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Q9H2P9

- DPH5_HUMAN

UniProt

Q9H2P9 - DPH5_HUMAN

Protein

Diphthine synthase

Gene

DPH5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 2 (10 Oct 2003)
      Previous versions | rss
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    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 (EEF2), 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

    GO - Biological processi

    1. peptidyl-diphthamide biosynthetic process from peptidyl-histidine Source: UniProtKB

    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
    ORF Names:AD-018, CGI-30, HSPC143, NPD015
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:24270. DPH5.

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA142671956.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 285285Diphthine synthasePRO_0000156133Add
    BLAST

    Proteomic databases

    MaxQBiQ9H2P9.
    PaxDbiQ9H2P9.
    PRIDEiQ9H2P9.

    PTM databases

    PhosphoSiteiQ9H2P9.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9H2P9.
    BgeeiQ9H2P9.
    CleanExiHS_DPH5.
    GenevestigatoriQ9H2P9.

    Organism-specific databases

    HPAiHPA046439.

    Interactioni

    Protein-protein interaction databases

    BioGridi119637. 1 interaction.
    STRINGi9606.ENSP00000359127.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9H2P9.
    SMRiQ9H2P9. 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.
    HOGENOMiHOG000205302.
    HOVERGENiHBG044879.
    InParanoidiQ9H2P9.
    KOiK00586.
    OMAiQQMCTVD.
    OrthoDBiEOG7Q2N64.
    PhylomeDBiQ9H2P9.
    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.

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9H2P9-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MLYLIGLGLG DAKDITVKGL EVVRRCSRVY LEAYTSVLTV GKEALEEFYG    50
    RKLVVADREE VEQEADNILK DADISDVAFL VVGDPFGATT HSDLVLRATK 100
    LGIPYRVIHN ASIMNAVGCC GLQLYKFGET VSIVFWTDTW RPESFFDKVK 150
    KNRQNGMHTL CLLDIKVKEQ SLENLIKGRK IYEPPRYMSV NQAAQQLLEI 200
    VQNQRIRGEE PAVTEETLCV GLARVGADDQ KIAAGTLRQM CTVDLGEPLH 250
    SLIITGGSIH PMEMEMLSLF SIPENSSESQ SINGL 285
    Length:285
    Mass (Da):31,651
    Last modified:October 10, 2003 - v2
    Checksum:i1348631C25BC624E
    GO
    Isoform 2 (identifier: Q9H2P9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         85-137: PFGATTHSDLVLRATKLGIPYRVIHNASIMNAVGCCGLQLYKFGETVSIVFWT → HL

    Note: No experimental confirmation available.

    Show »
    Length:234
    Mass (Da):26,122
    Checksum:iCAA1ABE0A11AF714
    GO
    Isoform 3 (identifier: Q9H2P9-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         88-143: ATTHSDLVLRATKLGIPYRVIHNASIMNAVGCCGLQLYKFGETVSIVFWTDTWRPE → HLETR

    Note: No experimental confirmation available.

    Show »
    Length:234
    Mass (Da):26,025
    Checksum:i86A9E6761145DFBA
    GO
    Isoform 4 (identifier: Q9H2P9-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         117-141: VGCCGLQLYKFGETVSIVFWTDTWR → EAAGGYRYISLERQVLLVFGQTLGG

    Note: No experimental confirmation available.

    Show »
    Length:285
    Mass (Da):31,440
    Checksum:i2784D835EB96EFC2
    GO
    Isoform 5 (identifier: Q9H2P9-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         134-137: VFWT → MLISVMLHSLWLVIHL

    Note: No experimental confirmation available.

    Show »
    Length:297
    Mass (Da):33,005
    Checksum:iE0D27EEEF0B9849D
    GO
    Isoform 6 (identifier: Q9H2P9-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         212-212: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:284
    Mass (Da):31,580
    Checksum:i862A9762E32AA574
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti107 – 1071V → G in AAG44563. 1 PublicationCurated
    Sequence conflicti285 – 2851L → FEHRYFHCLM in AAF67485. (PubMed:10931946)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei85 – 13753PFGAT…IVFWT → HL in isoform 2. 1 PublicationVSP_008508Add
    BLAST
    Alternative sequencei88 – 14356ATTHS…TWRPE → HLETR in isoform 3. 1 PublicationVSP_008509Add
    BLAST
    Alternative sequencei117 – 14125VGCCG…TDTWR → EAAGGYRYISLERQVLLVFG QTLGG in isoform 4. 1 PublicationVSP_008510Add
    BLAST
    Alternative sequencei134 – 1374VFWT → MLISVMLHSLWLVIHL in isoform 5. 1 PublicationVSP_008511
    Alternative sequencei212 – 2121Missing in isoform 6. 1 PublicationVSP_043444

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF132964 mRNA. Translation: AAD27739.1.
    AF157319 mRNA. Translation: AAF67485.1.
    AF161492 mRNA. Translation: AAF29107.1.
    AF248965 mRNA. Translation: AAG44563.1.
    AK289351 mRNA. Translation: BAF82040.1.
    AC093157 Genomic DNA. No translation available.
    CH471097 Genomic DNA. Translation: EAW72933.1.
    CH471097 Genomic DNA. Translation: EAW72937.1.
    CH471097 Genomic DNA. Translation: EAW72938.1.
    CH471097 Genomic DNA. Translation: EAW72940.1.
    BC053857 mRNA. Translation: AAH53857.1.
    CCDSiCCDS41358.1. [Q9H2P9-1]
    CCDS41359.1. [Q9H2P9-6]
    RefSeqiNP_001070862.1. NM_001077394.1. [Q9H2P9-1]
    NP_001070863.1. NM_001077395.1. [Q9H2P9-6]
    NP_057042.2. NM_015958.2. [Q9H2P9-1]
    UniGeneiHs.440776.

    Genome annotation databases

    EnsembliENST00000342173; ENSP00000339630; ENSG00000117543. [Q9H2P9-6]
    ENST00000370109; ENSP00000359127; ENSG00000117543. [Q9H2P9-1]
    ENST00000488176; ENSP00000418282; ENSG00000117543. [Q9H2P9-1]
    GeneIDi51611.
    KEGGihsa:51611.
    UCSCiuc001dtr.2. human. [Q9H2P9-6]
    uc001dts.2. human. [Q9H2P9-1]
    uc001dty.2. human. [Q9H2P9-5]

    Polymorphism databases

    DMDMi46397414.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF132964 mRNA. Translation: AAD27739.1 .
    AF157319 mRNA. Translation: AAF67485.1 .
    AF161492 mRNA. Translation: AAF29107.1 .
    AF248965 mRNA. Translation: AAG44563.1 .
    AK289351 mRNA. Translation: BAF82040.1 .
    AC093157 Genomic DNA. No translation available.
    CH471097 Genomic DNA. Translation: EAW72933.1 .
    CH471097 Genomic DNA. Translation: EAW72937.1 .
    CH471097 Genomic DNA. Translation: EAW72938.1 .
    CH471097 Genomic DNA. Translation: EAW72940.1 .
    BC053857 mRNA. Translation: AAH53857.1 .
    CCDSi CCDS41358.1. [Q9H2P9-1 ]
    CCDS41359.1. [Q9H2P9-6 ]
    RefSeqi NP_001070862.1. NM_001077394.1. [Q9H2P9-1 ]
    NP_001070863.1. NM_001077395.1. [Q9H2P9-6 ]
    NP_057042.2. NM_015958.2. [Q9H2P9-1 ]
    UniGenei Hs.440776.

    3D structure databases

    ProteinModelPortali Q9H2P9.
    SMRi Q9H2P9. Positions 1-270.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119637. 1 interaction.
    STRINGi 9606.ENSP00000359127.

    PTM databases

    PhosphoSitei Q9H2P9.

    Polymorphism databases

    DMDMi 46397414.

    Proteomic databases

    MaxQBi Q9H2P9.
    PaxDbi Q9H2P9.
    PRIDEi Q9H2P9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000342173 ; ENSP00000339630 ; ENSG00000117543 . [Q9H2P9-6 ]
    ENST00000370109 ; ENSP00000359127 ; ENSG00000117543 . [Q9H2P9-1 ]
    ENST00000488176 ; ENSP00000418282 ; ENSG00000117543 . [Q9H2P9-1 ]
    GeneIDi 51611.
    KEGGi hsa:51611.
    UCSCi uc001dtr.2. human. [Q9H2P9-6 ]
    uc001dts.2. human. [Q9H2P9-1 ]
    uc001dty.2. human. [Q9H2P9-5 ]

    Organism-specific databases

    CTDi 51611.
    GeneCardsi GC01M101455.
    H-InvDB HIX0023161.
    HGNCi HGNC:24270. DPH5.
    HPAi HPA046439.
    MIMi 611075. gene.
    neXtProti NX_Q9H2P9.
    PharmGKBi PA142671956.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1798.
    HOGENOMi HOG000205302.
    HOVERGENi HBG044879.
    InParanoidi Q9H2P9.
    KOi K00586.
    OMAi QQMCTVD.
    OrthoDBi EOG7Q2N64.
    PhylomeDBi Q9H2P9.
    TreeFami TF105603.

    Enzyme and pathway databases

    UniPathwayi UPA00559 .

    Miscellaneous databases

    ChiTaRSi DPH5. human.
    GeneWikii DPH5.
    GenomeRNAii 51611.
    NextBioi 55510.
    PROi Q9H2P9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H2P9.
    Bgeei Q9H2P9.
    CleanExi HS_DPH5.
    Genevestigatori Q9H2P9.

    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

    1. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
      Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
      Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Adrenal gland.
    3. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
      Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
      , Gu J., Chen S.-J., Chen Z.
      Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Umbilical cord blood.
    4. Yang Y., Xu X., Gao G., Xiao H., Chen Z., Han Z.
      Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
      Tissue: Pituitary.
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
    6. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] (ISOFORM 1).
      Tissue: Eye.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "A modified form of diphthamide causes immunotoxin resistance in a lymphoma cell line with a deletion of the WDR85 gene."
      Wei H., Bera T.K., Wayne A.S., Xiang L., Colantonio S., Chertov O., Pastan I.
      J. Biol. Chem. 288:12305-12312(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DIPHTHAMIDE BIOSYNTHESIS.

    Entry informationi

    Entry nameiDPH5_HUMAN
    AccessioniPrimary (citable) accession number: Q9H2P9
    Secondary accession number(s): A8JZY6
    , D3DT62, Q9P017, Q9P0I4, Q9Y319
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 10, 2003
    Last sequence update: October 10, 2003
    Last modified: October 1, 2014
    This is version 106 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3