ID   EF2KT_HUMAN             Reviewed;         330 AA.
AC   Q96G04; D3DUF0; Q96S85;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 2.
DT   17-JUN-2020, entry version 124.
DE   RecName: Full=Protein-lysine N-methyltransferase EEF2KMT {ECO:0000305};
DE            EC=2.1.1.- {ECO:0000269|PubMed:25231979};
DE   AltName: Full=eEF2-lysine methyltransferase;
DE            Short=eEF2-KMT;
GN   Name=EEF2KMT {ECO:0000312|HGNC:HGNC:32221};
GN   Synonyms=FAM86A {ECO:0000312|HGNC:HGNC:32221}; ORFNames=SB153;
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] (ISOFORM 2).
RA   Li N., Zhang M., Wan T., Zhang W., Cao X.;
RL   Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASP-272.
RA   Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASP-272.
RC   TISSUE=Lung;
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   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [5]
RP   INTERACTION WITH FAM86B2 AND FAM86C1, AND SUBCELLULAR LOCATION.
RX   PubMed=23349634; DOI=10.1371/journal.pgen.1003210;
RA   Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.;
RT   "A newly uncovered group of distantly related lysine methyltransferases
RT   preferentially interact with molecular chaperones to regulate their
RT   activity.";
RL   PLoS Genet. 9:E1003210-E1003210(2013).
RN   [6]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=25231979; DOI=10.1074/jbc.m114.601658;
RA   Davydova E., Ho A.Y., Malecki J., Moen A., Enserink J.M., Jakobsson M.E.,
RA   Loenarz C., Falnes P.O.;
RT   "Identification and characterization of a novel evolutionarily conserved
RT   lysine-specific methyltransferase targeting eukaryotic translation
RT   elongation factor 2 (eEF2).";
RL   J. Biol. Chem. 289:30499-30510(2014).
CC   -!- FUNCTION: Catalyzes the trimethylation of eukaryotic elongation factor
CC       2 (EEF2) on 'Lys-525'. {ECO:0000269|PubMed:25231979}.
CC   -!- SUBUNIT: Interacts with FAM86B2 and FAM86C1.
CC       {ECO:0000269|PubMed:23349634}.
CC   -!- INTERACTION:
CC       Q96G04; P00492: HPRT1; NbExp=3; IntAct=EBI-747840, EBI-748210;
CC       Q96G04; Q13099: IFT88; NbExp=3; IntAct=EBI-747840, EBI-347427;
CC       Q96G04; Q86T90: KIAA1328; NbExp=3; IntAct=EBI-747840, EBI-3437878;
CC       Q96G04; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-747840, EBI-739832;
CC       Q96G04; P51843: NR0B1; NbExp=3; IntAct=EBI-747840, EBI-946109;
CC       Q96G04; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-747840, EBI-79165;
CC       Q96G04; P31321: PRKAR1B; NbExp=3; IntAct=EBI-747840, EBI-2805516;
CC       Q96G04; Q9NRG1: PRTFDC1; NbExp=8; IntAct=EBI-747840, EBI-739759;
CC       Q96G04; Q15645: TRIP13; NbExp=3; IntAct=EBI-747840, EBI-358993;
CC       Q96G04; O14771: ZNF213; NbExp=3; IntAct=EBI-747840, EBI-12838388;
CC       Q96G04; P13682: ZNF35; NbExp=3; IntAct=EBI-747840, EBI-11041653;
CC       Q96G04; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-747840, EBI-4395669;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23349634}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q96G04-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96G04-2; Sequence=VSP_017097;
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. EEF2KMT family. {ECO:0000305}.
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DR   EMBL; AY037162; AAK67640.1; -; mRNA.
DR   EMBL; CH471112; EAW85235.1; -; Genomic_DNA.
DR   EMBL; CH471112; EAW85236.1; -; Genomic_DNA.
DR   EMBL; BC010084; AAH10084.1; -; mRNA.
DR   CCDS; CCDS10529.1; -. [Q96G04-1]
DR   CCDS; CCDS10530.1; -. [Q96G04-2]
DR   RefSeq; NP_001275958.1; NM_001289029.1.
DR   RefSeq; NP_958802.1; NM_201400.3. [Q96G04-1]
DR   RefSeq; NP_963892.1; NM_201598.3. [Q96G04-2]
DR   BioGRID; 128213; 14.
DR   IntAct; Q96G04; 16.
DR   STRING; 9606.ENSP00000398502; -.
DR   iPTMnet; Q96G04; -.
DR   PhosphoSitePlus; Q96G04; -.
DR   BioMuta; EEF2KMT; -.
DR   DMDM; 85700958; -.
DR   jPOST; Q96G04; -.
DR   MassIVE; Q96G04; -.
DR   MaxQB; Q96G04; -.
DR   PaxDb; Q96G04; -.
DR   PeptideAtlas; Q96G04; -.
DR   PRIDE; Q96G04; -.
DR   ProteomicsDB; 76581; -. [Q96G04-1]
DR   ProteomicsDB; 76582; -. [Q96G04-2]
DR   Antibodypedia; 55831; 56 antibodies.
DR   DNASU; 196483; -.
DR   Ensembl; ENST00000427587; ENSP00000398502; ENSG00000118894. [Q96G04-1]
DR   Ensembl; ENST00000458008; ENSP00000389710; ENSG00000118894. [Q96G04-2]
DR   GeneID; 196483; -.
DR   KEGG; hsa:196483; -.
DR   UCSC; uc002cyo.4; human. [Q96G04-1]
DR   CTD; 196483; -.
DR   DisGeNET; 196483; -.
DR   EuPathDB; HostDB:ENSG00000118894.14; -.
DR   GeneCards; EEF2KMT; -.
DR   HGNC; HGNC:32221; EEF2KMT.
DR   HPA; ENSG00000118894; Low tissue specificity.
DR   MIM; 615263; gene.
DR   neXtProt; NX_Q96G04; -.
DR   OpenTargets; ENSG00000118894; -.
DR   PharmGKB; PA142671858; -.
DR   eggNOG; KOG2497; Eukaryota.
DR   eggNOG; ENOG410ZQK4; LUCA.
DR   GeneTree; ENSGT00510000047003; -.
DR   HOGENOM; CLU_038942_0_0_1; -.
DR   InParanoid; Q96G04; -.
DR   KO; K22696; -.
DR   OMA; FCHQYLQ; -.
DR   OrthoDB; 958308at2759; -.
DR   PhylomeDB; Q96G04; -.
DR   TreeFam; TF326304; -.
DR   Reactome; R-HSA-8876725; Protein methylation.
DR   BioGRID-ORCS; 196483; 423 hits in 781 CRISPR screens.
DR   ChiTaRS; EEF2KMT; human.
DR   GenomeRNAi; 196483; -.
DR   Pharos; Q96G04; Tdark.
DR   PRO; PR:Q96G04; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; Q96G04; protein.
DR   Bgee; ENSG00000118894; Expressed in testis and 123 other tissues.
DR   ExpressionAtlas; Q96G04; baseline and differential.
DR   Genevisible; Q96G04; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0018023; P:peptidyl-lysine trimethylation; IDA:UniProtKB.
DR   GO; GO:0006479; P:protein methylation; TAS:Reactome.
DR   InterPro; IPR029426; FAM86.
DR   InterPro; IPR019410; Methyltransf_16.
DR   InterPro; IPR029063; SAM-dependent_MTases.
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   Polymorphism; Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..330
FT                   /note="Protein-lysine N-methyltransferase EEF2KMT"
FT                   /id="PRO_0000076218"
FT   REGION          165..167
FT                   /note="S-adenosyl-L-methionine binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H867"
FT   BINDING         139
FT                   /note="S-adenosyl-L-methionine; via amide nitrogen"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H867"
FT   BINDING         228
FT                   /note="S-adenosyl-L-methionine; via amide nitrogen"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H867"
FT   BINDING         247
FT                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H867"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000244|PubMed:22814378"
FT   VAR_SEQ         81..114
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_017097"
FT   VARIANT         123
FT                   /note="S -> C (in dbSNP:rs9673733)"
FT                   /id="VAR_033854"
FT   VARIANT         230
FT                   /note="V -> I (in dbSNP:rs148557961)"
FT                   /id="VAR_067704"
FT   VARIANT         270
FT                   /note="R -> W (in dbSNP:rs3204207)"
FT                   /id="VAR_060160"
FT   VARIANT         272
FT                   /note="H -> D (in dbSNP:rs12928528)"
FT                   /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2"
FT                   /id="VAR_067705"
FT   VARIANT         329
FT                   /note="T -> I (in dbSNP:rs760584474)"
FT                   /id="VAR_067706"
SQ   SEQUENCE   330 AA;  36915 MW;  1C1B37B9F6D2EE52 CRC64;
     MAPEENAGTE LLLQSFERRF LAARTLRSFP WQSLEAKLRD SSDSELLRDI LHKTVKHPVC
     VKHPPSVKYA RCFLSELIKK HEAVHTEPLD ELYEALAETL MAKESTQGHR SYLLPSGGSV
     TLSESTAIIS YGTTGLVTWD AALYLAEWAI ENPAVFTNRT VLELGSGAGL TGLAICKMCR
     PRAYIFSDCH SRVLEQLRGN VLLNGLSLEA DITAKLDSPR VTVAQLDWDV ATVHQLSAFQ
     PDVVIAADVL YCPEAIMSLV GVLRRLAACR EHQRAPEVYV AFTVRNPETC QLFTTELGRA
     GIRWEVEPRH EQKLFPYEEH LEMAMLNLTL
//