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   07-APR-2021, entry version 152.
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};
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};
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.
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).
CC   -!- FUNCTION: Protein-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   -!- 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   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; 85 antibodies.
DR   DNASU; 221143; -.
DR   Ensembl; ENST00000382754; ENSP00000372202; ENSG00000150456.
DR   Ensembl; ENST00000382758; ENSP00000372206; ENSG00000150456.
DR   GeneID; 221143; -.
DR   KEGG; hsa:221143; -.
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:ENSG00000150456.10; -.
DR   eggNOG; KOG3350; Eukaryota.
DR   GeneTree; ENSGT00390000016366; -.
DR   HOGENOM; CLU_074410_2_1_1; -.
DR   InParanoid; Q8WVE0; -.
DR   OMA; EFVSYAN; -.
DR   OrthoDB; 1272987at2759; -.
DR   PhylomeDB; Q8WVE0; -.
DR   TreeFam; TF106153; -.
DR   PathwayCommons; Q8WVE0; -.
DR   Reactome; R-HSA-8876725; Protein methylation.
DR   BioGRID-ORCS; 221143; 11 hits in 993 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 quadriceps femoris and 213 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.
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
//