EF2KT_MOUSE
ID EF2KT_MOUSE Reviewed; 335 AA.
AC Q3UZW7; Q3TQL2; Q80XE2; Q9CS89;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Protein-lysine N-methyltransferase EEF2KMT {ECO:0000305};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q96G04};
DE AltName: Full=eEF2-lysine methyltransferase;
DE Short=eEF2-KMT;
GN Name=Eef2kmt; Synonyms=Fam86, Fam86a;
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] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Pituitary;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Olfactory epithelium;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas, and Spleen;
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: Catalyzes the trimethylation of eukaryotic elongation factor
CC 2 (EEF2) on 'Lys-525'. {ECO:0000250|UniProtKB:Q96G04}.
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:Q96G04};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54193;
CC Evidence={ECO:0000250|UniProtKB:Q96G04};
CC -!- SUBUNIT: Interacts with FAM86B2 and FAM86C1P.
CC {ECO:0000250|UniProtKB:Q96G04}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96G04}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3UZW7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UZW7-2; Sequence=VSP_033329;
CC Name=3;
CC IsoId=Q3UZW7-3; Sequence=VSP_033330;
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. EEF2KMT family. {ECO:0000305}.
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DR EMBL; AK017533; BAB30795.3; -; mRNA.
DR EMBL; AK133590; BAE21738.1; -; mRNA.
DR EMBL; AK163493; BAE37370.1; -; mRNA.
DR EMBL; AC124576; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC051078; AAH51078.1; -; mRNA.
DR CCDS; CCDS27935.1; -. [Q3UZW7-1]
DR RefSeq; NP_081722.1; NM_027446.2. [Q3UZW7-1]
DR AlphaFoldDB; Q3UZW7; -.
DR SMR; Q3UZW7; -.
DR STRING; 10090.ENSMUSP00000068003; -.
DR PhosphoSitePlus; Q3UZW7; -.
DR EPD; Q3UZW7; -.
DR MaxQB; Q3UZW7; -.
DR PaxDb; Q3UZW7; -.
DR PRIDE; Q3UZW7; -.
DR ProteomicsDB; 277687; -. [Q3UZW7-1]
DR ProteomicsDB; 277688; -. [Q3UZW7-2]
DR ProteomicsDB; 277689; -. [Q3UZW7-3]
DR DNASU; 70511; -.
DR Ensembl; ENSMUST00000064635; ENSMUSP00000068003; ENSMUSG00000022544. [Q3UZW7-1]
DR GeneID; 70511; -.
DR KEGG; mmu:70511; -.
DR UCSC; uc007ybz.1; mouse. [Q3UZW7-1]
DR UCSC; uc007yca.1; mouse. [Q3UZW7-3]
DR CTD; 196483; -.
DR MGI; MGI:1917761; Eef2kmt.
DR VEuPathDB; HostDB:ENSMUSG00000022544; -.
DR eggNOG; KOG2497; Eukaryota.
DR GeneTree; ENSGT00510000047003; -.
DR HOGENOM; CLU_038942_0_0_1; -.
DR InParanoid; Q3UZW7; -.
DR OMA; TGFFHST; -.
DR OrthoDB; 958308at2759; -.
DR PhylomeDB; Q3UZW7; -.
DR TreeFam; TF326304; -.
DR Reactome; R-MMU-8876725; Protein methylation.
DR BioGRID-ORCS; 70511; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Eef2kmt; mouse.
DR PRO; PR:Q3UZW7; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q3UZW7; protein.
DR Bgee; ENSMUSG00000022544; Expressed in humerus cartilage element and 97 other tissues.
DR ExpressionAtlas; Q3UZW7; baseline and differential.
DR Genevisible; Q3UZW7; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0018023; P:peptidyl-lysine trimethylation; ISS:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR029426; FAM86_N.
DR InterPro; IPR019410; Methyltransf_16.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR14614; PTHR14614; 1.
DR Pfam; PF14904; FAM86; 1.
DR Pfam; PF10294; Methyltransf_16; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Methyltransferase;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..335
FT /note="Protein-lysine N-methyltransferase EEF2KMT"
FT /id="PRO_0000076219"
FT BINDING 139
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H867"
FT BINDING 165..167
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H867"
FT BINDING 228
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H867"
FT BINDING 247
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H867"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q96G04"
FT VAR_SEQ 1..100
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033329"
FT VAR_SEQ 297..335
FT /note="DRAGIYWEEVPPHTGKLFPYEEHSAIVILKLVLTSRHGV -> GQFPTCGPP
FT FCHEEGLKTGLTLR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033330"
FT CONFLICT 3
FT /note="P -> R (in Ref. 1; BAE37370)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 335 AA; 36940 MW; 8CEF3DF903359520 CRC64;
MAPEDHEGAT SLLQSFERRF LAARALPSFP WQSLEEKLKD PSGSELLLAI LQRTVKHPVC
VQHGPSVKYA RCFLSKLIKK HEAVPTEPLD ALYEALAEVL MTQESTQCHR SYLLPSGNSV
TLSESTAIVS HGTTGLVTWD AALYLAEWAI ENPAAFTDRT ILELGSGAGL TGLAICKACC
PRAYIFSDCH AQVLEQLRGN VLLNGFSLEP HTPIDAGSSK VTVAQLDWDE VTASQLSAFQ
ADVVIAADVL YCWEMTLSLV RVLKMLEDCQ RKSAPDVYVA YTIRSQDTGK LFIEELDRAG
IYWEEVPPHT GKLFPYEEHS AIVILKLVLT SRHGV
