CPLM-020228

Genbank Nucleotide ID

N-terminal Xaa-Pro-Lys N-methyltransferase 1

Protein Synonyms/Alias

Alpha N-terminal protein methyltransferase 1A; Methyltransferase-like protein 11A; N-terminal RCC1 methyltransferase; X-Pro-Lys N-terminal protein methyltransferase 1A; NTM1A; N-terminal Xaa-Pro-Lys N-methyltransferase 1, N-terminally processed

C9orf32; METTL11A; NRMT; AD-003

Homo sapiens (Human)

Position	Peptide	Type	References
10	SEVIEDEKQFYSKAK	ubiquitination	[1, 2]
17	KQFYSKAKTYWKQIP	ubiquitination	[2]
59	FLREGPNKTGTSCAL	ubiquitination	[2, 3, 4, 5, 6]
109	TYLGEEGKRVRNYFC	ubiquitination	[2, 3]

[1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[4] Global identification of modular cullin-RING ligase substrates.
Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
[5] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
[6] Integrated proteomic analysis of post-translational modifications by serial enrichment.
Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]

Functional Description

Alpha-N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]- Pro-Lys when the initiator Met is cleaved. Specifically catalyzes mono-, di- or tri-methylation of exposed alpha-amino group of Ala or Ser residue in the [Ala/Ser]-Pro-Lys motif and mono- or di- methylation of Pro in the Pro-Pro-Lys motif. 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.

REGION 91 93 S-adenosyl-L-methionine binding.
REGION 119 120 S-adenosyl-L-methionine binding.
BINDING 69 69 S-adenosyl-L-methionine; via carbonyl
BINDING 74 74 S-adenosyl-L-methionine.
BINDING 135 135 S-adenosyl-L-methionine; via carbonyl
MOD_RES 1 1 N-acetylmethionine.
MOD_RES 2 2 N-acetylthreonine; in N-terminal Xaa-Pro-

3D-structure; Acetylation; Alternative splicing; Complete proteome; Direct protein sequencing; Methyltransferase; Nucleus; Reference proteome; S-adenosyl-L-methionine; Transferase.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005737; C:cytoplasm; IDA:HPA.
GO:0005634; C:nucleus; IDA:UniProtKB.
GO:0008276; F:protein methyltransferase activity; IDA:UniProtKB.
GO:0007059; P:chromosome segregation; IMP:UniProtKB.
GO:0018012; P:N-terminal peptidyl-alanine trimethylation; IEA:Compara.
GO:0018016; P:N-terminal peptidyl-proline dimethylation; IDA:UniProtKB.
GO:0035572; P:N-terminal peptidyl-serine dimethylation; IDA:UniProtKB.
GO:0035573; P:N-terminal peptidyl-serine trimethylation; IDA:UniProtKB.
GO:0007051; P:spindle organization; IMP:UniProtKB.

IPR008576; DUF858_MeTrfase_lik.

PF05891; Methyltransf_PK