEVAEacetylation[1, 2, 3, 8, 11]
119KIASAIMKAADEVAEsuccinylation[3]
119KIASAIMKAADEVAEubiquitination[4]
128ADEVAEGKLNDHFPLacetylation[1]
170GGELGSKKPVHPNDHacetylation[2, 8]
210VLLPGLQKLHDALSAacetylation[1, 2, 3, 11]
210VLLPGLQKLHDALSAsuccinylation[3]
220DALSAKSKEFAQVIKacetylation[1, 2, 3, 11]
220DALSAKSKEFAQVIKsuccinylation[3]
220DALSAKSKEFAQVIKubiquitination[4]
227KEFAQVIKIGRTHTQacetylation[8]
289TRIGFAEKVAAKVAAubiquitination[4]
293FAEKVAAKVAALTGLacetylation[8]
474KIAKTAHKNGSTLKEacetylation[5]
Reference
 [1] 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]
 [2] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [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] 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]
 [5] 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]
 [6] 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]
 [7] Mitochondrial acetylome analysis in a mouse model of alcohol-induced liver injury utilizing SIRT3 knockout mice.
 Fritz KS, Galligan JJ, Hirschey MD, Verdin E, Petersen DR.
 J Proteome Res. 2012 Mar 2;11(3):1633-43. [PMID: 22309199]
 [8] 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]
 [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] Circadian acetylome reveals regulation of mitochondrial metabolic pathways.
 Masri S, Patel VR, Eckel-Mahan KL, Peleg S, Forne I, Ladurner AG, Baldi P, Imhof A, Sassone-Corsi P.
 Proc Natl Acad Sci U S A. 2013 Feb 26;110(9):3339-44. [PMID: 23341599]
 [11] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654
Functional Description
  
Sequence Annotation
 REGION 173 176 B site (By similarity).
 REGION 183 185 Substrate binding (By similarity).
 BINDING 144 144 Substrate (By similarity).
 MOD_RES 63 63 N6-acetyllysine.
 MOD_RES 77 77 N6-acetyllysine (By similarity).
 MOD_RES 112 112 N6-acetyllysine.
 MOD_RES 289 289 N6-acetyllysine (By similarity).
 MOD_RES 474 474 N6-acetyllysine.  
Keyword
 Acetylation; Alternative initiation; Complete proteome; Cytoplasm; Direct protein sequencing; Lyase; Mitochondrion; Reference proteome; Transit peptide; Tricarboxylic acid cycle. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 507 AA 
Protein Sequence
MYRALRLLAR SRRLLRVPSA GAAVSGEATT LPRCAPNVAR MASQNSFRVE FDTFGELKVP 60
TDKYYGAQTV RSTMNFKIGG ATERMPIPVI QAFGILKRAA AEVNQEYGLD PKIASAIMKA 120
ADEVAEGKLN DHFPLVVWQT GSGTQTNMNV NEVISNRAIE MLGGELGSKK PVHPNDHVNK 180
SQSSNDTFPT AMHIAAAVEV HKVLLPGLQK LHDALSAKSK EFAQVIKIGR THTQDAVPLT 240
LGQEFSGYVQ QVQYAMVRIK AAMPRIYELA AGGTAVGTGL NTRIGFAEKV AAKVAALTGL 300
PFVTAPNKFE ALAAHDALVE LSGAMNTAAC SLMKIANDIR FLGSGPRSGL GELILPENEP 360
GSSIMPGKVN PTQCEAMTMV AAQVMGNHVA VTVGGSNGHF ELNVFKPMMI KNVLHSARLL 420
GDASVSFTDN CVVGIQANTE RINKLMNESL MLVTALNPHI GYDKAAKIAK TAHKNGSTLK 480
ETAIELGYLT AEQFDEWVKP KDMLGPK 507 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0045239; C:tricarboxylic acid cycle enzyme complex; IEA:InterPro.
 GO:0004333; F:fumarate hydratase activity; IEA:EC.
 GO:0006106; P:fumarate metabolic process; IEA:InterPro.
 GO:0048873; P:homeostasis of number of cells within a tissue; IMP:MGI.
 GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway. 
Interpro
 IPR005677; Fum_hydII.
 IPR024083; Fumarase/histidase_N.
 IPR018951; Fumarase_C_C.
 IPR000362; Fumarate_lyase.
 IPR020557; Fumarate_lyase_CS.
 IPR022761; Fumarate_lyase_N.
 IPR008948; L-Aspartase-like. 
Pfam
 PF10415; FumaraseC_C
 PF00206; Lyase_1 
SMART
  
PROSITE
 PS00163; FUMARATE_LYASES 
PRINTS
 PR00149; FUMRATELYASE.