ID DPH2_HUMAN Reviewed; 489 AA. AC Q9BQC3; A8MVC9; B2RDE3; B4DNI8; O60623; DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 03-MAY-2023, entry version 162. DE RecName: Full=2-(3-amino-3-carboxypropyl)histidine synthase subunit 2 {ECO:0000305}; DE AltName: Full=Diphthamide biosynthesis protein 2; DE AltName: Full=Diphtheria toxin resistance protein 2 {ECO:0000305}; DE AltName: Full=S-adenosyl-L-methionine:L-histidine 3-amino-3-carboxypropyltransferase 2 {ECO:0000305}; GN Name=DPH2; Synonyms=DPH2L2; 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 [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RX PubMed=9782084; DOI=10.1006/geno.1998.5420; RA Schultz D.C., Balasara B.R., Testa J.R., Godwin A.K.; RT "Cloning and localization of a human diphthamide biosynthesis-like protein- RT 2 gene, DPH2L2."; RL Genomics 52:186-191(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Tongue; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [4] 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 [5] 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Colon, Kidney, and Pancreas; 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-435; SER-446 AND THR-467, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [10] 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-456 AND THR-467, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and 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 [14] RP FUNCTION, PATHWAY, INVOLVEMENT IN DEDSSH2, AND VARIANTS DEDSSH2 CYS-201 AND RP 308-GLN--GLY-489 DEL. RX PubMed=32576952; DOI=10.1038/s41431-020-0668-y; RA Hawer H., Mendelsohn B.A., Mayer K., Kung A., Malhotra A., Tuupanen S., RA Schleit J., Brinkmann U., Schaffrath R.; RT "Diphthamide-deficiency syndrome: a novel human developmental disorder and RT ribosomopathy."; RL Eur. J. Hum. Genet. 28:1497-1508(2020). CC -!- FUNCTION: Required for the first step of diphthamide biosynthesis, a CC post-translational modification of histidine which occurs in elongation CC factor 2 (PubMed:32576952). DPH1 and DPH2 transfer a 3-amino-3- CC carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a CC histidine residue, the reaction is assisted by a reduction system CC comprising DPH3 and a NADH-dependent reductase (By similarity). CC Facilitates the reduction of the catalytic iron-sulfur cluster found in CC the DPH1 subunit (By similarity). {ECO:0000250|UniProtKB:P32461, CC ECO:0000269|PubMed:32576952}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250|UniProtKB:P32461}; CC Note=Binds 1 [4Fe-4S] cluster per subunit. The cluster facilitates the CC reduction of the catalytic iron-sulfur cluster in the DPH1 subunit. CC {ECO:0000250|UniProtKB:P32461}; CC -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis. CC {ECO:0000305|PubMed:32576952}. CC -!- SUBUNIT: Component of the 2-(3-amino-3-carboxypropyl)histidine synthase CC complex composed of DPH1, DPH2, DPH3 and a NADH-dependent reductase (By CC similarity). Interacts with DPH1 (By similarity). CC {ECO:0000250|UniProtKB:P32461, ECO:0000250|UniProtKB:Q9CR25}. CC -!- INTERACTION: CC Q9BQC3; Q24JT5: CRYGA; NbExp=3; IntAct=EBI-10237931, EBI-10239205; CC Q9BQC3; O95363: FARS2; NbExp=3; IntAct=EBI-10237931, EBI-2513774; CC Q9BQC3; Q16552: IL17A; NbExp=3; IntAct=EBI-10237931, EBI-10237926; CC Q9BQC3; P61326: MAGOH; NbExp=3; IntAct=EBI-10237931, EBI-299134; CC Q9BQC3; Q8IVT2: MISP; NbExp=3; IntAct=EBI-10237931, EBI-2555085; CC Q9BQC3; Q9HC98-4: NEK6; NbExp=3; IntAct=EBI-10237931, EBI-11750983; CC Q9BQC3; Q07912-2: TNK2; NbExp=3; IntAct=EBI-10237931, EBI-11994780; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9BQC3-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9BQC3-2; Sequence=VSP_047151; CC Name=3; CC IsoId=Q9BQC3-3; Sequence=VSP_056052, VSP_056053; CC -!- TISSUE SPECIFICITY: Strongly expressed in skeletal muscle. Moderately CC expressed in heart, small intestine, liver, pancreas, testis and colon. CC Weakly expressed in brain, placenta, kidney, spleen, thymus, prostate, CC ovary and lymphocytes. {ECO:0000269|PubMed:9782084}. CC -!- DISEASE: Developmental delay with short stature, dysmorphic facial CC features, and sparse hair 2 (DEDSSH2) [MIM:620062]: An autosomal CC recessive syndrome characterized by developmental delay with variably CC impaired intellectual development and speech delay, short stature, CC abnormal head circumference, dysmorphic facial features, and sparse CC scalp hair. Affected individuals may have other abnormalities, CC including congenital cardiac defects and distal skeletal anomalies. CC {ECO:0000269|PubMed:32576952}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the DPH1/DPH2 family. DPH2 subfamily. CC {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; AF053003; AAC18086.1; -; mRNA. DR EMBL; AK297933; BAG60250.1; -; mRNA. DR EMBL; AK315506; BAG37890.1; -; mRNA. DR EMBL; BT007431; AAP36099.1; -; mRNA. DR EMBL; AL357079; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471059; EAX07070.1; -; Genomic_DNA. DR EMBL; BC001389; AAH01389.1; -; mRNA. DR EMBL; BC003181; AAH03181.1; -; mRNA. DR EMBL; BC016956; AAH16956.1; -; mRNA. DR CCDS; CCDS41314.1; -. [Q9BQC3-2] DR CCDS; CCDS504.1; -. [Q9BQC3-1] DR RefSeq; NP_001034678.1; NM_001039589.1. [Q9BQC3-2] DR RefSeq; NP_001306095.1; NM_001319166.1. DR RefSeq; NP_001306098.1; NM_001319169.1. [Q9BQC3-3] DR RefSeq; NP_001375.2; NM_001384.4. [Q9BQC3-1] DR AlphaFoldDB; Q9BQC3; -. DR SMR; Q9BQC3; -. DR BioGRID; 108136; 53. DR IntAct; Q9BQC3; 15. DR STRING; 9606.ENSP00000255108; -. DR GlyCosmos; Q9BQC3; 1 site, 1 glycan. DR GlyGen; Q9BQC3; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; Q9BQC3; -. DR PhosphoSitePlus; Q9BQC3; -. DR BioMuta; DPH2; -. DR DMDM; 74761201; -. DR EPD; Q9BQC3; -. DR jPOST; Q9BQC3; -. DR MassIVE; Q9BQC3; -. DR MaxQB; Q9BQC3; -. DR PaxDb; Q9BQC3; -. DR PeptideAtlas; Q9BQC3; -. DR ProteomicsDB; 2169; -. DR ProteomicsDB; 4698; -. DR ProteomicsDB; 78655; -. [Q9BQC3-1] DR Antibodypedia; 32411; 403 antibodies from 25 providers. DR DNASU; 1802; -. DR Ensembl; ENST00000255108.8; ENSP00000255108.3; ENSG00000132768.14. [Q9BQC3-1] DR Ensembl; ENST00000396758.6; ENSP00000379981.2; ENSG00000132768.14. [Q9BQC3-2] DR GeneID; 1802; -. DR KEGG; hsa:1802; -. DR MANE-Select; ENST00000255108.8; ENSP00000255108.3; NM_001384.5; NP_001375.2. DR UCSC; uc001ckz.4; human. [Q9BQC3-1] DR AGR; HGNC:3004; -. DR CTD; 1802; -. DR DisGeNET; 1802; -. DR GeneCards; DPH2; -. DR HGNC; HGNC:3004; DPH2. DR HPA; ENSG00000132768; Low tissue specificity. DR MalaCards; DPH2; -. DR MIM; 603456; gene. DR MIM; 620062; phenotype. DR neXtProt; NX_Q9BQC3; -. DR OpenTargets; ENSG00000132768; -. DR PharmGKB; PA27462; -. DR VEuPathDB; HostDB:ENSG00000132768; -. DR eggNOG; KOG2648; Eukaryota. DR GeneTree; ENSGT00940000153694; -. DR HOGENOM; CLU_884407_0_0_1; -. DR InParanoid; Q9BQC3; -. DR OMA; IEGWVVV; -. DR OrthoDB; 5491765at2759; -. DR PhylomeDB; Q9BQC3; -. DR TreeFam; TF313832; -. DR PathwayCommons; Q9BQC3; -. DR Reactome; R-HSA-5358493; Synthesis of diphthamide-EEF2. DR SignaLink; Q9BQC3; -. DR UniPathway; UPA00559; -. DR BioGRID-ORCS; 1802; 223 hits in 1168 CRISPR screens. DR ChiTaRS; DPH2; human. DR GenomeRNAi; 1802; -. DR Pharos; Q9BQC3; Tbio. DR PRO; PR:Q9BQC3; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9BQC3; protein. DR Bgee; ENSG00000132768; Expressed in gastrocnemius and 173 other tissues. DR ExpressionAtlas; Q9BQC3; baseline and differential. DR Genevisible; Q9BQC3; HS. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB. DR GO; GO:0090560; F:2-(3-amino-3-carboxypropyl)histidine synthase activity; EXP:Reactome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; ISS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0017183; P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine; IMP:UniProtKB. DR Gene3D; 3.40.50.11840; Diphthamide synthesis DPH1/DPH2 domain 1; 1. DR Gene3D; 3.40.50.11860; Diphthamide synthesis DPH1/DPH2 domain 3; 1. DR InterPro; IPR010014; DHP2. DR InterPro; IPR016435; DPH1/DPH2. DR InterPro; IPR042263; DPH1/DPH2_1. DR InterPro; IPR042265; DPH1/DPH2_3. DR PANTHER; PTHR10762:SF2; 2-(3-AMINO-3-CARBOXYPROPYL)HISTIDINE SYNTHASE SUBUNIT 2; 1. DR PANTHER; PTHR10762; DIPHTHAMIDE BIOSYNTHESIS PROTEIN; 1. DR Pfam; PF01866; Diphthamide_syn; 1. DR SFLD; SFLDG01121; Diphthamide_biosynthesis; 1. DR SFLD; SFLDF00408; Diphthamide_biosynthesis_famil; 1. DR SFLD; SFLDS00032; Radical_SAM_3-amino-3-carboxyp; 1. DR TIGRFAMs; TIGR00322; diphth2_R; 1. DR TIGRFAMs; TIGR00272; DPH2; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Disease variant; Dwarfism; KW Ectodermal dysplasia; Hypotrichosis; Intellectual disability; Iron; KW Iron-sulfur; Metal-binding; Phosphoprotein; Reference proteome. FT CHAIN 1..489 FT /note="2-(3-amino-3-carboxypropyl)histidine synthase FT subunit 2" FT /id="PRO_0000307889" FT BINDING 89 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250|UniProtKB:P32461" FT BINDING 110 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250|UniProtKB:P32461" FT BINDING 341 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250|UniProtKB:P32461" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 7 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 435 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 446 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 456 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 467 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 488 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT VAR_SEQ 1..26 FT /note="MESMFSSPAEAALQRETGVPGLLTPL -> MLWLWLHDWRRRQGQRCSFWVT FT QPTA (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056052" FT VAR_SEQ 27..161 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056053" FT VAR_SEQ 162..389 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_047151" FT VARIANT 201 FT /note="R -> C (in DEDSSH2; severely impairs diphthamide FT modification of elongation factor 2; dbSNP:rs767455462)" FT /evidence="ECO:0000269|PubMed:32576952" FT /id="VAR_086299" FT VARIANT 308..489 FT /note="Missing (in DEDSSH2; severely impairs diphthamide FT modification of elongation factor 2; dbSNP:rs755058688)" FT /evidence="ECO:0000269|PubMed:32576952" FT /id="VAR_086300" FT CONFLICT 125..153 FT /note="RQRSVALELCVKAFEAQNPDPKAPVVLLS -> SSTFCGLGTLCQDLWGPKP FT RPQSACGAAG (in Ref. 1; AAC18086)" FT /evidence="ECO:0000305" FT CONFLICT 266 FT /note="R -> G (in Ref. 1; AAC18086)" FT /evidence="ECO:0000305" FT CONFLICT 435 FT /note="T -> N (in Ref. 1; AAC18086)" FT /evidence="ECO:0000305" FT CONFLICT 449 FT /note="A -> V (in Ref. 1; AAC18086)" FT /evidence="ECO:0000305" SQ SEQUENCE 489 AA; 52083 MW; 2908FB7E816E3AEF CRC64; MESMFSSPAE AALQRETGVP GLLTPLPDLD GVYELERVAG FVRDLGCERV ALQFPDQLLG DAVAVAARLE ETTGSKMFIL GDTAYGSCCV DVLGAEQAGA QALIHFGPAC LSPPARPLPV AFVLRQRSVA LELCVKAFEA QNPDPKAPVV LLSEPACAHA LEALATLLRP RYLDLLVSSP AFPQPVGSLS PEPMPLERFG RRFPLAPGRR LEEYGAFYVG GSKASPDPDL DPDLSRLLLG WAPGQPFSSC CPDTGKTQDE GARAGRLRAR RRYLVERARD ARVVGLLAGT LGVAQHREAL AHLRNLTQAA GKRSYVLALG RPTPAKLANF PEVDVFVLLA CPLGALAPQL SGSFFQPILA PCELEAACNP AWPPPGLAPH LTHYADLLPG SPFHVALPPP ESELWETPDV SLITGDLRPP PAWKSSNDHG SLALTPRPQL ELAESSPAAS FLSSRSWQGL EPRLGQTPVT EAVSGRRGIA IAYEDEGSG //