ID NTM1A_HUMAN Reviewed; 223 AA. AC Q9BV86; A8K4J2; A8K8G7; Q5SZB9; Q9UI28; DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 24-JAN-2024, entry version 191. DE RecName: Full=N-terminal Xaa-Pro-Lys N-methyltransferase 1; DE EC=2.1.1.244 {ECO:0000269|PubMed:20668449}; DE AltName: Full=Alpha N-terminal protein methyltransferase 1A; DE AltName: Full=Methyltransferase-like protein 11A; DE AltName: Full=N-terminal RCC1 methyltransferase; DE AltName: Full=X-Pro-Lys N-terminal protein methyltransferase 1A; DE Short=NTM1A; DE Contains: DE RecName: Full=N-terminal Xaa-Pro-Lys N-methyltransferase 1, N-terminally processed; GN Name=NTMT1; Synonyms=C9orf32, METTL11A, NRMT, NRMT1; ORFNames=AD-003; 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 1). RC TISSUE=Adrenal gland; RX PubMed=10931946; DOI=10.1073/pnas.160270997; RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J., RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., RA Chen M.-D., Chen J.-L.; RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis RT and full-length cDNA cloning."; RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Teratocarcinoma, and Testis; 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]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain, and 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 [5] RP PROTEIN SEQUENCE OF 2-15 AND 79-85, CLEAVAGE OF INITIATOR METHIONINE, RP ACETYLATION AT THR-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=B-cell lymphoma; RA Bienvenut W.V.; RL Submitted (OCT-2004) to UniProtKB. RN [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, CLEAVAGE OF RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [7] RP FUNCTION. RX PubMed=20481588; DOI=10.1021/bi100428x; RA Webb K.J., Lipson R.S., Al-Hadid Q., Whitelegge J.P., Clarke S.G.; RT "Identification of protein N-terminal methyltransferases in yeast and RT humans."; RL Biochemistry 49:5225-5235(2010). RN [8] RP FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY, RP SUBCELLULAR LOCATION, S-ADENOSYL-L-METHIONINE-BINDING, AND MUTAGENESIS OF RP ASP-167; ASN-168; ASP-177; ASP-180 AND SER-182. RX PubMed=20668449; DOI=10.1038/nature09343; RA Tooley C.E., Petkowski J.J., Muratore-Schroeder T.L., Balsbaugh J.L., RA Shabanowitz J., Sabat M., Minor W., Hunt D.F., Macara I.G.; RT "NRMT is an alpha-N-methyltransferase that methylates RCC1 and RT retinoblastoma protein."; RL Nature 466:1125-1128(2010). RN [9] 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 [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [11] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=24090352; DOI=10.1042/bj20131163; RA Petkowski J.J., Bonsignore L.A., Tooley J.G., Wilkey D.W., Merchant M.L., RA Macara I.G., Schaner Tooley C.E.; RT "NRMT2 is an N-terminal monomethylase that primes for its homologue RT NRMT1."; RL Biochem. J. 456:453-462(2013). RN [12] RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 2-223 IN COMPLEX WITH RP S-ADENOSYL-L-HOMOCYSTEINE. RG Structural genomics consortium (SGC); RT "The crystal structure of human AD-003 protein in complex with S-adenosyl- RT L-homocysteine."; RL Submitted (FEB-2009) to the PDB data bank. RN [13] {ECO:0007744|PDB:5CVD} RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) IN COMPLEXES WITH CENPA; HISTONE H2B RP AND S-ADENOSYL-HOMOCYSTEINE, FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS RP OF TYR-19; TRP-20; TRP-136; ASP-167; ASN-168; ASP-177 AND ASP-180. RX PubMed=26543159; DOI=10.1101/gad.270926.115; RA Wu R., Yue Y., Zheng X., Li H.; RT "Molecular basis for histone N-terminal methylation by NRMT1."; RL Genes Dev. 29:2337-2342(2015). RN [14] {ECO:0007744|PDB:5E1B, ECO:0007744|PDB:5E1D, ECO:0007744|PDB:5E1M, ECO:0007744|PDB:5E1O, ECO:0007744|PDB:5E2A, ECO:0007744|PDB:5E2B} RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEXES WITH PEPTIDE SUBSTRATES RP AND S-ADENOSYL-HOMOCYSTEINE. RX PubMed=26543161; DOI=10.1101/gad.270611.115; RA Dong C., Mao Y., Tempel W., Qin S., Li L., Loppnau P., Huang R., Min J.; RT "Structural basis for substrate recognition by the human N-terminal RT methyltransferase 1."; RL Genes Dev. 29:2343-2348(2015). CC -!- FUNCTION: Distributive alpha-N-methyltransferase that methylates the N- CC terminus of target proteins containing the N-terminal motif CC [Ala/Gly/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. CC Specifically catalyzes mono-, di- or tri-methylation of the exposed CC alpha-amino group of the Ala, Gly or Ser residue in the [Ala/Gly/Ser]- CC Pro-Lys motif and mono- or di-methylation of Pro in the Pro-Pro-Lys CC motif. Some of the substrates may be primed by NTMT2-mediated CC monomethylation (PubMed:24090352). Catalyzes the trimethylation of the CC N-terminal Gly in CENPA (after removal of Met-1). Responsible for the CC N-terminal methylation of KLHL31, MYL2, MYL3, RB1, RCC1, RPL23A and CC SET. Required during mitosis for normal bipolar spindle formation and CC chromosome segregation via its action on RCC1. CC {ECO:0000269|PubMed:20481588, ECO:0000269|PubMed:20668449, CC ECO:0000269|PubMed:24090352, ECO:0000269|PubMed:26543159}. CC -!- CATALYTIC ACTIVITY: CC Reaction=N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl- CC L-methionine = 3 H(+) + N-terminal N,N,N-trimethyl-L-alanyl-L-prolyl- CC L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:54712, Rhea:RHEA-COMP:13785, Rhea:RHEA-COMP:13971, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:138057, ChEBI:CHEBI:138315; EC=2.1.1.244; CC Evidence={ECO:0000269|PubMed:20668449, ECO:0000269|PubMed:26543159}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N-terminal L-seryl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl- CC L-methionine = 3 H(+) + N-terminal N,N,N-trimethyl-L-seryl-L-prolyl- CC L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:54724, Rhea:RHEA-COMP:13789, Rhea:RHEA-COMP:13973, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:138061, ChEBI:CHEBI:138317; EC=2.1.1.244; CC Evidence={ECO:0000269|PubMed:20668449, ECO:0000269|PubMed:26543159}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N-terminal L-prolyl-L-prolyl-L-lysyl-[protein] + 2 S-adenosyl- CC L-methionine = 2 H(+) + N-terminal N,N-dimethyl-L-prolyl-L-prolyl-L- CC lysyl-[protein] + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:54736, CC Rhea:RHEA-COMP:13787, Rhea:RHEA-COMP:13974, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:138059, CC ChEBI:CHEBI:138318; EC=2.1.1.244; CC Evidence={ECO:0000269|PubMed:20668449, ECO:0000269|PubMed:26543159}; CC -!- INTERACTION: CC Q9BV86; Q49A26-4: GLYR1; NbExp=3; IntAct=EBI-373016, EBI-12143817; CC Q9BV86; P18754: RCC1; NbExp=4; IntAct=EBI-373016, EBI-992720; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20668449, CC ECO:0000269|PubMed:24090352}. Note=Predominantly nuclear CC (PubMed:24090352). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9BV86-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9BV86-2; Sequence=VSP_039886; CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. NTM1 family. CC {ECO:0000305}. 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; AF110776; AAF14859.1; -; mRNA. DR EMBL; AK290957; BAF83646.1; -; mRNA. DR EMBL; AK292332; BAF85021.1; -; mRNA. DR EMBL; AK298840; BAG60968.1; -; mRNA. DR EMBL; AL590369; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC001396; AAH01396.1; -; mRNA. DR EMBL; BC033234; AAH33234.1; -; mRNA. DR CCDS; CCDS35160.1; -. [Q9BV86-1] DR CCDS; CCDS69682.1; -. [Q9BV86-2] DR RefSeq; NP_001273725.1; NM_001286796.1. [Q9BV86-1] DR RefSeq; NP_001273726.1; NM_001286797.1. [Q9BV86-1] DR RefSeq; NP_001273727.1; NM_001286798.1. [Q9BV86-1] DR RefSeq; NP_001273728.1; NM_001286799.1. [Q9BV86-1] DR RefSeq; NP_001273729.1; NM_001286800.1. [Q9BV86-2] DR RefSeq; NP_001273730.1; NM_001286801.1. [Q9BV86-2] DR RefSeq; NP_001273731.1; NM_001286802.1. DR RefSeq; NP_001273732.1; NM_001286803.1. DR RefSeq; NP_054783.2; NM_014064.3. [Q9BV86-1] DR PDB; 2EX4; X-ray; 1.75 A; A/B=2-222. DR PDB; 5CVD; X-ray; 1.30 A; A/B=1-223. DR PDB; 5CVE; X-ray; 1.50 A; A/B=1-223. DR PDB; 5E1B; X-ray; 1.65 A; A/B=2-223. DR PDB; 5E1D; X-ray; 1.45 A; A/B=2-223. DR PDB; 5E1M; X-ray; 1.75 A; A/B=2-223. DR PDB; 5E1O; X-ray; 2.00 A; A/B=2-223. DR PDB; 5E2A; X-ray; 1.75 A; A/B=2-223. DR PDB; 5E2B; X-ray; 1.95 A; A/B=2-223. DR PDB; 6DTN; X-ray; 1.48 A; B=2-223. DR PDB; 6KDQ; X-ray; 1.50 A; A/B=1-223. DR PDB; 6PVA; X-ray; 1.84 A; B=2-223. DR PDB; 6PVB; X-ray; 1.50 A; B=2-223. DR PDB; 6WH8; X-ray; 1.73 A; A/B=2-223. DR PDB; 6WJ7; X-ray; 1.42 A; B=2-223. DR PDB; 7K3D; X-ray; 2.34 A; A/B=2-223. DR PDB; 7SS1; X-ray; 2.40 A; A/B=2-223. DR PDB; 7U1M; X-ray; 3.17 A; A/B=2-223. DR PDBsum; 2EX4; -. DR PDBsum; 5CVD; -. DR PDBsum; 5CVE; -. DR PDBsum; 5E1B; -. DR PDBsum; 5E1D; -. DR PDBsum; 5E1M; -. DR PDBsum; 5E1O; -. DR PDBsum; 5E2A; -. DR PDBsum; 5E2B; -. DR PDBsum; 6DTN; -. DR PDBsum; 6KDQ; -. DR PDBsum; 6PVA; -. DR PDBsum; 6PVB; -. DR PDBsum; 6WH8; -. DR PDBsum; 6WJ7; -. DR PDBsum; 7K3D; -. DR PDBsum; 7SS1; -. DR PDBsum; 7U1M; -. DR AlphaFoldDB; Q9BV86; -. DR SMR; Q9BV86; -. DR BioGRID; 118810; 68. DR DIP; DIP-31241N; -. DR IntAct; Q9BV86; 14. DR STRING; 9606.ENSP00000483489; -. DR BindingDB; Q9BV86; -. DR ChEMBL; CHEMBL4523442; -. DR GlyGen; Q9BV86; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9BV86; -. DR MetOSite; Q9BV86; -. DR PhosphoSitePlus; Q9BV86; -. DR BioMuta; NTMT1; -. DR DMDM; 74761281; -. DR EPD; Q9BV86; -. DR jPOST; Q9BV86; -. DR MassIVE; Q9BV86; -. DR MaxQB; Q9BV86; -. DR PaxDb; 9606-ENSP00000483489; -. DR PeptideAtlas; Q9BV86; -. DR ProteomicsDB; 79180; -. [Q9BV86-1] DR ProteomicsDB; 79181; -. [Q9BV86-2] DR Pumba; Q9BV86; -. DR TopDownProteomics; Q9BV86-1; -. [Q9BV86-1] DR Antibodypedia; 17874; 185 antibodies from 27 providers. DR DNASU; 28989; -. DR Ensembl; ENST00000372480.1; ENSP00000361558.1; ENSG00000148335.15. [Q9BV86-1] DR Ensembl; ENST00000372481.7; ENSP00000361559.3; ENSG00000148335.15. [Q9BV86-2] DR Ensembl; ENST00000372483.9; ENSP00000361561.4; ENSG00000148335.15. [Q9BV86-1] DR Ensembl; ENST00000372486.5; ENSP00000361564.1; ENSG00000148335.15. [Q9BV86-1] DR Ensembl; ENST00000611055.4; ENSP00000483489.1; ENSG00000148335.15. [Q9BV86-1] DR Ensembl; ENST00000613644.4; ENSP00000478521.1; ENSG00000148335.15. [Q9BV86-1] DR GeneID; 28989; -. DR KEGG; hsa:28989; -. DR MANE-Select; ENST00000372483.9; ENSP00000361561.4; NM_014064.4; NP_054783.2. DR UCSC; uc004byd.3; human. [Q9BV86-1] DR AGR; HGNC:23373; -. DR CTD; 28989; -. DR DisGeNET; 28989; -. DR GeneCards; NTMT1; -. DR HGNC; HGNC:23373; NTMT1. DR HPA; ENSG00000148335; Low tissue specificity. DR MIM; 613560; gene. DR neXtProt; NX_Q9BV86; -. DR OpenTargets; ENSG00000148335; -. DR PharmGKB; PA162395788; -. DR VEuPathDB; HostDB:ENSG00000148335; -. DR eggNOG; KOG3178; Eukaryota. DR GeneTree; ENSGT00390000008371; -. DR HOGENOM; CLU_055356_3_1_1; -. DR InParanoid; Q9BV86; -. DR OMA; PVRMYCL; -. DR PhylomeDB; Q9BV86; -. DR TreeFam; TF314174; -. DR BioCyc; MetaCyc:ENSG00000148335-MONOMER; -. DR BRENDA; 2.1.1.244; 2681. DR PathwayCommons; Q9BV86; -. DR SignaLink; Q9BV86; -. DR BioGRID-ORCS; 28989; 19 hits in 1159 CRISPR screens. DR ChiTaRS; NTMT1; human. DR EvolutionaryTrace; Q9BV86; -. DR GenomeRNAi; 28989; -. DR Pharos; Q9BV86; Tchem. DR PRO; PR:Q9BV86; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q9BV86; Protein. DR Bgee; ENSG00000148335; Expressed in left testis and 181 other cell types or tissues. DR ExpressionAtlas; Q9BV86; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0042054; F:histone methyltransferase activity; IDA:UniProtKB. DR GO; GO:0071885; F:N-terminal protein N-methyltransferase activity; IDA:UniProtKB. DR GO; GO:0008276; F:protein methyltransferase activity; IDA:UniProtKB. DR GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB. DR GO; GO:0018013; P:N-terminal peptidyl-glycine methylation; IDA:UniProtKB. DR GO; GO:0018016; P:N-terminal peptidyl-proline dimethylation; IDA:UniProtKB. DR GO; GO:0035572; P:N-terminal peptidyl-serine dimethylation; IDA:UniProtKB. DR GO; GO:0035573; P:N-terminal peptidyl-serine trimethylation; IDA:UniProtKB. DR GO; GO:0007051; P:spindle organization; IMP:UniProtKB. DR CDD; cd02440; AdoMet_MTases; 1. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR InterPro; IPR008576; MeTrfase_NTM1. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR PANTHER; PTHR12753; AD-003 - RELATED; 1. DR PANTHER; PTHR12753:SF1; N-TERMINAL XAA-PRO-LYS N-METHYLTRANSFERASE 1; 1. DR Pfam; PF05891; Methyltransf_PK; 1. DR PIRSF; PIRSF016958; DUF858_MeTrfase_lik; 1. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. DR Genevisible; Q9BV86; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing; KW Methyltransferase; Nucleus; Reference proteome; S-adenosyl-L-methionine; KW Transferase. FT CHAIN 1..223 FT /note="N-terminal Xaa-Pro-Lys N-methyltransferase 1" FT /id="PRO_0000423228" FT INIT_MET 1 FT /note="Removed; alternate" FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895" FT CHAIN 2..223 FT /note="N-terminal Xaa-Pro-Lys N-methyltransferase 1, N- FT terminally processed" FT /id="PRO_0000119288" FT BINDING 69 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000269|PubMed:26543159, FT ECO:0000269|PubMed:26543161, ECO:0007744|PDB:2EX4, FT ECO:0007744|PDB:5CVD, ECO:0007744|PDB:5CVE, FT ECO:0007744|PDB:5E1D, ECO:0007744|PDB:5E1M, FT ECO:0007744|PDB:5E1O, ECO:0007744|PDB:5E2A, FT ECO:0007744|PDB:5E2B" FT BINDING 74 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000269|PubMed:26543159, FT ECO:0000269|PubMed:26543161, ECO:0007744|PDB:2EX4, FT ECO:0007744|PDB:5CVD, ECO:0007744|PDB:5CVE, FT ECO:0007744|PDB:5E1D, ECO:0007744|PDB:5E1M, FT ECO:0007744|PDB:5E1O, ECO:0007744|PDB:5E2A, FT ECO:0007744|PDB:5E2B" FT BINDING 91..93 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000269|PubMed:26543159, FT ECO:0000269|PubMed:26543161, ECO:0007744|PDB:2EX4, FT ECO:0007744|PDB:5CVD, ECO:0007744|PDB:5CVE, FT ECO:0007744|PDB:5E1D, ECO:0007744|PDB:5E1M, FT ECO:0007744|PDB:5E1O, ECO:0007744|PDB:5E2A, FT ECO:0007744|PDB:5E2B" FT BINDING 119..120 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000269|PubMed:26543159, FT ECO:0000269|PubMed:26543161, ECO:0007744|PDB:2EX4, FT ECO:0007744|PDB:5CVD, ECO:0007744|PDB:5CVE, FT ECO:0007744|PDB:5E1D, ECO:0007744|PDB:5E1M, FT ECO:0007744|PDB:5E1O, ECO:0007744|PDB:5E2A, FT ECO:0007744|PDB:5E2B" FT BINDING 135 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000269|PubMed:26543159, FT ECO:0000269|PubMed:26543161, ECO:0007744|PDB:2EX4, FT ECO:0007744|PDB:5CVD, ECO:0007744|PDB:5CVE, FT ECO:0007744|PDB:5E1D, ECO:0007744|PDB:5E1M, FT ECO:0007744|PDB:5E1O, ECO:0007744|PDB:5E2A, FT ECO:0007744|PDB:5E2B" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:19413330" FT MOD_RES 2 FT /note="N-acetylthreonine; in N-terminal Xaa-Pro-Lys N- FT methyltransferase 1, N-terminally processed" FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895" FT VAR_SEQ 111..223 FT /note="VRNYFCCGLQDFTPEPDSYDVIWIQWVIGHLTDQHLAEFLRRCKGSLRPNGI FT IVIKDNMAQEGVILDDVDSSVCRDLDVVRRIICSAGLSLLAEERQENLPDEIYHVYSFA FT LR -> ATSPISTWPSSCGAARAASAPTASSSSKTTWPRRA (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_039886" FT MUTAGEN 19 FT /note="Y->A,F: Decreased methyltransferase activity with FT CENPA." FT /evidence="ECO:0000269|PubMed:26543159" FT MUTAGEN 19 FT /note="Y->A: Reduced methyltransferase activity with FT CENPA." FT /evidence="ECO:0000269|PubMed:26543159" FT MUTAGEN 20 FT /note="W->A,M,Y: Nearly abolishes methyltransferase FT activity with CENPA." FT /evidence="ECO:0000269|PubMed:26543159" FT MUTAGEN 136 FT /note="W->L: Strongly reduces methyltransferase activity FT with CENPA." FT /evidence="ECO:0000269|PubMed:26543159" FT MUTAGEN 167 FT /note="D->A: Does not affect methyltransferase activity." FT /evidence="ECO:0000269|PubMed:20668449" FT MUTAGEN 167 FT /note="D->N,Q: Abolishes methyltransferase activity with FT CENPA." FT /evidence="ECO:0000269|PubMed:26543159" FT MUTAGEN 168 FT /note="N->A: Decreased methyltransferase activity." FT /evidence="ECO:0000269|PubMed:20668449, FT ECO:0000269|PubMed:26543159" FT MUTAGEN 168 FT /note="N->K: Loss of methyltransferase activity." FT /evidence="ECO:0000269|PubMed:20668449" FT MUTAGEN 177 FT /note="D->A: Induces a slight decrease in methyltransferase FT activity." FT /evidence="ECO:0000269|PubMed:20668449" FT MUTAGEN 177 FT /note="D->K: Induces a strong decrease in methyltransferase FT activity." FT /evidence="ECO:0000269|PubMed:20668449" FT MUTAGEN 177 FT /note="D->N: Strongly reduces methyltransferase activity FT with CENPA." FT /evidence="ECO:0000269|PubMed:26543159" FT MUTAGEN 180 FT /note="D->A: Induces a decrease in methyltransferase FT activity." FT /evidence="ECO:0000269|PubMed:20668449" FT MUTAGEN 180 FT /note="D->K: Induces a strong decrease in methyltransferase FT activity." FT /evidence="ECO:0000269|PubMed:20668449" FT MUTAGEN 180 FT /note="D->N: Reduced methyltransferase activity with FT CENPA." FT /evidence="ECO:0000269|PubMed:26543159" FT MUTAGEN 182 FT /note="S->A: Induces a slight decrease in methyltransferase FT activity." FT /evidence="ECO:0000269|PubMed:20668449" FT MUTAGEN 182 FT /note="S->K: Induces a strong decrease in methyltransferase FT activity." FT /evidence="ECO:0000269|PubMed:20668449" FT CONFLICT 25 FT /note="P -> L (in Ref. 2; BAF85021)" FT /evidence="ECO:0000305" FT CONFLICT 39 FT /note="S -> SS (in Ref. 1; AAF14859)" FT /evidence="ECO:0000305" FT CONFLICT 131 FT /note="V -> A (in Ref. 2; BAF83646)" FT /evidence="ECO:0000305" FT HELIX 2..4 FT /evidence="ECO:0007829|PDB:5CVD" FT HELIX 9..21 FT /evidence="ECO:0007829|PDB:5CVD" FT HELIX 27..30 FT /evidence="ECO:0007829|PDB:5CVD" FT TURN 31..33 FT /evidence="ECO:0007829|PDB:5CVD" FT HELIX 35..37 FT /evidence="ECO:0007829|PDB:5CVD" FT HELIX 38..54 FT /evidence="ECO:0007829|PDB:5CVD" FT STRAND 55..58 FT /evidence="ECO:0007829|PDB:5CVD" FT STRAND 63..68 FT /evidence="ECO:0007829|PDB:5CVD" FT TURN 71..73 FT /evidence="ECO:0007829|PDB:5CVD" FT HELIX 74..78 FT /evidence="ECO:0007829|PDB:5CVD" FT TURN 79..83 FT /evidence="ECO:0007829|PDB:5CVD" FT STRAND 85..92 FT /evidence="ECO:0007829|PDB:5CVD" FT HELIX 94..103 FT /evidence="ECO:0007829|PDB:5CVD" FT HELIX 105..110 FT /evidence="ECO:0007829|PDB:5CVD" FT STRAND 111..116 FT /evidence="ECO:0007829|PDB:5CVD" FT HELIX 119..121 FT /evidence="ECO:0007829|PDB:5CVD" FT STRAND 129..136 FT /evidence="ECO:0007829|PDB:5CVD" FT HELIX 138..140 FT /evidence="ECO:0007829|PDB:5CVD" FT HELIX 143..156 FT /evidence="ECO:0007829|PDB:5CVD" FT STRAND 157..177 FT /evidence="ECO:0007829|PDB:5CVD" FT TURN 178..181 FT /evidence="ECO:0007829|PDB:5CVD" FT STRAND 182..186 FT /evidence="ECO:0007829|PDB:5CVD" FT HELIX 187..196 FT /evidence="ECO:0007829|PDB:5CVD" FT STRAND 200..206 FT /evidence="ECO:0007829|PDB:5CVD" FT STRAND 216..223 FT /evidence="ECO:0007829|PDB:5CVD" SQ SEQUENCE 223 AA; 25387 MW; 4A0EC492D9B52C49 CRC64; MTSEVIEDEK QFYSKAKTYW KQIPPTVDGM LGGYGHISSI DINSSRKFLQ RFLREGPNKT GTSCALDCGA GIGRITKRLL LPLFREVDMV DITEDFLVQA KTYLGEEGKR VRNYFCCGLQ DFTPEPDSYD VIWIQWVIGH LTDQHLAEFL RRCKGSLRPN GIIVIKDNMA QEGVILDDVD SSVCRDLDVV RRIICSAGLS LLAEERQENL PDEIYHVYSF ALR //