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Q9BV86 (NTM1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
N-terminal RCC1 methyltransferase
X-Pro-Lys N-terminal protein methyltransferase 1A
Short name=NTM1A
Gene names
Name:NTMT1
Synonyms:C9orf32, METTL11A, NRMT, NRMT1
ORF Names:AD-003
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length223 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Distributive 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. 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. Ref.7 Ref.8 Ref.11

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].

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

Subcellular location

Nucleus. Note: Predominantly nuclear. Ref.8 Ref.11

Sequence similarities

Belongs to the methyltransferase superfamily. NTM1 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DIS3Q9Y2L11EBI-373016,EBI-373539

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BV86-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9BV86-2)

The sequence of this isoform differs from the canonical sequence as follows:
     111-223: VRNYFCCGLQ...IYHVYSFALR → ATSPISTWPSSCGAARAASAPTASSSSKTTWPRRA
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 223223N-terminal Xaa-Pro-Lys N-methyltransferase 1
PRO_0000423228
Initiator methionine11Removed; alternate Ref.5
Chain2 – 223222N-terminal Xaa-Pro-Lys N-methyltransferase 1, N-terminally processed
PRO_0000119288

Regions

Region91 – 933S-adenosyl-L-methionine binding
Region119 – 1202S-adenosyl-L-methionine binding

Sites

Binding site691S-adenosyl-L-methionine; via carbonyl oxygen
Binding site741S-adenosyl-L-methionine
Binding site1351S-adenosyl-L-methionine; via carbonyl oxygen

Amino acid modifications

Modified residue11N-acetylmethionine Ref.6
Modified residue21N-acetylthreonine; in N-terminal Xaa-Pro-Lys N-methyltransferase 1, N-terminally processed Ref.5 Ref.6 Ref.10

Natural variations

Alternative sequence111 – 223113VRNYF…SFALR → ATSPISTWPSSCGAARAASA PTASSSSKTTWPRRA in isoform 2.
VSP_039886

Experimental info

Mutagenesis1671D → A: Does not affect methyltransferase activity. Ref.8
Mutagenesis1681N → A: Induces a strong decrease in methyltransferase activity. Ref.8
Mutagenesis1681N → K: Loss of methyltransferase activity. Ref.8
Mutagenesis1771D → A: Induces a slight decrease in methyltransferase activity. Ref.8
Mutagenesis1771D → K: Induces a strong decrease in methyltransferase activity. Ref.8
Mutagenesis1801D → A: Induces a decrease in methyltransferase activity. Ref.8
Mutagenesis1801D → K: Induces a strong decrease in methyltransferase activity. Ref.8
Mutagenesis1821S → A: Induces a slight decrease in methyltransferase activity. Ref.8
Mutagenesis1821S → K: Induces a strong decrease in methyltransferase activity. Ref.8
Sequence conflict251P → L in BAF85021. Ref.2
Sequence conflict391S → SS in AAF14859. Ref.1
Sequence conflict1311V → A in BAF83646. Ref.2

Secondary structure

......................................... 223
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 4A0EC492D9B52C49

FASTA22325,387
        10         20         30         40         50         60 
MTSEVIEDEK QFYSKAKTYW KQIPPTVDGM LGGYGHISSI DINSSRKFLQ RFLREGPNKT 

        70         80         90        100        110        120 
GTSCALDCGA GIGRITKRLL LPLFREVDMV DITEDFLVQA KTYLGEEGKR VRNYFCCGLQ 

       130        140        150        160        170        180 
DFTPEPDSYD VIWIQWVIGH LTDQHLAEFL RRCKGSLRPN GIIVIKDNMA QEGVILDDVD 

       190        200        210        220 
SSVCRDLDVV RRIICSAGLS LLAEERQENL PDEIYHVYSF ALR 

« Hide

Isoform 2 [UniParc].

Checksum: 4D5E90507357F03B
Show »

FASTA14515,896

References

« Hide 'large scale' references
[1]"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning."
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. expand/collapse author list , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Adrenal gland.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Teratocarcinoma and Testis.
[3]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
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] (ISOFORM 1).
Tissue: Brain and Skin.
[5]Bienvenut W.V.
Submitted (OCT-2004) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-15 AND 79-85, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[6]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"Identification of protein N-terminal methyltransferases in yeast and humans."
Webb K.J., Lipson R.S., Al-Hadid Q., Whitelegge J.P., Clarke S.G.
Biochemistry 49:5225-5235(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"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, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, S-ADENOSYL-L-METHIONINE-BINDING, MUTAGENESIS OF ASP-167; ASN-168; ASP-177; ASP-180 AND SER-182.
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"NRMT2 is an N-terminal monomethylase that primes for its homologue NRMT1."
Petkowski J.J., Bonsignore L.A., Tooley J.G., Wilkey D.W., Merchant M.L., Macara I.G., Schaner Tooley C.E.
Biochem. J. 456:453-462(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[12]"The crystal structure of human AD-003 protein in complex with S-adenosyl-L-homocysteine."
Structural genomics consortium (SGC)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 2-223 IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF110776 mRNA. Translation: AAF14859.1.
AK290957 mRNA. Translation: BAF83646.1.
AK292332 mRNA. Translation: BAF85021.1.
AK298840 mRNA. Translation: BAG60968.1.
AL590369 Genomic DNA. Translation: CAI14507.1.
AL590369 Genomic DNA. Translation: CAI14508.1.
BC001396 mRNA. Translation: AAH01396.1.
BC033234 mRNA. Translation: AAH33234.1.
CCDSCCDS35160.1. [Q9BV86-1]
CCDS69682.1. [Q9BV86-2]
RefSeqNP_001273725.1. NM_001286796.1. [Q9BV86-1]
NP_001273726.1. NM_001286797.1. [Q9BV86-1]
NP_001273727.1. NM_001286798.1. [Q9BV86-1]
NP_001273728.1. NM_001286799.1. [Q9BV86-1]
NP_001273729.1. NM_001286800.1. [Q9BV86-2]
NP_001273730.1. NM_001286801.1. [Q9BV86-2]
NP_001273731.1. NM_001286802.1.
NP_001273732.1. NM_001286803.1.
NP_054783.2. NM_014064.3. [Q9BV86-1]
UniGeneHs.744027.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EX4X-ray1.75A/B2-222[»]
ProteinModelPortalQ9BV86.
SMRQ9BV86. Positions 2-223.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118810. 12 interactions.
DIPDIP-31241N.
IntActQ9BV86. 2 interactions.
STRING9606.ENSP00000361558.

PTM databases

PhosphoSiteQ9BV86.

Polymorphism databases

DMDM74761281.

Proteomic databases

MaxQBQ9BV86.
PaxDbQ9BV86.
PRIDEQ9BV86.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000372480; ENSP00000361558; ENSG00000148335. [Q9BV86-1]
ENST00000372481; ENSP00000361559; ENSG00000148335. [Q9BV86-2]
ENST00000372483; ENSP00000361561; ENSG00000148335. [Q9BV86-1]
ENST00000372486; ENSP00000361564; ENSG00000148335. [Q9BV86-1]
GeneID28989.
KEGGhsa:28989.
UCSCuc004byd.1. human. [Q9BV86-1]
uc011mbs.1. human. [Q9BV86-2]

Organism-specific databases

CTD28989.
GeneCardsGC09P132372.
H-InvDBHIX0008452.
HGNCHGNC:23373. NTMT1.
HPAHPA020092.
MIM613560. gene.
neXtProtNX_Q9BV86.
PharmGKBPA162395788.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG278169.
HOGENOMHOG000161910.
HOVERGENHBG054992.
InParanoidQ9BV86.
KOK16219.
OMAWCQWCVG.
OrthoDBEOG7ZPNM6.
PhylomeDBQ9BV86.
TreeFamTF314174.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000148335-MONOMER.

Gene expression databases

BgeeQ9BV86.
CleanExHS_METTL11A.
GenevestigatorQ9BV86.

Family and domain databases

Gene3D3.40.50.150. 1 hit.
InterProIPR008576. DUF858_MeTrfase_lik.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PANTHERPTHR12753. PTHR12753. 1 hit.
PfamPF05891. Methyltransf_PK. 1 hit.
[Graphical view]
PIRSFPIRSF016958. DUF858_MeTrfase_lik. 1 hit.
SUPFAMSSF53335. SSF53335. 1 hit.
ProtoNetSearch...

Other

ChiTaRSMETTL11A. human.
EvolutionaryTraceQ9BV86.
GenomeRNAi28989.
NextBio51905.
PROQ9BV86.
SOURCESearch...

Entry information

Entry nameNTM1A_HUMAN
AccessionPrimary (citable) accession number: Q9BV86
Secondary accession number(s): A8K4J2 expand/collapse secondary AC list , A8K8G7, Q5SZB9, Q9UI28
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 121 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM