DPH2_HUMAN
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-AUG-2022, entry version 158.
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 DIPHTHAMINE-DEFICIENCY SYNDROME, AND
RP VARIANTS DIPHTHAMINE-DEFICIENCY SYNDROME CYS-201 AND 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: Note=Defects in DPH2 may be the cause of diphthamide-
CC deficiency syndrome (PubMed:32576952). Affected individuals may present
CC with infantile macrocephaly, developmental delay, short stature,
CC dysmorphic craniofacial features, and congenital heart disease
CC (PubMed:32576952). {ECO:0000269|PubMed:32576952}.
CC -!- SIMILARITY: Belongs to the DPH1/DPH2 family. DPH2 subfamily.
CC {ECO:0000305}.
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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; 46.
DR IntAct; Q9BQC3; 15.
DR STRING; 9606.ENSP00000255108; -.
DR GlyGen; Q9BQC3; 1 site, 1 O-linked glycan (1 site).
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 PRIDE; Q9BQC3; -.
DR ProteomicsDB; 2169; -.
DR ProteomicsDB; 4698; -.
DR ProteomicsDB; 78655; -. [Q9BQC3-1]
DR Antibodypedia; 32411; 401 antibodies from 24 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 CTD; 1802; -.
DR DisGeNET; 1802; -.
DR GeneCards; DPH2; -.
DR HGNC; HGNC:3004; DPH2.
DR HPA; ENSG00000132768; Low tissue specificity.
DR MIM; 603456; gene.
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; PFNNMYD; -.
DR OrthoDB; 750182at2759; -.
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; 205 hits in 1090 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:0017183; P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine; IMP:UniProtKB.
DR Gene3D; 3.40.50.11840; -; 1.
DR Gene3D; 3.40.50.11860; -; 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; PTHR10762; 1.
DR PANTHER; PTHR10762:SF2; PTHR10762:SF2; 1.
DR Pfam; PF01866; Diphthamide_syn; 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 (found in a patient with diphthamide-
FT deficiency syndrome; probable disease-associated variant;
FT severely impairs diphthamide modification of elongation
FT factor 2.; dbSNP:rs767455462)"
FT /evidence="ECO:0000269|PubMed:32576952"
FT /id="VAR_086299"
FT VARIANT 308..489
FT /note="Missing (found in a patient with diphthamide-
FT deficiency syndrome; probable disease-associated variant;
FT severely impairs diphthamide modification of elongation
FT 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
