CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015784
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Diphthine--ammonia ligase 
Protein Synonyms/Alias
 ATP-binding domain-containing protein 4; Diphthamide synthase; Diphthamide synthetase; Protein DPH6 homolog 
Gene Name
 DPH6 
Gene Synonyms/Alias
 ATPBD4 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
87DTRQVYTKCEGDEVEubiquitination[1]
101EDLYELLKLVKEKEEubiquitination[1, 2]
131IRVENVCKRLNLQPLubiquitination[1]
174ALGLDPDKHLGKTLDubiquitination[3]
178DPDKHLGKTLDQMEPubiquitination[1, 2]
192PYLIELSKKYGVHVCubiquitination[1, 2, 4, 5]
193YLIELSKKYGVHVCGubiquitination[1]
250LELHLEDKVSSVPDNubiquitination[1]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [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] 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] 
Functional Description
 Amidase that catalyzes the last step of diphthamide biosynthesis using ammonium and ATP. Diphthamide biosynthesis consists in the conversion of an L-histidine residue in the translation elongation factor eEF-2 (EEF2) to diphthamide (Probable). 
Sequence Annotation
  
Keyword
 Alternative splicing; ATP-binding; Complete proteome; Ligase; Nucleotide-binding; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 267 AA 
Protein Sequence
MRVAALISGG KDSCYNMMQC IAAGHQIVAL ANLRPAENQV GSDELDSYMY QTVGHHAIDL 60
YAEAMALPLY RRTIRGRSLD TRQVYTKCEG DEVEDLYELL KLVKEKEEVE GISVGAILSD 120
YQRIRVENVC KRLNLQPLAY LWQRNQEDLL REMISSNIQA MIIKVAALGL DPDKHLGKTL 180
DQMEPYLIEL SKKYGVHVCG EGGEYETFTL DCPLFKKKII VDSSEVVIHS ADAFAPVAYL 240
RFLELHLEDK VSSVPDNYRT SNYIYNF 267 
Gene Ontology
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0017178; F:diphthine-ammonia ligase activity; TAS:UniProtKB.
 GO:0017183; P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine; TAS:UniProtKB. 
Interpro
 IPR002761; DUF71_dom.
 IPR014729; Rossmann-like_a/b/a_fold. 
Pfam
 PF01902; ATP_bind_4 
SMART
  
PROSITE
  
PRINTS