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N-terminal Xaa-Pro-Lys N-methyltransferase 1 (EC 2.1.1.244) (Alpha N-terminal protein methyltransferase 1A) (Methyltransferase-like protein 11A) (N-terminal RCC1 methyltransferase) (X-Pro-Lys N-terminal protein methyltransferase 1A) (NTM1A) [Cleaved into: N-terminal Xaa-Pro-Lys N-methyltransferase 1, N-terminally processed]

 NTM1A_HUMAN             Reviewed;         223 AA.
Q9BV86; A8K4J2; A8K8G7; Q5SZB9; Q9UI28;
08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
18-JUL-2018, entry version 157.
RecName: Full=N-terminal Xaa-Pro-Lys N-methyltransferase 1;
EC=2.1.1.244 {ECO:0000269|PubMed:20668449};
AltName: Full=Alpha N-terminal protein methyltransferase 1A;
AltName: Full=Methyltransferase-like protein 11A;
AltName: Full=N-terminal RCC1 methyltransferase;
AltName: Full=X-Pro-Lys N-terminal protein methyltransferase 1A;
Short=NTM1A;
Contains:
RecName: Full=N-terminal Xaa-Pro-Lys N-methyltransferase 1, N-terminally processed;
Name=NTMT1; Synonyms=C9orf32, METTL11A, NRMT, NRMT1; ORFNames=AD-003;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Adrenal gland;
PubMed=10931946; DOI=10.1073/pnas.160270997;
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., 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.;
"Gene expression profiling in the human hypothalamus-pituitary-adrenal
axis and full-length cDNA cloning.";
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Teratocarcinoma, and Testis;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
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.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 2-15 AND 79-85, CLEAVAGE OF INITIATOR METHIONINE,
ACETYLATION AT THR-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V.;
Submitted (OCT-2004) to UniProtKB.
[6]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, CLEAVAGE OF
INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[7]
FUNCTION.
PubMed=20481588; DOI=10.1021/bi100428x;
Webb K.J., Lipson R.S., Al-Hadid Q., Whitelegge J.P., Clarke S.G.;
"Identification of protein N-terminal methyltransferases in yeast and
humans.";
Biochemistry 49:5225-5235(2010).
[8]
FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY,
SUBCELLULAR LOCATION, S-ADENOSYL-L-METHIONINE-BINDING, AND MUTAGENESIS
OF ASP-167; ASN-168; ASP-177; ASP-180 AND SER-182.
PubMed=20668449; DOI=10.1038/nature09343;
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.;
"NRMT is an alpha-N-methyltransferase that methylates RCC1 and
retinoblastoma protein.";
Nature 466:1125-1128(2010).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[11]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=24090352; DOI=10.1042/BJ20131163;
Petkowski J.J., Bonsignore L.A., Tooley J.G., Wilkey D.W.,
Merchant M.L., Macara I.G., Schaner Tooley C.E.;
"NRMT2 is an N-terminal monomethylase that primes for its homologue
NRMT1.";
Biochem. J. 456:453-462(2013).
[12]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 2-223 IN COMPLEX WITH
S-ADENOSYL-L-HOMOCYSTEINE.
Structural genomics consortium (SGC);
"The crystal structure of human AD-003 protein in complex with S-
adenosyl-L-homocysteine.";
Submitted (FEB-2009) to the PDB data bank.
[13] {ECO:0000244|PDB:5CVD}
X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) IN COMPLEXES WITH CENPA;
HISTONE H2B AND S-ADENOSYL-HOMOCYSTEINE, FUNCTION, CATALYTIC ACTIVITY,
AND MUTAGENESIS OF TYR-19; TRP-20; TRP-136; ASP-167; ASN-168; ASP-177
AND ASP-180.
PubMed=26543159; DOI=10.1101/gad.270926.115;
Wu R., Yue Y., Zheng X., Li H.;
"Molecular basis for histone N-terminal methylation by NRMT1.";
Genes Dev. 29:2337-2342(2015).
[14] {ECO:0000244|PDB:5E1B, ECO:0000244|PDB:5E1D, ECO:0000244|PDB:5E1M, ECO:0000244|PDB:5E1O, ECO:0000244|PDB:5E2A, ECO:0000244|PDB:5E2B}
X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEXES WITH PEPTIDE
SUBSTRATES AND S-ADENOSYL-HOMOCYSTEINE.
PubMed=26543161; DOI=10.1101/gad.270611.115;
Dong C., Mao Y., Tempel W., Qin S., Li L., Loppnau P., Huang R.,
Min J.;
"Structural basis for substrate recognition by the human N-terminal
methyltransferase 1.";
Genes Dev. 29:2343-2348(2015).
-!- 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
METTL11B-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. {ECO:0000269|PubMed:20481588,
ECO:0000269|PubMed:20668449, ECO:0000269|PubMed:24090352,
ECO:0000269|PubMed:26543159}.
-!- 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]. {ECO:0000269|PubMed:20668449,
ECO:0000269|PubMed:26543159}.
-!- CATALYTIC ACTIVITY: 2 S-adenosyl-L-methionine + N-terminal-PPK-
[protein] = 2 S-adenosyl-L-homocysteine + N-terminal-N,N-dimethyl-
N-PPK-[protein]. {ECO:0000269|PubMed:20668449,
ECO:0000269|PubMed:26543159}.
-!- INTERACTION:
P18754:RCC1; NbExp=4; IntAct=EBI-373016, EBI-992720;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20668449,
ECO:0000269|PubMed:24090352}. Note=Predominantly nuclear
(PubMed:24090352).
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9BV86-1; Sequence=Displayed;
Name=2;
IsoId=Q9BV86-2; Sequence=VSP_039886;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the methyltransferase superfamily. NTM1
family. {ECO:0000305}.
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EMBL; AF110776; AAF14859.1; -; mRNA.
EMBL; AK290957; BAF83646.1; -; mRNA.
EMBL; AK292332; BAF85021.1; -; mRNA.
EMBL; AK298840; BAG60968.1; -; mRNA.
EMBL; AL590369; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC001396; AAH01396.1; -; mRNA.
EMBL; BC033234; AAH33234.1; -; mRNA.
CCDS; CCDS35160.1; -. [Q9BV86-1]
CCDS; CCDS69682.1; -. [Q9BV86-2]
RefSeq; NP_001273725.1; NM_001286796.1. [Q9BV86-1]
RefSeq; NP_001273726.1; NM_001286797.1. [Q9BV86-1]
RefSeq; NP_001273727.1; NM_001286798.1. [Q9BV86-1]
RefSeq; NP_001273728.1; NM_001286799.1. [Q9BV86-1]
RefSeq; NP_001273729.1; NM_001286800.1. [Q9BV86-2]
RefSeq; NP_001273730.1; NM_001286801.1. [Q9BV86-2]
RefSeq; NP_001273731.1; NM_001286802.1.
RefSeq; NP_001273732.1; NM_001286803.1.
RefSeq; NP_054783.2; NM_014064.3. [Q9BV86-1]
UniGene; Hs.744027; -.
PDB; 2EX4; X-ray; 1.75 A; A/B=2-222.
PDB; 5CVD; X-ray; 1.30 A; A/B=1-223.
PDB; 5CVE; X-ray; 1.50 A; A/B=1-223.
PDB; 5E1B; X-ray; 1.65 A; A/B=2-223.
PDB; 5E1D; X-ray; 1.45 A; A/B=2-223.
PDB; 5E1M; X-ray; 1.75 A; A/B=2-223.
PDB; 5E1O; X-ray; 2.00 A; A/B=2-223.
PDB; 5E2A; X-ray; 1.75 A; A/B=2-223.
PDB; 5E2B; X-ray; 1.95 A; A/B=2-223.
PDBsum; 2EX4; -.
PDBsum; 5CVD; -.
PDBsum; 5CVE; -.
PDBsum; 5E1B; -.
PDBsum; 5E1D; -.
PDBsum; 5E1M; -.
PDBsum; 5E1O; -.
PDBsum; 5E2A; -.
PDBsum; 5E2B; -.
ProteinModelPortal; Q9BV86; -.
SMR; Q9BV86; -.
BioGrid; 118810; 25.
DIP; DIP-31241N; -.
IntAct; Q9BV86; 8.
STRING; 9606.ENSP00000361558; -.
iPTMnet; Q9BV86; -.
PhosphoSitePlus; Q9BV86; -.
DMDM; 74761281; -.
EPD; Q9BV86; -.
MaxQB; Q9BV86; -.
PaxDb; Q9BV86; -.
PeptideAtlas; Q9BV86; -.
PRIDE; Q9BV86; -.
ProteomicsDB; 79180; -.
ProteomicsDB; 79181; -. [Q9BV86-2]
TopDownProteomics; Q9BV86-1; -. [Q9BV86-1]
Ensembl; ENST00000372480; ENSP00000361558; ENSG00000148335. [Q9BV86-1]
Ensembl; ENST00000372481; ENSP00000361559; ENSG00000148335. [Q9BV86-2]
Ensembl; ENST00000372483; ENSP00000361561; ENSG00000148335. [Q9BV86-1]
Ensembl; ENST00000372486; ENSP00000361564; ENSG00000148335. [Q9BV86-1]
Ensembl; ENST00000611055; ENSP00000483489; ENSG00000148335. [Q9BV86-1]
Ensembl; ENST00000613644; ENSP00000478521; ENSG00000148335. [Q9BV86-1]
GeneID; 28989; -.
KEGG; hsa:28989; -.
UCSC; uc004byd.3; human. [Q9BV86-1]
CTD; 28989; -.
EuPathDB; HostDB:ENSG00000148335.14; -.
GeneCards; NTMT1; -.
H-InvDB; HIX0008452; -.
HGNC; HGNC:23373; NTMT1.
HPA; HPA020092; -.
HPA; HPA058420; -.
MIM; 613560; gene.
neXtProt; NX_Q9BV86; -.
OpenTargets; ENSG00000148335; -.
PharmGKB; PA162395788; -.
eggNOG; KOG3178; Eukaryota.
eggNOG; ENOG410XS7T; LUCA.
GeneTree; ENSGT00390000008371; -.
HOGENOM; HOG000161910; -.
HOVERGEN; HBG054992; -.
InParanoid; Q9BV86; -.
KO; K16219; -.
OMA; PVYMIAC; -.
OrthoDB; EOG091G0NA7; -.
PhylomeDB; Q9BV86; -.
TreeFam; TF314174; -.
BioCyc; MetaCyc:ENSG00000148335-MONOMER; -.
BRENDA; 2.1.1.244; 2681.
ChiTaRS; NTMT1; human.
EvolutionaryTrace; Q9BV86; -.
GenomeRNAi; 28989; -.
PRO; PR:Q9BV86; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000148335; -.
CleanEx; HS_METTL11A; -.
ExpressionAtlas; Q9BV86; baseline and differential.
Genevisible; Q9BV86; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0042054; F:histone methyltransferase activity; IDA:UniProtKB.
GO; GO:0071885; F:N-terminal protein N-methyltransferase activity; IDA:UniProtKB.
GO; GO:0008276; F:protein methyltransferase activity; IDA:UniProtKB.
GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB.
GO; GO:0016571; P:histone methylation; IDA:UniProtKB.
GO; GO:0018011; P:N-terminal peptidyl-alanine methylation; IBA:GO_Central.
GO; GO:0018012; P:N-terminal peptidyl-alanine trimethylation; IEA:Ensembl.
GO; GO:0018013; P:N-terminal peptidyl-glycine methylation; IDA:UniProtKB.
GO; GO:0018016; P:N-terminal peptidyl-proline dimethylation; IDA:UniProtKB.
GO; GO:0035572; P:N-terminal peptidyl-serine dimethylation; IDA:UniProtKB.
GO; GO:0035573; P:N-terminal peptidyl-serine trimethylation; IDA:UniProtKB.
GO; GO:0007051; P:spindle organization; IMP:UniProtKB.
InterPro; IPR008576; MeTrfase_NTM1.
InterPro; IPR029063; SAM-dependent_MTases.
PANTHER; PTHR12753; PTHR12753; 1.
Pfam; PF05891; Methyltransf_PK; 1.
PIRSF; PIRSF016958; DUF858_MeTrfase_lik; 1.
SUPFAM; SSF53335; SSF53335; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Direct protein sequencing; Methyltransferase; Nucleus;
Reference proteome; S-adenosyl-L-methionine; Transferase.
CHAIN 1 223 N-terminal Xaa-Pro-Lys N-
methyltransferase 1.
/FTId=PRO_0000423228.
INIT_MET 1 1 Removed; alternate.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000269|Ref.5}.
CHAIN 2 223 N-terminal Xaa-Pro-Lys N-
methyltransferase 1, N-terminally
processed.
/FTId=PRO_0000119288.
REGION 91 93 S-adenosyl-L-methionine binding.
{ECO:0000244|PDB:2EX4,
ECO:0000244|PDB:5CVD,
ECO:0000244|PDB:5CVE,
ECO:0000244|PDB:5E1D,
ECO:0000244|PDB:5E1M,
ECO:0000244|PDB:5E1O,
ECO:0000244|PDB:5E2A,
ECO:0000244|PDB:5E2B,
ECO:0000269|PubMed:26543159,
ECO:0000269|PubMed:26543161}.
REGION 119 120 S-adenosyl-L-methionine binding.
{ECO:0000244|PDB:2EX4,
ECO:0000244|PDB:5CVD,
ECO:0000244|PDB:5CVE,
ECO:0000244|PDB:5E1D,
ECO:0000244|PDB:5E1M,
ECO:0000244|PDB:5E1O,
ECO:0000244|PDB:5E2A,
ECO:0000244|PDB:5E2B,
ECO:0000269|PubMed:26543159,
ECO:0000269|PubMed:26543161}.
BINDING 69 69 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000244|PDB:2EX4,
ECO:0000244|PDB:5CVD,
ECO:0000244|PDB:5CVE,
ECO:0000244|PDB:5E1D,
ECO:0000244|PDB:5E1M,
ECO:0000244|PDB:5E1O,
ECO:0000244|PDB:5E2A,
ECO:0000244|PDB:5E2B,
ECO:0000269|PubMed:26543159,
ECO:0000269|PubMed:26543161}.
BINDING 74 74 S-adenosyl-L-methionine.
{ECO:0000244|PDB:2EX4,
ECO:0000244|PDB:5CVD,
ECO:0000244|PDB:5CVE,
ECO:0000244|PDB:5E1D,
ECO:0000244|PDB:5E1M,
ECO:0000244|PDB:5E1O,
ECO:0000244|PDB:5E2A,
ECO:0000244|PDB:5E2B,
ECO:0000269|PubMed:26543159,
ECO:0000269|PubMed:26543161}.
BINDING 135 135 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000244|PDB:2EX4,
ECO:0000244|PDB:5CVD,
ECO:0000244|PDB:5CVE,
ECO:0000244|PDB:5E1D,
ECO:0000244|PDB:5E1M,
ECO:0000244|PDB:5E1O,
ECO:0000244|PDB:5E2A,
ECO:0000244|PDB:5E2B,
ECO:0000269|PubMed:26543159,
ECO:0000269|PubMed:26543161}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 2 2 N-acetylthreonine; in N-terminal Xaa-Pro-
Lys N-methyltransferase 1, N-terminally
processed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000269|Ref.5}.
VAR_SEQ 111 223 VRNYFCCGLQDFTPEPDSYDVIWIQWVIGHLTDQHLAEFLR
RCKGSLRPNGIIVIKDNMAQEGVILDDVDSSVCRDLDVVRR
IICSAGLSLLAEERQENLPDEIYHVYSFALR -> ATSPIS
TWPSSCGAARAASAPTASSSSKTTWPRRA (in isoform
2). {ECO:0000303|PubMed:14702039}.
/FTId=VSP_039886.
MUTAGEN 19 19 Y->A,F: Decreased methyltransferase
activity with CENPA.
{ECO:0000269|PubMed:26543159}.
MUTAGEN 19 19 Y->A: Reduced methyltransferase activity
with CENPA.
{ECO:0000269|PubMed:26543159}.
MUTAGEN 20 20 W->A,M,Y: Nearly abolishes
methyltransferase activity with CENPA.
{ECO:0000269|PubMed:26543159}.
MUTAGEN 136 136 W->L: Strongly reduces methyltransferase
activity with CENPA.
{ECO:0000269|PubMed:26543159}.
MUTAGEN 167 167 D->A: Does not affect methyltransferase
activity. {ECO:0000269|PubMed:20668449}.
MUTAGEN 167 167 D->N,Q: Abolishes methyltransferase
activity with CENPA.
{ECO:0000269|PubMed:26543159}.
MUTAGEN 168 168 N->A: Decreased methyltransferase
activity. {ECO:0000269|PubMed:20668449,
ECO:0000269|PubMed:26543159}.
MUTAGEN 168 168 N->K: Loss of methyltransferase activity.
{ECO:0000269|PubMed:20668449}.
MUTAGEN 177 177 D->A: Induces a slight decrease in
methyltransferase activity.
{ECO:0000269|PubMed:20668449}.
MUTAGEN 177 177 D->K: Induces a strong decrease in
methyltransferase activity.
{ECO:0000269|PubMed:20668449}.
MUTAGEN 177 177 D->N: Strongly reduces methyltransferase
activity with CENPA.
{ECO:0000269|PubMed:26543159}.
MUTAGEN 180 180 D->A: Induces a decrease in
methyltransferase activity.
{ECO:0000269|PubMed:20668449}.
MUTAGEN 180 180 D->K: Induces a strong decrease in
methyltransferase activity.
{ECO:0000269|PubMed:20668449}.
MUTAGEN 180 180 D->N: Reduced methyltransferase activity
with CENPA.
{ECO:0000269|PubMed:26543159}.
MUTAGEN 182 182 S->A: Induces a slight decrease in
methyltransferase activity.
{ECO:0000269|PubMed:20668449}.
MUTAGEN 182 182 S->K: Induces a strong decrease in
methyltransferase activity.
{ECO:0000269|PubMed:20668449}.
CONFLICT 25 25 P -> L (in Ref. 2; BAF85021).
{ECO:0000305}.
CONFLICT 39 39 S -> SS (in Ref. 1; AAF14859).
{ECO:0000305}.
CONFLICT 131 131 V -> A (in Ref. 2; BAF83646).
{ECO:0000305}.
HELIX 2 4 {ECO:0000244|PDB:5CVD}.
HELIX 9 21 {ECO:0000244|PDB:5CVD}.
HELIX 27 30 {ECO:0000244|PDB:5CVD}.
TURN 31 33 {ECO:0000244|PDB:5CVD}.
HELIX 35 37 {ECO:0000244|PDB:5CVD}.
HELIX 38 54 {ECO:0000244|PDB:5CVD}.
STRAND 55 58 {ECO:0000244|PDB:5CVD}.
STRAND 63 68 {ECO:0000244|PDB:5CVD}.
TURN 71 73 {ECO:0000244|PDB:5CVD}.
HELIX 74 78 {ECO:0000244|PDB:5CVD}.
TURN 79 83 {ECO:0000244|PDB:5CVD}.
STRAND 85 92 {ECO:0000244|PDB:5CVD}.
HELIX 94 103 {ECO:0000244|PDB:5CVD}.
HELIX 105 110 {ECO:0000244|PDB:5CVD}.
STRAND 111 116 {ECO:0000244|PDB:5CVD}.
HELIX 119 121 {ECO:0000244|PDB:5CVD}.
STRAND 129 136 {ECO:0000244|PDB:5CVD}.
HELIX 138 140 {ECO:0000244|PDB:5CVD}.
HELIX 143 156 {ECO:0000244|PDB:5CVD}.
STRAND 157 177 {ECO:0000244|PDB:5CVD}.
TURN 178 181 {ECO:0000244|PDB:5CVD}.
STRAND 182 186 {ECO:0000244|PDB:5CVD}.
HELIX 187 196 {ECO:0000244|PDB:5CVD}.
STRAND 200 206 {ECO:0000244|PDB:5CVD}.
STRAND 216 223 {ECO:0000244|PDB:5CVD}.
SEQUENCE 223 AA; 25387 MW; 4A0EC492D9B52C49 CRC64;
MTSEVIEDEK QFYSKAKTYW KQIPPTVDGM LGGYGHISSI DINSSRKFLQ RFLREGPNKT
GTSCALDCGA GIGRITKRLL LPLFREVDMV DITEDFLVQA KTYLGEEGKR VRNYFCCGLQ
DFTPEPDSYD VIWIQWVIGH LTDQHLAEFL RRCKGSLRPN GIIVIKDNMA QEGVILDDVD
SSVCRDLDVV RRIICSAGLS LLAEERQENL PDEIYHVYSF ALR


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