UniProt Accession

 DPH5_HUMAN; Q9H2P9; A8JZY6; D3DT62; Q9P017; Q9P0I4; Q9Y319 

Genbank Protein ID

 AF132964; AF157319; AF161492; AF248965; AK289351; AC093157; CH471097; CH471097; CH471097; CH471097; BC053857 

Genbank Nucleotide ID

 AAD27739.1; AAF67485.1; AAF29107.1; AAG44563.1; BAF82040.1; EAW72933.1; EAW72937.1; EAW72938.1; EAW72940.1; AAH53857.1 

Protein Name

 Diphthine synthase 

Protein Synonyms/Alias

 Diphthamide biosynthesis methyltransferase 

Gene Name

 DPH5 

Gene Synonyms/Alias

 AD-018; CGI-30; HSPC143; NPD015 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
18	DAKDITVKGLEVVRR	ubiquitination	[1, 2, 3]
100	DLVLRATKLGIPYRV	ubiquitination	[2, 3, 4]
126	CCGLQLYKFGETVSI	ubiquitination	[1]
177	QSLENLIKGRKIYEP	ubiquitination	[1, 3]
180	ENLIKGRKIYEPPRY	ubiquitination	[1]
231	RVGADDQKIAAGTLR	ubiquitination	[1, 2, 4, 5]

Reference

 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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] 

Functional Description

 S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF- 2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis (By similarity). 

Sequence Annotation

 REGION 112 113 S-adenosyl-L-methionine binding (By
 BINDING 9 9 S-adenosyl-L-methionine; via carbonyl
 BINDING 84 84 S-adenosyl-L-methionine; via amide
 BINDING 87 87 S-adenosyl-L-methionine; via carbonyl
 BINDING 163 163 S-adenosyl-L-methionine; via amide
 BINDING 225 225 S-adenosyl-L-methionine; via amide
 BINDING 250 250 S-adenosyl-L-methionine; via carbonyl  

Keyword

 Alternative splicing; Complete proteome; Methyltransferase; Reference proteome; S-adenosyl-L-methionine; Transferase. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 285 AA 

Protein Sequence

Gene Ontology

 GO:0004164; F:diphthine synthase activity; NAS:UniProtKB.
 GO:0017183; P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine; NAS:UniProtKB. 

Interpro

 IPR000878; 4pyrrol_Mease.
 IPR014777; 4pyrrole_Mease_sub1.
 IPR014776; 4pyrrole_Mease_sub2.
 IPR004551; Dphthn_synthase. 

Pfam

 PF00590; TP_methylase 

SMART

  

PROSITE

  

PRINTS