NTM1A_HUMAN
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 03-AUG-2022, entry version 183.
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}.
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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 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 AlphaFoldDB; Q9BV86; -.
DR SMR; Q9BV86; -.
DR BioGRID; 118810; 53.
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; Q9BV86; -.
DR PeptideAtlas; Q9BV86; -.
DR PRIDE; Q9BV86; -.
DR ProteomicsDB; 79180; -. [Q9BV86-1]
DR ProteomicsDB; 79181; -. [Q9BV86-2]
DR TopDownProteomics; Q9BV86-1; -. [Q9BV86-1]
DR Antibodypedia; 17874; 170 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 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-MON; -.
DR BRENDA; 2.1.1.244; 2681.
DR PathwayCommons; Q9BV86; -.
DR SignaLink; Q9BV86; -.
DR BioGRID-ORCS; 28989; 19 hits in 1080 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 179 other tissues.
DR ExpressionAtlas; Q9BV86; baseline and differential.
DR Genevisible; Q9BV86; HS.
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:0008168; F:methyltransferase activity; IBA:GO_Central.
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:0016571; P:histone methylation; IDA:UniProtKB.
DR GO; GO:0018011; P:N-terminal peptidyl-alanine methylation; IBA:GO_Central.
DR GO; GO:0018012; P:N-terminal peptidyl-alanine trimethylation; IEA:Ensembl.
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:0035568; P:N-terminal peptidyl-proline methylation; IBA:GO_Central.
DR GO; GO:0035572; P:N-terminal peptidyl-serine dimethylation; IDA:UniProtKB.
DR GO; GO:0035570; P:N-terminal peptidyl-serine methylation; IBA:GO_Central.
DR GO; GO:0035573; P:N-terminal peptidyl-serine trimethylation; IDA:UniProtKB.
DR GO; GO:0006480; P:N-terminal protein amino acid methylation; IBA:GO_Central.
DR GO; GO:0007051; P:spindle organization; IMP:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR008576; MeTrfase_NTM1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR12753; PTHR12753; 1.
DR Pfam; PF05891; Methyltransf_PK; 1.
DR PIRSF; PIRSF016958; DUF858_MeTrfase_lik; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
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
