EFMT2_MOUSE
ID EFMT2_MOUSE Reviewed; 244 AA.
AC Q9D853; Q4V9Y9;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=EEF1A lysine methyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_03188};
DE EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_03188};
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 Synonyms=Mettl10 {ECO:0000255|HAMAP-Rule:MF_03188,
GN ECO:0000312|MGI:MGI:1919346};
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=Small intestine;
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=Embryo;
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, Kidney, 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-318'. {ECO:0000255|HAMAP-
CC Rule:MF_03188}.
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:Q5JPI9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54193;
CC Evidence={ECO:0000250|UniProtKB:Q5JPI9};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03188}.
CC Nucleus {ECO:0000255|HAMAP-Rule:MF_03188}.
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; AK008476; BAB25689.1; -; mRNA.
DR EMBL; BC096622; AAH96622.1; -; mRNA.
DR EMBL; BC116375; AAI16376.1; -; mRNA.
DR CCDS; CCDS21927.1; -.
DR RefSeq; NP_082371.1; NM_028095.1.
DR AlphaFoldDB; Q9D853; -.
DR SMR; Q9D853; -.
DR BioGRID; 215149; 5.
DR STRING; 10090.ENSMUSP00000033257; -.
DR iPTMnet; Q9D853; -.
DR PhosphoSitePlus; Q9D853; -.
DR EPD; Q9D853; -.
DR MaxQB; Q9D853; -.
DR PaxDb; Q9D853; -.
DR PeptideAtlas; Q9D853; -.
DR PRIDE; Q9D853; -.
DR ProteomicsDB; 277765; -.
DR DNASU; 72096; -.
DR Ensembl; ENSMUST00000033257; ENSMUSP00000033257; ENSMUSG00000030960.
DR GeneID; 72096; -.
DR KEGG; mmu:72096; -.
DR UCSC; uc009kcm.1; mouse.
DR CTD; 399818; -.
DR MGI; MGI:1919346; Eef1akmt2.
DR VEuPathDB; HostDB:ENSMUSG00000030960; -.
DR eggNOG; KOG1271; Eukaryota.
DR GeneTree; ENSGT00390000013399; -.
DR HOGENOM; CLU_044783_2_1_1; -.
DR InParanoid; Q9D853; -.
DR OMA; LGTKQYW; -.
DR OrthoDB; 1422013at2759; -.
DR PhylomeDB; Q9D853; -.
DR TreeFam; TF313057; -.
DR Reactome; R-MMU-8876725; Protein methylation.
DR BioGRID-ORCS; 72096; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Eef1akmt2; mouse.
DR PRO; PR:Q9D853; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9D853; protein.
DR Bgee; ENSMUSG00000030960; Expressed in manus and 230 other tissues.
DR ExpressionAtlas; Q9D853; baseline and differential.
DR Genevisible; Q9D853; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0008168; F:methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0018027; P:peptidyl-lysine dimethylation; IBA:GO_Central.
DR GO; GO:0018022; P:peptidyl-lysine methylation; ISS:UniProtKB.
DR GO; GO:0018026; P:peptidyl-lysine monomethylation; IBA:GO_Central.
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 Cytoplasm; Methyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..244
FT /note="EEF1A lysine methyltransferase 2"
FT /id="PRO_0000325883"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JPI9"
FT CONFLICT 104
FT /note="N -> D (in Ref. 2; AAH96622)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 244 AA; 26864 MW; C2A0DEBEBDBDABED CRC64;
MNADAEGHSG AVVPAQSPEG SSAADDFVPS ALGTREHWDA VYERELRTFQ EYGDTGEIWF
GEESMNRLIR WMQKHKIPLD ASVLDIGTGN GVFLVELVKH GFSNITGIDY SPSAIKLSAS
ILEKEGLSNI NLKVEDFLNP STKLSGFHVC VDKGTYDAIS LNPDNAIEKR KQYVMSLSRV
LEVKGFFLIT SCNWTKAELL DAFSEGFELF EELPTPKFSF GGRSGNTVAA LVFQKRGTSL
DKIS
