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Protein

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

Gene

Ntmt1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Some of the substrates may be primed by METTL11B-mediated monomethylation. Required during mitosis for normal bipolar spindle formation and chromosome segregation via its action on RCC1 (By similarity). Responsible for the N-terminal methylation of KLHL31, MYL2, MYL3, RB1, RCC1, RPL23A and SET.By similarity1 Publication

Catalytic activityi

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].
2 S-adenosyl-L-methionine + N-terminal-PPK-[protein] = 2 S-adenosyl-L-homocysteine + N-terminal-N,N-dimethyl-N-PPK-[protein].

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei69 – 691S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
Binding sitei74 – 741S-adenosyl-L-methionineBy similarity
Binding sitei135 – 1351S-adenosyl-L-methionine; via carbonyl oxygenBy similarity

GO - Molecular functioni

  • protein methyltransferase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
N-terminal Xaa-Pro-Lys N-methyltransferase 1 (EC:2.1.1.244)
Alternative name(s):
Alpha N-terminal protein methyltransferase 1A
Methyltransferase-like protein 11A
X-Pro-Lys N-terminal protein methyltransferase 1A
Short name:
NTM1A
Cleaved into the following chain:
Gene namesi
Name:Ntmt1
Synonyms:Mettl11a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1913867. Ntmt1.

Subcellular locationi

  • Nucleus By similarity

  • Note: Predominantly nuclear.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 223223N-terminal Xaa-Pro-Lys N-methyltransferase 1PRO_0000119289Add
BLAST
Initiator methionineiRemoved; alternateBy similarity
Chaini2 – 223222N-terminal Xaa-Pro-Lys N-methyltransferase 1, N-terminally processedPRO_0000423229Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei2 – 21N-acetylthreonine; in N-terminal Xaa-Pro-Lys N-methyltransferase 1, N-terminally processedBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ8R2U4.
MaxQBiQ8R2U4.
PaxDbiQ8R2U4.
PRIDEiQ8R2U4.

PTM databases

PhosphoSiteiQ8R2U4.

Expressioni

Gene expression databases

BgeeiQ8R2U4.
ExpressionAtlasiQ8R2U4. baseline and differential.
GenevisibleiQ8R2U4. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000035303.

Structurei

3D structure databases

ProteinModelPortaliQ8R2U4.
SMRiQ8R2U4. Positions 2-223.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni91 – 933S-adenosyl-L-methionine bindingBy similarity
Regioni119 – 1202S-adenosyl-L-methionine bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3178. Eukaryota.
ENOG410XS7T. LUCA.
GeneTreeiENSGT00390000008371.
HOGENOMiHOG000161910.
HOVERGENiHBG054992.
InParanoidiQ8R2U4.
KOiK16219.
OMAiGHLTDDH.
OrthoDBiEOG7ZPNM6.
PhylomeDBiQ8R2U4.
TreeFamiTF314174.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR008576. MeTrfase_NTM1.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR12753. PTHR12753. 1 hit.
PfamiPF05891. Methyltransf_PK. 1 hit.
[Graphical view]
PIRSFiPIRSF016958. DUF858_MeTrfase_lik. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8R2U4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSEVIEDEK QFYSKAKTYW KQIPPTVDGM LGGYGHISNI DLNSSRKFLQ
60 70 80 90 100
RFLREGPNKT GTSCALDCGA GIGRITKRLL LPLFRVVDMV DVTEDFLAKA
110 120 130 140 150
KTYLGEEGKR VRNYFCCGLQ DFSPEPGSYD VIWIQWVIGH LTDQHLAEFL
160 170 180 190 200
RRCKRGLRPN GIIVIKDNMA QEGVILDDVD SSVCRDLEVV RRIIRTAGLS
210 220
LLAEERQENL PDEIYHVYSF ALR
Length:223
Mass (Da):25,420
Last modified:January 23, 2007 - v3
Checksum:i07822C8CB2F65CA1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK154783 mRNA. Translation: BAE32826.1.
AL844532 Genomic DNA. Translation: CAM17872.1.
CH466542 Genomic DNA. Translation: EDL08489.1.
CH466542 Genomic DNA. Translation: EDL08490.1.
BC027220 mRNA. Translation: AAH27220.1.
CCDSiCCDS15886.1.
RefSeqiNP_733480.1. NM_170592.2.
XP_006498289.1. XM_006498226.2.
UniGeneiMm.33167.

Genome annotation databases

EnsembliENSMUST00000041830; ENSMUSP00000035303; ENSMUSG00000026857.
GeneIDi66617.
KEGGimmu:66617.
UCSCiuc008jcv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK154783 mRNA. Translation: BAE32826.1.
AL844532 Genomic DNA. Translation: CAM17872.1.
CH466542 Genomic DNA. Translation: EDL08489.1.
CH466542 Genomic DNA. Translation: EDL08490.1.
BC027220 mRNA. Translation: AAH27220.1.
CCDSiCCDS15886.1.
RefSeqiNP_733480.1. NM_170592.2.
XP_006498289.1. XM_006498226.2.
UniGeneiMm.33167.

3D structure databases

ProteinModelPortaliQ8R2U4.
SMRiQ8R2U4. Positions 2-223.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000035303.

PTM databases

PhosphoSiteiQ8R2U4.

Proteomic databases

EPDiQ8R2U4.
MaxQBiQ8R2U4.
PaxDbiQ8R2U4.
PRIDEiQ8R2U4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000041830; ENSMUSP00000035303; ENSMUSG00000026857.
GeneIDi66617.
KEGGimmu:66617.
UCSCiuc008jcv.1. mouse.

Organism-specific databases

CTDi28989.
MGIiMGI:1913867. Ntmt1.

Phylogenomic databases

eggNOGiKOG3178. Eukaryota.
ENOG410XS7T. LUCA.
GeneTreeiENSGT00390000008371.
HOGENOMiHOG000161910.
HOVERGENiHBG054992.
InParanoidiQ8R2U4.
KOiK16219.
OMAiGHLTDDH.
OrthoDBiEOG7ZPNM6.
PhylomeDBiQ8R2U4.
TreeFamiTF314174.

Miscellaneous databases

NextBioi322184.
PROiQ8R2U4.
SOURCEiSearch...

Gene expression databases

BgeeiQ8R2U4.
ExpressionAtlasiQ8R2U4. baseline and differential.
GenevisibleiQ8R2U4. MM.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR008576. MeTrfase_NTM1.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR12753. PTHR12753. 1 hit.
PfamiPF05891. Methyltransf_PK. 1 hit.
[Graphical view]
PIRSFiPIRSF016958. DUF858_MeTrfase_lik. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: NOD.
    Tissue: Dendritic cell.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Czech II.
    Tissue: Mammary tumor.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Liver, Spleen and Testis.
  6. "NRMT is an alpha-N-methyltransferase that methylates RCC1 and retinoblastoma protein."
    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.
    Nature 466:1125-1128(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiNTM1A_MOUSE
AccessioniPrimary (citable) accession number: Q8R2U4
Secondary accession number(s): A2APZ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 110 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.