ID   MET18_HUMAN             Reviewed;         372 AA.
AC   O95568; B2R9T5;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   24-JAN-2024, entry version 159.
DE   RecName: Full=Histidine protein methyltransferase 1 homolog {ECO:0000305|PubMed:33693809};
DE            EC=2.1.1.85 {ECO:0000269|PubMed:33693809, ECO:0000269|PubMed:35674491};
DE   AltName: Full=Arsenic-transactivated protein 2 {ECO:0000303|Ref.1};
DE            Short=AsTP2 {ECO:0000303|Ref.1};
DE   AltName: Full=Methyltransferase-like protein 18 {ECO:0000312|HGNC:HGNC:28793};
GN   Name=METTL18 {ECO:0000303|PubMed:33693809,
GN   ECO:0000312|HGNC:HGNC:28793};
GN   Synonyms=ASTP2 {ECO:0000303|Ref.1}, C1orf156
GN   {ECO:0000312|HGNC:HGNC:28793};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Wu S.-H., Cheng J., Zheng Y.-J., Liu Y., Zhang Y.-X.;
RT   "Cloning and identification of human AsTP2 gene transactivated by arsenic
RT   trioxide.";
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Rhodes S.;
RL   Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Subthalamic nucleus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA   Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA   Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72 AND SER-77, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [11]
RP   FUNCTION, AND INTERACTION WITH GRWD1; HSP70 AND HSP90 FAMILY MEMBERS.
RX   PubMed=23349634; DOI=10.1371/journal.pgen.1003210;
RA   Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.;
RT   "A newly uncovered group of distantly related lysine methyltransferases
RT   preferentially interact with molecular chaperones to regulate their
RT   activity.";
RL   PLoS Genet. 9:E1003210-E1003210(2013).
RN   [12]
RP   FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH RPL3, SUBCELLULAR LOCATION,
RP   METHYLATION AT HIS-154, MOTIF, AND MUTAGENESIS OF HIS-154; ASP-217 AND
RP   250-LYS-ARG-251.
RX   PubMed=33693809; DOI=10.1093/nar/gkab088;
RA   Malecki J.M., Odonohue M.F., Kim Y., Jakobsson M.E., Gessa L., Pinto R.,
RA   Wu J., Davydova E., Moen A., Olsen J.V., Thiede B., Gleizes P.E.,
RA   Leidel S.A., Falnes P.O.;
RT   "Human METTL18 is a histidine-specific methyltransferase that targets RPL3
RT   and affects ribosome biogenesis and function.";
RL   Nucleic Acids Res. 49:3185-3203(2021).
RN   [13]
RP   FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF 193-ASP--GLY-197.
RX   PubMed=35674491; DOI=10.7554/elife.72780;
RA   Matsuura-Suzuki E., Shimazu T., Takahashi M., Kotoshiba K., Suzuki T.,
RA   Kashiwagi K., Sohtome Y., Akakabe M., Sodeoka M., Dohmae N., Ito T.,
RA   Shinkai Y., Iwasaki S.;
RT   "METTL18-mediated histidine methylation of RPL3 modulates translation
RT   elongation for proteostasis maintenance.";
RL   Elife 11:0-0(2022).
RN   [14] {ECO:0007744|PDB:4RFQ}
RP   X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 63-372 IN COMPLEX WITH
RP   S-ADENOSYL-L-METHIONINE, AND REGION.
RA   Ravichandran M., Tempel W., Li Y., Walker J.R., Bountra C.,
RA   Arrowsmith C.H., Edwards A.M., Brown P.J., Hong B.S.;
RT   "Human Methyltransferase-Like 18.";
RL   Submitted (SEP-2014) to the PDB data bank.
CC   -!- FUNCTION: Protein-L-histidine N-tele-methyltransferase that
CC       specifically monomethylates RPL3, thereby regulating translation
CC       elongation (PubMed:23349634, PubMed:33693809, PubMed:35674491).
CC       Histidine methylation of RPL3 regulates translation elongation by
CC       slowing ribosome traversal on tyrosine codons: slower elongation
CC       provides enough time for proper folding of synthesized proteins and
CC       prevents cellular aggregation of tyrosine-rich proteins
CC       (PubMed:35674491). {ECO:0000269|PubMed:23349634,
CC       ECO:0000269|PubMed:33693809, ECO:0000269|PubMed:35674491}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-histidyl-[protein] + S-adenosyl-L-methionine = H(+) +
CC         N(tele)-methyl-L-histidyl-[protein] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:19369, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:11600,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16367, ChEBI:CHEBI:29979,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.85;
CC         Evidence={ECO:0000269|PubMed:33693809, ECO:0000269|PubMed:35674491};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19370;
CC         Evidence={ECO:0000269|PubMed:33693809, ECO:0000269|PubMed:35674491};
CC   -!- SUBUNIT: Interacts with GRWD1 and members of the heat shock protein 90
CC       and 70 families; these proteins may possibly be methylation substrates
CC       for the enzyme. {ECO:0000269|PubMed:23349634}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:33693809}.
CC       Nucleus {ECO:0000269|PubMed:33693809}. Nucleus, nucleolus
CC       {ECO:0000269|PubMed:33693809}.
CC   -!- PTM: Monomethylated at His-154 through automethylation
CC       (PubMed:33693809). Automethylation at His-154 positively regulates the
CC       methyltransferase activity toward RPL3 (PubMed:33693809). Probably
CC       methylated on other residues (PubMed:33693809).
CC       {ECO:0000269|PubMed:33693809}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. METTL18
CC       family. {ECO:0000305}.
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DR   EMBL; AY744366; AAU95377.1; -; mRNA.
DR   EMBL; AL035369; CAA23019.1; -; mRNA.
DR   EMBL; CR450330; CAG29326.1; -; mRNA.
DR   EMBL; AK313909; BAG36632.1; -; mRNA.
DR   EMBL; AL021940; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471067; EAW90861.1; -; Genomic_DNA.
DR   EMBL; BC008679; AAH08679.1; -; mRNA.
DR   CCDS; CCDS1284.1; -.
DR   RefSeq; NP_001307128.1; NM_001320199.1.
DR   RefSeq; NP_001307130.1; NM_001320201.1.
DR   RefSeq; NP_219486.1; NM_033418.3.
DR   RefSeq; XP_006711690.1; XM_006711627.3.
DR   PDB; 4RFQ; X-ray; 2.40 A; A=63-372.
DR   PDBsum; 4RFQ; -.
DR   AlphaFoldDB; O95568; -.
DR   SMR; O95568; -.
DR   BioGRID; 124936; 78.
DR   IntAct; O95568; 7.
DR   MINT; O95568; -.
DR   STRING; 9606.ENSP00000307975; -.
DR   CarbonylDB; O95568; -.
DR   iPTMnet; O95568; -.
DR   PhosphoSitePlus; O95568; -.
DR   BioMuta; METTL18; -.
DR   EPD; O95568; -.
DR   jPOST; O95568; -.
DR   MassIVE; O95568; -.
DR   MaxQB; O95568; -.
DR   PaxDb; 9606-ENSP00000307975; -.
DR   PeptideAtlas; O95568; -.
DR   ProteomicsDB; 50944; -.
DR   Pumba; O95568; -.
DR   Antibodypedia; 34368; 49 antibodies from 12 providers.
DR   DNASU; 92342; -.
DR   Ensembl; ENST00000303469.6; ENSP00000307077.2; ENSG00000171806.12.
DR   Ensembl; ENST00000310392.5; ENSP00000307975.4; ENSG00000171806.12.
DR   GeneID; 92342; -.
DR   KEGG; hsa:92342; -.
DR   MANE-Select; ENST00000310392.5; ENSP00000307975.4; NM_033418.4; NP_219486.1.
DR   UCSC; uc001ggn.6; human.
DR   AGR; HGNC:28793; -.
DR   CTD; 92342; -.
DR   DisGeNET; 92342; -.
DR   GeneCards; METTL18; -.
DR   HGNC; HGNC:28793; METTL18.
DR   HPA; ENSG00000171806; Low tissue specificity.
DR   MIM; 615255; gene.
DR   neXtProt; NX_O95568; -.
DR   OpenTargets; ENSG00000171806; -.
DR   PharmGKB; PA142672407; -.
DR   VEuPathDB; HostDB:ENSG00000171806; -.
DR   eggNOG; KOG2920; Eukaryota.
DR   GeneTree; ENSGT00390000000464; -.
DR   HOGENOM; CLU_038704_0_1_1; -.
DR   InParanoid; O95568; -.
DR   OMA; LCKCRFF; -.
DR   OrthoDB; 276605at2759; -.
DR   PhylomeDB; O95568; -.
DR   TreeFam; TF320884; -.
DR   PathwayCommons; O95568; -.
DR   SignaLink; O95568; -.
DR   BioGRID-ORCS; 92342; 27 hits in 1157 CRISPR screens.
DR   ChiTaRS; METTL18; human.
DR   GenomeRNAi; 92342; -.
DR   Pharos; O95568; Tdark.
DR   PRO; PR:O95568; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; O95568; Protein.
DR   Bgee; ENSG00000171806; Expressed in primordial germ cell in gonad and 192 other cell types or tissues.
DR   ExpressionAtlas; O95568; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR   GO; GO:0031072; F:heat shock protein binding; IPI:UniProtKB.
DR   GO; GO:0018064; F:protein-L-histidine N-tele-methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0018026; P:peptidyl-lysine monomethylation; IDA:UniProtKB.
DR   GO; GO:0090069; P:regulation of ribosome biogenesis; IMP:UniProtKB.
DR   GO; GO:2000232; P:regulation of rRNA processing; IMP:UniProtKB.
DR   GO; GO:0006417; P:regulation of translation; IMP:UniProtKB.
DR   GO; GO:0006448; P:regulation of translational elongation; IDA:UniProtKB.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR019410; Methyltransf_16.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR14614; HEPATOCELLULAR CARCINOMA-ASSOCIATED ANTIGEN; 1.
DR   PANTHER; PTHR14614:SF39; HISTIDINE PROTEIN METHYLTRANSFERASE 1 HOMOLOG; 1.
DR   Pfam; PF13489; Methyltransf_23; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   Genevisible; O95568; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Methylation; Methyltransferase; Nucleus;
KW   Phosphoprotein; Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..372
FT                   /note="Histidine protein methyltransferase 1 homolog"
FT                   /id="PRO_0000247199"
FT   REGION          30..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          68..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           247..253
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000269|PubMed:33693809"
FT   COMPBIAS        35..55
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..91
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         168..172
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000269|Ref.14, ECO:0007744|PDB:4RFQ"
FT   BINDING         195
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000269|Ref.14, ECO:0000305|PubMed:35674491,
FT                   ECO:0007744|PDB:4RFQ"
FT   BINDING         216..218
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000269|Ref.14, ECO:0007744|PDB:4RFQ"
FT   BINDING         268..270
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000269|Ref.14, ECO:0007744|PDB:4RFQ"
FT   BINDING         293
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000269|Ref.14, ECO:0007744|PDB:4RFQ"
FT   MOD_RES         72
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17525332,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         77
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         154
FT                   /note="Tele-methylhistidine; by autocatalysis"
FT                   /evidence="ECO:0000269|PubMed:33693809"
FT   VARIANT         10
FT                   /note="E -> D (in dbSNP:rs10489177)"
FT                   /id="VAR_027087"
FT   VARIANT         309
FT                   /note="F -> L (in dbSNP:rs34396097)"
FT                   /id="VAR_054050"
FT   VARIANT         318
FT                   /note="R -> H (in dbSNP:rs35984232)"
FT                   /id="VAR_054051"
FT   VARIANT         325
FT                   /note="A -> V (in dbSNP:rs16862686)"
FT                   /id="VAR_027088"
FT   VARIANT         360
FT                   /note="K -> M (in dbSNP:rs13375701)"
FT                   /id="VAR_027089"
FT   MUTAGEN         154
FT                   /note="H->A: No effect on automethylation. Loss of
FT                   protein-L-histidine N-tele-methyltransferase activity
FT                   toward RPL3."
FT                   /evidence="ECO:0000269|PubMed:33693809"
FT   MUTAGEN         193..197
FT                   /note="DLGCG->KLRCR: Abolished protein-L-histidine
FT                   N-tele-methyltransferase activity."
FT                   /evidence="ECO:0000269|PubMed:35674491"
FT   MUTAGEN         217
FT                   /note="D->A: Loss of protein-L-histidine
FT                   N-tele-methyltransferase activity."
FT                   /evidence="ECO:0000269|PubMed:33693809"
FT   MUTAGEN         250..251
FT                   /note="KR->GG: Decreased localization to the nucleus."
FT                   /evidence="ECO:0000269|PubMed:33693809"
FT   HELIX           86..88
FT                   /evidence="ECO:0007829|PDB:4RFQ"
FT   STRAND          92..94
FT                   /evidence="ECO:0007829|PDB:4RFQ"
FT   STRAND          101..103
FT                   /evidence="ECO:0007829|PDB:4RFQ"
FT   HELIX           109..113
FT                   /evidence="ECO:0007829|PDB:4RFQ"
FT   STRAND          116..120
FT                   /evidence="ECO:0007829|PDB:4RFQ"
FT   STRAND          124..126
FT                   /evidence="ECO:0007829|PDB:4RFQ"
FT   STRAND          130..138
FT                   /evidence="ECO:0007829|PDB:4RFQ"
FT   STRAND          162..164
FT                   /evidence="ECO:0007829|PDB:4RFQ"
FT   HELIX           170..181
FT                   /evidence="ECO:0007829|PDB:4RFQ"
FT   STRAND          190..194
FT                   /evidence="ECO:0007829|PDB:4RFQ"
FT   HELIX           200..207
FT                   /evidence="ECO:0007829|PDB:4RFQ"
FT   STRAND          211..218
FT                   /evidence="ECO:0007829|PDB:4RFQ"
FT   HELIX           220..225
FT                   /evidence="ECO:0007829|PDB:4RFQ"
FT   HELIX           227..233
FT                   /evidence="ECO:0007829|PDB:4RFQ"
FT   HELIX           257..262
FT                   /evidence="ECO:0007829|PDB:4RFQ"
FT   STRAND          263..268
FT                   /evidence="ECO:0007829|PDB:4RFQ"
FT   HELIX           270..278
FT                   /evidence="ECO:0007829|PDB:4RFQ"
FT   STRAND          280..283
FT                   /evidence="ECO:0007829|PDB:4RFQ"
FT   STRAND          287..294
FT                   /evidence="ECO:0007829|PDB:4RFQ"
FT   HELIX           299..301
FT                   /evidence="ECO:0007829|PDB:4RFQ"
FT   HELIX           302..312
FT                   /evidence="ECO:0007829|PDB:4RFQ"
FT   STRAND          313..326
FT                   /evidence="ECO:0007829|PDB:4RFQ"
FT   TURN            328..330
FT                   /evidence="ECO:0007829|PDB:4RFQ"
FT   HELIX           334..344
FT                   /evidence="ECO:0007829|PDB:4RFQ"
FT   STRAND          346..355
FT                   /evidence="ECO:0007829|PDB:4RFQ"
FT   STRAND          357..359
FT                   /evidence="ECO:0007829|PDB:4RFQ"
FT   STRAND          361..368
FT                   /evidence="ECO:0007829|PDB:4RFQ"
SQ   SEQUENCE   372 AA;  42148 MW;  3F0C1599035BA8B1 CRC64;
     MTFQFNFTIE DHLENELTPI RDGALTLDSS KELSVSESQK GEERDRKCSA EQFDLPQDHL
     WEHKSMENAA PSQDTDSPLS AASSSRNLEP HGKQPSLRAA KEHAMPKDLK KMLENKVIET
     LPGFQHVKLS VVKTILLKEN FPGENIVSKS FSSHSDLITG VYEGGLKIWE CTFDLLAYFT
     KAKVKFAGKK VLDLGCGSGL LGITAFKGGS KEIHFQDYNS MVIDEVTLPN VVANSTLEDE
     ENDVNEPDVK RCRKPKVTQL YKCRFFSGEW SEFCKLVLSS EKLFVKYDLI LTSETIYNPD
     YYSNLHQTFL RLLSKNGRVL LASKAHYFGV GGGVHLFQKF VEERDVFKTR ILKIIDEGLK
     RFIIEITFKF PG
//