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N-terminal Xaa-Pro-Lys N-methyltransferase 1 (EC 2.1.1.244) (Alpha N-terminal protein methyltransferase 1A) (Methyltransferase-like protein 11A) (X-Pro-Lys N-terminal protein methyltransferase 1A) (NTM1A) [Cleaved into: N-terminal Xaa-Pro-Lys N-methyltransferase 1, N-terminally processed]

 NTM1A_MOUSE             Reviewed;         223 AA.
Q8R2U4; A2APZ4;
08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
12-SEP-2018, entry version 123.
RecName: Full=N-terminal Xaa-Pro-Lys N-methyltransferase 1;
EC=2.1.1.244 {ECO:0000269|PubMed:20668449};
AltName: Full=Alpha N-terminal protein methyltransferase 1A;
AltName: Full=Methyltransferase-like protein 11A;
AltName: Full=X-Pro-Lys N-terminal protein methyltransferase 1A;
Short=NTM1A;
Contains:
RecName: Full=N-terminal Xaa-Pro-Lys N-methyltransferase 1, N-terminally processed;
Name=Ntmt1; Synonyms=Mettl11a;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=NOD; TISSUE=Dendritic cell;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Czech II; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Heart, Liver, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=20668449; DOI=10.1038/nature09343;
Tooley C.E., Petkowski J.J., Muratore-Schroeder T.L., Balsbaugh J.L.,
Shabanowitz J., Sabat M., Minor W., Hunt D.F., Macara I.G.;
"NRMT is an alpha-N-methyltransferase that methylates RCC1 and
retinoblastoma protein.";
Nature 466:1125-1128(2010).
-!- FUNCTION: Distributive alpha-N-methyltransferase that methylates
the N-terminus of target proteins containing the N-terminal motif
[Ala/Gly/Pro/Ser]-Pro-Lys when the initiator Met is cleaved.
Specifically catalyzes mono-, di- or tri-methylation of the
exposed alpha-amino group of the Ala, Gly or Ser residue in the
[Ala/Gly/Ser]-Pro-Lys motif and mono- or di-methylation of Pro in
the Pro-Pro-Lys motif (PubMed:20668449). Some of the substrates
may be primed by METTL11B-mediated monomethylation. Catalyzes the
trimethylation of the N-terminal Gly in CENPA (after removal of
Met-1) (By similarity). Responsible for the N-terminal methylation
of KLHL31, MYL2, MYL3, RB1, RCC1, RPL23A and SET. Required during
mitosis for normal bipolar spindle formation and chromosome
segregation via its action on RCC1 (PubMed:20668449).
{ECO:0000250|UniProtKB:Q9BV86, ECO:0000269|PubMed:20668449}.
-!- CATALYTIC ACTIVITY: 3 S-adenosyl-L-methionine + N-terminal-
(A,S)PK-[protein] = 3 S-adenosyl-L-homocysteine + N-terminal-
N,N,N-trimethyl-N-(A,S)PK-[protein].
{ECO:0000269|PubMed:20668449}.
-!- CATALYTIC ACTIVITY: 2 S-adenosyl-L-methionine + N-terminal-PPK-
[protein] = 2 S-adenosyl-L-homocysteine + N-terminal-N,N-dimethyl-
N-PPK-[protein]. {ECO:0000269|PubMed:20668449}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BV86}.
Note=Predominantly nuclear. {ECO:0000250|UniProtKB:Q9BV86}.
-!- SIMILARITY: Belongs to the methyltransferase superfamily. NTM1
family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AK154783; BAE32826.1; -; mRNA.
EMBL; AL844532; CAM17872.1; -; Genomic_DNA.
EMBL; CH466542; EDL08489.1; -; Genomic_DNA.
EMBL; CH466542; EDL08490.1; -; Genomic_DNA.
EMBL; BC027220; AAH27220.1; -; mRNA.
CCDS; CCDS15886.1; -.
RefSeq; NP_733480.1; NM_170592.2.
RefSeq; XP_006498289.1; XM_006498226.3.
UniGene; Mm.33167; -.
ProteinModelPortal; Q8R2U4; -.
SMR; Q8R2U4; -.
STRING; 10090.ENSMUSP00000035303; -.
PhosphoSitePlus; Q8R2U4; -.
EPD; Q8R2U4; -.
MaxQB; Q8R2U4; -.
PaxDb; Q8R2U4; -.
PeptideAtlas; Q8R2U4; -.
PRIDE; Q8R2U4; -.
Ensembl; ENSMUST00000041830; ENSMUSP00000035303; ENSMUSG00000026857.
GeneID; 66617; -.
KEGG; mmu:66617; -.
UCSC; uc008jcv.1; mouse.
CTD; 28989; -.
MGI; MGI:1913867; Ntmt1.
eggNOG; KOG3178; Eukaryota.
eggNOG; ENOG410XS7T; LUCA.
GeneTree; ENSGT00390000008371; -.
HOGENOM; HOG000161910; -.
HOVERGEN; HBG054992; -.
InParanoid; Q8R2U4; -.
KO; K16219; -.
OMA; PVYMIAC; -.
OrthoDB; EOG091G0NA7; -.
PhylomeDB; Q8R2U4; -.
TreeFam; TF314174; -.
PRO; PR:Q8R2U4; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000026857; Expressed in 260 organ(s), highest expression level in ear vesicle.
ExpressionAtlas; Q8R2U4; baseline and differential.
Genevisible; Q8R2U4; MM.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0042054; F:histone methyltransferase activity; ISS:UniProtKB.
GO; GO:0071885; F:N-terminal protein N-methyltransferase activity; ISS:UniProtKB.
GO; GO:0008276; F:protein methyltransferase activity; IDA:UniProtKB.
GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB.
GO; GO:0016571; P:histone methylation; ISS:UniProtKB.
GO; GO:0018012; P:N-terminal peptidyl-alanine trimethylation; IDA:UniProtKB.
GO; GO:0018013; P:N-terminal peptidyl-glycine methylation; ISS:UniProtKB.
GO; GO:0018016; P:N-terminal peptidyl-proline dimethylation; IDA:UniProtKB.
GO; GO:0035572; P:N-terminal peptidyl-serine dimethylation; ISS:UniProtKB.
GO; GO:0035570; P:N-terminal peptidyl-serine methylation; IBA:GO_Central.
GO; GO:0035573; P:N-terminal peptidyl-serine trimethylation; ISS:UniProtKB.
GO; GO:0007051; P:spindle organization; ISS:UniProtKB.
InterPro; IPR008576; MeTrfase_NTM1.
InterPro; IPR029063; SAM-dependent_MTases.
PANTHER; PTHR12753; PTHR12753; 1.
Pfam; PF05891; Methyltransf_PK; 1.
PIRSF; PIRSF016958; DUF858_MeTrfase_lik; 1.
SUPFAM; SSF53335; SSF53335; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Methyltransferase; Nucleus;
Reference proteome; S-adenosyl-L-methionine; Transferase.
CHAIN 1 223 N-terminal Xaa-Pro-Lys N-
methyltransferase 1.
/FTId=PRO_0000423229.
INIT_MET 1 1 Removed; alternate.
{ECO:0000250|UniProtKB:Q9BV86}.
CHAIN 2 223 N-terminal Xaa-Pro-Lys N-
methyltransferase 1, N-terminally
processed.
/FTId=PRO_0000119289.
REGION 91 93 S-adenosyl-L-methionine binding.
{ECO:0000250|UniProtKB:Q9BV86}.
REGION 119 120 S-adenosyl-L-methionine binding.
{ECO:0000250|UniProtKB:Q9BV86}.
BINDING 69 69 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000250|UniProtKB:Q9BV86}.
BINDING 74 74 S-adenosyl-L-methionine.
{ECO:0000250|UniProtKB:Q9BV86}.
BINDING 135 135 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000250|UniProtKB:Q9BV86}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:Q9BV86}.
MOD_RES 2 2 N-acetylthreonine; in N-terminal Xaa-Pro-
Lys N-methyltransferase 1, N-terminally
processed.
{ECO:0000250|UniProtKB:Q9BV86}.
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


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