EFMT1_HUMAN
ID EFMT1_HUMAN Reviewed; 214 AA.
AC Q8WVE0; B5G4V1;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=EEF1A lysine methyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_03187, ECO:0000312|HGNC:HGNC:27351};
DE EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_03187, ECO:0000269|PubMed:26545399, ECO:0000269|PubMed:28663172};
DE AltName: Full=N(6)-adenine-specific DNA methyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_03187};
DE AltName: Full=Protein-lysine N-methyltransferase N6AMT2 {ECO:0000255|HAMAP-Rule:MF_03187};
DE AltName: Full=eEF1A-KMT {ECO:0000303|PubMed:26545399};
GN Name=EEF1AKMT1 {ECO:0000255|HAMAP-Rule:MF_03187,
GN ECO:0000312|HGNC:HGNC:27351};
GN Synonyms=N6AMT2 {ECO:0000255|HAMAP-Rule:MF_03187};
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=Epididymis;
RX PubMed=18390568; DOI=10.1093/dnares/dsn005;
RA Li J.Y., Wang H.Y., Liu J., Liu Q., Zhang J.S., Wan F.C., Liu F.J.,
RA Jin S.H., Zhang Y.L.;
RT "Transcriptome analysis of a cDNA library from adult human epididymis.";
RL DNA Res. 15:115-122(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [3]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [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=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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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, AND CATALYTIC ACTIVITY.
RX PubMed=26545399; DOI=10.1074/mcp.m115.052449;
RA Hamey J.J., Winter D.L., Yagoub D., Overall C.M., Hart-Smith G.,
RA Wilkins M.R.;
RT "Novel N-terminal and lysine methyltransferases that target translation
RT elongation factor 1A in yeast and human.";
RL Mol. Cell. Proteomics 15:164-176(2016).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=28663172; DOI=10.1074/mcp.m116.066308;
RA Hamey J.J., Wienert B., Quinlan K.G.R., Wilkins M.R.;
RT "METTL21B Is a Novel Human Lysine Methyltransferase of Translation
RT Elongation Factor 1A: Discovery by CRISPR/Cas9 Knockout.";
RL Mol. Cell. Proteomics 16:2229-2242(2017).
CC -!- FUNCTION: Protein N-lysine methyltransferase that selectively catalyzes
CC the trimethylation of EEF1A at 'Lys-79'. {ECO:0000255|HAMAP-
CC Rule:MF_03187, ECO:0000269|PubMed:26545399,
CC ECO:0000269|PubMed:28663172}.
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:26545399, ECO:0000269|PubMed:28663172};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54193;
CC Evidence={ECO:0000305|PubMed:26545399};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03187}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. EFM5 family. {ECO:0000255|HAMAP-Rule:MF_03187}.
CC -!- CAUTION: Was originally thought to be an N(6)-adenine-specific DNA
CC methyltransferase based on primary sequence and predicted secondary
CC structure. {ECO:0000255|HAMAP-Rule:MF_03187}.
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DR EMBL; DQ823637; ABK41021.1; -; mRNA.
DR EMBL; AL512652; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471075; EAX08277.1; -; Genomic_DNA.
DR EMBL; BC018091; AAH18091.1; -; mRNA.
DR CCDS; CCDS9293.1; -.
DR RefSeq; NP_001305868.1; NM_001318939.1.
DR RefSeq; NP_777588.1; NM_174928.2.
DR RefSeq; XP_016875921.1; XM_017020432.1.
DR AlphaFoldDB; Q8WVE0; -.
DR SMR; Q8WVE0; -.
DR BioGRID; 128690; 10.
DR IntAct; Q8WVE0; 6.
DR STRING; 9606.ENSP00000372206; -.
DR iPTMnet; Q8WVE0; -.
DR PhosphoSitePlus; Q8WVE0; -.
DR BioMuta; EEF1AKMT1; -.
DR DMDM; 74751547; -.
DR EPD; Q8WVE0; -.
DR jPOST; Q8WVE0; -.
DR MassIVE; Q8WVE0; -.
DR MaxQB; Q8WVE0; -.
DR PaxDb; Q8WVE0; -.
DR PeptideAtlas; Q8WVE0; -.
DR PRIDE; Q8WVE0; -.
DR ProteomicsDB; 74781; -.
DR Antibodypedia; 22330; 92 antibodies from 16 providers.
DR DNASU; 221143; -.
DR Ensembl; ENST00000382754.4; ENSP00000372202.4; ENSG00000150456.11.
DR Ensembl; ENST00000382758.6; ENSP00000372206.1; ENSG00000150456.11.
DR GeneID; 221143; -.
DR KEGG; hsa:221143; -.
DR MANE-Select; ENST00000382758.6; ENSP00000372206.1; NM_001318939.2; NP_001305868.1.
DR UCSC; uc001uno.2; human.
DR CTD; 221143; -.
DR DisGeNET; 221143; -.
DR GeneCards; EEF1AKMT1; -.
DR HGNC; HGNC:27351; EEF1AKMT1.
DR HPA; ENSG00000150456; Low tissue specificity.
DR MIM; 617793; gene.
DR neXtProt; NX_Q8WVE0; -.
DR OpenTargets; ENSG00000150456; -.
DR PharmGKB; PA162396671; -.
DR VEuPathDB; HostDB:ENSG00000150456; -.
DR eggNOG; KOG3350; Eukaryota.
DR GeneTree; ENSGT00390000016366; -.
DR HOGENOM; CLU_074410_2_1_1; -.
DR InParanoid; Q8WVE0; -.
DR OMA; HKCNFRP; -.
DR OrthoDB; 1272987at2759; -.
DR PhylomeDB; Q8WVE0; -.
DR TreeFam; TF106153; -.
DR BRENDA; 2.1.1.244; 2681.
DR PathwayCommons; Q8WVE0; -.
DR Reactome; R-HSA-8876725; Protein methylation.
DR SignaLink; Q8WVE0; -.
DR BioGRID-ORCS; 221143; 14 hits in 1068 CRISPR screens.
DR GenomeRNAi; 221143; -.
DR Pharos; Q8WVE0; Tdark.
DR PRO; PR:Q8WVE0; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q8WVE0; protein.
DR Bgee; ENSG00000150456; Expressed in cardiac muscle of right atrium and 180 other tissues.
DR ExpressionAtlas; Q8WVE0; baseline and differential.
DR Genevisible; Q8WVE0; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0008168; F:methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0018022; P:peptidyl-lysine methylation; IDA:UniProtKB.
DR GO; GO:0006479; P:protein methylation; TAS:Reactome.
DR HAMAP; MF_03187; Methyltr_EFM5; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR019369; Efm5/EEF1AKMT1.
DR InterPro; IPR041370; Mlase_EEF1AKMT1/ZCCHC4.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR13200; PTHR13200; 1.
DR Pfam; PF10237; N6-adenineMlase; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Methyltransferase; Phosphoprotein;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..214
FT /note="EEF1A lysine methyltransferase 1"
FT /id="PRO_0000311294"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 193
FT /note="T -> N (in dbSNP:rs11549810)"
FT /id="VAR_037216"
SQ SEQUENCE 214 AA; 24506 MW; 6E16B4052B696552 CRC64;
MSDLEDDETP QLSAHALAAL QEFYAEQKQQ IEPGEDDKYN IGIIEENWQL SQFWYSQETA
LQLAQEAIAA VGEGGRIACV SAPSVYQKLR ELCRENFSIY IFEYDKRFAM YGEEFIFYDY
NNPLDLPERI AAHSFDIVIA DPPYLSEECL RKTSETVKYL TRGKILLCTG AIMEEQAAEL
LGVKMCTFVP RHTRNLANEF RCYVNYDSGL DCGI
