MET18_HUMAN
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 03-AUG-2022, entry version 152.
DE RecName: Full=Histidine protein methyltransferase 1 homolog {ECO:0000305|PubMed:33693809};
DE EC=2.1.1.85 {ECO:0000269|PubMed:33693809};
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:0000312|HGNC:HGNC:28793};
GN Synonyms=ASTP2 {ECO:0000303|Ref.1}, C1orf156 {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] {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 (PubMed:23349634, PubMed:33693809).
CC Through the methylation of RPL3 regulates the dynamics of pre-rRNA
CC processing, ribosome biogenesis, and translation (PubMed:33693809).
CC {ECO:0000269|PubMed:23349634, ECO:0000269|PubMed:33693809}.
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};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19370;
CC Evidence={ECO:0000269|PubMed:33693809};
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; O95568; -.
DR PeptideAtlas; O95568; -.
DR PRIDE; O95568; -.
DR ProteomicsDB; 50944; -.
DR Antibodypedia; 34368; 44 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 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; CKCRFFS; -.
DR OrthoDB; 803097at2759; -.
DR PhylomeDB; O95568; -.
DR TreeFam; TF320884; -.
DR PathwayCommons; O95568; -.
DR SignaLink; O95568; -.
DR BioGRID-ORCS; 92342; 27 hits in 1079 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 calcaneal tendon and 191 other tissues.
DR ExpressionAtlas; O95568; baseline and differential.
DR Genevisible; O95568; HS.
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:0042038; P:peptidyl-histidine methylation, to form tele-methylhistidine; IBA:GO_Central.
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 Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR019410; Methyltransf_16.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR14614; PTHR14614; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
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.13, ECO:0007744|PDB:4RFQ"
FT BINDING 195
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|Ref.13, 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.13, 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.13, ECO:0007744|PDB:4RFQ"
FT BINDING 293
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|Ref.13, 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 protein-
FT L-histidine N-tele-methyltransferase activity toward RPL3."
FT /evidence="ECO:0000269|PubMed:33693809"
FT MUTAGEN 217
FT /note="D->A: Loss of protein-L-histidine N-tele-
FT 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
