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Protein

Diphthine methyl ester synthase

Gene

Dph5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

S-adenosyl-L-methionine-dependent methyltransferase that catalyzes four methylations of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine methyl ester. The four successive methylation reactions represent the second step of diphthamide biosynthesis.By similarity1 Publication

Catalytic activityi

4 S-adenosyl-L-methionine + 2-((3S)-3-carboxy-3-aminopropyl)-L-histidine-[translation elongation factor 2] = 4 S-adenosyl-L-homocysteine + diphthine methyl ester-[translation elongation factor 2].By similarity

Pathway:ipeptidyl-diphthamide biosynthesis

This protein is involved in the pathway peptidyl-diphthamide biosynthesis, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway peptidyl-diphthamide biosynthesis and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei9 – 91S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
Binding sitei84 – 841S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei87 – 871S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
Binding sitei163 – 1631S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei225 – 2251S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei250 – 2501S-adenosyl-L-methionine; via carbonyl oxygenBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

ReactomeiREACT_333333. Synthesis of diphthamide-EEF2.
UniPathwayiUPA00559.

Names & Taxonomyi

Protein namesi
Recommended name:
Diphthine methyl ester synthase (EC:2.1.1.314)
Alternative name(s):
Diphthamide biosynthesis methyltransferase
Gene namesi
Name:Dph5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1916990. Dph5.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 281281Diphthine methyl ester synthasePRO_0000156134Add
BLAST

Proteomic databases

MaxQBiQ9CWQ0.
PaxDbiQ9CWQ0.
PRIDEiQ9CWQ0.

PTM databases

PhosphoSiteiQ9CWQ0.

Expressioni

Gene expression databases

CleanExiMM_DPH5.
ExpressionAtlasiQ9CWQ0. baseline and differential.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000043730.

Structurei

3D structure databases

ProteinModelPortaliQ9CWQ0.
SMRiQ9CWQ0. Positions 1-270.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni112 – 1132S-adenosyl-L-methionine bindingBy similarity

Sequence similaritiesi

Belongs to the diphthine synthase family.Curated

Phylogenomic databases

eggNOGiCOG1798.
GeneTreeiENSGT00390000010568.
HOGENOMiHOG000205302.
HOVERGENiHBG044879.
InParanoidiQ9CWQ0.
KOiK00586.
OMAiTLQQMCT.
TreeFamiTF105603.

Family and domain databases

Gene3Di3.30.950.10. 1 hit.
3.40.1010.10. 1 hit.
HAMAPiMF_01084. Diphthine_synth.
InterProiIPR000878. 4pyrrol_Mease.
IPR014777. 4pyrrole_Mease_sub1.
IPR014776. 4pyrrole_Mease_sub2.
IPR004551. Dphthn_synthase.
[Graphical view]
PfamiPF00590. TP_methylase. 1 hit.
[Graphical view]
PIRSFiPIRSF036432. Diphthine_synth. 1 hit.
SUPFAMiSSF53790. SSF53790. 1 hit.
TIGRFAMsiTIGR00522. dph5. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9CWQ0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLYLIGLGLG DAKDITVKGL EVVRRCSRVY LEAYTSVLTV GKEALEEFYG
60 70 80 90 100
RKLILADREE VEQEADNIFK DADVSDVAFL VVGDPFGATT HSDLILRATK
110 120 130 140 150
LGIPYQVIHN ASIMNAVGCC GLQLYRFGET VSIVFWTDTW RPESFFDKVK
160 170 180 190 200
RNRANGMHTL CLLDIKVKEQ SLENLIRGRK IYEPPRYMSV NQAAQQLLEI
210 220 230 240 250
VQNHRARGEE PAITEETLCV GLARVGAEDQ KIAAGTLQQM CTVSLGEPLH
260 270 280
SLVITGGNLH PLEMEMLSLF SIPESQSTDG L
Length:281
Mass (Da):31,218
Last modified:October 3, 2012 - v2
Checksum:i28AEC5E6ABBC3C1F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161T → K in BAB26968 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK010475 mRNA. Translation: BAB26968.1.
AC131113 Genomic DNA. No translation available.
CH466532 Genomic DNA. Translation: EDL12395.1.
BC060372 mRNA. Translation: AAH60372.1.
CCDSiCCDS17782.1.
RefSeqiNP_081469.2. NM_027193.2.
UniGeneiMm.5915.

Genome annotation databases

EnsembliENSMUST00000043342; ENSMUSP00000043730; ENSMUSG00000033554.
ENSMUST00000189799; ENSMUSP00000140958; ENSMUSG00000033554.
GeneIDi69740.
KEGGimmu:69740.
UCSCiuc008rbs.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK010475 mRNA. Translation: BAB26968.1.
AC131113 Genomic DNA. No translation available.
CH466532 Genomic DNA. Translation: EDL12395.1.
BC060372 mRNA. Translation: AAH60372.1.
CCDSiCCDS17782.1.
RefSeqiNP_081469.2. NM_027193.2.
UniGeneiMm.5915.

3D structure databases

ProteinModelPortaliQ9CWQ0.
SMRiQ9CWQ0. Positions 1-270.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000043730.

PTM databases

PhosphoSiteiQ9CWQ0.

Proteomic databases

MaxQBiQ9CWQ0.
PaxDbiQ9CWQ0.
PRIDEiQ9CWQ0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000043342; ENSMUSP00000043730; ENSMUSG00000033554.
ENSMUST00000189799; ENSMUSP00000140958; ENSMUSG00000033554.
GeneIDi69740.
KEGGimmu:69740.
UCSCiuc008rbs.1. mouse.

Organism-specific databases

CTDi51611.
MGIiMGI:1916990. Dph5.

Phylogenomic databases

eggNOGiCOG1798.
GeneTreeiENSGT00390000010568.
HOGENOMiHOG000205302.
HOVERGENiHBG044879.
InParanoidiQ9CWQ0.
KOiK00586.
OMAiTLQQMCT.
TreeFamiTF105603.

Enzyme and pathway databases

UniPathwayiUPA00559.
ReactomeiREACT_333333. Synthesis of diphthamide-EEF2.

Miscellaneous databases

NextBioi330226.
PROiQ9CWQ0.
SOURCEiSearch...

Gene expression databases

CleanExiMM_DPH5.
ExpressionAtlasiQ9CWQ0. baseline and differential.

Family and domain databases

Gene3Di3.30.950.10. 1 hit.
3.40.1010.10. 1 hit.
HAMAPiMF_01084. Diphthine_synth.
InterProiIPR000878. 4pyrrol_Mease.
IPR014777. 4pyrrole_Mease_sub1.
IPR014776. 4pyrrole_Mease_sub2.
IPR004551. Dphthn_synthase.
[Graphical view]
PfamiPF00590. TP_methylase. 1 hit.
[Graphical view]
PIRSFiPIRSF036432. Diphthine_synth. 1 hit.
SUPFAMiSSF53790. SSF53790. 1 hit.
TIGRFAMsiTIGR00522. dph5. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryonic stem cell.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Olfactory epithelium.
  5. "Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2."
    Liu S., Milne G.T., Kuremsky J.G., Fink G.R., Leppla S.H.
    Mol. Cell. Biol. 24:9487-9497(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiDPH5_MOUSE
AccessioniPrimary (citable) accession number: Q9CWQ0
Secondary accession number(s): Q6PAC5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: October 3, 2012
Last modified: June 24, 2015
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.