F86B2_HUMAN
ID F86B2_HUMAN Reviewed; 330 AA.
AC P0C5J1;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Putative protein N-methyltransferase FAM86B2 {ECO:0000305};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:P47163};
GN Name=FAM86B2;
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 GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [2]
RP INTERACTION WITH EEF2KMT.
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).
CC -!- SUBUNIT: Interacts with EEF2KMT. {ECO:0000269|PubMed:23349634}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. EEF2KMT family. {ECO:0000305}.
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DR EMBL; AC087203; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS59092.1; -.
DR RefSeq; NP_001131082.1; NM_001137610.1.
DR AlphaFoldDB; P0C5J1; -.
DR SMR; P0C5J1; -.
DR BioGRID; 575703; 17.
DR STRING; 9606.ENSP00000262365; -.
DR GlyGen; P0C5J1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P0C5J1; -.
DR PhosphoSitePlus; P0C5J1; -.
DR BioMuta; FAM86B2; -.
DR DMDM; 160010887; -.
DR jPOST; P0C5J1; -.
DR MassIVE; P0C5J1; -.
DR MaxQB; P0C5J1; -.
DR PaxDb; P0C5J1; -.
DR PeptideAtlas; P0C5J1; -.
DR PRIDE; P0C5J1; -.
DR ProteomicsDB; 52308; -.
DR TopDownProteomics; P0C5J1; -.
DR DNASU; 653333; -.
DR Ensembl; ENST00000262365.9; ENSP00000262365.4; ENSG00000145002.13.
DR GeneID; 653333; -.
DR KEGG; hsa:653333; -.
DR MANE-Select; ENST00000262365.9; ENSP00000262365.4; NM_001137610.3; NP_001131082.1.
DR UCSC; uc003wvt.5; human.
DR CTD; 653333; -.
DR GeneCards; FAM86B2; -.
DR HGNC; HGNC:32222; FAM86B2.
DR HPA; ENSG00000145002; Low tissue specificity.
DR MIM; 616123; gene.
DR neXtProt; NX_P0C5J1; -.
DR PharmGKB; PA142671860; -.
DR VEuPathDB; HostDB:ENSG00000145002; -.
DR eggNOG; KOG2497; Eukaryota.
DR GeneTree; ENSGT00510000047003; -.
DR HOGENOM; CLU_038942_0_0_1; -.
DR InParanoid; P0C5J1; -.
DR OMA; DESAQCH; -.
DR OrthoDB; 958308at2759; -.
DR PhylomeDB; P0C5J1; -.
DR TreeFam; TF326304; -.
DR PathwayCommons; P0C5J1; -.
DR SignaLink; P0C5J1; -.
DR BioGRID-ORCS; 653333; 46 hits in 985 CRISPR screens.
DR GenomeRNAi; 653333; -.
DR Pharos; P0C5J1; Tdark.
DR PRO; PR:P0C5J1; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P0C5J1; protein.
DR Bgee; ENSG00000145002; Expressed in right uterine tube and 93 other tissues.
DR ExpressionAtlas; P0C5J1; baseline and differential.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..330
FT /note="Putative protein N-methyltransferase FAM86B2"
FT /id="PRO_0000307639"
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 VARIANT 43
FT /note="D -> Y (in dbSNP:rs2684093)"
FT /id="VAR_036617"
FT VARIANT 285
FT /note="R -> S (in dbSNP:rs7817085)"
FT /id="VAR_036618"
SQ SEQUENCE 330 AA; 36771 MW; 666286D16B038099 CRC64;
MAPEENAGTE LLLQGFERRF LAVRTLRSFP WQSLEAKLRD SSDSELLRDI LQKTVRHPVC
VKHPPSVKYA WCFLSELIKK HEAVHTEPLD KLYEVLAETL MAKESTQGHR SYLLSSGGSV
TLSKSTAIIS HGTTGLVTWD AALYLAEWAI ENPAAFINRT VLELGSGAGL TGLAICKMCR
PRAYIFSDPH SRILEQLRGN VLLNGLSLEA DITGNLDSPR VTVAQLDWDV AMVHQLSAFQ
PDVVIAADVL YCPEAIVSLV GVLQRLAACR EHKRAPEVYV AFTVRNPETC QLFTTELGRD
GIRWEAEAHH DQKLFPYGEH LEMAMLNLTL
