Overview
| Uniprot ID | Q9BV86 |
|---|
| Protein Name | N-terminal Xaa-Pro-Lys N-methyltransferase 1 |
|---|
| Gene Name | NTMT1 |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 15 |
DEKQFYSKAKTYWKQ |
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. Some of the substrates may be primed by NTMT2-mediated monomethylation (PubMed:24090352). Catalyzes the trimethylation of the N-terminal Gly in CENPA (after removal of Met-1). 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
Protein Sequence
10
MTSEVIEDEK
20
QFYSKAKTYW
30
KQIPPTVDGM
40
LGGYGHISSI
50
DINSSRKFLQ
60
RFLREGPNKT
70
GTSCALDCGA
80
GIGRITKRLL
90
LPLFREVDMV
100
DITEDFLVQA
110
KTYLGEEGKR
120
VRNYFCCGLQ
130
DFTPEPDSYD
140
VIWIQWVIGH
150
LTDQHLAEFL
160
RRCKGSLRPN
170
GIIVIKDNMA
180
QEGVILDDVD
190
SSVCRDLDVV
200
RRIICSAGLS
210
LLAEERQENL
220
PDEIYHVYSF
ALR
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0005829 |
cytosol |
| Cellular Component |
GO:0005654 |
nucleoplasm |
| Cellular Component |
GO:0005634 |
nucleus |
| Molecular Function |
GO:0042054 |
histone methyltransferase activity |
| Molecular Function |
GO:0071885 |
N-terminal protein N-methyltransferase activity |
| Molecular Function |
GO:0008276 |
protein methyltransferase activity |
| Biological Process |
GO:0007059 |
chromosome segregation |
| Biological Process |
GO:0018013 |
N-terminal peptidyl-glycine methylation |
| Biological Process |
GO:0018016 |
N-terminal peptidyl-proline dimethylation |
| Biological Process |
GO:0035572 |
N-terminal peptidyl-serine dimethylation |
| Biological Process |
GO:0035573 |
N-terminal peptidyl-serine trimethylation |
| Biological Process |
GO:0007051 |
spindle organization |
Reference
[1] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.