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Q9BV86

- NTM1A_HUMAN

UniProt

Q9BV86 - NTM1A_HUMAN

Protein

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

Gene

NTMT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    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 RCC1.3 Publications

    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 oxygen
    Binding sitei74 – 741S-adenosyl-L-methionine
    Binding sitei135 – 1351S-adenosyl-L-methionine; via carbonyl oxygen

    GO - Molecular functioni

    1. protein methyltransferase activity Source: UniProtKB

    GO - Biological processi

    1. chromosome segregation Source: UniProtKB
    2. N-terminal peptidyl-alanine trimethylation Source: Ensembl
    3. N-terminal peptidyl-proline dimethylation Source: UniProtKB
    4. N-terminal peptidyl-serine dimethylation Source: UniProtKB
    5. N-terminal peptidyl-serine trimethylation Source: UniProtKB
    6. spindle organization Source: UniProtKB

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Enzyme and pathway databases

    BioCyciMetaCyc:ENSG00000148335-MONOMER.

    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
    N-terminal RCC1 methyltransferase
    X-Pro-Lys N-terminal protein methyltransferase 1A
    Short name:
    NTM1A
    Cleaved into the following chain:
    Gene namesi
    Name:NTMT1
    Synonyms:C9orf32, METTL11A, NRMT, NRMT1
    ORF Names:AD-003
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:23373. NTMT1.

    Subcellular locationi

    Nucleus 2 Publications
    Note: Predominantly nuclear.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi167 – 1671D → A: Does not affect methyltransferase activity. 1 Publication
    Mutagenesisi168 – 1681N → A: Induces a strong decrease in methyltransferase activity. 1 Publication
    Mutagenesisi168 – 1681N → K: Loss of methyltransferase activity. 1 Publication
    Mutagenesisi177 – 1771D → A: Induces a slight decrease in methyltransferase activity. 1 Publication
    Mutagenesisi177 – 1771D → K: Induces a strong decrease in methyltransferase activity. 1 Publication
    Mutagenesisi180 – 1801D → A: Induces a decrease in methyltransferase activity. 1 Publication
    Mutagenesisi180 – 1801D → K: Induces a strong decrease in methyltransferase activity. 1 Publication
    Mutagenesisi182 – 1821S → A: Induces a slight decrease in methyltransferase activity. 1 Publication
    Mutagenesisi182 – 1821S → K: Induces a strong decrease in methyltransferase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA162395788.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 223223N-terminal Xaa-Pro-Lys N-methyltransferase 1PRO_0000423228Add
    BLAST
    Initiator methioninei1 – 11Removed; alternate2 Publications
    Chaini2 – 223222N-terminal Xaa-Pro-Lys N-methyltransferase 1, N-terminally processedPRO_0000119288Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei2 – 21N-acetylthreonine; in N-terminal Xaa-Pro-Lys N-methyltransferase 1, N-terminally processed3 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9BV86.
    PaxDbiQ9BV86.
    PRIDEiQ9BV86.

    PTM databases

    PhosphoSiteiQ9BV86.

    Expressioni

    Gene expression databases

    BgeeiQ9BV86.
    CleanExiHS_METTL11A.
    GenevestigatoriQ9BV86.

    Organism-specific databases

    HPAiHPA020092.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DIS3Q9Y2L11EBI-373016,EBI-373539

    Protein-protein interaction databases

    BioGridi118810. 12 interactions.
    DIPiDIP-31241N.
    IntActiQ9BV86. 2 interactions.
    STRINGi9606.ENSP00000361558.

    Structurei

    Secondary structure

    1
    223
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi2 – 54
    Helixi9 – 2113
    Helixi27 – 304
    Turni31 – 333
    Helixi35 – 373
    Helixi38 – 5013
    Helixi51 – 533
    Beta strandi63 – 686
    Turni71 – 733
    Helixi74 – 785
    Turni79 – 835
    Beta strandi85 – 928
    Helixi94 – 10310
    Helixi105 – 1106
    Beta strandi111 – 1166
    Helixi119 – 1213
    Beta strandi129 – 1368
    Helixi138 – 1403
    Helixi143 – 15614
    Beta strandi157 – 17721
    Turni178 – 1814
    Beta strandi182 – 1865
    Helixi187 – 19610
    Beta strandi200 – 2067
    Beta strandi216 – 2227

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2EX4X-ray1.75A/B2-222[»]
    ProteinModelPortaliQ9BV86.
    SMRiQ9BV86. Positions 2-223.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9BV86.

    Family & Domainsi

    Region

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

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG278169.
    HOGENOMiHOG000161910.
    HOVERGENiHBG054992.
    InParanoidiQ9BV86.
    KOiK16219.
    OMAiWCQWCVG.
    OrthoDBiEOG7ZPNM6.
    PhylomeDBiQ9BV86.
    TreeFamiTF314174.

    Family and domain databases

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

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9BV86-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MTSEVIEDEK QFYSKAKTYW KQIPPTVDGM LGGYGHISSI DINSSRKFLQ    50
    RFLREGPNKT GTSCALDCGA GIGRITKRLL LPLFREVDMV DITEDFLVQA 100
    KTYLGEEGKR VRNYFCCGLQ DFTPEPDSYD VIWIQWVIGH LTDQHLAEFL 150
    RRCKGSLRPN GIIVIKDNMA QEGVILDDVD SSVCRDLDVV RRIICSAGLS 200
    LLAEERQENL PDEIYHVYSF ALR 223
    Length:223
    Mass (Da):25,387
    Last modified:January 23, 2007 - v3
    Checksum:i4A0EC492D9B52C49
    GO
    Isoform 2 (identifier: Q9BV86-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         111-223: VRNYFCCGLQ...IYHVYSFALR → ATSPISTWPSSCGAARAASAPTASSSSKTTWPRRA

    Note: No experimental confirmation available.

    Show »
    Length:145
    Mass (Da):15,896
    Checksum:i4D5E90507357F03B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti25 – 251P → L in BAF85021. (PubMed:14702039)Curated
    Sequence conflicti39 – 391S → SS in AAF14859. (PubMed:10931946)Curated
    Sequence conflicti131 – 1311V → A in BAF83646. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei111 – 223113VRNYF…SFALR → ATSPISTWPSSCGAARAASA PTASSSSKTTWPRRA in isoform 2. 1 PublicationVSP_039886Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS35160.1. [Q9BV86-1]
    CCDS69682.1. [Q9BV86-2]
    RefSeqiNP_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]
    UniGeneiHs.744027.

    Genome annotation databases

    EnsembliENST00000372480; ENSP00000361558; ENSG00000148335. [Q9BV86-1]
    ENST00000372481; ENSP00000361559; ENSG00000148335. [Q9BV86-2]
    ENST00000372483; ENSP00000361561; ENSG00000148335. [Q9BV86-1]
    ENST00000372486; ENSP00000361564; ENSG00000148335. [Q9BV86-1]
    GeneIDi28989.
    KEGGihsa:28989.
    UCSCiuc004byd.1. human. [Q9BV86-1]
    uc011mbs.1. human. [Q9BV86-2]

    Polymorphism databases

    DMDMi74761281.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS35160.1. [Q9BV86-1 ]
    CCDS69682.1. [Q9BV86-2 ]
    RefSeqi NP_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 ]
    UniGenei Hs.744027.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2EX4 X-ray 1.75 A/B 2-222 [» ]
    ProteinModelPortali Q9BV86.
    SMRi Q9BV86. Positions 2-223.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118810. 12 interactions.
    DIPi DIP-31241N.
    IntActi Q9BV86. 2 interactions.
    STRINGi 9606.ENSP00000361558.

    PTM databases

    PhosphoSitei Q9BV86.

    Polymorphism databases

    DMDMi 74761281.

    Proteomic databases

    MaxQBi Q9BV86.
    PaxDbi Q9BV86.
    PRIDEi Q9BV86.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000372480 ; ENSP00000361558 ; ENSG00000148335 . [Q9BV86-1 ]
    ENST00000372481 ; ENSP00000361559 ; ENSG00000148335 . [Q9BV86-2 ]
    ENST00000372483 ; ENSP00000361561 ; ENSG00000148335 . [Q9BV86-1 ]
    ENST00000372486 ; ENSP00000361564 ; ENSG00000148335 . [Q9BV86-1 ]
    GeneIDi 28989.
    KEGGi hsa:28989.
    UCSCi uc004byd.1. human. [Q9BV86-1 ]
    uc011mbs.1. human. [Q9BV86-2 ]

    Organism-specific databases

    CTDi 28989.
    GeneCardsi GC09P132372.
    H-InvDB HIX0008452.
    HGNCi HGNC:23373. NTMT1.
    HPAi HPA020092.
    MIMi 613560. gene.
    neXtProti NX_Q9BV86.
    PharmGKBi PA162395788.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG278169.
    HOGENOMi HOG000161910.
    HOVERGENi HBG054992.
    InParanoidi Q9BV86.
    KOi K16219.
    OMAi WCQWCVG.
    OrthoDBi EOG7ZPNM6.
    PhylomeDBi Q9BV86.
    TreeFami TF314174.

    Enzyme and pathway databases

    BioCyci MetaCyc:ENSG00000148335-MONOMER.

    Miscellaneous databases

    ChiTaRSi METTL11A. human.
    EvolutionaryTracei Q9BV86.
    GenomeRNAii 28989.
    NextBioi 51905.
    PROi Q9BV86.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9BV86.
    CleanExi HS_METTL11A.
    Genevestigatori Q9BV86.

    Family and domain databases

    Gene3Di 3.40.50.150. 1 hit.
    InterProi IPR008576. DUF858_MeTrfase_lik.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view ]
    PANTHERi PTHR12753. PTHR12753. 1 hit.
    Pfami PF05891. Methyltransf_PK. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF016958. DUF858_MeTrfase_lik. 1 hit.
    SUPFAMi SSF53335. SSF53335. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. 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.
      , 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.
      , 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. 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. 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.

    Entry informationi

    Entry nameiNTM1A_HUMAN
    AccessioniPrimary (citable) accession number: Q9BV86
    Secondary accession number(s): A8K4J2
    , A8K8G7, Q5SZB9, Q9UI28
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 8, 2005
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 122 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3