ANKMT_HUMAN
ID ANKMT_HUMAN Reviewed; 235 AA.
AC Q9BQD7; A2IDD4;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Adenine nucleotide translocase lysine N-methyltransferase {ECO:0000303|PubMed:31213526};
DE Short=ANT-KMT {ECO:0000303|PubMed:31213526};
DE EC=2.1.1.- {ECO:0000269|PubMed:31213526};
GN Name=ANTKMT {ECO:0000303|PubMed:31213526, ECO:0000312|HGNC:HGNC:14152};
GN Synonyms=C16orf24 {ECO:0000312|HGNC:HGNC:14152},
GN FAM173A {ECO:0000303|PubMed:31213526, ECO:0000312|HGNC:HGNC:14152};
GN ORFNames=RJD7 {ECO:0000303|PubMed:11157797};
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=11157797; DOI=10.1093/hmg/10.4.339;
RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C.,
RA Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.;
RT "Sequence, structure and pathology of the fully annotated terminal 2 Mb of
RT the short arm of human chromosome 16.";
RL Hum. Mol. Genet. 10:339-352(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, and Uterus;
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS
RP OF 1-MET--LEU-42; 1-MET--PRO-76 AND GLU-105.
RX PubMed=31213526; DOI=10.1074/jbc.ra119.009045;
RA Malecki J., Willemen H.L.D.M., Pinto R., Ho A.Y.Y., Moen A., Eijkelkamp N.,
RA Falnes P.O.;
RT "Human FAM173A is a mitochondrial lysine-specific methyltransferase that
RT targets adenine nucleotide translocase and affects mitochondrial
RT respiration.";
RL J. Biol. Chem. 294:11654-11664(2019).
CC -!- FUNCTION: Mitochondrial protein-lysine N-methyltransferase that
CC trimethylates adenine nucleotide translocases ANT2/SLC25A5 and
CC ANT3/SLC25A6, thereby regulating mitochondrial respiration
CC (PubMed:31213526). Probably also trimethylates ANT1/SLC25A4
CC (PubMed:31213526). {ECO:0000269|PubMed:31213526}.
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:0000269|PubMed:31213526};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54193;
CC Evidence={ECO:0000269|PubMed:31213526};
CC -!- INTERACTION:
CC Q9BQD7; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-713602, EBI-11524452;
CC Q9BQD7; Q9NX04: C1orf109; NbExp=3; IntAct=EBI-713602, EBI-8643161;
CC Q9BQD7; Q8N4L8: CCDC24; NbExp=3; IntAct=EBI-713602, EBI-1104933;
CC Q9BQD7; Q9UI47-2: CTNNA3; NbExp=3; IntAct=EBI-713602, EBI-11962928;
CC Q9BQD7; Q86UW9: DTX2; NbExp=3; IntAct=EBI-713602, EBI-740376;
CC Q9BQD7; Q5VUJ9-2: EFCAB2; NbExp=3; IntAct=EBI-713602, EBI-13317131;
CC Q9BQD7; Q9NW38: FANCL; NbExp=3; IntAct=EBI-713602, EBI-2339898;
CC Q9BQD7; Q8WUI4-6: HDAC7; NbExp=3; IntAct=EBI-713602, EBI-12094670;
CC Q9BQD7; O14964: HGS; NbExp=3; IntAct=EBI-713602, EBI-740220;
CC Q9BQD7; O14770-4: MEIS2; NbExp=3; IntAct=EBI-713602, EBI-8025850;
CC Q9BQD7; Q13064: MKRN3; NbExp=3; IntAct=EBI-713602, EBI-2340269;
CC Q9BQD7; Q9HBI0: PARVG; NbExp=3; IntAct=EBI-713602, EBI-3921217;
CC Q9BQD7; Q92569: PIK3R3; NbExp=3; IntAct=EBI-713602, EBI-79893;
CC Q9BQD7; Q96I34: PPP1R16A; NbExp=3; IntAct=EBI-713602, EBI-710402;
CC Q9BQD7; P36508: ZNF76; NbExp=3; IntAct=EBI-713602, EBI-7254550;
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000269|PubMed:31213526}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: The pre-methyltransferase (preMT) region is responsible for
CC mitochondrial localization. {ECO:0000269|PubMed:31213526}.
CC -!- SIMILARITY: Belongs to the ANT/ATPSC lysine N-methyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AE006464; AAK61248.1; -; Genomic_DNA.
DR EMBL; Z98258; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471112; EAW85746.1; -; Genomic_DNA.
DR EMBL; BC001181; AAH01181.1; -; mRNA.
DR EMBL; BC002624; AAH02624.1; -; mRNA.
DR CCDS; CCDS10423.1; -.
DR RefSeq; NP_076422.1; NM_023933.2.
DR AlphaFoldDB; Q9BQD7; -.
DR SMR; Q9BQD7; -.
DR BioGRID; 122439; 24.
DR IntAct; Q9BQD7; 24.
DR STRING; 9606.ENSP00000454380; -.
DR iPTMnet; Q9BQD7; -.
DR PhosphoSitePlus; Q9BQD7; -.
DR BioMuta; FAM173A; -.
DR DMDM; 74752238; -.
DR EPD; Q9BQD7; -.
DR jPOST; Q9BQD7; -.
DR MassIVE; Q9BQD7; -.
DR MaxQB; Q9BQD7; -.
DR PaxDb; Q9BQD7; -.
DR PeptideAtlas; Q9BQD7; -.
DR PRIDE; Q9BQD7; -.
DR ProteomicsDB; 78660; -.
DR Antibodypedia; 51954; 13 antibodies from 8 providers.
DR DNASU; 65990; -.
DR Ensembl; ENST00000569529.6; ENSP00000454380.1; ENSG00000103254.10.
DR GeneID; 65990; -.
DR KEGG; hsa:65990; -.
DR MANE-Select; ENST00000569529.6; ENSP00000454380.1; NM_023933.3; NP_076422.1.
DR UCSC; uc002cje.5; human.
DR CTD; 65990; -.
DR DisGeNET; 65990; -.
DR GeneCards; ANTKMT; -.
DR HGNC; HGNC:14152; ANTKMT.
DR HPA; ENSG00000103254; Low tissue specificity.
DR MIM; 618566; gene.
DR neXtProt; NX_Q9BQD7; -.
DR OpenTargets; ENSG00000103254; -.
DR VEuPathDB; HostDB:ENSG00000103254; -.
DR eggNOG; KOG4058; Eukaryota.
DR GeneTree; ENSGT00390000014771; -.
DR HOGENOM; CLU_068443_4_2_1; -.
DR InParanoid; Q9BQD7; -.
DR OMA; HEFRIPG; -.
DR OrthoDB; 1605787at2759; -.
DR PhylomeDB; Q9BQD7; -.
DR TreeFam; TF314984; -.
DR PathwayCommons; Q9BQD7; -.
DR SignaLink; Q9BQD7; -.
DR BioGRID-ORCS; 65990; 12 hits in 1076 CRISPR screens.
DR GenomeRNAi; 65990; -.
DR Pharos; Q9BQD7; Tdark.
DR PRO; PR:Q9BQD7; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9BQD7; protein.
DR Bgee; ENSG00000103254; Expressed in anterior cingulate cortex and 163 other tissues.
DR ExpressionAtlas; Q9BQD7; baseline and differential.
DR Genevisible; Q9BQD7; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; 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:1905273; P:positive regulation of proton-transporting ATP synthase activity, rotational mechanism; IBA:GO_Central.
DR GO; GO:1905706; P:regulation of mitochondrial ATP synthesis coupled proton transport; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR026170; FAM173A/B.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR13610; PTHR13610; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Membrane; Methyltransferase; Mitochondrion; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..235
FT /note="Adenine nucleotide translocase lysine N-
FT methyltransferase"
FT /id="PRO_0000263721"
FT TRANSMEM 20..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..22
FT /note="N-terminal sequence (NTS)"
FT /evidence="ECO:0000303|PubMed:31213526"
FT REGION 43..77
FT /note="Methyltransferase (MTase)"
FT /evidence="ECO:0000303|PubMed:31213526"
FT REGION 43..77
FT /note="Pre-methyltransferase (preMT)"
FT /evidence="ECO:0000303|PubMed:31213526"
FT REGION 215..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 1..76
FT /note="Missing: Abolished mitochondrial localization."
FT /evidence="ECO:0000269|PubMed:31213526"
FT MUTAGEN 1..42
FT /note="Missing: Does not affect mitochondrial
FT localization."
FT /evidence="ECO:0000269|PubMed:31213526"
FT MUTAGEN 105
FT /note="E->A: Abolished methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:31213526"
SQ SEQUENCE 235 AA; 25130 MW; 11B10F2DCF27701A CRC64;
MEQDDPVEAL TELRERRLGA LELLQAAAGS GLAAYAVWAL LLQPGFRRVP LRLQVPYVGA
SARQVEHVLS LLRGRPGKTV DLGSGDGRIV LAAHRCGLRP AVGYELNPWL VALARLHAWR
AGCAGSVCYR RKDLWKVSLR DCRNVSVFLA PSVLPLLEDK LRTELPAGAR VVSGRFPLPT
WQPVTAVGEG LDRVWAYDVP EGGQAGEAAS SRIPIQAAPG PSSAPIPGGL ISQAS
