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Q9CWQ0

- DPH5_MOUSE

UniProt

Q9CWQ0 - DPH5_MOUSE

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Protein

Diphthine synthase

Gene

Dph5

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

Functioni

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 (EFE2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.1 Publication

Catalytic activityi

3 S-adenosyl-L-methionine + 2-(3-carboxy-3-aminopropyl)-L-histidine-[translation elongation factor 2] = 3 S-adenosyl-L-homocysteine + 2-(3-carboxy-3-(trimethylammonio)propyl)-L-histidine-[translation elongation factor 2].

Pathwayi

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

  1. diphthine synthase activity Source: UniProtKB-EC

GO - Biological processi

  1. peptidyl-diphthamide biosynthetic process from peptidyl-histidine Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

UniPathwayiUPA00559.

Names & Taxonomyi

Protein namesi
Recommended name:
Diphthine synthase (EC:2.1.1.98)
Alternative name(s):
Diphthamide biosynthesis methyltransferase
Gene namesi
Name:Dph5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:1916990. Dph5.

PTM / Processingi

Molecule processing

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

Proteomic databases

MaxQBiQ9CWQ0.
PaxDbiQ9CWQ0.
PRIDEiQ9CWQ0.

PTM databases

PhosphoSiteiQ9CWQ0.

Expressioni

Gene expression databases

CleanExiMM_DPH5.
ExpressionAtlasiQ9CWQ0. baseline and differential.
GenevestigatoriQ9CWQ0.

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.
OMAiANCPAVA.
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 .
CCDSi CCDS17782.1.
RefSeqi NP_081469.2. NM_027193.2.
UniGenei Mm.5915.

3D structure databases

ProteinModelPortali Q9CWQ0.
SMRi Q9CWQ0. Positions 1-270.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q9CWQ0.

Proteomic databases

MaxQBi Q9CWQ0.
PaxDbi Q9CWQ0.
PRIDEi Q9CWQ0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000043342 ; ENSMUSP00000043730 ; ENSMUSG00000033554 .
ENSMUST00000189799 ; ENSMUSP00000140958 ; ENSMUSG00000033554 .
GeneIDi 69740.
KEGGi mmu:69740.
UCSCi uc008rbs.1. mouse.

Organism-specific databases

CTDi 51611.
MGIi MGI:1916990. Dph5.

Phylogenomic databases

eggNOGi COG1798.
GeneTreei ENSGT00390000010568.
HOGENOMi HOG000205302.
HOVERGENi HBG044879.
InParanoidi Q9CWQ0.
KOi K00586.
OMAi ANCPAVA.
TreeFami TF105603.

Enzyme and pathway databases

UniPathwayi UPA00559 .

Miscellaneous databases

NextBioi 330226.
PROi Q9CWQ0.
SOURCEi Search...

Gene expression databases

CleanExi MM_DPH5.
ExpressionAtlasi Q9CWQ0. baseline and differential.
Genevestigatori Q9CWQ0.

Family and domain databases

Gene3Di 3.30.950.10. 1 hit.
3.40.1010.10. 1 hit.
HAMAPi MF_01084. Diphthine_synth.
InterProi IPR000878. 4pyrrol_Mease.
IPR014777. 4pyrrole_Mease_sub1.
IPR014776. 4pyrrole_Mease_sub2.
IPR004551. Dphthn_synthase.
[Graphical view ]
Pfami PF00590. TP_methylase. 1 hit.
[Graphical view ]
PIRSFi PIRSF036432. Diphthine_synth. 1 hit.
SUPFAMi SSF53790. SSF53790. 1 hit.
TIGRFAMsi TIGR00522. dph5. 1 hit.
ProtoNeti Search...

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: October 29, 2014
This is version 87 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