ETKMT_HUMAN
ID ETKMT_HUMAN Reviewed; 262 AA.
AC Q8IXQ9; D3DUW3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Electron transfer flavoprotein beta subunit lysine methyltransferase {ECO:0000303|PubMed:25416781};
DE EC=2.1.1.- {ECO:0000269|PubMed:25023281, ECO:0000269|PubMed:25416781};
DE AltName: Full=ETFB lysine methyltransferase {ECO:0000303|PubMed:25416781};
DE Short=ETFB-KMT {ECO:0000303|PubMed:25416781};
DE AltName: Full=Protein N-lysine methyltransferase METTL20;
DE Flags: Precursor;
GN Name=ETFBKMT {ECO:0000312|HGNC:HGNC:28739}; Synonyms=C12orf72, METTL20;
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 [LARGE SCALE MRNA].
RC TISSUE=Cervix;
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Testis;
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 [4]
RP IDENTIFICATION.
RX PubMed=22948820; DOI=10.1038/ncomms2041;
RA Kernstock S., Davydova E., Jakobsson M., Moen A., Pettersen S.,
RA Maelandsmo G.M., Egge-Jacobsen W., Falnes P.O.;
RT "Lysine methylation of VCP by a member of a novel human protein
RT methyltransferase family.";
RL Nat. Commun. 3:1038-1038(2012).
RN [5]
RP INTERACTION WITH HSPD1, AND SUBCELLULAR LOCATION.
RX PubMed=23349634; DOI=10.1371/journal.pgen.1003210;
RA Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.;
RT "A newly uncovered group of distantly related lysine methyltransferases
RT preferentially interact with molecular chaperones to regulate their
RT activity.";
RL PLoS Genet. 9:E1003210-E1003210(2013).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=25023281; DOI=10.1074/jbc.m114.580464;
RA Rhein V.F., Carroll J., He J., Ding S., Fearnley I.M., Walker J.E.;
RT "Human METTL20 methylates lysine residues adjacent to the recognition loop
RT of the electron transfer flavoprotein in mitochondria.";
RL J. Biol. Chem. 289:24640-24651(2014).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP ASP-121.
RX PubMed=25416781; DOI=10.1074/jbc.m114.614115;
RA Malecki J., Ho A.Y., Moen A., Dahl H.A., Falnes P.O.;
RT "Human METTL20 is a mitochondrial lysine methyltransferase that targets the
RT beta subunit of electron transfer flavoprotein (ETFbeta) and modulates its
RT activity.";
RL J. Biol. Chem. 290:423-434(2015).
CC -!- FUNCTION: Protein-lysine methyltransferase that selectively
CC trimethylates the flavoprotein ETFB in mitochondria (PubMed:25023281,
CC PubMed:25416781). Thereby, may negatively regulate the function of ETFB
CC in electron transfer from Acyl-CoA dehydrogenases to the main
CC respiratory chain (PubMed:25416781). {ECO:0000269|PubMed:25023281,
CC ECO:0000269|PubMed:25416781}.
CC -!- SUBUNIT: Interacts with HSPD1; this protein may possibly be a
CC methylation substrate. {ECO:0000269|PubMed:23349634}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23349634}.
CC Mitochondrion matrix {ECO:0000269|PubMed:25023281,
CC ECO:0000305|PubMed:25416781}. Note=Concentrated in cytoplasmic granular
CC foci. {ECO:0000269|PubMed:23349634}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. ETFBKMT
CC family. {ECO:0000305}.
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DR EMBL; AK290248; BAF82937.1; -; mRNA.
DR EMBL; CH471116; EAW88545.1; -; Genomic_DNA.
DR EMBL; CH471116; EAW88547.1; -; Genomic_DNA.
DR EMBL; CH471116; EAW88548.1; -; Genomic_DNA.
DR EMBL; BC039107; AAH39107.1; -; mRNA.
DR EMBL; BC039535; AAH39535.1; -; mRNA.
DR CCDS; CCDS8724.1; -.
DR RefSeq; NP_001129335.1; NM_001135863.1.
DR RefSeq; NP_001129336.1; NM_001135864.1.
DR RefSeq; NP_776163.1; NM_173802.3.
DR AlphaFoldDB; Q8IXQ9; -.
DR SMR; Q8IXQ9; -.
DR BioGRID; 129005; 34.
DR IntAct; Q8IXQ9; 3.
DR STRING; 9606.ENSP00000350353; -.
DR iPTMnet; Q8IXQ9; -.
DR PhosphoSitePlus; Q8IXQ9; -.
DR BioMuta; ETFBKMT; -.
DR DMDM; 74759679; -.
DR EPD; Q8IXQ9; -.
DR MassIVE; Q8IXQ9; -.
DR PaxDb; Q8IXQ9; -.
DR PeptideAtlas; Q8IXQ9; -.
DR PRIDE; Q8IXQ9; -.
DR ProteomicsDB; 71049; -.
DR Antibodypedia; 24685; 35 antibodies from 14 providers.
DR DNASU; 254013; -.
DR Ensembl; ENST00000357721.3; ENSP00000350353.3; ENSG00000139160.13.
DR Ensembl; ENST00000395763.7; ENSP00000379112.3; ENSG00000139160.13.
DR Ensembl; ENST00000412352.6; ENSP00000396123.2; ENSG00000139160.13.
DR Ensembl; ENST00000538463.5; ENSP00000441421.1; ENSG00000139160.13.
DR GeneID; 254013; -.
DR KEGG; hsa:254013; -.
DR MANE-Select; ENST00000357721.3; ENSP00000350353.3; NM_001135863.2; NP_001129335.1.
DR UCSC; uc001rkl.4; human.
DR CTD; 254013; -.
DR GeneCards; ETFBKMT; -.
DR HGNC; HGNC:28739; ETFBKMT.
DR HPA; ENSG00000139160; Low tissue specificity.
DR MIM; 615256; gene.
DR neXtProt; NX_Q8IXQ9; -.
DR OpenTargets; ENSG00000139160; -.
DR PharmGKB; PA164716777; -.
DR VEuPathDB; HostDB:ENSG00000139160; -.
DR eggNOG; ENOG502QUSY; Eukaryota.
DR GeneTree; ENSGT00940000162982; -.
DR HOGENOM; CLU_074455_2_1_1; -.
DR InParanoid; Q8IXQ9; -.
DR OMA; ILNCELN; -.
DR OrthoDB; 1585716at2759; -.
DR PhylomeDB; Q8IXQ9; -.
DR TreeFam; TF314934; -.
DR PathwayCommons; Q8IXQ9; -.
DR Reactome; R-HSA-8876725; Protein methylation.
DR SignaLink; Q8IXQ9; -.
DR BioGRID-ORCS; 254013; 8 hits in 1065 CRISPR screens.
DR ChiTaRS; ETFBKMT; human.
DR GenomeRNAi; 254013; -.
DR Pharos; Q8IXQ9; Tbio.
DR PRO; PR:Q8IXQ9; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q8IXQ9; protein.
DR Bgee; ENSG00000139160; Expressed in buccal mucosa cell and 116 other tissues.
DR ExpressionAtlas; Q8IXQ9; baseline and differential.
DR Genevisible; Q8IXQ9; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0031072; F:heat shock protein binding; IPI:UniProtKB.
DR GO; GO:0008276; F:protein methyltransferase activity; IBA:GO_Central.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IMP:UniProtKB.
DR GO; GO:1904733; P:negative regulation of electron transfer activity; IMP:UniProtKB.
DR GO; GO:1904736; P:negative regulation of fatty acid beta-oxidation using acyl-CoA dehydrogenase; IMP:UniProtKB.
DR GO; GO:0018022; P:peptidyl-lysine methylation; IMP:UniProtKB.
DR GO; GO:0018023; P:peptidyl-lysine trimethylation; IMP:UniProtKB.
DR GO; GO:0006479; P:protein methylation; TAS:Reactome.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Methyltransferase; Mitochondrion; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..38
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 39..262
FT /note="Electron transfer flavoprotein beta subunit lysine
FT methyltransferase"
FT /id="PRO_0000318709"
FT MUTAGEN 121
FT /note="D->A: Loss of lysine methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:25416781"
SQ SEQUENCE 262 AA; 29461 MW; 4A784F2DFA6A4216 CRC64;
MALSLGWKAH RNHCGLLLQA LRSSGLLLFP CGQCPWRGAG SFLDPEIKAF LEENTEVTSS
GSLTPEIQLR LLTPRCKFWW ERADLWPHSD PYWAIYWPGG QALSRYLLDN PDVVRGKSVL
DLGSGCGATA IAAKMSGASR ILANDIDPIA GMAITLNCEL NRLNPFPILI QNILNLEQDK
WDLVVLGDMF YDEDLADSLH QWLKKCFWTY RTRVLIGDPG RPQFSGHSIQ HHLHKVVEYS
LLESTRQENS GLTTSTVWGF QP
