NTM1A_MOUSE
ID NTM1A_MOUSE Reviewed; 223 AA.
AC Q8R2U4; A2APZ4;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 140.
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=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=Mettl11a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Dendritic cell;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Liver, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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).
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 (PubMed:20668449). Some of the substrates may be primed by NTMT2-
CC mediated monomethylation. Catalyzes the trimethylation of the N-
CC terminal Gly in CENPA (after removal of Met-1) (By similarity).
CC Responsible for the N-terminal methylation of KLHL31, MYL2, MYL3, RB1,
CC RCC1, RPL23A and SET. Required during mitosis for normal bipolar
CC spindle formation and chromosome segregation via its action on RCC1
CC (PubMed:20668449). {ECO:0000250|UniProtKB:Q9BV86,
CC ECO:0000269|PubMed:20668449}.
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};
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};
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};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BV86}.
CC Note=Predominantly nuclear. {ECO:0000250|UniProtKB:Q9BV86}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. NTM1 family.
CC {ECO:0000305}.
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DR EMBL; AK154783; BAE32826.1; -; mRNA.
DR EMBL; AL844532; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466542; EDL08489.1; -; Genomic_DNA.
DR EMBL; CH466542; EDL08490.1; -; Genomic_DNA.
DR EMBL; BC027220; AAH27220.1; -; mRNA.
DR CCDS; CCDS15886.1; -.
DR RefSeq; NP_733480.1; NM_170592.2.
DR RefSeq; XP_006498289.1; XM_006498226.3.
DR AlphaFoldDB; Q8R2U4; -.
DR SMR; Q8R2U4; -.
DR BioGRID; 211599; 2.
DR STRING; 10090.ENSMUSP00000035303; -.
DR PhosphoSitePlus; Q8R2U4; -.
DR EPD; Q8R2U4; -.
DR MaxQB; Q8R2U4; -.
DR PaxDb; Q8R2U4; -.
DR PeptideAtlas; Q8R2U4; -.
DR PRIDE; Q8R2U4; -.
DR ProteomicsDB; 291917; -.
DR Antibodypedia; 17874; 170 antibodies from 27 providers.
DR DNASU; 66617; -.
DR Ensembl; ENSMUST00000041830; ENSMUSP00000035303; ENSMUSG00000026857.
DR GeneID; 66617; -.
DR KEGG; mmu:66617; -.
DR UCSC; uc008jcv.1; mouse.
DR CTD; 28989; -.
DR MGI; MGI:1913867; Ntmt1.
DR VEuPathDB; HostDB:ENSMUSG00000026857; -.
DR eggNOG; KOG3178; Eukaryota.
DR GeneTree; ENSGT00390000008371; -.
DR HOGENOM; CLU_055356_3_1_1; -.
DR InParanoid; Q8R2U4; -.
DR OMA; PVRMYCL; -.
DR OrthoDB; 1528533at2759; -.
DR PhylomeDB; Q8R2U4; -.
DR TreeFam; TF314174; -.
DR BioGRID-ORCS; 66617; 0 hits in 72 CRISPR screens.
DR PRO; PR:Q8R2U4; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8R2U4; protein.
DR Bgee; ENSMUSG00000026857; Expressed in saccule of membranous labyrinth and 238 other tissues.
DR ExpressionAtlas; Q8R2U4; baseline and differential.
DR Genevisible; Q8R2U4; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0042054; F:histone methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR GO; GO:0071885; F:N-terminal protein N-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008276; F:protein methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB.
DR GO; GO:0016571; P:histone methylation; ISS:UniProtKB.
DR GO; GO:0018011; P:N-terminal peptidyl-alanine methylation; IBA:GO_Central.
DR GO; GO:0018012; P:N-terminal peptidyl-alanine trimethylation; IDA:UniProtKB.
DR GO; GO:0018013; P:N-terminal peptidyl-glycine methylation; ISS: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; ISS:UniProtKB.
DR GO; GO:0035570; P:N-terminal peptidyl-serine methylation; IBA:GO_Central.
DR GO; GO:0035573; P:N-terminal peptidyl-serine trimethylation; ISS:UniProtKB.
DR GO; GO:0006480; P:N-terminal protein amino acid methylation; IBA:GO_Central.
DR GO; GO:0007051; P:spindle organization; ISS: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 Acetylation; Methyltransferase; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..223
FT /note="N-terminal Xaa-Pro-Lys N-methyltransferase 1"
FT /id="PRO_0000423229"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9BV86"
FT CHAIN 2..223
FT /note="N-terminal Xaa-Pro-Lys N-methyltransferase 1, N-
FT terminally processed"
FT /id="PRO_0000119289"
FT BINDING 69
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9BV86"
FT BINDING 74
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9BV86"
FT BINDING 91..93
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9BV86"
FT BINDING 119..120
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9BV86"
FT BINDING 135
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9BV86"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9BV86"
FT MOD_RES 2
FT /note="N-acetylthreonine; in N-terminal Xaa-Pro-Lys N-
FT methyltransferase 1, N-terminally processed"
FT /evidence="ECO:0000250|UniProtKB:Q9BV86"
SQ SEQUENCE 223 AA; 25420 MW; 07822C8CB2F65CA1 CRC64;
MTSEVIEDEK QFYSKAKTYW KQIPPTVDGM LGGYGHISNI DLNSSRKFLQ RFLREGPNKT
GTSCALDCGA GIGRITKRLL LPLFRVVDMV DVTEDFLAKA KTYLGEEGKR VRNYFCCGLQ
DFSPEPGSYD VIWIQWVIGH LTDQHLAEFL RRCKRGLRPN GIIVIKDNMA QEGVILDDVD
SSVCRDLEVV RRIIRTAGLS LLAEERQENL PDEIYHVYSF ALR
