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Electron transfer flavoprotein beta subunit lysine methyltransferase (EC 2.1.1.-) (ETFB lysine methyltransferase) (ETFB-KMT) (Protein N-lysine methyltransferase METTL20)

 ETKMT_HUMAN             Reviewed;         262 AA.
Q8IXQ9; D3DUW3;
26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
20-DEC-2017, entry version 120.
RecName: Full=Electron transfer flavoprotein beta subunit lysine methyltransferase {ECO:0000303|PubMed:25416781};
EC=2.1.1.- {ECO:0000269|PubMed:25023281, ECO:0000269|PubMed:25416781};
AltName: Full=ETFB lysine methyltransferase {ECO:0000303|PubMed:25416781};
Short=ETFB-KMT {ECO:0000303|PubMed:25416781};
AltName: Full=Protein N-lysine methyltransferase METTL20;
Flags: Precursor;
Name=ETFBKMT {ECO:0000312|HGNC:HGNC:28739};
Synonyms=C12orf72, METTL20;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cervix;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
IDENTIFICATION.
PubMed=22948820; DOI=10.1038/ncomms2041;
Kernstock S., Davydova E., Jakobsson M., Moen A., Pettersen S.,
Maelandsmo G.M., Egge-Jacobsen W., Falnes P.O.;
"Lysine methylation of VCP by a member of a novel human protein
methyltransferase family.";
Nat. Commun. 3:1038-1038(2012).
[5]
INTERACTION WITH HSPD1, AND SUBCELLULAR LOCATION.
PubMed=23349634; DOI=10.1371/journal.pgen.1003210;
Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.;
"A newly uncovered group of distantly related lysine
methyltransferases preferentially interact with molecular chaperones
to regulate their activity.";
PLoS Genet. 9:E1003210-E1003210(2013).
[6]
FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
PubMed=25023281; DOI=10.1074/jbc.M114.580464;
Rhein V.F., Carroll J., He J., Ding S., Fearnley I.M., Walker J.E.;
"Human METTL20 methylates lysine residues adjacent to the recognition
loop of the electron transfer flavoprotein in mitochondria.";
J. Biol. Chem. 289:24640-24651(2014).
[7]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
ASP-121.
PubMed=25416781; DOI=10.1074/jbc.M114.614115;
Malecki J., Ho A.Y., Moen A., Dahl H.A., Falnes P.O.;
"Human METTL20 is a mitochondrial lysine methyltransferase that
targets the beta subunit of electron transfer flavoprotein (ETFbeta)
and modulates its activity.";
J. Biol. Chem. 290:423-434(2015).
-!- FUNCTION: Protein-lysine methyltransferase that selectively
trimethylates the flavoprotein ETFB in mitochondria
(PubMed:25023281, PubMed:25416781). Thereby, may negatively
regulate the function of ETFB in electron transfer from Acyl-CoA
dehydrogenases to the main respiratory chain (PubMed:25416781).
{ECO:0000269|PubMed:25023281, ECO:0000269|PubMed:25416781}.
-!- SUBUNIT: Interacts with HSPD1; this protein may possibly be a
methylation substrate. {ECO:0000269|PubMed:23349634}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23349634}.
Mitochondrion matrix {ECO:0000269|PubMed:25023281,
ECO:0000305|PubMed:25416781}. Note=Concentrated in cytoplasmic
granular foci. {ECO:0000269|PubMed:23349634}.
-!- SIMILARITY: Belongs to the methyltransferase superfamily. ETFBKMT
family. {ECO:0000305}.
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EMBL; AK290248; BAF82937.1; -; mRNA.
EMBL; CH471116; EAW88545.1; -; Genomic_DNA.
EMBL; CH471116; EAW88547.1; -; Genomic_DNA.
EMBL; CH471116; EAW88548.1; -; Genomic_DNA.
EMBL; BC039107; AAH39107.1; -; mRNA.
EMBL; BC039535; AAH39535.1; -; mRNA.
CCDS; CCDS8724.1; -.
RefSeq; NP_001129335.1; NM_001135863.1.
RefSeq; NP_001129336.1; NM_001135864.1.
RefSeq; NP_776163.1; NM_173802.3.
UniGene; Hs.740628; -.
ProteinModelPortal; Q8IXQ9; -.
BioGrid; 129005; 12.
STRING; 9606.ENSP00000350353; -.
iPTMnet; Q8IXQ9; -.
PhosphoSitePlus; Q8IXQ9; -.
BioMuta; METTL20; -.
DMDM; 74759679; -.
PaxDb; Q8IXQ9; -.
PeptideAtlas; Q8IXQ9; -.
PRIDE; Q8IXQ9; -.
DNASU; 254013; -.
Ensembl; ENST00000357721; ENSP00000350353; ENSG00000139160.
Ensembl; ENST00000395763; ENSP00000379112; ENSG00000139160.
Ensembl; ENST00000412352; ENSP00000396123; ENSG00000139160.
Ensembl; ENST00000538463; ENSP00000441421; ENSG00000139160.
GeneID; 254013; -.
KEGG; hsa:254013; -.
UCSC; uc001rkl.4; human.
CTD; 254013; -.
EuPathDB; HostDB:ENSG00000139160.13; -.
GeneCards; ETFBKMT; -.
HGNC; HGNC:28739; ETFBKMT.
HPA; HPA039024; -.
MIM; 615256; gene.
neXtProt; NX_Q8IXQ9; -.
OpenTargets; ENSG00000139160; -.
PharmGKB; PA164716777; -.
eggNOG; ENOG410IH4U; Eukaryota.
eggNOG; COG3897; LUCA.
GeneTree; ENSGT00390000002528; -.
HOGENOM; HOG000226047; -.
HOVERGEN; HBG107714; -.
InParanoid; Q8IXQ9; -.
OMA; CELNQLN; -.
OrthoDB; EOG091G0J2A; -.
PhylomeDB; Q8IXQ9; -.
TreeFam; TF314934; -.
Reactome; R-HSA-8876725; Protein methylation.
GenomeRNAi; 254013; -.
PRO; PR:Q8IXQ9; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000139160; -.
ExpressionAtlas; Q8IXQ9; baseline and differential.
Genevisible; Q8IXQ9; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0031072; F:heat shock protein binding; IPI:UniProtKB.
GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IMP:UniProtKB.
GO; GO:1904733; P:negative regulation of electron transfer activity; IMP:UniProtKB.
GO; GO:1904736; P:negative regulation of fatty acid beta-oxidation using acyl-CoA dehydrogenase; IMP:UniProtKB.
GO; GO:0018022; P:peptidyl-lysine methylation; IMP:UniProtKB.
GO; GO:0018023; P:peptidyl-lysine trimethylation; IMP:UniProtKB.
GO; GO:0006479; P:protein methylation; TAS:Reactome.
InterPro; IPR029063; SAM-dependent_MTases.
SUPFAM; SSF53335; SSF53335; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Methyltransferase; Mitochondrion;
Reference proteome; Transferase; Transit peptide.
TRANSIT 1 38 Mitochondrion.
{ECO:0000303|PubMed:25023281,
ECO:0000303|PubMed:25416781}.
CHAIN 39 262 Electron transfer flavoprotein beta
subunit lysine methyltransferase.
/FTId=PRO_0000318709.
MUTAGEN 121 121 D->A: Loss of lysine methyltransferase
activity. {ECO:0000269|PubMed:25416781}.
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


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