EFMT2_HUMAN
ID EFMT2_HUMAN Reviewed; 291 AA.
AC Q5JPI9; A8MPY7;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=EEF1A lysine methyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_03188, ECO:0000312|HGNC:HGNC:33787};
DE EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_03188, ECO:0000269|PubMed:25144183};
DE AltName: Full=Methyltransferase-like protein 10 {ECO:0000255|HAMAP-Rule:MF_03188};
DE AltName: Full=Protein-lysine N-methyltransferase METTL10 {ECO:0000255|HAMAP-Rule:MF_03188};
GN Name=EEF1AKMT2 {ECO:0000255|HAMAP-Rule:MF_03188,
GN ECO:0000312|HGNC:HGNC:33787};
GN Synonyms=C10orf138, METTL10 {ECO:0000255|HAMAP-Rule:MF_03188};
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=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 85-ASP--GLY-91, AND
RP CATALYTIC ACTIVITY.
RX PubMed=25144183; DOI=10.1371/journal.pone.0105394;
RA Shimazu T., Barjau J., Sohtome Y., Sodeoka M., Shinkai Y.;
RT "Selenium-based S-adenosylmethionine analog reveals the mammalian seven-
RT beta-strand methyltransferase METTL10 to be an EF1A1 lysine
RT methyltransferase.";
RL PLoS ONE 9:E105394-E105394(2014).
CC -!- FUNCTION: Protein-lysine methyltransferase that selectively catalyzes
CC the trimethylation of EEF1A at 'Lys-318'. {ECO:0000255|HAMAP-
CC Rule:MF_03188, ECO:0000269|PubMed:25144183}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:54192, Rhea:RHEA-COMP:9752, Rhea:RHEA-
CC COMP:13826, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961;
CC Evidence={ECO:0000269|PubMed:25144183};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54193;
CC Evidence={ECO:0000305|PubMed:25144183};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03188,
CC ECO:0000269|PubMed:25144183}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03188,
CC ECO:0000269|PubMed:25144183}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. EFM4 family. {ECO:0000255|HAMAP-Rule:MF_03188}.
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DR EMBL; AL832292; CAI46179.1; -; mRNA.
DR EMBL; AC068896; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS31307.1; -.
DR RefSeq; NP_001291396.1; NM_001304467.1.
DR RefSeq; NP_997719.2; NM_212554.3.
DR AlphaFoldDB; Q5JPI9; -.
DR SMR; Q5JPI9; -.
DR BioGRID; 134421; 32.
DR STRING; 9606.ENSP00000357829; -.
DR iPTMnet; Q5JPI9; -.
DR PhosphoSitePlus; Q5JPI9; -.
DR BioMuta; EEF1AKMT2; -.
DR DMDM; 172044620; -.
DR EPD; Q5JPI9; -.
DR jPOST; Q5JPI9; -.
DR MassIVE; Q5JPI9; -.
DR MaxQB; Q5JPI9; -.
DR PaxDb; Q5JPI9; -.
DR PeptideAtlas; Q5JPI9; -.
DR PRIDE; Q5JPI9; -.
DR ProteomicsDB; 63019; -.
DR Antibodypedia; 32382; 112 antibodies from 20 providers.
DR DNASU; 399818; -.
DR Ensembl; ENST00000368836.7; ENSP00000357829.2; ENSG00000203791.15.
DR GeneID; 399818; -.
DR KEGG; hsa:399818; -.
DR MANE-Select; ENST00000368836.7; ENSP00000357829.2; NM_212554.4; NP_997719.2.
DR UCSC; uc001lhy.2; human.
DR CTD; 399818; -.
DR DisGeNET; 399818; -.
DR GeneCards; EEF1AKMT2; -.
DR HGNC; HGNC:33787; EEF1AKMT2.
DR HPA; ENSG00000203791; Low tissue specificity.
DR MIM; 617794; gene.
DR neXtProt; NX_Q5JPI9; -.
DR OpenTargets; ENSG00000203791; -.
DR PharmGKB; PA162395769; -.
DR VEuPathDB; HostDB:ENSG00000203791; -.
DR eggNOG; KOG1271; Eukaryota.
DR GeneTree; ENSGT00390000013399; -.
DR HOGENOM; CLU_044783_2_0_1; -.
DR InParanoid; Q5JPI9; -.
DR OrthoDB; 1422013at2759; -.
DR PhylomeDB; Q5JPI9; -.
DR TreeFam; TF313057; -.
DR PathwayCommons; Q5JPI9; -.
DR Reactome; R-HSA-8876725; Protein methylation.
DR BioGRID-ORCS; 399818; 25 hits in 1042 CRISPR screens.
DR GenomeRNAi; 399818; -.
DR Pharos; Q5JPI9; Tbio.
DR PRO; PR:Q5JPI9; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q5JPI9; protein.
DR Bgee; ENSG00000203791; Expressed in ventricular zone and 169 other tissues.
DR ExpressionAtlas; Q5JPI9; baseline and differential.
DR Genevisible; Q5JPI9; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0008168; F:methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0018027; P:peptidyl-lysine dimethylation; IBA:GO_Central.
DR GO; GO:0018022; P:peptidyl-lysine methylation; IDA:UniProtKB.
DR GO; GO:0018026; P:peptidyl-lysine monomethylation; IBA:GO_Central.
DR GO; GO:0006479; P:protein methylation; TAS:Reactome.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_03188; Methyltr_EFM4; 1.
DR InterPro; IPR026635; Efm4/METTL10.
DR InterPro; IPR025714; Methyltranfer_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF13847; Methyltransf_31; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Methyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..291
FT /note="EEF1A lysine methyltransferase 2"
FT /id="PRO_0000325882"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 67
FT /note="R -> Q (in dbSNP:rs4347339)"
FT /id="VAR_050295"
FT MUTAGEN 85..91
FT /note="DIGTGNG->AIATANA: Highly reduces methylation
FT activity toward EEF1A1."
FT /evidence="ECO:0000269|PubMed:25144183"
FT CONFLICT 8
FT /note="G -> S (in Ref. 1; CAI46179)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="L -> LL (in Ref. 1; CAI46179)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 291 AA; 31830 MW; E7A4486A4D1CCA50 CRC64;
MSSGADGGGG AAVAARSDKG SPGEDGFVPS ALGTREHWDA VYERELQTFR EYGDTGEIWF
GEESMNRLIR WMQKHKIPLD ASVLDIGTGN GVFLVELAKF GFSNITGIDY SPSAIQLSGS
IIEKEGLSNI KLKVEDFLNL STQLSGFHIC IDKGTFDAIS LNPDNAIEKR KQYVKSLSRV
LKVKGFFLIT SCNWTKEELL NEFSEGWSTV AGFWLTAALT SWAQAIFSTS ASRVGGTTGT
HHHAWIIFVF LAETRFCHVV QAGLELLGSS DSPTWPPKVL GLYHARPSLA F
