ID N6MT1_HUMAN Reviewed; 214 AA. AC Q9Y5N5; B2RA97; Q96F73; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 27-SEP-2017, sequence version 4. DT 03-AUG-2022, entry version 170. DE RecName: Full=Methyltransferase N6AMT1 {ECO:0000305}; DE AltName: Full=HemK methyltransferase family member 2 {ECO:0000303|PubMed:18539146}; DE Short=M.HsaHemK2P; DE AltName: Full=Lysine N-methyltransferase 9 {ECO:0000303|PubMed:31061526}; DE EC=2.1.1.- {ECO:0000269|PubMed:31061526, ECO:0000305|PubMed:31632689}; DE AltName: Full=Methylarsonite methyltransferase N6AMT1; DE EC=2.1.1.- {ECO:0000269|PubMed:21193388, ECO:0000269|PubMed:25997655}; DE AltName: Full=Protein N(5)-glutamine methyltransferase {ECO:0000305}; DE EC=2.1.1.- {ECO:0000269|PubMed:18539146, ECO:0000269|PubMed:31061526, ECO:0000269|PubMed:31636962, ECO:0000305|PubMed:31632689}; GN Name=N6AMT1 {ECO:0000303|PubMed:30017583, ECO:0000312|HGNC:HGNC:16021}; GN Synonyms=C21orf127 {ECO:0000312|HGNC:HGNC:16021}, GN HEMK2 {ECO:0000303|PubMed:18539146}, KMT9 {ECO:0000303|PubMed:31061526}, GN PRED28 {ECO:0000250|UniProtKB:Q6SKR2}; 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 [MRNA] (ISOFORM 1). RA Reboul J., Misseri Y., Bonnerot C., Mogensen E., Lutfalla G.; RT "Identification of a novel putative eukaryotic DNA-methyltransferase."; RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Cerebellum; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS LYS-146 AND RP LYS-166. RX PubMed=10830953; DOI=10.1038/35012518; RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U., RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.; RT "The DNA sequence of human chromosome 21."; RL Nature 405:311-319(2000). RN [4] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Skin; 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 [6] RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH TRMT112. RX PubMed=18539146; DOI=10.1016/j.febslet.2008.05.045; RA Figaro S., Scrima N., Buckingham R.H., Heurgue-Hamard V.; RT "HemK2 protein, encoded on human chromosome 21, methylates translation RT termination factor eRF1."; RL FEBS Lett. 582:2352-2356(2008). RN [7] RP FUNCTION. RX PubMed=20606008; DOI=10.1128/mcb.00218-10; RA Liu P., Nie S., Li B., Yang Z.Q., Xu Z.M., Fei J., Lin C., Zeng R., RA Xu G.L.; RT "Deficiency in a glutamine-specific methyltransferase for release factor RT causes mouse embryonic lethality."; RL Mol. Cell. Biol. 30:4245-4253(2010). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [9] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=21193388; DOI=10.1289/ehp.1002733; RA Ren X., Aleshin M., Jo W.J., Dills R., Kalman D.A., Vulpe C.D., Smith M.T., RA Zhang L.; RT "Involvement of N-6 adenine-specific DNA methyltransferase 1 (N6AMT1) in RT arsenic biomethylation and its role in arsenic-induced toxicity."; RL Environ. Health Perspect. 119:771-777(2011). RN [10] RP SUBUNIT. RX PubMed=25851604; DOI=10.1091/mbc.e15-02-0073; RA Zorbas C., Nicolas E., Wacheul L., Huvelle E., Heurgue-Hamard V., RA Lafontaine D.L.; RT "The human 18S rRNA base methyltransferases DIMT1L and WBSCR22-TRMT112 but RT not rRNA modification are required for ribosome biogenesis."; RL Mol. Biol. Cell 26:2080-2095(2015). RN [11] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=25997655; DOI=10.1093/toxsci/kfv101; RA Zhang H., Ge Y., He P., Chen X., Carina A., Qiu Y., Aga D.S., Ren X.; RT "Interactive effects of N6AMT1 and As3MT in arsenic biomethylation."; RL Toxicol. Sci. 146:354-362(2015). RN [12] RP CAUTION. RX PubMed=30392959; DOI=10.1016/j.cell.2018.10.006; RA Xie Q., Wu T.P., Gimple R.C., Li Z., Prager B.C., Wu Q., Yu Y., Wang P., RA Wang Y., Gorkin D.U., Zhang C., Dowiak A.V., Lin K., Zeng C., Sui Y., RA Kim L.J.Y., Miller T.E., Jiang L., Lee C.H., Huang Z., Fang X., Zhai K., RA Mack S.C., Sander M., Bao S., Kerstetter-Fogle A.E., Sloan A.E., Xiao A.Z., RA Rich J.N.; RT "N6-methyladenine DNA modification in glioblastoma."; RL Cell 175:1228-1243(2018). RN [13] RP MUTAGENESIS OF 122-ASN--TYR-125. RX PubMed=30017583; DOI=10.1016/j.molcel.2018.06.015; RA Xiao C.L., Zhu S., He M., Chen D., Zhang Q., Chen Y., Yu G., Liu J., RA Xie S.Q., Luo F., Liang Z., Wang D.P., Bo X.C., Gu X.F., Wang K., Yan G.R.; RT "N6-methyladenine DNA modification in the human genome."; RL Mol. Cell 71:306-318(2018). RN [14] RP ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), INTERACTION WITH TRMT112, AND RP UBIQUITINATION. RX PubMed=31466382; DOI=10.3390/biom9090422; RA Leetsi L., Ounap K., Abroi A., Kurg R.; RT "The Common Partner of Several Methyltransferases TRMT112 Regulates the RT Expression of N6AMT1 Isoforms in Mammalian Cells."; RL Biomolecules 9:0-0(2019). RN [15] RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH TRMT112. RX PubMed=31632689; DOI=10.1038/s41421-019-0119-5; RA Woodcock C.B., Yu D., Zhang X., Cheng X.; RT "Human HemK2/KMT9/N6AMT1 is an active protein methyltransferase, but does RT not act on DNA in vitro, in the presence of Trm112."; RL Cell Discov. 5:50-50(2019). RN [16] RP FUNCTION, AND CAUTION. RX PubMed=32203414; DOI=10.1038/s41589-020-0504-2; RA Musheev M.U., Baumgaertner A., Krebs L., Niehrs C.; RT "The origin of genomic N6-methyl-deoxyadenosine in mammalian cells."; RL Nat. Chem. Biol. 16:630-634(2020). RN [17] RP INTERACTION WITH TRMT112. RX PubMed=34948388; DOI=10.3390/ijms222413593; RA Brumele B., Mutso M., Telanne L., Ounap K., Spunde K., Abroi A., Kurg R.; RT "Human TRMT112-Methyltransferase Network Consists of Seven Partners RT Interacting with a Common Co-Factor."; RL Int. J. Mol. Sci. 22:13593-13593(2021). RN [18] {ECO:0007744|PDB:6KMR, ECO:0007744|PDB:6KMS} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH RP S-ADENOSYL-L-METHIONINE AND TRMT112, FUNCTION, CATALYTIC ACTIVITY, RP INTERACTION WITH TRMT112, AND MUTAGENESIS OF GLU-24; GLU-27; ASP-28; RP GLU-51; LEU-72; ASP-77; ILE-78; ALA-83; ASP-103; LEU-108; ASN-122; GLU-132; RP GLU-139; ARG-154; GLU-176 AND GLU-204. RX PubMed=31636962; DOI=10.1038/s41421-019-0121-y; RA Li W., Shi Y., Zhang T., Ye J., Ding J.; RT "Structural insight into human N6amt1-Trm112 complex functioning as a RT protein methyltransferase."; RL Cell Discov. 5:51-51(2019). RN [19] {ECO:0007744|PDB:6H1D, ECO:0007744|PDB:6H1E} RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 8-214 IN COMPLEX WITH RP S-ADENOSYL-L-METHIONINE AND TRMT112, FUNCTION, CATALYTIC ACTIVITY, RP INTERACTION WITH TRMT112, AND MUTAGENESIS OF ASP-103; ASN-122 AND TYR-125. RX PubMed=31061526; DOI=10.1038/s41594-019-0219-9; RA Metzger E., Wang S., Urban S., Willmann D., Schmidt A., Offermann A., RA Allen A., Sum M., Obier N., Cottard F., Ulferts S., Preca B.T., Hermann B., RA Maurer J., Greschik H., Hornung V., Einsle O., Perner S., Imhof A., RA Jung M., Schule R.; RT "KMT9 monomethylates histone H4 lysine 12 and controls proliferation of RT prostate cancer cells."; RL Nat. Struct. Mol. Biol. 26:361-371(2019). CC -!- FUNCTION: Methyltransferase that can methylate proteins and, to a lower CC extent, arsenic (PubMed:18539146, PubMed:21193388, PubMed:30017583, CC PubMed:31636962, PubMed:31061526). Catalytic subunit of a heterodimer CC with TRMT112, which monomethylates 'Lys-12' of histone H4 (H4K12me1), a CC modification present at the promoters of numerous genes encoding cell CC cycle regulators (PubMed:31061526). Catalytic subunit of a heterodimer CC with TRMT112, which catalyzes N5-methylation of Glu residue of proteins CC with a Gly-Gln-Xaa-Xaa-Xaa-Arg motif (PubMed:18539146, PubMed:31632689, CC PubMed:31636962). Methylates ETF1 on 'Gln-185'; ETF1 needs to be CC complexed to ERF3 in its GTP-bound form to be efficiently methylated CC (PubMed:18539146, PubMed:20606008, PubMed:31636962, PubMed:31061526). CC May also play a role in the modulation of arsenic-induced toxicity by CC mediating the conversion of monomethylarsonous acid (3+) into the less CC toxic dimethylarsonic acid (PubMed:21193388, PubMed:25997655). It CC however only plays a limited role in arsenic metabolism compared with CC AS3MT (PubMed:25997655). {ECO:0000269|PubMed:18539146, CC ECO:0000269|PubMed:20606008, ECO:0000269|PubMed:21193388, CC ECO:0000269|PubMed:25997655, ECO:0000269|PubMed:30017583, CC ECO:0000269|PubMed:31061526, ECO:0000269|PubMed:31632689, CC ECO:0000269|PubMed:31636962}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) + N(6)- CC methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; CC Evidence={ECO:0000269|PubMed:31061526, ECO:0000305|PubMed:31632689}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10025; CC Evidence={ECO:0000269|PubMed:31061526, ECO:0000305|PubMed:31632689}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-glutaminyl-[protein] + S-adenosyl-L-methionine = H(+) + CC N(5)-methyl-L-glutaminyl-[protein] + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:57452, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:14895, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30011, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61891; CC Evidence={ECO:0000269|PubMed:18539146, ECO:0000269|PubMed:31061526, CC ECO:0000269|PubMed:31636962, ECO:0000305|PubMed:31632689}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57453; CC Evidence={ECO:0000269|PubMed:18539146, ECO:0000269|PubMed:31061526, CC ECO:0000269|PubMed:31636962, ECO:0000305|PubMed:31632689}; CC -!- CATALYTIC ACTIVITY: CC Reaction=methylarsonous acid + S-adenosyl-L-methionine = CC dimethylarsinate + 2 H(+) + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:11684, ChEBI:CHEBI:15378, ChEBI:CHEBI:16223, CC ChEBI:CHEBI:17826, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; CC Evidence={ECO:0000269|PubMed:21193388, ECO:0000269|PubMed:25997655}; CC -!- SUBUNIT: Heterodimer; heterodimerization with TRMT112 is required for CC S-adenosyl-L-methionine-binding. {ECO:0000269|PubMed:18539146, CC ECO:0000269|PubMed:25851604, ECO:0000269|PubMed:31061526, CC ECO:0000269|PubMed:31466382, ECO:0000269|PubMed:31632689, CC ECO:0000269|PubMed:31636962, ECO:0000269|PubMed:34948388}. CC -!- SUBUNIT: [Isoform 2]: Does not interact with TRMT112. CC {ECO:0000269|PubMed:31466382}. CC -!- INTERACTION: CC Q9Y5N5; Q9UI30: TRMT112; NbExp=2; IntAct=EBI-7966667, EBI-373326; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6SKR2}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1 {ECO:0000303|PubMed:31466382}; Synonyms=Alpha CC {ECO:0000303|PubMed:18539146}, N6AMT1iso1 CC {ECO:0000303|PubMed:31466382}; CC IsoId=Q9Y5N5-1; Sequence=Displayed; CC Name=2 {ECO:0000303|PubMed:31466382}; Synonyms=Beta CC {ECO:0000303|PubMed:18539146}, N6AMT1iso2 CC {ECO:0000303|PubMed:31466382}; CC IsoId=Q9Y5N5-2; Sequence=VSP_040294; CC -!- TISSUE SPECIFICITY: Widely expressed, with highest expression in CC parathyroid and pituitary glands, followed by adrenal gland and kidney, CC and lowest expression in leukocytes and mammary gland. CC {ECO:0000269|PubMed:21193388}. CC -!- PTM: [Isoform 1]: Ubiquitinated, leading to its degradation by the CC proteasome. {ECO:0000269|PubMed:31466382}. CC -!- PTM: [Isoform 2]: Ubiquitinated, leading to its degradation by the CC proteasome. {ECO:0000269|PubMed:31466382}. CC -!- SIMILARITY: Belongs to the eukaryotic/archaeal PrmC-related family. CC {ECO:0000305}. CC -!- CAUTION: Was reported to have N(6)-adenine-specific DNA CC methyltransferase by mediating methylation of DNA on the 6th position CC of adenine (N(6)-methyladenosine) (PubMed:30017583). The existence of CC N(6)-methyladenosine on DNA is unclear in mammals (PubMed:32203414). CC According to a report, the majority of N(6)-methyladenosine in DNA CC originates from RNA catabolism via a nucleotide salvage pathway and is CC misincorporated by DNA polymerases, arguing against a role as CC epigenetic DNA mark in mammalian cells (PubMed:32203414). Moreover, CC subsequent studies could not confirm the role of N6AMT1 as a N(6)- CC adenine-specific DNA methyltransferase (PubMed:30392959, CC PubMed:31632689, PubMed:31636962). {ECO:0000269|PubMed:30017583, CC ECO:0000269|PubMed:30392959, ECO:0000269|PubMed:31632689, CC ECO:0000269|PubMed:31636962, ECO:0000269|PubMed:32203414}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF139682; AAD38520.1; -; mRNA. DR EMBL; AK314100; BAG36794.1; -; mRNA. DR EMBL; AF227510; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL163248; CAB90428.1; -; Genomic_DNA. DR EMBL; AMYH02037685; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF570251; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF457188; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KC877845; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471079; EAX09939.1; -; Genomic_DNA. DR EMBL; CH471079; EAX09940.1; -; Genomic_DNA. DR EMBL; CH471079; EAX09941.1; -; Genomic_DNA. DR EMBL; BC011554; AAH11554.1; -; mRNA. DR CCDS; CCDS33525.1; -. [Q9Y5N5-2] DR CCDS; CCDS33526.1; -. [Q9Y5N5-1] DR RefSeq; NP_037372.4; NM_013240.5. [Q9Y5N5-1] DR RefSeq; NP_877426.4; NM_182749.4. [Q9Y5N5-2] DR PDB; 6H1D; X-ray; 1.94 A; A=8-214. DR PDB; 6H1E; X-ray; 1.90 A; A=8-214. DR PDB; 6K0X; X-ray; 2.20 A; A=2-214. DR PDB; 6KHS; X-ray; 1.90 A; A=1-214. DR PDB; 6KMR; X-ray; 2.00 A; B=1-214. DR PDB; 6KMS; X-ray; 3.20 A; C/D=1-214. DR PDB; 6PED; X-ray; 2.30 A; A=1-214. DR PDBsum; 6H1D; -. DR PDBsum; 6H1E; -. DR PDBsum; 6K0X; -. DR PDBsum; 6KHS; -. DR PDBsum; 6KMR; -. DR PDBsum; 6KMS; -. DR PDBsum; 6PED; -. DR AlphaFoldDB; Q9Y5N5; -. DR SMR; Q9Y5N5; -. DR BioGRID; 118872; 7. DR IntAct; Q9Y5N5; 5. DR MINT; Q9Y5N5; -. DR STRING; 9606.ENSP00000303584; -. DR BioMuta; N6AMT1; -. DR DMDM; 313104228; -. DR EPD; Q9Y5N5; -. DR jPOST; Q9Y5N5; -. DR MassIVE; Q9Y5N5; -. DR MaxQB; Q9Y5N5; -. DR PaxDb; Q9Y5N5; -. DR PeptideAtlas; Q9Y5N5; -. DR PRIDE; Q9Y5N5; -. DR ProteomicsDB; 86454; -. [Q9Y5N5-1] DR ProteomicsDB; 86455; -. [Q9Y5N5-2] DR Antibodypedia; 22362; 193 antibodies from 25 providers. DR DNASU; 29104; -. DR Ensembl; ENST00000303775.10; ENSP00000303584.5; ENSG00000156239.12. [Q9Y5N5-1] DR Ensembl; ENST00000351429.7; ENSP00000286764.4; ENSG00000156239.12. [Q9Y5N5-2] DR Ensembl; ENST00000460212.1; ENSP00000436490.1; ENSG00000156239.12. [Q9Y5N5-1] DR GeneID; 29104; -. DR KEGG; hsa:29104; -. DR MANE-Select; ENST00000303775.10; ENSP00000303584.5; NM_013240.6; NP_037372.4. DR UCSC; uc002ymo.3; human. DR UCSC; uc002ymp.3; human. [Q9Y5N5-1] DR CTD; 29104; -. DR DisGeNET; 29104; -. DR GeneCards; N6AMT1; -. DR HGNC; HGNC:16021; N6AMT1. DR HPA; ENSG00000156239; Low tissue specificity. DR MIM; 614553; gene. DR neXtProt; NX_Q9Y5N5; -. DR OpenTargets; ENSG00000156239; -. DR PharmGKB; PA162396656; -. DR VEuPathDB; HostDB:ENSG00000156239; -. DR eggNOG; KOG3191; Eukaryota. DR GeneTree; ENSGT00390000013073; -. DR InParanoid; Q9Y5N5; -. DR OMA; EWDDWME; -. DR OrthoDB; 1450330at2759; -. DR PhylomeDB; Q9Y5N5; -. DR TreeFam; TF314919; -. DR BioCyc; MetaCyc:ENSG00000156239-MON; -. DR BRENDA; 2.1.1.137; 2681. DR BRENDA; 2.1.1.72; 2681. DR PathwayCommons; Q9Y5N5; -. DR Reactome; R-HSA-156581; Methylation. DR Reactome; R-HSA-72764; Eukaryotic Translation Termination. DR SignaLink; Q9Y5N5; -. DR BioGRID-ORCS; 29104; 346 hits in 1093 CRISPR screens. DR ChiTaRS; N6AMT1; human. DR GenomeRNAi; 29104; -. DR Pharos; Q9Y5N5; Tbio. DR PRO; PR:Q9Y5N5; -. DR Proteomes; UP000005640; Chromosome 21. DR RNAct; Q9Y5N5; protein. DR Bgee; ENSG00000156239; Expressed in ventricular zone and 122 other tissues. DR Genevisible; Q9Y5N5; HS. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0035657; C:eRF1 methyltransferase complex; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; IDA:MGI. DR GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IDA:UniProtKB. DR GO; GO:0030792; F:methylarsonite methyltransferase activity; IDA:UniProtKB. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0008276; F:protein methyltransferase activity; IDA:UniProtKB. DR GO; GO:0036009; F:protein-glutamine N-methyltransferase activity; IDA:UniProtKB. DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; IDA:UniProtKB. DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central. DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IDA:UniProtKB. DR GO; GO:0018872; P:arsonoacetate metabolic process; IDA:UniProtKB. DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW. DR GO; GO:0032775; P:DNA methylation on adenine; IDA:UniProtKB. DR GO; GO:0034968; P:histone lysine methylation; IDA:UniProtKB. DR GO; GO:0032259; P:methylation; IDA:UniProtKB. DR GO; GO:0018364; P:peptidyl-glutamine methylation; IDA:UniProtKB. DR GO; GO:0030307; P:positive regulation of cell growth; IDA:MGI. DR GO; GO:0009404; P:toxin metabolic process; IDA:UniProtKB. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR004557; PrmC-related. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR InterPro; IPR007848; Small_mtfrase_dom. DR Pfam; PF05175; MTS; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00537; hemK_rel_arch; 1. DR PROSITE; PS00092; N6_MTASE; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Chromatin regulator; Methyltransferase; KW Nucleus; Reference proteome; S-adenosyl-L-methionine; Transferase; KW Ubl conjugation. FT CHAIN 1..214 FT /note="Methyltransferase N6AMT1" FT /id="PRO_0000088049" FT REGION 103..104 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000269|PubMed:31061526, FT ECO:0000269|PubMed:31636962, ECO:0007744|PDB:6H1D, FT ECO:0007744|PDB:6H1E, ECO:0007744|PDB:6KMR, FT ECO:0007744|PDB:6KMS" FT BINDING 24 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:31061526, FT ECO:0007744|PDB:6H1E" FT BINDING 29 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000269|PubMed:31061526, FT ECO:0000269|PubMed:31636962, ECO:0007744|PDB:6H1D, FT ECO:0007744|PDB:6H1E, ECO:0007744|PDB:6KMR, FT ECO:0007744|PDB:6KMS" FT BINDING 51..53 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000269|PubMed:31061526, FT ECO:0000269|PubMed:31636962, ECO:0007744|PDB:6H1D, FT ECO:0007744|PDB:6H1E, ECO:0007744|PDB:6KMR, FT ECO:0007744|PDB:6KMS" FT BINDING 77 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000269|PubMed:31061526, FT ECO:0000269|PubMed:31636962, ECO:0007744|PDB:6H1D, FT ECO:0007744|PDB:6H1E, ECO:0007744|PDB:6KMR, FT ECO:0007744|PDB:6KMS" FT BINDING 122..125 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P0ACC1" FT BINDING 122 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000269|PubMed:31061526, FT ECO:0000269|PubMed:31636962, ECO:0000305|PubMed:30017583, FT ECO:0007744|PDB:6H1D, ECO:0007744|PDB:6H1E, FT ECO:0007744|PDB:6KMR, ECO:0007744|PDB:6KMS" FT BINDING 122 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:31061526, FT ECO:0007744|PDB:6H1E" FT BINDING 204 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:31061526, FT ECO:0007744|PDB:6H1E" FT VAR_SEQ 105..132 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_040294" FT VARIANT 34 FT /note="D -> N (in dbSNP:rs1997607)" FT /id="VAR_060445" FT VARIANT 146 FT /note="R -> K (in dbSNP:rs2205447)" FT /evidence="ECO:0000269|PubMed:10830953" FT /id="VAR_060446" FT VARIANT 166 FT /note="R -> K (in dbSNP:rs2205446)" FT /evidence="ECO:0000269|PubMed:10830953" FT /id="VAR_060447" FT MUTAGEN 24 FT /note="E->K: Reduced protein N(5)-glutamine FT methyltransferase activity." FT /evidence="ECO:0000269|PubMed:31636962" FT MUTAGEN 27 FT /note="E->K: Abolished protein N(5)-glutamine FT methyltransferase activity." FT /evidence="ECO:0000269|PubMed:31636962" FT MUTAGEN 28 FT /note="D->N: Abolished protein N(5)-glutamine FT methyltransferase activity." FT /evidence="ECO:0000269|PubMed:31636962" FT MUTAGEN 51 FT /note="E->A: Abolished protein N(5)-glutamine FT methyltransferase activity." FT /evidence="ECO:0000269|PubMed:31636962" FT MUTAGEN 72 FT /note="L->D: Strongly reduced protein N(5)-glutamine FT methyltransferase activity." FT /evidence="ECO:0000269|PubMed:31636962" FT MUTAGEN 77 FT /note="D->A: Abolished protein N(5)-glutamine FT methyltransferase activity." FT /evidence="ECO:0000269|PubMed:31636962" FT MUTAGEN 78 FT /note="I->A: Abolished protein N(5)-glutamine FT methyltransferase activity." FT /evidence="ECO:0000269|PubMed:31636962" FT MUTAGEN 83 FT /note="A->D: Strongly reduced protein N(5)-glutamine FT methyltransferase activity." FT /evidence="ECO:0000269|PubMed:31636962" FT MUTAGEN 103 FT /note="D->A: Abolished protein N(5)-glutamine FT methyltransferase activity. Abolished histone-lysine FT methyltransferase activity." FT /evidence="ECO:0000269|PubMed:31061526, FT ECO:0000269|PubMed:31636962" FT MUTAGEN 108 FT /note="L->D: Strongly reduced protein N(5)-glutamine FT methyltransferase activity." FT /evidence="ECO:0000269|PubMed:31636962" FT MUTAGEN 122..125 FT /note="NPPY->AAAA: Abolished DNA methyltransferase FT activity." FT /evidence="ECO:0000269|PubMed:30017583" FT MUTAGEN 122 FT /note="N->A: Abolished protein N(5)-glutamine FT methyltransferase activity. Abolished histone-lysine FT methyltransferase activity." FT /evidence="ECO:0000269|PubMed:31061526, FT ECO:0000269|PubMed:31636962" FT MUTAGEN 125 FT /note="Y->A: Abolished protein N(5)-glutamine FT methyltransferase activity without affecting histone-lysine FT methyltransferase activity." FT /evidence="ECO:0000269|PubMed:31061526" FT MUTAGEN 132 FT /note="E->K: Abolished protein N(5)-glutamine FT methyltransferase activity." FT /evidence="ECO:0000269|PubMed:31636962" FT MUTAGEN 139 FT /note="E->K: Reduced protein N(5)-glutamine FT methyltransferase activity." FT /evidence="ECO:0000269|PubMed:31636962" FT MUTAGEN 154 FT /note="R->A: Slightly reduced protein N(5)-glutamine FT methyltransferase activity." FT /evidence="ECO:0000269|PubMed:31636962" FT MUTAGEN 176 FT /note="E->K: Abolished protein N(5)-glutamine FT methyltransferase activity." FT /evidence="ECO:0000269|PubMed:31636962" FT MUTAGEN 204 FT /note="E->K: Abolished protein N(5)-glutamine FT methyltransferase activity." FT /evidence="ECO:0000269|PubMed:31636962" FT TURN 12..15 FT /evidence="ECO:0007829|PDB:6H1E" FT HELIX 17..19 FT /evidence="ECO:0007829|PDB:6H1E" FT HELIX 27..38 FT /evidence="ECO:0007829|PDB:6KHS" FT HELIX 40..43 FT /evidence="ECO:0007829|PDB:6KHS" FT STRAND 48..53 FT /evidence="ECO:0007829|PDB:6KHS" FT HELIX 58..67 FT /evidence="ECO:0007829|PDB:6KHS" FT STRAND 71..79 FT /evidence="ECO:0007829|PDB:6KHS" FT HELIX 80..93 FT /evidence="ECO:0007829|PDB:6KHS" FT STRAND 98..103 FT /evidence="ECO:0007829|PDB:6KHS" FT TURN 104..107 FT /evidence="ECO:0007829|PDB:6KHS" FT TURN 109..115 FT /evidence="ECO:0007829|PDB:6KHS" FT STRAND 116..121 FT /evidence="ECO:0007829|PDB:6KHS" FT HELIX 130..132 FT /evidence="ECO:0007829|PDB:6KHS" FT HELIX 138..141 FT /evidence="ECO:0007829|PDB:6KHS" FT HELIX 146..148 FT /evidence="ECO:0007829|PDB:6KHS" FT HELIX 150..155 FT /evidence="ECO:0007829|PDB:6KHS" FT HELIX 156..158 FT /evidence="ECO:0007829|PDB:6KHS" FT HELIX 159..162 FT /evidence="ECO:0007829|PDB:6KHS" FT STRAND 163..174 FT /evidence="ECO:0007829|PDB:6KHS" FT HELIX 175..177 FT /evidence="ECO:0007829|PDB:6KHS" FT HELIX 179..188 FT /evidence="ECO:0007829|PDB:6KHS" FT STRAND 192..201 FT /evidence="ECO:0007829|PDB:6KHS" FT STRAND 204..212 FT /evidence="ECO:0007829|PDB:6KHS" SQ SEQUENCE 214 AA; 22957 MW; 65512C91DC85ADDB CRC64; MAGENFATPF HGHVGRGAFS DVYEPAEDTF LLLDALEAAA AELAGVEICL EVGSGSGVVS AFLASMIGPQ ALYMCTDINP EAAACTLETA RCNKVHIQPV ITDLVKGLLP RLTEKVDLLV FNPPYVVTPP QEVGSHGIEA AWAGGRNGRE VMDRFFPLVP DLLSPRGLFY LVTIKENNPE EILKIMKTKG LQGTTALSRQ AGQETLSVLK FTKS //