ID SYIM_HUMAN Reviewed; 1012 AA. AC Q9NSE4; B2RPG8; Q1M2P9; Q6PI85; Q7L439; Q86WU9; Q96D91; Q9H9Q8; Q9NW42; DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 02-MAY-2006, sequence version 2. DT 27-MAR-2024, entry version 182. DE RecName: Full=Isoleucine--tRNA ligase, mitochondrial {ECO:0000305}; DE EC=6.1.1.5 {ECO:0000250|UniProtKB:P00956}; DE AltName: Full=Isoleucyl-tRNA synthetase; DE Short=IleRS; DE Flags: Precursor; GN Name=IARS2 {ECO:0000312|HGNC:HGNC:29685}; 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]. RA Shan Y.X., Guo Z.K., Huang C.Q., Ye G.M., Tang W.W., Yu L.; RT "Cloning and characterization of human mitochondrial isoleucine tRNA RT synthetase gene."; RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] 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 [3] 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 [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 20-1012. RC TISSUE=Brain; RA Shiba K., Suzuki N., Shigesada K., Schimmel P., Noda T.; RT "Structure and evolution of two human isoleucyl-tRNA synthetases."; RL Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, Liver, Placenta, and Skin; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 142-1012. 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 [7] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-189; LYS-233; LYS-241; LYS-775 RP AND LYS-781, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [8] 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 [9] RP INVOLVEMENT IN CAGSSS, VARIANT CAGSSS LEU-909, AND VARIANT LYS-708. RX PubMed=25130867; DOI=10.1002/humu.22629; RG FORGE Canada Consortium; RA Schwartzentruber J., Buhas D., Majewski J., Sasarman F., RA Papillon-Cavanagh S., Thiffaut I., Sheldon K.M., Massicotte C., Patry L., RA Simon M., Zare A.S., McKernan K.J., Michaud J., Boles R.G., Deal C.L., RA Desilets V., Shoubridge E.A., Samuels M.E.; RT "Mutation in the nuclear-encoded mitochondrial isoleucyl-tRNA synthetase RT IARS2 in patients with cataracts, growth hormone deficiency with short RT stature, partial sensorineural deafness, and peripheral neuropathy or with RT Leigh syndrome."; RL Hum. Mutat. 35:1285-1289(2014). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [12] RP VARIANT CAGSSS ARG-874. RX PubMed=28328135; DOI=10.1002/ajmg.a.38116; RA Moosa S., Haagerup A., Gregersen P.A., Petersen K.K., Altmueller J., RA Thiele H., Nuernberg P., Cho T.J., Kim O.H., Nishimura G., Wollnik B., RA Vogel I.; RT "Confirmation of CAGSSS syndrome as a distinct entity in a Danish patient RT with a novel homozygous mutation in IARS2."; RL Am. J. Med. Genet. A 173:1102-1108(2017). RN [13] RP VARIANTS CAGSSS ARG-761 AND SER-909. RX PubMed=30419932; DOI=10.1186/s12881-018-0709-3; RA Vona B., Maroofian R., Bellacchio E., Najafi M., Thompson K., Alahmad A., RA He L., Ahangari N., Rad A., Shahrokhzadeh S., Bahena P., Mittag F., RA Traub F., Movaffagh J., Amiri N., Doosti M., Boostani R., Shirzadeh E., RA Haaf T., Diodato D., Schmidts M., Taylor R.W., Karimiani E.G.; RT "Expanding the clinical phenotype of IARS2-related mitochondrial disease."; RL BMC Med. Genet. 19:196-196(2018). RN [14] RP VARIANTS CAGSSS SER-227 AND HIS-817. RX PubMed=30041933; DOI=10.1016/j.braindev.2018.06.010; RA Takezawa Y., Fujie H., Kikuchi A., Niihori T., Funayama R., Shirota M., RA Nakayama K., Aoki Y., Sasaki M., Kure S.; RT "Novel IARS2 mutations in Japanese siblings with CAGSSS, Leigh, and West RT syndrome."; RL Brain Dev. 40:934-938(2018). RN [15] RP VARIANTS CAGSSS ARG-203; 816-ARG--LYS-1012 DEL AND LEU-859. RX PubMed=29914532; DOI=10.1186/s13023-018-0828-0; RA Li J., Leng Y., Han S., Yan L., Lu C., Luo Y., Zhang X., Cao L.; RT "Clinical and genetic characteristics of Chinese patients with familial or RT sporadic pediatric cataract."; RL Orphanet J. Rare Dis. 13:94-94(2018). CC -!- FUNCTION: Aminoacyl-tRNA synthetase that catalyzes the specific CC attachment of isoleucine to its cognate tRNA (tRNA(Ile)). CC {ECO:0000250|UniProtKB:P00956}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L- CC isoleucyl-tRNA(Ile); Xref=Rhea:RHEA:11060, Rhea:RHEA-COMP:9666, CC Rhea:RHEA-COMP:9695, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:58045, ChEBI:CHEBI:78442, ChEBI:CHEBI:78528, CC ChEBI:CHEBI:456215; EC=6.1.1.5; CC Evidence={ECO:0000250|UniProtKB:P00956}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11061; CC Evidence={ECO:0000305}; CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000305}. CC -!- DISEASE: Cataracts, growth hormone deficiency, sensory neuropathy, CC sensorineural hearing loss, and skeletal dysplasia (CAGSSS) CC [MIM:616007]: An autosomal recessive disorder characterized by CC cataracts, short-stature secondary to growth hormone deficiency, CC sensorineural hearing deficit, peripheral sensory neuropathy, skeletal CC dysplasia, scoliosis, and facial dysmorphism. CC {ECO:0000269|PubMed:25130867, ECO:0000269|PubMed:28328135, CC ECO:0000269|PubMed:29914532, ECO:0000269|PubMed:30041933, CC ECO:0000269|PubMed:30419932}. Note=The disease may be caused by CC variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA91544.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAB14164.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; AY267462; AAP94033.1; -; mRNA. DR EMBL; AC103590; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; D28500; BAA95147.1; -; mRNA. DR EMBL; CH471100; EAW93305.1; -; Genomic_DNA. DR EMBL; BC010218; AAH10218.2; -; mRNA. DR EMBL; BC040376; AAH40376.2; -; mRNA. DR EMBL; BC047880; AAH47880.3; -; mRNA. DR EMBL; BC137438; AAI37439.1; -; mRNA. DR EMBL; AK001188; BAA91544.1; ALT_FRAME; mRNA. DR EMBL; AK022665; BAB14164.1; ALT_INIT; mRNA. DR CCDS; CCDS1523.1; -. DR RefSeq; NP_060530.3; NM_018060.3. DR AlphaFoldDB; Q9NSE4; -. DR SMR; Q9NSE4; -. DR BioGRID; 120824; 285. DR IntAct; Q9NSE4; 82. DR MINT; Q9NSE4; -. DR STRING; 9606.ENSP00000355889; -. DR ChEMBL; CHEMBL4105821; -. DR DrugBank; DB00167; Isoleucine. DR GlyGen; Q9NSE4; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9NSE4; -. DR MetOSite; Q9NSE4; -. DR PhosphoSitePlus; Q9NSE4; -. DR SwissPalm; Q9NSE4; -. DR BioMuta; IARS2; -. DR DMDM; 94730583; -. DR CPTAC; CPTAC-393; -. DR CPTAC; CPTAC-394; -. DR EPD; Q9NSE4; -. DR jPOST; Q9NSE4; -. DR MassIVE; Q9NSE4; -. DR MaxQB; Q9NSE4; -. DR PaxDb; 9606-ENSP00000355889; -. DR PeptideAtlas; Q9NSE4; -. DR ProteomicsDB; 82542; -. DR Pumba; Q9NSE4; -. DR Antibodypedia; 20735; 184 antibodies from 29 providers. DR DNASU; 55699; -. DR Ensembl; ENST00000366922.3; ENSP00000355889.2; ENSG00000067704.10. DR GeneID; 55699; -. DR KEGG; hsa:55699; -. DR MANE-Select; ENST00000366922.3; ENSP00000355889.2; NM_018060.4; NP_060530.3. DR UCSC; uc001hmc.4; human. DR AGR; HGNC:29685; -. DR CTD; 55699; -. DR DisGeNET; 55699; -. DR GeneCards; IARS2; -. DR HGNC; HGNC:29685; IARS2. DR HPA; ENSG00000067704; Low tissue specificity. DR MalaCards; IARS2; -. DR MIM; 612801; gene. DR MIM; 616007; phenotype. DR neXtProt; NX_Q9NSE4; -. DR OpenTargets; ENSG00000067704; -. DR Orphanet; 436174; Cataract-growth hormone deficiency-sensory neuropathy-sensorineural hearing loss-skeletal dysplasia syndrome. DR PharmGKB; PA142671670; -. DR VEuPathDB; HostDB:ENSG00000067704; -. DR eggNOG; KOG0433; Eukaryota. DR GeneTree; ENSGT00550000074910; -. DR HOGENOM; CLU_001493_7_2_1; -. DR InParanoid; Q9NSE4; -. DR OMA; HCWRCKT; -. DR OrthoDB; 656at2759; -. DR PhylomeDB; Q9NSE4; -. DR TreeFam; TF300518; -. DR BRENDA; 6.1.1.5; 2681. DR PathwayCommons; Q9NSE4; -. DR Reactome; R-HSA-379726; Mitochondrial tRNA aminoacylation. DR SignaLink; Q9NSE4; -. DR BioGRID-ORCS; 55699; 654 hits in 1131 CRISPR screens. DR ChiTaRS; IARS2; human. DR GenomeRNAi; 55699; -. DR Pharos; Q9NSE4; Tchem. DR PRO; PR:Q9NSE4; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9NSE4; Protein. DR Bgee; ENSG00000067704; Expressed in diaphragm and 219 other cell types or tissues. DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome. DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central. DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004822; F:isoleucine-tRNA ligase activity; IBA:GO_Central. DR GO; GO:0000049; F:tRNA binding; IEA:InterPro. DR GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IBA:GO_Central. DR GO; GO:0032543; P:mitochondrial translation; IBA:GO_Central. DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; TAS:Reactome. DR CDD; cd07960; Anticodon_Ia_Ile_BEm; 1. DR Gene3D; 1.10.730.20; -; 1. DR Gene3D; 3.40.50.620; HUPs; 2. DR Gene3D; 1.10.10.830; Ile-tRNA synthetase CP2 domain-like; 1. DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1. DR HAMAP; MF_02002; Ile_tRNA_synth_type1; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR002300; aa-tRNA-synth_Ia. DR InterPro; IPR033708; Anticodon_Ile_BEm. DR InterPro; IPR002301; Ile-tRNA-ligase. DR InterPro; IPR023585; Ile-tRNA-ligase_type1. DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd. DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit. DR InterPro; IPR010663; Znf_FPG/IleRS. DR NCBIfam; TIGR00392; ileS; 1. DR PANTHER; PTHR42765:SF1; ISOLEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR42765; SOLEUCYL-TRNA SYNTHETASE; 1. DR Pfam; PF08264; Anticodon_1; 1. DR Pfam; PF00133; tRNA-synt_1; 1. DR Pfam; PF06827; zf-FPG_IleRS; 1. DR PRINTS; PR00984; TRNASYNTHILE. DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1. DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1. DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. DR Genevisible; Q9NSE4; HS. PE 1: Evidence at protein level; KW Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Cataract; Deafness; KW Disease variant; Ligase; Mitochondrion; Neuropathy; Nucleotide-binding; KW Protein biosynthesis; Reference proteome; Transit peptide. FT TRANSIT 1..48 FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN 49..1012 FT /note="Isoleucine--tRNA ligase, mitochondrial" FT /id="PRO_0000233335" FT MOTIF 116..126 FT /note="'HIGH' region" FT /evidence="ECO:0000305" FT MOTIF 664..668 FT /note="'KMSKS' region" FT /evidence="ECO:0000305" FT BINDING 664 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P00956" FT BINDING 667 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P00956" FT MOD_RES 74 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8BIJ6" FT MOD_RES 74 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8BIJ6" FT MOD_RES 189 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 194 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8BIJ6" FT MOD_RES 233 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 241 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 241 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8BIJ6" FT MOD_RES 479 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8BIJ6" FT MOD_RES 500 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8BIJ6" FT MOD_RES 725 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8BIJ6" FT MOD_RES 775 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 775 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8BIJ6" FT MOD_RES 781 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 781 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8BIJ6" FT VARIANT 14 FT /note="A -> V (in dbSNP:rs2577154)" FT /id="VAR_059862" FT VARIANT 203 FT /note="G -> R (in CAGSSS; uncertain significance; FT dbSNP:rs1428331445)" FT /evidence="ECO:0000269|PubMed:29914532" FT /id="VAR_084826" FT VARIANT 227 FT /note="F -> S (in CAGSSS; uncertain significance; FT dbSNP:rs1571845061)" FT /evidence="ECO:0000269|PubMed:30041933" FT /id="VAR_083400" FT VARIANT 522 FT /note="I -> V (in dbSNP:rs11800305)" FT /id="VAR_034526" FT VARIANT 708 FT /note="E -> K (found in a patient with Leigh syndrome; FT uncertain significance; dbSNP:rs143722284)" FT /evidence="ECO:0000269|PubMed:25130867" FT /id="VAR_072590" FT VARIANT 761 FT /note="H -> R (in CAGSSS; uncertain significance; FT dbSNP:rs1571863769)" FT /evidence="ECO:0000269|PubMed:30419932" FT /id="VAR_083401" FT VARIANT 816..1012 FT /note="Missing (in CAGSSS; uncertain significance; FT dbSNP:rs532672867)" FT /evidence="ECO:0000269|PubMed:29914532" FT /id="VAR_084827" FT VARIANT 817 FT /note="R -> H (in CAGSSS; uncertain significance; FT dbSNP:rs146618526)" FT /evidence="ECO:0000269|PubMed:30041933" FT /id="VAR_083402" FT VARIANT 859 FT /note="F -> L (in CAGSSS; uncertain significance; FT dbSNP:rs199840959)" FT /evidence="ECO:0000269|PubMed:29914532" FT /id="VAR_084828" FT VARIANT 874 FT /note="G -> R (in CAGSSS; uncertain significance; FT dbSNP:rs151241066)" FT /evidence="ECO:0000269|PubMed:28328135" FT /id="VAR_083403" FT VARIANT 909 FT /note="P -> L (in CAGSSS; uncertain significance; FT dbSNP:rs587783070)" FT /evidence="ECO:0000269|PubMed:25130867" FT /id="VAR_072591" FT VARIANT 909 FT /note="P -> S (in CAGSSS; uncertain significance; FT dbSNP:rs1571865562)" FT /evidence="ECO:0000269|PubMed:30419932" FT /id="VAR_083404" FT CONFLICT 647 FT /note="P -> L (in Ref. 6; BAB14164)" FT /evidence="ECO:0000305" FT CONFLICT 907 FT /note="I -> T (in Ref. 6; BAB14164)" FT /evidence="ECO:0000305" SQ SEQUENCE 1012 AA; 113792 MW; 7AAAC0C9DAD7A8C7 CRC64; MRWGLRPRGP GAAALATARS LWGTPRLPCS PGWQGATKRL LVRSVSGASN HQPNSNSGRY RDTVLLPQTS FPMKLLGRQQ PDTELEIQQK CGFSELYSWQ RERKVKTEFC LHDGPPYANG DPHVGHALNK ILKDIANRFH MMNGSKIHFV PGWDCHGLPI EIKVLSELGR EAQNLSAMEI RKKARSFAKA AIEKQKSAFI RWGIMADWNN CYYTFDGKYE AKQLRTFYQM YDKGLVYRSY KPVFWSPSSR TALAEAELEY NPEHVSRSIY VKFPLLKPSP KLASLIDGSS PVSILVWTTQ PWTIPANEAV CYMPESKYAV VKCSKSGDLY VLAADKVASV ASTLETTFET ISTLSGVDLE NGTCSHPLIP DKASPLLPAN HVTMAKGTGL VHTAPAHGME DYGVASQHNL PMDCLVDEDG VFTDVAGPEL QNKAVLEEGT DVVIKMLQTA KNLLKEEKLV HSYPYDWRTK KPVVIRASKQ WFINITDIKT AAKELLKKVK FIPGSALNGM VEMMDRRPYW CISRQRVWGV PIPVFHHKTK DEYLINSQTT EHIVKLVEQH GSDIWWTLPP EQLLPKEVLS EVGGPDALEY VPGQDILDIW FDSGTSWSYV LPGPDQRADL YLEGKDQLGG WFQSSLLTSV AARKRAPYKT VIVHGFTLGE KGEKMSKSLG NVIHPDVVVN GGQDQSKEPP YGADVLRWWV ADSNVFTEVA IGPSVLNAAR DDISKLRNTL RFLLGNVADF NPETDSIPVN DMYVIDQYML HLLQDLANKI TELYKQYDFG KVVRLLRTFY TRELSNFYFS IIKDRLYCEK ENDPKRRSCQ TALVEILDVI VRSFAPILPH LAEEVFQHIP YIKEPKSVFR TGWISTSSIW KKPGLEEAVE SACAMRDSFL GSIPGKNAAE YKVITVIEPG LLFEIIEMLQ SEETSSTSQL NELMMASEST LLAQEPREMT ADVIELKGKF LINLEGGDIR EESSYKVIVM PTTKEKCPRC WKYTAESSDT LCPRCAEVVS GK //