EFTU_HUMAN
ID EFTU_HUMAN Reviewed; 452 AA.
AC P49411; O15276;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 223.
DE RecName: Full=Elongation factor Tu, mitochondrial;
DE Short=EF-Tu;
DE AltName: Full=P43;
DE Flags: Precursor;
GN Name=TUFM;
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].
RC TISSUE=Liver;
RX PubMed=8547323; DOI=10.1016/0167-4781(95)00176-x;
RA Woriax V.L., Burkhart W.A., Spremulli L.L.;
RT "Cloning, sequence analysis and expression of mammalian mitochondrial
RT protein synthesis elongation factor Tu.";
RL Biochim. Biophys. Acta 1264:347-356(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=7828719; DOI=10.1016/0014-5793(94)01403-n;
RA Wells J., Henkler F., Leversha M., Koshy R.;
RT "A mitochondrial elongation factor-like protein is over-expressed in
RT tumours and differentially expressed in normal tissues.";
RL FEBS Lett. 358:119-125(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart, and Kidney;
RX PubMed=9332382; DOI=10.1016/s0378-1119(97)00279-5;
RA Ling M., Merante F., Chen H.-S., Duff C., Duncan A.M.V., Robinson B.H.;
RT "The human mitochondrial elongation factor Tu (EF-Tu) gene: cDNA sequence,
RT genomic localization, genomic structure, and identification of a
RT pseudogene.";
RL Gene 197:325-336(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Placenta;
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 PROTEIN SEQUENCE OF 44-54.
RC TISSUE=Heart;
RA Dunn M.J.;
RL Submitted (MAR-1996) to UniProtKB.
RN [7]
RP PROTEIN SEQUENCE OF 44-53.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [8]
RP PROTEIN SEQUENCE OF 239-271, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Vishwanath V.;
RL Submitted (MAR-2007) to UniProtKB.
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 379-395.
RA Jacobs H.T., Smurthwaite L., Koshy R.;
RT "Human genomic sequences encoding mitochondrial elongation factor EF-Tu:
RT evidence for post-endosymbiotic intron insertion.";
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-79; LYS-88; LYS-256 AND LYS-418,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [12]
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 [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NLRX1 AND ATG16L1.
RX PubMed=22749352; DOI=10.1016/j.immuni.2012.03.025;
RA Lei Y., Wen H., Yu Y., Taxman D.J., Zhang L., Widman D.G., Swanson K.V.,
RA Wen K.W., Damania B., Moore C.B., Giguere P.M., Siderovski D.P.,
RA Hiscott J., Razani B., Semenkovich C.F., Chen X., Ting J.P.;
RT "The mitochondrial proteins NLRX1 and TUFM form a complex that regulates
RT type I interferon and autophagy.";
RL Immunity 36:933-946(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-278, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [15]
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 [16]
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 [17]
RP VARIANT COXPD4 GLN-336.
RX PubMed=17160893; DOI=10.1086/510559;
RA Valente L., Tiranti V., Marsano R.M., Malfatti E., Fernandez-Vizarra E.,
RA Donnini C., Mereghetti P., De Gioia L., Burlina A., Castellan C.,
RA Comi G.P., Savasta S., Ferrero I., Zeviani M.;
RT "Infantile encephalopathy and defective mitochondrial DNA translation in
RT patients with mutations of mitochondrial elongation factors EFG1 and
RT EFTu.";
RL Am. J. Hum. Genet. 80:44-58(2007).
RN [18]
RP FUNCTION, AND INTERACTION WITH HUMAN PARAINFLUENZA VIRUS TYPE 3 MATRIX
RP PROTEIN (MICROBIAL INFECTION).
RX PubMed=28407488; DOI=10.1016/j.chom.2017.03.004;
RA Ding B., Zhang L., Li Z., Zhong Y., Tang Q., Qin Y., Chen M.;
RT "The Matrix Protein of Human Parainfluenza Virus Type 3 Induces Mitophagy
RT that Suppresses Interferon Responses.";
RL Cell Host Microbe 21:538-547(2017).
RN [19]
RP INTERACTION WITH HANTAAN HANTAVIRUS GLYCOPROTEIN N (MICROBIAL INFECTION).
RX PubMed=31091447; DOI=10.1016/j.celrep.2019.04.061;
RA Wang K., Ma H., Liu H., Ye W., Li Z., Cheng L., Zhang L., Lei Y., Shen L.,
RA Zhang F.;
RT "The Glycoprotein and Nucleocapsid Protein of Hantaviruses Manipulate
RT Autophagy Flux to Restrain Host Innate Immune Responses.";
RL Cell Rep. 27:2075-2091.e5(2019).
CC -!- FUNCTION: Promotes the GTP-dependent binding of aminoacyl-tRNA to the
CC A-site of ribosomes during protein biosynthesis. Also plays a role in
CC the regulation of autophagy and innate immunity. Recruits ATG5-ATG12
CC and NLRX1 at mitochondria and serves as a checkpoint of the RIG-
CC I/DDX58-MAVS pathway. In turn, inhibits RLR-mediated type I interferon
CC while promoting autophagy. {ECO:0000269|PubMed:22749352,
CC ECO:0000269|PubMed:28407488}.
CC -!- SUBUNIT: Interacts with NLRX1 (PubMed:22749352). Interacts with ATG16L1
CC (PubMed:22749352). {ECO:0000269|PubMed:22749352}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human parainfluenza virus
CC 3 matrix protein; this interaction inhibits RLR-mediated type I
CC interferon production while promoting autophagy.
CC {ECO:0000269|PubMed:28407488}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Hantaan hantavirus
CC glycoprotein N; this interaction contributes to the virus-induced
CC degradation of mitochondria by autophagy, which leads to degradation of
CC MAVS and inhibition of type I interferon (IFN) responses.
CC {ECO:0000269|PubMed:31091447}.
CC -!- INTERACTION:
CC P49411; Q15041: ARL6IP1; NbExp=3; IntAct=EBI-359097, EBI-714543;
CC P49411; Q96DZ9: CMTM5; NbExp=3; IntAct=EBI-359097, EBI-2548702;
CC P49411; Q8IZU0: FAM9B; NbExp=4; IntAct=EBI-359097, EBI-10175124;
CC P49411; Q8IVP5: FUNDC1; NbExp=3; IntAct=EBI-359097, EBI-3059266;
CC P49411; Q86UT6: NLRX1; NbExp=2; IntAct=EBI-359097, EBI-3893071;
CC P49411; P03427: PB2; Xeno; NbExp=9; IntAct=EBI-359097, EBI-8430745;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:22749352}.
CC -!- DISEASE: Combined oxidative phosphorylation deficiency 4 (COXPD4)
CC [MIM:610678]: A mitochondrial disease resulting in neonatal lactic
CC acidosis, rapidly progressive encephalopathy, severely decreased
CC mitochondrial protein synthesis, and combined deficiency of mtDNA-
CC related mitochondrial respiratory chain complexes.
CC {ECO:0000269|PubMed:17160893}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01059}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC60647.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH01633.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH10041.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L38995; AAB00499.1; -; mRNA.
DR EMBL; S75463; AAC60647.1; ALT_INIT; mRNA.
DR EMBL; X84694; CAA59169.1; -; mRNA.
DR EMBL; AC133550; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001633; AAH01633.2; ALT_INIT; mRNA.
DR EMBL; BC010041; AAH10041.2; ALT_INIT; mRNA.
DR EMBL; Y11797; CAA72493.1; -; Genomic_DNA.
DR PIR; S62767; S62767.
DR PIR; S68466; S68466.
DR RefSeq; NP_003312.3; NM_003321.4.
DR RefSeq; XP_016879108.1; XM_017023619.1.
DR PDB; 7A5G; EM; 4.33 A; Z=1-452.
DR PDB; 7O9K; EM; 3.10 A; t=1-452.
DR PDBsum; 7A5G; -.
DR PDBsum; 7O9K; -.
DR AlphaFoldDB; P49411; -.
DR SMR; P49411; -.
DR BioGRID; 113135; 610.
DR CORUM; P49411; -.
DR IntAct; P49411; 122.
DR MINT; P49411; -.
DR STRING; 9606.ENSP00000322439; -.
DR ChEMBL; CHEMBL4105970; -.
DR DrugBank; DB04315; Guanosine-5'-Diphosphate.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR CarbonylDB; P49411; -.
DR GlyGen; P49411; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; P49411; -.
DR MetOSite; P49411; -.
DR PhosphoSitePlus; P49411; -.
DR SwissPalm; P49411; -.
DR BioMuta; TUFM; -.
DR DMDM; 1706611; -.
DR DOSAC-COBS-2DPAGE; P49411; -.
DR OGP; P49411; -.
DR REPRODUCTION-2DPAGE; IPI00027107; -.
DR SWISS-2DPAGE; P49411; -.
DR UCD-2DPAGE; P49411; -.
DR EPD; P49411; -.
DR jPOST; P49411; -.
DR MassIVE; P49411; -.
DR MaxQB; P49411; -.
DR PaxDb; P49411; -.
DR PeptideAtlas; P49411; -.
DR PRIDE; P49411; -.
DR ProteomicsDB; 56003; -.
DR TopDownProteomics; P49411; -.
DR ABCD; P49411; 2 sequenced antibodies.
DR Antibodypedia; 13151; 329 antibodies from 30 providers.
DR DNASU; 7284; -.
DR Ensembl; ENST00000313511.8; ENSP00000322439.3; ENSG00000178952.11.
DR GeneID; 7284; -.
DR KEGG; hsa:7284; -.
DR UCSC; uc002drh.2; human.
DR CTD; 7284; -.
DR DisGeNET; 7284; -.
DR GeneCards; TUFM; -.
DR HGNC; HGNC:12420; TUFM.
DR HPA; ENSG00000178952; Low tissue specificity.
DR MalaCards; TUFM; -.
DR MIM; 602389; gene.
DR MIM; 610678; phenotype.
DR neXtProt; NX_P49411; -.
DR Orphanet; 254925; Combined oxidative phosphorylation defect type 4.
DR PharmGKB; PA37082; -.
DR VEuPathDB; HostDB:ENSG00000178952; -.
DR eggNOG; KOG0460; Eukaryota.
DR HOGENOM; CLU_007265_0_0_1; -.
DR InParanoid; P49411; -.
DR OrthoDB; 491836at2759; -.
DR PhylomeDB; P49411; -.
DR TreeFam; TF300432; -.
DR PathwayCommons; P49411; -.
DR Reactome; R-HSA-5389840; Mitochondrial translation elongation.
DR Reactome; R-HSA-9754560; SARS-CoV-2 modulates autophagy.
DR SignaLink; P49411; -.
DR SIGNOR; P49411; -.
DR BioGRID-ORCS; 7284; 248 hits in 1081 CRISPR screens.
DR ChiTaRS; TUFM; human.
DR GeneWiki; TUFM; -.
DR GenomeRNAi; 7284; -.
DR Pharos; P49411; Tchem.
DR PRO; PR:P49411; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P49411; protein.
DR Bgee; ENSG00000178952; Expressed in mucosa of transverse colon and 97 other tissues.
DR ExpressionAtlas; P49411; baseline and differential.
DR Genevisible; P49411; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003746; F:translation elongation factor activity; IDA:UniProtKB.
DR GO; GO:0070125; P:mitochondrial translational elongation; IBA:GO_Central.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0006414; P:translational elongation; IDA:UniProtKB.
DR CDD; cd01884; EF_Tu; 1.
DR CDD; cd03697; EFTU_II; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR041709; EF-Tu_GTP-bd.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR033720; EFTU_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004541; Transl_elong_EFTu/EF1A_bac/org.
DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF03143; GTP_EFTU_D3; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00485; EF-Tu; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Disease variant;
KW Elongation factor; GTP-binding; Host-virus interaction; Mitochondrion;
KW Nucleotide-binding; Phosphoprotein; Primary mitochondrial disease;
KW Protein biosynthesis; Reference proteome; Transit peptide.
FT TRANSIT 1..43
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:12665801, ECO:0000269|Ref.6"
FT CHAIN 44..452
FT /note="Elongation factor Tu, mitochondrial"
FT /id="PRO_0000007462"
FT DOMAIN 55..251
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 64..71
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 105..109
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 126..129
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 181..184
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 219..221
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT BINDING 64..71
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 126..130
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 181..184
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 79
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 88
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 88
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BFR5"
FT MOD_RES 234
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BFR5"
FT MOD_RES 256
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 278
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 286
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BFR5"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BFR5"
FT MOD_RES 361
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BFR5"
FT MOD_RES 418
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VARIANT 336
FT /note="R -> Q (in COXPD4)"
FT /evidence="ECO:0000269|PubMed:17160893"
FT /id="VAR_031902"
FT CONFLICT 195..197
FT /note="Missing (in Ref. 2; AAC60647)"
FT /evidence="ECO:0000305"
FT CONFLICT 384
FT /note="D -> N (in Ref. 1; AAB00499 and 9; CAA72493)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 452 AA; 49542 MW; E37274ABFFDB5FC7 CRC64;
MAAATLLRAT PHFSGLAAGR TFLLQGLLRL LKAPALPLLC RGLAVEAKKT YVRDKPHVNV
GTIGHVDHGK TTLTAAITKI LAEGGGAKFK KYEEIDNAPE ERARGITINA AHVEYSTAAR
HYAHTDCPGH ADYVKNMITG TAPLDGCILV VAANDGPMPQ TREHLLLARQ IGVEHVVVYV
NKADAVQDSE MVELVELEIR ELLTEFGYKG EETPVIVGSA LCALEGRDPE LGLKSVQKLL
DAVDTYIPVP ARDLEKPFLL PVEAVYSVPG RGTVVTGTLE RGILKKGDEC ELLGHSKNIR
TVVTGIEMFH KSLERAEAGD NLGALVRGLK REDLRRGLVM VKPGSIKPHQ KVEAQVYILS
KEEGGRHKPF VSHFMPVMFS LTWDMACRII LPPEKELAMP GEDLKFNLIL RQPMILEKGQ
RFTLRDGNRT IGTGLVTNTL AMTEEEKNIK WG
