ID DPH5_HUMAN Reviewed; 285 AA. AC Q9H2P9; A8JZY6; D3DT62; Q9P017; Q9P0I4; Q9Y319; DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 10-OCT-2003, sequence version 2. DT 27-MAR-2024, entry version 164. DE RecName: Full=Diphthine methyl ester synthase; DE EC=2.1.1.314; DE AltName: Full=Diphthamide biosynthesis methyltransferase; GN Name=DPH5; ORFNames=AD-018, CGI-30, HSPC143, NPD015; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). RX PubMed=10810093; DOI=10.1101/gr.10.5.703; RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.; RT "Identification of novel human genes evolutionarily conserved in RT Caenorhabditis elegans by comparative proteomics."; RL Genome Res. 10:703-713(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Adrenal gland; RX PubMed=10931946; DOI=10.1073/pnas.160270997; RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J., RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., RA Chen M.-D., Chen J.-L.; RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis RT and full-length cDNA cloning."; RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Umbilical cord blood; RX PubMed=11042152; DOI=10.1101/gr.140200; RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.; RT "Cloning and functional analysis of cDNAs with open reading frames for 300 RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor RT cells."; RL Genome Res. 10:1546-1560(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Pituitary; RA Yang Y., Xu X., Gao G., Xiao H., Chen Z., Han Z.; RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Eye; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [10] RP FUNCTION IN DIPHTHAMIDE BIOSYNTHESIS. RX PubMed=23486472; DOI=10.1074/jbc.m113.461343; RA Wei H., Bera T.K., Wayne A.S., Xiang L., Colantonio S., Chertov O., RA Pastan I.; RT "A modified form of diphthamide causes immunotoxin resistance in a lymphoma RT cell line with a deletion of the WDR85 gene."; RL J. Biol. Chem. 288:12305-12312(2013). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [12] RP INVOLVEMENT IN NEDSFF, VARIANTS NEDSFF SER-110; 207-ARG--LEU-285 DEL AND RP ARG-260, AND CHARACTERIZATION OF VARIANTS NEDSFF SER-110; 207-ARG--LEU-285 RP DEL AND ARG-260. RX PubMed=35482014; DOI=10.1016/j.gim.2022.03.014; RG Undiagnosed Diseases Network; RA Shankar S.P., Grimsrud K., Lanoue L., Egense A., Willis B., Hoerberg J., RA AlAbdi L., Mayer K., Uetkuer K., Monaghan K.G., Krier J., Stoler J., RA Alnemer M., Shankar P.R., Schaffrath R., Alkuraya F.S., Brinkmann U., RA Eriksson L.A., Lloyd K., Rauen K.A.; RT "A novel DPH5-related diphthamide-deficiency syndrome causing embryonic RT lethality or profound neurodevelopmental disorder."; RL Genet. Med. 24:1567-1582(2022). RN [13] RP ERRATUM OF PUBMED:35482014. RX PubMed=36205747; DOI=10.1016/j.gim.2022.07.021; RG Undiagnosed Diseases Network; RA Shankar S.P., Grimsrud K., Lanoue L., Egense A., Willis B., Hoerberg J., RA AlAbdi L., Mayer K., Uetkuer K., Monaghan K.G., Krier J., Stoler J., RA Alnemer M., Shankar P.R., Schaffrath R., Alkuraya F.S., Brinkmann U., RA Eriksson L.A., Lloyd K., Rauen K.A.; RL Genet. Med. 24:2207-2207(2022). CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that CC catalyzes four methylations of the modified target histidine residue in CC translation elongation factor 2 (EF-2), to form an intermediate called CC diphthine methyl ester. The four successive methylation reactions CC represent the second step of diphthamide biosynthesis. CC {ECO:0000250|UniProtKB:P32469, ECO:0000269|PubMed:23486472}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation CC elongation factor 2] + 4 S-adenosyl-L-methionine = diphthine methyl CC ester-[translation elongation factor 2] + 3 H(+) + 4 S-adenosyl-L- CC homocysteine; Xref=Rhea:RHEA:42652, Rhea:RHEA-COMP:9749, Rhea:RHEA- CC COMP:10173, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:73995, ChEBI:CHEBI:79005; EC=2.1.1.314; CC Evidence={ECO:0000250|UniProtKB:P32469}; CC -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; CC IsoId=Q9H2P9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9H2P9-2; Sequence=VSP_008508; CC Name=3; CC IsoId=Q9H2P9-3; Sequence=VSP_008509; CC Name=4; CC IsoId=Q9H2P9-4; Sequence=VSP_008510; CC Name=5; CC IsoId=Q9H2P9-5; Sequence=VSP_008511; CC Name=6; CC IsoId=Q9H2P9-6; Sequence=VSP_043444; CC -!- DISEASE: Neurodevelopmental disorder with short stature, prominent CC forehead, and feeding difficulties (NEDSFF) [MIM:620070]: An autosomal CC recessive disorder characterized by distinct craniofacial features, CC multisystem dysfunction, profound neurodevelopmental delays, and CC neonatal death. {ECO:0000269|PubMed:35482014}. Note=The disease is CC caused by variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the diphthine synthase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF132964; AAD27739.1; -; mRNA. DR EMBL; AF157319; AAF67485.1; -; mRNA. DR EMBL; AF161492; AAF29107.1; -; mRNA. DR EMBL; AF248965; AAG44563.1; -; mRNA. DR EMBL; AK289351; BAF82040.1; -; mRNA. DR EMBL; AC093157; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471097; EAW72933.1; -; Genomic_DNA. DR EMBL; CH471097; EAW72937.1; -; Genomic_DNA. DR EMBL; CH471097; EAW72938.1; -; Genomic_DNA. DR EMBL; CH471097; EAW72940.1; -; Genomic_DNA. DR EMBL; BC053857; AAH53857.1; -; mRNA. DR CCDS; CCDS41358.1; -. [Q9H2P9-1] DR CCDS; CCDS41359.1; -. [Q9H2P9-6] DR RefSeq; NP_001070862.1; NM_001077394.1. [Q9H2P9-1] DR RefSeq; NP_001070863.1; NM_001077395.1. [Q9H2P9-6] DR RefSeq; NP_057042.2; NM_015958.2. [Q9H2P9-1] DR RefSeq; XP_016856949.1; XM_017001460.1. DR AlphaFoldDB; Q9H2P9; -. DR SMR; Q9H2P9; -. DR BioGRID; 119637; 26. DR IntAct; Q9H2P9; 2. DR STRING; 9606.ENSP00000359127; -. DR DrugBank; DB01752; S-adenosyl-L-homocysteine. DR GlyGen; Q9H2P9; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9H2P9; -. DR PhosphoSitePlus; Q9H2P9; -. DR BioMuta; DPH5; -. DR DMDM; 46397414; -. DR EPD; Q9H2P9; -. DR jPOST; Q9H2P9; -. DR MassIVE; Q9H2P9; -. DR MaxQB; Q9H2P9; -. DR PaxDb; 9606-ENSP00000359127; -. DR PeptideAtlas; Q9H2P9; -. DR ProteomicsDB; 80572; -. [Q9H2P9-1] DR ProteomicsDB; 80573; -. [Q9H2P9-2] DR ProteomicsDB; 80574; -. [Q9H2P9-3] DR ProteomicsDB; 80575; -. [Q9H2P9-4] DR ProteomicsDB; 80576; -. [Q9H2P9-5] DR ProteomicsDB; 80577; -. [Q9H2P9-6] DR Pumba; Q9H2P9; -. DR Antibodypedia; 33698; 35 antibodies from 9 providers. DR DNASU; 51611; -. DR Ensembl; ENST00000342173.11; ENSP00000339630.7; ENSG00000117543.22. [Q9H2P9-6] DR Ensembl; ENST00000370109.8; ENSP00000359127.3; ENSG00000117543.22. [Q9H2P9-1] DR Ensembl; ENST00000427040.3; ENSP00000394364.3; ENSG00000117543.22. [Q9H2P9-1] DR Ensembl; ENST00000488176.1; ENSP00000418282.1; ENSG00000117543.22. [Q9H2P9-1] DR GeneID; 51611; -. DR KEGG; hsa:51611; -. DR MANE-Select; ENST00000370109.8; ENSP00000359127.3; NM_015958.3; NP_057042.2. DR UCSC; uc001dtr.4; human. [Q9H2P9-1] DR AGR; HGNC:24270; -. DR CTD; 51611; -. DR DisGeNET; 51611; -. DR GeneCards; DPH5; -. DR HGNC; HGNC:24270; DPH5. DR HPA; ENSG00000117543; Low tissue specificity. DR MalaCards; DPH5; -. DR MIM; 611075; gene. DR MIM; 620070; phenotype. DR neXtProt; NX_Q9H2P9; -. DR OpenTargets; ENSG00000117543; -. DR PharmGKB; PA142671956; -. DR VEuPathDB; HostDB:ENSG00000117543; -. DR eggNOG; KOG3123; Eukaryota. DR GeneTree; ENSGT00390000010568; -. DR HOGENOM; CLU_066040_1_0_1; -. DR InParanoid; Q9H2P9; -. DR OMA; TAGDPMV; -. DR OrthoDB; 1093496at2759; -. DR PhylomeDB; Q9H2P9; -. DR TreeFam; TF105603; -. DR BRENDA; 2.1.1.314; 2681. DR PathwayCommons; Q9H2P9; -. DR Reactome; R-HSA-5358493; Synthesis of diphthamide-EEF2. DR SignaLink; Q9H2P9; -. DR SIGNOR; Q9H2P9; -. DR UniPathway; UPA00559; -. DR BioGRID-ORCS; 51611; 166 hits in 1180 CRISPR screens. DR ChiTaRS; DPH5; human. DR GeneWiki; DPH5; -. DR GenomeRNAi; 51611; -. DR Pharos; Q9H2P9; Tbio. DR PRO; PR:Q9H2P9; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9H2P9; Protein. DR Bgee; ENSG00000117543; Expressed in body of pancreas and 209 other cell types or tissues. DR ExpressionAtlas; Q9H2P9; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0004164; F:diphthine synthase activity; EXP:Reactome. DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW. DR GO; GO:0017183; P:protein histidyl modification to diphthamide; ISS:UniProtKB. DR CDD; cd11647; DHP5_DphB; 1. DR HAMAP; MF_01084; Diphthine_synth; 1. DR InterPro; IPR000878; 4pyrrol_Mease. DR InterPro; IPR035996; 4pyrrol_Methylase_sf. DR InterPro; IPR014777; 4pyrrole_Mease_sub1. DR InterPro; IPR014776; 4pyrrole_Mease_sub2. DR InterPro; IPR004551; Dphthn_synthase. DR NCBIfam; TIGR00522; dph5; 1. DR PANTHER; PTHR10882:SF0; DIPHTHINE METHYL ESTER SYNTHASE; 1. DR PANTHER; PTHR10882; DIPHTHINE SYNTHASE; 1. DR Pfam; PF00590; TP_methylase; 1. DR PIRSF; PIRSF036432; Diphthine_synth; 1. DR SUPFAM; SSF53790; Tetrapyrrole methylase; 1. DR Genevisible; Q9H2P9; HS. PE 1: Evidence at protein level; KW Alternative splicing; Disease variant; Intellectual disability; KW Methyltransferase; Phosphoprotein; Reference proteome; KW S-adenosyl-L-methionine; Transferase. FT CHAIN 1..285 FT /note="Diphthine methyl ester synthase" FT /id="PRO_0000156133" FT BINDING 9 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250" FT BINDING 84 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250" FT BINDING 87 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250" FT BINDING 112..113 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250" FT BINDING 163 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250" FT BINDING 225 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250" FT BINDING 250 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250" FT MOD_RES 171 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 85..137 FT /note="PFGATTHSDLVLRATKLGIPYRVIHNASIMNAVGCCGLQLYKFGETVSIVFW FT T -> HL (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10931946" FT /id="VSP_008508" FT VAR_SEQ 88..143 FT /note="ATTHSDLVLRATKLGIPYRVIHNASIMNAVGCCGLQLYKFGETVSIVFWTDT FT WRPE -> HLETR (in isoform 3)" FT /evidence="ECO:0000303|PubMed:11042152" FT /id="VSP_008509" FT VAR_SEQ 117..141 FT /note="VGCCGLQLYKFGETVSIVFWTDTWR -> EAAGGYRYISLERQVLLVFGQTL FT GG (in isoform 4)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_008510" FT VAR_SEQ 134..137 FT /note="VFWT -> MLISVMLHSLWLVIHL (in isoform 5)" FT /evidence="ECO:0000303|PubMed:10810093" FT /id="VSP_008511" FT VAR_SEQ 212 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043444" FT VARIANT 110 FT /note="N -> S (in NEDSFF; decreased function in diphthamide FT biosynthesis shown in a yeast assay system)" FT /evidence="ECO:0000269|PubMed:35482014" FT /id="VAR_087842" FT VARIANT 207..285 FT /note="Missing (in NEDSFF; loss of function in diphthamide FT biosynthesis shown in a yeast assay system)" FT /evidence="ECO:0000269|PubMed:35482014" FT /id="VAR_087843" FT VARIANT 260 FT /note="H -> R (in NEDSFF; results in multisystem FT abnormalities in a homozygous mouse knockin model; FT decreased function in diphthamide biosynthesis shown in a FT yeast assay system)" FT /evidence="ECO:0000269|PubMed:35482014" FT /id="VAR_087844" FT CONFLICT 107 FT /note="V -> G (in Ref. 4; AAG44563)" FT /evidence="ECO:0000305" FT CONFLICT 285 FT /note="L -> FEHRYFHCLM (in Ref. 2; AAF67485)" FT /evidence="ECO:0000305" SQ SEQUENCE 285 AA; 31651 MW; 1348631C25BC624E CRC64; MLYLIGLGLG DAKDITVKGL EVVRRCSRVY LEAYTSVLTV GKEALEEFYG RKLVVADREE VEQEADNILK DADISDVAFL VVGDPFGATT HSDLVLRATK LGIPYRVIHN ASIMNAVGCC GLQLYKFGET VSIVFWTDTW RPESFFDKVK KNRQNGMHTL CLLDIKVKEQ SLENLIKGRK IYEPPRYMSV NQAAQQLLEI VQNQRIRGEE PAVTEETLCV GLARVGADDQ KIAAGTLRQM CTVDLGEPLH SLIITGGSIH PMEMEMLSLF SIPENSSESQ SINGL //