UniProt Accession

 FUMH_HUMAN; P07954 

Genbank Protein ID

 U59309; U48857; BT009839; BC003108; BC017444; M15502 

Genbank Nucleotide ID

 AAB66354.1; AAD00071.1; AAP88841.1; AAH03108.1; AAH17444.1; AAA52483.1 

Protein Name

 Fumarate hydratase, mitochondrial 

Protein Synonyms/Alias

 Fumarase 

Gene Name

 FH 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
61	YDTFGELKVPNDKYY	acetylation	[1]
66	ELKVPNDKYYGAQTV	acetylation	[1, 2, 3, 4]
66	ELKVPNDKYYGAQTV	ubiquitination	[5]
80	VRSTMNFKIGGVTER	acetylation	[1, 2, 3]
94	RMPTPVIKAFGILKR	acetylation	[1, 2, 3]
94	RMPTPVIKAFGILKR	ubiquitination	[5, 6, 7]
100	IKAFGILKRAAAEVN	ubiquitination	[4, 5]
115	QDYGLDPKIANAIMK	acetylation	[1, 4]
172	LGGELGSKIPVHPND	acetylation	[8]
230	KEFAQIIKIGRTHTQ	ubiquitination	[5]
256	SGYVQQVKYAMTRIK	acetylation	[1, 2]
292	TRIGFAEKVAAKVAA	acetylation	[1, 2, 4]
292	TRIGFAEKVAAKVAA	ubiquitination	[4, 5]
504	FDEWVKPKDMLGPK*	acetylation	[1]

Reference

 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [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] 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]
 [8] 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] 

Functional Description

 Also acts as a tumor suppressor. 

Sequence Annotation

 REGION 176 179 B site (By similarity).
 REGION 186 188 Substrate binding (By similarity).
 BINDING 147 147 Substrate (By similarity).
 MOD_RES 66 66 N6-acetyllysine.
 MOD_RES 80 80 N6-acetyllysine.
 MOD_RES 94 94 N6-acetyllysine.
 MOD_RES 115 115 N6-acetyllysine (By similarity).
 MOD_RES 256 256 N6-acetyllysine.
 MOD_RES 292 292 N6-acetyllysine.
 MOD_RES 477 477 N6-acetyllysine (By similarity).  

Keyword

 3D-structure; Acetylation; Alternative initiation; Complete proteome; Cytoplasm; Direct protein sequencing; Disease mutation; Lyase; Mitochondrion; Reference proteome; Transit peptide; Tricarboxylic acid cycle; Tumor suppressor. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 510 AA 

Protein Sequence

Gene Ontology

 GO:0005759; C:mitochondrial matrix; TAS:Reactome.
 GO:0045239; C:tricarboxylic acid cycle enzyme complex; IEA:InterPro.
 GO:0004333; F:fumarate hydratase activity; EXP:Reactome.
 GO:0006106; P:fumarate metabolic process; TAS:ProtInc.
 GO:0048873; P:homeostasis of number of cells within a tissue; IEA:Compara.
 GO:0006099; P:tricarboxylic acid cycle; TAS:Reactome. 

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.