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Q9BV86

- NTM1A_HUMAN

UniProt

Q9BV86 - NTM1A_HUMAN

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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

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-proline dimethylation Source: UniProtKB
  3. N-terminal peptidyl-serine dimethylation Source: UniProtKB
  4. N-terminal peptidyl-serine trimethylation Source: UniProtKB
  5. spindle organization Source: UniProtKB
Complete GO annotation...

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
Complete GO annotation...

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.
ExpressionAtlasiQ9BV86. baseline and differential.
GenevestigatoriQ9BV86.

Organism-specific databases

HPAiHPA020092.

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

BioGridi118810. 14 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 – 54Combined sources
Helixi9 – 2113Combined sources
Helixi27 – 304Combined sources
Turni31 – 333Combined sources
Helixi35 – 373Combined sources
Helixi38 – 5013Combined sources
Helixi51 – 533Combined sources
Beta strandi63 – 686Combined sources
Turni71 – 733Combined sources
Helixi74 – 785Combined sources
Turni79 – 835Combined sources
Beta strandi85 – 928Combined sources
Helixi94 – 10310Combined sources
Helixi105 – 1106Combined sources
Beta strandi111 – 1166Combined sources
Helixi119 – 1213Combined sources
Beta strandi129 – 1368Combined sources
Helixi138 – 1403Combined sources
Helixi143 – 15614Combined sources
Beta strandi157 – 17721Combined sources
Turni178 – 1814Combined sources
Beta strandi182 – 1865Combined sources
Helixi187 – 19610Combined sources
Beta strandi200 – 2067Combined sources
Beta strandi216 – 2227Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000008371.
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

        10         20         30         40         50
MTSEVIEDEK QFYSKAKTYW KQIPPTVDGM LGGYGHISSI DINSSRKFLQ
60 70 80 90 100
RFLREGPNKT GTSCALDCGA GIGRITKRLL LPLFREVDMV DITEDFLVQA
110 120 130 140 150
KTYLGEEGKR VRNYFCCGLQ DFTPEPDSYD VIWIQWVIGH LTDQHLAEFL
160 170 180 190 200
RRCKGSLRPN GIIVIKDNMA QEGVILDDVD SSVCRDLDVV RRIICSAGLS
210 220
LLAEERQENL PDEIYHVYSF ALR
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:
EMBLi
GenBanki
DDBJi
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]
ENST00000611055; ENSP00000483489; ENSG00000148335. [Q9BV86-1]
ENST00000613644; ENSP00000478521; 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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 14 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 ]
ENST00000611055 ; ENSP00000483489 ; ENSG00000148335 . [Q9BV86-1 ]
ENST00000613644 ; ENSP00000478521 ; 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.
GeneTreei ENSGT00390000008371.
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

EvolutionaryTracei Q9BV86.
GenomeRNAii 28989.
NextBioi 51905.
PROi Q9BV86.
SOURCEi Search...

Gene expression databases

Bgeei Q9BV86.
CleanExi HS_METTL11A.
ExpressionAtlasi Q9BV86. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 124 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