CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015159
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Fumarylacetoacetate hydrolase domain-containing protein 2B 
Protein Synonyms/Alias
  
Gene Name
 FAHD2B 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
203WLTRRNGKQWLLGKTacetylation[1, 2, 3]
203WLTRRNGKQWLLGKTubiquitination[4, 5]
209GKQWLLGKTFDTFCPubiquitination[6]
224LGPALVTKDSVADPHubiquitination[4, 6]
234VADPHNLKICCRVNGacetylation[1, 5]
234VADPHNLKICCRVNGubiquitination[4, 5, 6]
288PGVGVFRKPPVFLKKubiquitination[4]
295KPPVFLKKGDEVQCEubiquitination[4]
312ELGVIINKVV*****ubiquitination[4]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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
Functional Description
 May have hydrolase activity (By similarity). 
Sequence Annotation
  
Keyword
 Calcium; Complete proteome; Hydrolase; Magnesium; Metal-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 314 AA 
Protein Sequence
MLVSGRRRLL TALLQAQKWP FQPSRDMRLV QFRAPHLVGP HLGLETGNGG GVINLNAFDP 60
TLPKTMTQFL EQGEATLSVA RRALAAQLPV LPWSEVTFLA PVTWPDKVVC VGMNYVDHCK 120
EQNVPVPKEP IIFSKFASSI VGPYDEVVLP PQSQEVDWEV ELAVVIGKKG KHIKATDAMA 180
HVAGFTVAHD VSARDWLTRR NGKQWLLGKT FDTFCPLGPA LVTKDSVADP HNLKICCRVN 240
GEVVQSSNTN QMVFKTEDLI AWVSQFVTFY PGDVILTGTP PGVGVFRKPP VFLKKGDEVQ 300
CEIEELGVII NKVV 314 
Gene Ontology
 GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 
Interpro
 IPR002529; Fumarylacetoacetase_C.
 IPR011234; Fumarylacetoacetase_C-rel. 
Pfam
 PF01557; FAA_hydrolase 
SMART
  
PROSITE
  
PRINTS