TFB2M_HUMAN
ID TFB2M_HUMAN Reviewed; 396 AA.
AC Q9H5Q4; Q9H626;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Dimethyladenosine transferase 2, mitochondrial {ECO:0000305};
DE EC=2.1.1.- {ECO:0000305|PubMed:17031457};
DE AltName: Full=Hepatitis C virus NS5A-transactivated protein 5;
DE Short=HCV NS5A-transactivated protein 5;
DE AltName: Full=Mitochondrial 12S rRNA dimethylase 2;
DE AltName: Full=Mitochondrial transcription factor B2;
DE Short=h-mtTFB;
DE Short=h-mtTFB2;
DE Short=hTFB2M;
DE Short=mtTFB2;
DE AltName: Full=S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase 2;
DE Flags: Precursor;
GN Name=TFB2M {ECO:0000312|HGNC:HGNC:18559}; Synonyms=NS5ATP5;
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 Liu Y., Cheng J., Wang G., Wang J., Zhang L., Chen J., Li L.;
RT "Cloning and identification of human gene 5 transactivated by hepatitis C
RT virus NS5A protein.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Small intestine;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [5]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH POLRMT.
RX PubMed=12068295; DOI=10.1038/ng909;
RA Falkenberg M., Gaspari M., Rantanen A., Trifunovic A., Larsson N.-G.,
RA Gustafsson C.M.;
RT "Mitochondrial transcription factors B1 and B2 activate transcription of
RT human mtDNA.";
RL Nat. Genet. 31:289-294(2002).
RN [6]
RP FUNCTION, INTERACTION WITH TFAM, AND SAM-BINDING.
RX PubMed=12897151; DOI=10.1128/mcb.23.16.5816-5824.2003;
RA McCulloch V., Shadel G.S.;
RT "Human mitochondrial transcription factor B1 interacts with the C-terminal
RT activation region of h-mtTFA and stimulates transcription independently of
RT its RNA methyltransferase activity.";
RL Mol. Cell. Biol. 23:5816-5824(2003).
RN [7]
RP FUNCTION.
RX PubMed=15526033; DOI=10.1038/sj.emboj.7600465;
RA Gaspari M., Falkenberg M., Larsson N.-G., Gustafsson C.M.;
RT "The mitochondrial RNA polymerase contributes critically to promoter
RT specificity in mammalian cells.";
RL EMBO J. 23:4606-4614(2004).
RN [8]
RP INDUCTION.
RX PubMed=15684387; DOI=10.1128/mcb.25.4.1354-1366.2005;
RA Gleyzer N., Vercauteren K., Scarpulla R.C.;
RT "Control of mitochondrial transcription specificity factors (TFB1M and
RT TFB2M) by nuclear respiratory factors (NRF-1 and NRF-2) and PGC-1 family
RT coactivators.";
RL Mol. Cell. Biol. 25:1354-1366(2005).
RN [9]
RP ENZYME ACTIVITY, MUTAGENESIS OF GLY-105, AND FUNCTION.
RX PubMed=17031457; DOI=10.1007/s00239-006-0075-1;
RA Cotney J., Shadel G.S.;
RT "Evidence for an early gene duplication event in the evolution of the
RT mitochondrial transcription factor B family and maintenance of rRNA
RT methyltransferase activity in human mtTFB1 and mtTFB2.";
RL J. Mol. Evol. 63:707-717(2006).
RN [10]
RP FUNCTION.
RX PubMed=20410300; DOI=10.1074/jbc.c110.128918;
RA Litonin D., Sologub M., Shi Y., Savkina M., Anikin M., Falkenberg M.,
RA Gustafsson C.M., Temiakov D.;
RT "Human mitochondrial transcription revisited: only TFAM and TFB2M are
RT required for transcription of the mitochondrial genes in vitro.";
RL J. Biol. Chem. 285:18129-18133(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12] {ECO:0007744|PDB:6ERO, ECO:0007744|PDB:6ERP, ECO:0007744|PDB:6ERQ}
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 63-267 AND 295-396 IN COMPLEX
RP WITH POLRMT; TFAM AND DNA, SUBUNIT, MUTAGENESIS OF ARG-330 AND ARG-331,
RP REGION, AND FUNCTION.
RX PubMed=29149603; DOI=10.1016/j.cell.2017.10.036;
RA Hillen H.S., Morozov Y.I., Sarfallah A., Temiakov D., Cramer P.;
RT "Structural Basis of Mitochondrial Transcription Initiation.";
RL Cell 171:1072-1081.e10(2017).
RN [13]
RP VARIANTS THR-64 AND TYR-264.
RX PubMed=19096125; DOI=10.1155/2008/575323;
RA Alonso-Montes C., Castro M.G., Reguero J.R., Perrot A., Ozcelik C.,
RA Geier C., Posch M.G., Moris C., Alvarez V., Ruiz-Ortega M., Coto E.;
RT "Mitochondrial transcription factors TFA, TFB1 and TFB2: a search for DNA
RT variants/haplotypes and the risk of cardiac hypertrophy.";
RL Dis. Markers 25:131-139(2008).
RN [14]
RP VARIANTS PHE-48 AND THR-64.
RX PubMed=18980857; DOI=10.1016/j.parkreldis.2008.09.004;
RA Sanchez-Ferrero E., Coto E., Blazquez M., Ribacoba R., Guisasola L.M.,
RA Salvador C., Alvarez V.;
RT "Mutational screening of the mitochondrial transcription factors B1 and B2
RT (TFB1M and TFB2M) in Parkinson's disease.";
RL Parkinsonism Relat. Disord. 15:468-470(2009).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent rRNA methyltransferase
CC which may methylate two specific adjacent adenosines in the loop of a
CC conserved hairpin near the 3'-end of 12S mitochondrial rRNA (Probable).
CC Component of the mitochondrial transcription initiation complex,
CC composed at least of TFB2M, TFAM and POLRMT that is required for basal
CC transcription of mitochondrial DNA (PubMed:29149603, PubMed:12068295,
CC PubMed:20410300, PubMed:15526033). In this complex, TFAM recruits
CC POLRMT to a specific promoter whereas TFB2M induces structural changes
CC in POLRMT to enable promoter opening and trapping of the DNA non-
CC template strand (PubMed:29149603, PubMed:15526033). Stimulates
CC transcription independently of the methyltransferase activity
CC (PubMed:12897151). {ECO:0000269|PubMed:12068295,
CC ECO:0000269|PubMed:12897151, ECO:0000269|PubMed:15526033,
CC ECO:0000269|PubMed:20410300, ECO:0000269|PubMed:29149603,
CC ECO:0000305|PubMed:12897151, ECO:0000305|PubMed:17031457}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine in rRNA + S-adenosyl-L-methionine = H(+) + N(6)-
CC methyladenosine in rRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:58728, Rhea:RHEA-COMP:15198, Rhea:RHEA-COMP:15199,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74449;
CC Evidence={ECO:0000305|PubMed:17031457};
CC -!- SUBUNIT: Homodimer (PubMed:29149603). Component of the mitochondrial
CC transcription initiation complex, composed at least of TFB2M, TFAM and
CC POLRMT (PubMed:29149603). In this complex TFAM recruits POLRMT to the
CC promoter whereas TFB2M induces structural changes in POLRMT to enable
CC promoter opening and trapping of the DNA non-template strand
CC (PubMed:29149603). Interacts with mitochondrial RNA polymerase POLRMT
CC (PubMed:12068295). Interacts with TFAM (PubMed:12897151).
CC {ECO:0000269|PubMed:12068295, ECO:0000269|PubMed:12897151,
CC ECO:0000269|PubMed:29149603}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:12068295}.
CC -!- INDUCTION: By the nuclear respiratory factors NRF1 and NRF2/GABPB2 and
CC PGC-1 coactivators. {ECO:0000269|PubMed:15684387}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. rRNA adenine N(6)-methyltransferase family. KsgA
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01026}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15441.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF529366; AAQ09600.1; -; mRNA.
DR EMBL; AK026314; BAB15441.1; ALT_INIT; mRNA.
DR EMBL; AK026835; BAB15566.1; -; mRNA.
DR EMBL; AL356583; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003383; AAH03383.1; -; mRNA.
DR CCDS; CCDS1627.1; -.
DR RefSeq; NP_071761.1; NM_022366.2.
DR PDB; 6ERO; X-ray; 1.75 A; A/B=63-267, A/B=295-396.
DR PDB; 6ERP; X-ray; 4.50 A; F/J=21-396.
DR PDB; 6ERQ; X-ray; 4.50 A; F/J=22-396.
DR PDBsum; 6ERO; -.
DR PDBsum; 6ERP; -.
DR PDBsum; 6ERQ; -.
DR AlphaFoldDB; Q9H5Q4; -.
DR SMR; Q9H5Q4; -.
DR BioGRID; 122106; 101.
DR ComplexPortal; CPX-7241; Mitochondrial transcription initiation complex.
DR DIP; DIP-50540N; -.
DR IntAct; Q9H5Q4; 24.
DR MINT; Q9H5Q4; -.
DR STRING; 9606.ENSP00000355471; -.
DR GlyGen; Q9H5Q4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H5Q4; -.
DR MetOSite; Q9H5Q4; -.
DR PhosphoSitePlus; Q9H5Q4; -.
DR SwissPalm; Q9H5Q4; -.
DR BioMuta; TFB2M; -.
DR DMDM; 74752681; -.
DR EPD; Q9H5Q4; -.
DR jPOST; Q9H5Q4; -.
DR MassIVE; Q9H5Q4; -.
DR MaxQB; Q9H5Q4; -.
DR PaxDb; Q9H5Q4; -.
DR PeptideAtlas; Q9H5Q4; -.
DR PRIDE; Q9H5Q4; -.
DR ProteomicsDB; 80926; -.
DR Antibodypedia; 34721; 262 antibodies from 29 providers.
DR DNASU; 64216; -.
DR Ensembl; ENST00000366514.5; ENSP00000355471.4; ENSG00000162851.8.
DR GeneID; 64216; -.
DR KEGG; hsa:64216; -.
DR MANE-Select; ENST00000366514.5; ENSP00000355471.4; NM_022366.3; NP_071761.1.
DR UCSC; uc001ibn.4; human.
DR CTD; 64216; -.
DR DisGeNET; 64216; -.
DR GeneCards; TFB2M; -.
DR HGNC; HGNC:18559; TFB2M.
DR HPA; ENSG00000162851; Low tissue specificity.
DR MIM; 607055; gene.
DR neXtProt; NX_Q9H5Q4; -.
DR OpenTargets; ENSG00000162851; -.
DR PharmGKB; PA38348; -.
DR VEuPathDB; HostDB:ENSG00000162851; -.
DR eggNOG; KOG0820; Eukaryota.
DR GeneTree; ENSGT00950000183142; -.
DR HOGENOM; CLU_051778_1_0_1; -.
DR InParanoid; Q9H5Q4; -.
DR OMA; RAQACKK; -.
DR OrthoDB; 1169941at2759; -.
DR PhylomeDB; Q9H5Q4; -.
DR TreeFam; TF325100; -.
DR PathwayCommons; Q9H5Q4; -.
DR Reactome; R-HSA-163282; Mitochondrial transcription initiation.
DR Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
DR SignaLink; Q9H5Q4; -.
DR BioGRID-ORCS; 64216; 390 hits in 1071 CRISPR screens.
DR ChiTaRS; TFB2M; human.
DR GeneWiki; TFB2M; -.
DR GenomeRNAi; 64216; -.
DR Pharos; Q9H5Q4; Tbio.
DR PRO; PR:Q9H5Q4; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9H5Q4; protein.
DR Bgee; ENSG00000162851; Expressed in secondary oocyte and 190 other tissues.
DR Genevisible; Q9H5Q4; HS.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0034246; F:mitochondrial transcription factor activity; IDA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; IBA:GO_Central.
DR GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro.
DR GO; GO:0006390; P:mitochondrial transcription; IDA:GO_Central.
DR GO; GO:0031167; P:rRNA methylation; IBA:GO_Central.
DR GO; GO:0006391; P:transcription initiation from mitochondrial promoter; IDA:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR001737; KsgA/Erm.
DR InterPro; IPR020598; rRNA_Ade_methylase_Trfase_N.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016861; TFB2M.
DR PANTHER; PTHR11727; PTHR11727; 1.
DR PANTHER; PTHR11727:SF13; PTHR11727:SF13; 1.
DR Pfam; PF00398; RrnaAD; 1.
DR SMART; SM00650; rADc; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51689; SAM_RNA_A_N6_MT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Methyltransferase; Mitochondrion; Reference proteome;
KW RNA-binding; rRNA processing; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase; Transit peptide.
FT TRANSIT 1..19
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 20..396
FT /note="Dimethyladenosine transferase 2, mitochondrial"
FT /id="PRO_0000273179"
FT REGION 44..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..331
FT /note="DNA-binding"
FT /evidence="ECO:0000269|PubMed:29149603,
FT ECO:0007744|PDB:6ERP, ECO:0007744|PDB:6ERQ"
FT BINDING 75
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 124
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 150
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT VARIANT 48
FT /note="S -> F (in dbSNP:rs148620105)"
FT /evidence="ECO:0000269|PubMed:18980857"
FT /id="VAR_071249"
FT VARIANT 64
FT /note="A -> T (in dbSNP:rs143880306)"
FT /evidence="ECO:0000269|PubMed:18980857,
FT ECO:0000269|PubMed:19096125"
FT /id="VAR_071250"
FT VARIANT 156
FT /note="P -> L (in dbSNP:rs11585481)"
FT /id="VAR_030097"
FT VARIANT 264
FT /note="H -> Y (in dbSNP:rs12037377)"
FT /evidence="ECO:0000269|PubMed:19096125"
FT /id="VAR_030098"
FT MUTAGEN 105
FT /note="G->A: Abolishes methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:17031457"
FT MUTAGEN 330
FT /note="R->A: Impairs transcription initiation; when
FT associated with A-331."
FT /evidence="ECO:0000269|PubMed:29149603"
FT MUTAGEN 331
FT /note="R->A: Impairs transcription initiation; when
FT associated with A-330."
FT /evidence="ECO:0000269|PubMed:29149603"
FT CONFLICT 200..201
FT /note="EK -> GR (in Ref. 2; BAB15441)"
FT /evidence="ECO:0000305"
FT HELIX 78..89
FT /evidence="ECO:0007829|PDB:6ERO"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:6ERO"
FT HELIX 108..115
FT /evidence="ECO:0007829|PDB:6ERO"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:6ERO"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:6ERO"
FT HELIX 130..139
FT /evidence="ECO:0007829|PDB:6ERO"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:6ERO"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:6ERO"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:6ERO"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:6ERO"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:6ERO"
FT HELIX 169..176
FT /evidence="ECO:0007829|PDB:6ERO"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:6ERO"
FT HELIX 200..213
FT /evidence="ECO:0007829|PDB:6ERO"
FT HELIX 216..220
FT /evidence="ECO:0007829|PDB:6ERO"
FT STRAND 224..230
FT /evidence="ECO:0007829|PDB:6ERO"
FT HELIX 231..237
FT /evidence="ECO:0007829|PDB:6ERO"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:6ERO"
FT HELIX 249..257
FT /evidence="ECO:0007829|PDB:6ERO"
FT STRAND 258..267
FT /evidence="ECO:0007829|PDB:6ERO"
FT STRAND 295..303
FT /evidence="ECO:0007829|PDB:6ERO"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:6ERO"
FT TURN 314..316
FT /evidence="ECO:0007829|PDB:6ERO"
FT HELIX 317..329
FT /evidence="ECO:0007829|PDB:6ERO"
FT TURN 330..332
FT /evidence="ECO:0007829|PDB:6ERO"
FT HELIX 335..339
FT /evidence="ECO:0007829|PDB:6ERO"
FT TURN 340..342
FT /evidence="ECO:0007829|PDB:6ERO"
FT HELIX 347..353
FT /evidence="ECO:0007829|PDB:6ERO"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:6ERO"
FT HELIX 367..379
FT /evidence="ECO:0007829|PDB:6ERO"
SQ SEQUENCE 396 AA; 45349 MW; C13DC398974BB88F CRC64;
MWIPVVGLPR RLRLSALAGA GRFCILGSEA ATRKHLPARN HCGLSDSSPQ LWPEPDFRNP
PRKASKASLD FKRYVTDRRL AETLAQIYLG KPSRPPHLLL ECNPGPGILT QALLEAGAKV
VALESDKTFI PHLESLGKNL DGKLRVIHCD FFKLDPRSGG VIKPPAMSSR GLFKNLGIEA
VPWTADIPLK VVGMFPSRGE KRALWKLAYD LYSCTSIYKF GRIEVNMFIG EKEFQKLMAD
PGNPDLYHVL SVIWQLACEI KVLHMEPWSS FDIYTRKGPL ENPKRRELLD QLQQKLYLIQ
MIPRQNLFTK NLTPMNYNIF FHLLKHCFGR RSATVIDHLR SLTPLDARDI LMQIGKQEDE
KVVNMHPQDF KTLFETIERS KDCAYKWLYD ETLEDR
