EFMT1_MOUSE
ID EFMT1_MOUSE Reviewed; 214 AA.
AC Q9CY45; Q9CQR0;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=EEF1A lysine methyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_03187, ECO:0000312|MGI:MGI:1915293};
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|MGI:MGI:1915293};
GN Synonyms=N6amt2 {ECO:0000255|HAMAP-Rule:MF_03187};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Protein-lysine methyltransferase that selectively catalyzes
CC the trimethylation of EEF1A at 'Lys-79'. {ECO:0000255|HAMAP-
CC Rule:MF_03187}.
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:0000250|UniProtKB:Q8WVE0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54193;
CC Evidence={ECO:0000250|UniProtKB:Q8WVE0};
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH51925.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB23947.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB28017.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK005312; BAB23947.1; ALT_INIT; mRNA.
DR EMBL; AK010911; BAB27262.1; -; mRNA.
DR EMBL; AK012083; BAB28017.1; ALT_INIT; mRNA.
DR EMBL; BC051925; AAH51925.1; ALT_INIT; mRNA.
DR CCDS; CCDS27157.2; -.
DR RefSeq; NP_080802.1; NM_026526.2.
DR RefSeq; XP_006519546.1; XM_006519483.3.
DR AlphaFoldDB; Q9CY45; -.
DR STRING; 10090.ENSMUSP00000022518; -.
DR iPTMnet; Q9CY45; -.
DR PhosphoSitePlus; Q9CY45; -.
DR EPD; Q9CY45; -.
DR jPOST; Q9CY45; -.
DR MaxQB; Q9CY45; -.
DR PaxDb; Q9CY45; -.
DR PeptideAtlas; Q9CY45; -.
DR PRIDE; Q9CY45; -.
DR ProteomicsDB; 275442; -.
DR Antibodypedia; 22330; 92 antibodies from 16 providers.
DR DNASU; 68043; -.
DR Ensembl; ENSMUST00000239099; ENSMUSP00000159159; ENSMUSG00000021951.
DR GeneID; 68043; -.
DR KEGG; mmu:68043; -.
DR UCSC; uc007udd.1; mouse.
DR CTD; 221143; -.
DR MGI; MGI:1915293; Eef1akmt1.
DR VEuPathDB; HostDB:ENSMUSG00000021951; -.
DR eggNOG; KOG3350; Eukaryota.
DR GeneTree; ENSGT00390000016366; -.
DR InParanoid; Q9CY45; -.
DR OrthoDB; 1272987at2759; -.
DR PhylomeDB; Q9CY45; -.
DR TreeFam; TF106153; -.
DR Reactome; R-MMU-8876725; Protein methylation.
DR BioGRID-ORCS; 68043; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Eef1akmt1; mouse.
DR PRO; PR:Q9CY45; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9CY45; protein.
DR Bgee; ENSMUSG00000021951; Expressed in facial nucleus and 259 other tissues.
DR ExpressionAtlas; Q9CY45; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008168; F:methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0018022; P:peptidyl-lysine methylation; ISS:UniProtKB.
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:0000250|UniProtKB:Q8WVE0"
FT CHAIN 2..214
FT /note="EEF1A lysine methyltransferase 1"
FT /id="PRO_0000311295"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVE0"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVE0"
SQ SEQUENCE 214 AA; 24499 MW; E658B75D9B8FF2C5 CRC64;
MSESEDDDIP QLSSHTLAAL QEFYAEQKQS VNPRGDDKYN VGVIEENWQL SQFWYSQDTA
LRLAREAIDA AGEGGRIACV SAPSVYQKLR ELCREDSSVY IFEYDRRFAI YGDEFIFYDY
NHPLELPERI AAHSFDLVVA DPPYLSEECL RKTSETIQFL TRGKILLCTG AIMEEQAAQL
LGVKMCKFIP EHSRNLANEF RCYTNYDSGL DCEA
