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Protein

Electron transfer flavoprotein beta subunit lysine methyltransferase

Gene

ETFBKMT

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).2 Publications

GO - Molecular functioni

  • protein-lysine N-methyltransferase activity Source: UniProtKB

GO - Biological processi

  • negative regulation of electron carrier activity Source: UniProtKB
  • negative regulation of fatty acid beta-oxidation using acyl-CoA dehydrogenase Source: UniProtKB
  • peptidyl-lysine methylation Source: UniProtKB
  • peptidyl-lysine trimethylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Electron transfer flavoprotein beta subunit lysine methyltransferase1 Publication (EC:2.1.1.-2 Publications)
Alternative name(s):
ETFB lysine methyltransferase1 Publication
Short name:
ETFB-KMT1 Publication
Protein N-lysine methyltransferase METTL20
Gene namesi
Name:ETFBKMTImported
Synonyms:C12orf72, METTL20
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:28739. ETFBKMT.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi121 – 1211D → A: Loss of lysine methyltransferase activity. 1 Publication

Organism-specific databases

PharmGKBiPA164716777.

Polymorphism and mutation databases

BioMutaiMETTL20.
DMDMi74759679.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3838Mitochondrion2 PublicationsAdd
BLAST
Chaini39 – 262224Electron transfer flavoprotein beta subunit lysine methyltransferasePRO_0000318709Add
BLAST

Proteomic databases

PaxDbiQ8IXQ9.
PRIDEiQ8IXQ9.

PTM databases

iPTMnetiQ8IXQ9.

Expressioni

Gene expression databases

BgeeiQ8IXQ9.
ExpressionAtlasiQ8IXQ9. baseline and differential.
GenevisibleiQ8IXQ9. HS.

Organism-specific databases

HPAiHPA039024.

Interactioni

Subunit structurei

Interacts with HSPD1; this protein may possibly be a methylation substrate.1 Publication

Protein-protein interaction databases

BioGridi129005. 12 interactions.
STRINGi9606.ENSP00000350353.

Structurei

3D structure databases

ProteinModelPortaliQ8IXQ9.
SMRiQ8IXQ9. Positions 101-191.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410IH4U. Eukaryota.
COG3897. LUCA.
GeneTreeiENSGT00390000002528.
HOGENOMiHOG000226047.
HOVERGENiHBG107714.
InParanoidiQ8IXQ9.
OMAiEQDKWDL.
OrthoDBiEOG7FJH2B.
PhylomeDBiQ8IXQ9.
TreeFamiTF314934.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR029063. SAM-dependent_MTases.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8IXQ9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALSLGWKAH RNHCGLLLQA LRSSGLLLFP CGQCPWRGAG SFLDPEIKAF
60 70 80 90 100
LEENTEVTSS GSLTPEIQLR LLTPRCKFWW ERADLWPHSD PYWAIYWPGG
110 120 130 140 150
QALSRYLLDN PDVVRGKSVL DLGSGCGATA IAAKMSGASR ILANDIDPIA
160 170 180 190 200
GMAITLNCEL NRLNPFPILI QNILNLEQDK WDLVVLGDMF YDEDLADSLH
210 220 230 240 250
QWLKKCFWTY RTRVLIGDPG RPQFSGHSIQ HHLHKVVEYS LLESTRQENS
260
GLTTSTVWGF QP
Length:262
Mass (Da):29,461
Last modified:March 1, 2003 - v1
Checksum:i4A784F2DFA6A4216
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK290248 mRNA. Translation: BAF82937.1.
CH471116 Genomic DNA. Translation: EAW88545.1.
CH471116 Genomic DNA. Translation: EAW88547.1.
CH471116 Genomic DNA. Translation: EAW88548.1.
BC039107 mRNA. Translation: AAH39107.1.
BC039535 mRNA. Translation: AAH39535.1.
CCDSiCCDS8724.1.
RefSeqiNP_001129335.1. NM_001135863.1.
NP_001129336.1. NM_001135864.1.
NP_776163.1. NM_173802.3.
XP_006719123.1. XM_006719060.2.
UniGeneiHs.740628.

Genome annotation databases

EnsembliENST00000357721; ENSP00000350353; ENSG00000139160.
ENST00000395763; ENSP00000379112; ENSG00000139160.
ENST00000412352; ENSP00000396123; ENSG00000139160.
ENST00000538463; ENSP00000441421; ENSG00000139160.
GeneIDi254013.
KEGGihsa:254013.
UCSCiuc001rkl.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK290248 mRNA. Translation: BAF82937.1.
CH471116 Genomic DNA. Translation: EAW88545.1.
CH471116 Genomic DNA. Translation: EAW88547.1.
CH471116 Genomic DNA. Translation: EAW88548.1.
BC039107 mRNA. Translation: AAH39107.1.
BC039535 mRNA. Translation: AAH39535.1.
CCDSiCCDS8724.1.
RefSeqiNP_001129335.1. NM_001135863.1.
NP_001129336.1. NM_001135864.1.
NP_776163.1. NM_173802.3.
XP_006719123.1. XM_006719060.2.
UniGeneiHs.740628.

3D structure databases

ProteinModelPortaliQ8IXQ9.
SMRiQ8IXQ9. Positions 101-191.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi129005. 12 interactions.
STRINGi9606.ENSP00000350353.

PTM databases

iPTMnetiQ8IXQ9.

Polymorphism and mutation databases

BioMutaiMETTL20.
DMDMi74759679.

Proteomic databases

PaxDbiQ8IXQ9.
PRIDEiQ8IXQ9.

Protocols and materials databases

DNASUi254013.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000357721; ENSP00000350353; ENSG00000139160.
ENST00000395763; ENSP00000379112; ENSG00000139160.
ENST00000412352; ENSP00000396123; ENSG00000139160.
ENST00000538463; ENSP00000441421; ENSG00000139160.
GeneIDi254013.
KEGGihsa:254013.
UCSCiuc001rkl.4. human.

Organism-specific databases

CTDi254013.
GeneCardsiMETTL20.
HGNCiHGNC:28739. ETFBKMT.
HPAiHPA039024.
MIMi615256. gene.
neXtProtiNX_Q8IXQ9.
PharmGKBiPA164716777.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IH4U. Eukaryota.
COG3897. LUCA.
GeneTreeiENSGT00390000002528.
HOGENOMiHOG000226047.
HOVERGENiHBG107714.
InParanoidiQ8IXQ9.
OMAiEQDKWDL.
OrthoDBiEOG7FJH2B.
PhylomeDBiQ8IXQ9.
TreeFamiTF314934.

Miscellaneous databases

GenomeRNAii254013.
PROiQ8IXQ9.
SOURCEiSearch...

Gene expression databases

BgeeiQ8IXQ9.
ExpressionAtlasiQ8IXQ9. baseline and differential.
GenevisibleiQ8IXQ9. HS.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR029063. SAM-dependent_MTases.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Cervix.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain and Testis.
  4. "Lysine methylation of VCP by a member of a novel human protein methyltransferase family."
    Kernstock S., Davydova E., Jakobsson M., Moen A., Pettersen S., Maelandsmo G.M., Egge-Jacobsen W., Falnes P.O.
    Nat. Commun. 3:1038-1038(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  5. "A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity."
    Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.
    PLoS Genet. 9:E1003210-E1003210(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HSPD1, SUBCELLULAR LOCATION.
  6. "Human METTL20 methylates lysine residues adjacent to the recognition loop of the electron transfer flavoprotein in mitochondria."
    Rhein V.F., Carroll J., He J., Ding S., Fearnley I.M., Walker J.E.
    J. Biol. Chem. 289:24640-24651(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
  7. "Human METTL20 is a mitochondrial lysine methyltransferase that targets the beta subunit of electron transfer flavoprotein (ETFbeta) and modulates its activity."
    Malecki J., Ho A.Y., Moen A., Dahl H.A., Falnes P.O.
    J. Biol. Chem. 290:423-434(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-121.

Entry informationi

Entry nameiETKMT_HUMAN
AccessioniPrimary (citable) accession number: Q8IXQ9
Secondary accession number(s): D3DUW3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: March 1, 2003
Last modified: June 8, 2016
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families
  4. Uncharacterized protein families (UPF)
    List of uncharacterized protein family (UPF) entries

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.