SYIM_HUMAN
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 03-AUG-2022, entry version 173.
DE RecName: Full=Isoleucine--tRNA ligase, mitochondrial;
DE EC=6.1.1.5;
DE AltName: Full=Isoleucyl-tRNA synthetase;
DE Short=IleRS;
DE Flags: Precursor;
GN Name=IARS2;
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 -!- 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 -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
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};
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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; 245.
DR IntAct; Q9NSE4; 76.
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; Q9NSE4; -.
DR PeptideAtlas; Q9NSE4; -.
DR PRIDE; Q9NSE4; -.
DR ProteomicsDB; 82542; -.
DR Antibodypedia; 20735; 155 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 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; HLGTAWN; -.
DR OrthoDB; 59501at2759; -.
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; 640 hits in 1053 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 217 other tissues.
DR Genevisible; Q9NSE4; HS.
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; 3.40.50.620; -; 2.
DR Gene3D; 3.90.740.10; -; 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 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; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00392; ileS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
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:0000250"
FT MOTIF 664..668
FT /note="'KMSKS' region"
FT /evidence="ECO:0000250"
FT BINDING 667
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
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; unknown pathological
FT significance; dbSNP:rs1428331445)"
FT /evidence="ECO:0000269|PubMed:29914532"
FT /id="VAR_084826"
FT VARIANT 227
FT /note="F -> S (in CAGSSS; unknown pathological
FT significance; 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 unknown pathological significance; dbSNP:rs143722284)"
FT /evidence="ECO:0000269|PubMed:25130867"
FT /id="VAR_072590"
FT VARIANT 761
FT /note="H -> R (in CAGSSS; unknown pathological
FT significance; dbSNP:rs1571863769)"
FT /evidence="ECO:0000269|PubMed:30419932"
FT /id="VAR_083401"
FT VARIANT 816..1012
FT /note="Missing (in CAGSSS; unknown pathological
FT significance; dbSNP:rs532672867)"
FT /evidence="ECO:0000269|PubMed:29914532"
FT /id="VAR_084827"
FT VARIANT 817
FT /note="R -> H (in CAGSSS; unknown pathological
FT significance; dbSNP:rs146618526)"
FT /evidence="ECO:0000269|PubMed:30041933"
FT /id="VAR_083402"
FT VARIANT 859
FT /note="F -> L (in CAGSSS; unknown pathological
FT significance; dbSNP:rs199840959)"
FT /evidence="ECO:0000269|PubMed:29914532"
FT /id="VAR_084828"
FT VARIANT 874
FT /note="G -> R (in CAGSSS; unknown pathological
FT significance; dbSNP:rs151241066)"
FT /evidence="ECO:0000269|PubMed:28328135"
FT /id="VAR_083403"
FT VARIANT 909
FT /note="P -> L (in CAGSSS; unknown pathological
FT significance; dbSNP:rs587783070)"
FT /evidence="ECO:0000269|PubMed:25130867"
FT /id="VAR_072591"
FT VARIANT 909
FT /note="P -> S (in CAGSSS; unknown pathological
FT significance; 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
