ID NSUN4_HUMAN Reviewed; 384 AA. AC Q96CB9; A8K6S6; B3KQ50; B4DHA4; Q5TDF7; Q96AN8; Q9HAJ8; DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 29-MAY-2007, sequence version 2. DT 27-MAR-2024, entry version 152. DE RecName: Full=5-methylcytosine rRNA methyltransferase NSUN4; DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q95XR2}; DE AltName: Full=5-methylcytosine tRNA methyltransferase NSUN4 {ECO:0000305}; DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q95XR2}; DE AltName: Full=NOL1/NOP2/Sun domain family member 4; DE Flags: Precursor; GN Name=NSUN4; 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 [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4), AND VARIANTS RP ALA-51 AND VAL-365. RC TISSUE=Brain, Embryo, Placenta, and Testis; 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 [2] 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 96-384 (ISOFORM 2), AND VARIANT ALA-51. RC TISSUE=Colon, and Duodenum; 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 IDENTIFICATION BY 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 [6] 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 [7] RP FUNCTION, INTERACTION WITH MTERF4, AND SUBCELLULAR LOCATION. RX PubMed=21531335; DOI=10.1016/j.cmet.2011.04.002; RA Camara Y., Asin-Cayuela J., Park C.B., Metodiev M.D., Shi Y., RA Ruzzenente B., Kukat C., Habermann B., Wibom R., Hultenby K., Franz T., RA Erdjument-Bromage H., Tempst P., Hallberg B.M., Gustafsson C.M., RA Larsson N.G.; RT "MTERF4 regulates translation by targeting the methyltransferase NSUN4 to RT the mammalian mitochondrial ribosome."; RL Cell Metab. 13:527-539(2011). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and 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 [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 26-384 IN COMPLEX WITH MTERFD2, RP ACTIVE SITE, SUBCELLULAR LOCATION, AND MUTAGENESIS OF VAL-65; ARG-136; RP ILE-139 AND ARG-141. RX PubMed=22949673; DOI=10.1073/pnas.1210688109; RA Spahr H., Habermann B., Gustafsson C.M., Larsson N.G., Hallberg B.M.; RT "Structure of the human MTERF4-NSUN4 protein complex that regulates RT mitochondrial ribosome biogenesis."; RL Proc. Natl. Acad. Sci. U.S.A. 109:15253-15258(2012). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 26-384 IN COMPLEX WITH RP S-ADENOSYL-L-METHIONINE AND MTERFD2, FUNCTION IN METHYLATION OF 16S RRNA, RP AND SUBCELLULAR LOCATION. RX PubMed=23022348; DOI=10.1016/j.str.2012.08.027; RA Yakubovskaya E., Guja K.E., Mejia E., Castano S., Hambardjieva E., RA Choi W.S., Garcia-Diaz M.; RT "Structure of the essential MTERF4:NSUN4 protein complex reveals how an RT MTERF protein collaborates to facilitate rRNA modification."; RL Structure 20:1940-1947(2012). CC -!- FUNCTION: Involved in mitochondrial ribosome assembly. 5-methylcytosine CC rRNA methyltransferase that probably is involved in mitochondrial CC ribosome small subunit (SSU) maturation by methylation of mitochondrial CC 12S rRNA; the function is independent of MTERFD2/MTERF4 and assembled CC mitochondrial ribosome large subunit (LSU). Targeted to LSU by CC MTERFD2/MTERF4 and probably is involved in a final step in ribosome CC biogenesis to ensure that SSU and LSU are assembled. In vitro can CC methylate 16S rRNA of the LSU; the methylation is enhanced by CC MTERFD/MTERF4. {ECO:0000269|PubMed:21531335, CC ECO:0000269|PubMed:23022348}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a cytidine in rRNA + S-adenosyl-L-methionine = a 5- CC methylcytidine in rRNA + H(+) + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:61484, Rhea:RHEA-COMP:15836, Rhea:RHEA-COMP:15837, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; CC Evidence={ECO:0000250|UniProtKB:Q95XR2}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a cytidine in tRNA + S-adenosyl-L-methionine = a 5- CC methylcytidine in tRNA + H(+) + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:61468, Rhea:RHEA-COMP:13670, Rhea:RHEA-COMP:15827, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; CC Evidence={ECO:0000250|UniProtKB:Q95XR2}; CC -!- INTERACTION: CC Q96CB9-1; Q7Z6M4: MTERF4; NbExp=7; IntAct=EBI-16012886, EBI-948435; CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:21531335, CC ECO:0000269|PubMed:22949673, ECO:0000269|PubMed:23022348}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q96CB9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96CB9-2; Sequence=VSP_025972; CC Name=3; CC IsoId=Q96CB9-3; Sequence=VSP_025971, VSP_025973; CC Name=4; CC IsoId=Q96CB9-4; Sequence=VSP_045053; CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. RsmB/NOP family. {ECO:0000255|PROSITE-ProRule:PRU01023}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK021577; BAB13847.1; -; mRNA. DR EMBL; AK057420; BAG51912.1; -; mRNA. DR EMBL; AK291741; BAF84430.1; -; mRNA. DR EMBL; AK295003; BAG58065.1; -; mRNA. DR EMBL; AL122001; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471059; EAX06917.1; -; Genomic_DNA. DR EMBL; BC014441; AAH14441.1; -; mRNA. DR EMBL; BC016907; AAH16907.1; -; mRNA. DR CCDS; CCDS534.1; -. [Q96CB9-1] DR CCDS; CCDS57996.1; -. [Q96CB9-4] DR RefSeq; NP_001243056.1; NM_001256127.1. [Q96CB9-4] DR RefSeq; NP_001243057.1; NM_001256128.1. [Q96CB9-4] DR RefSeq; NP_950245.2; NM_199044.3. [Q96CB9-1] DR PDB; 4FP9; X-ray; 2.90 A; A/C/D/F=26-384. DR PDB; 4FZV; X-ray; 2.00 A; A=26-384. DR PDB; 7O9K; EM; 3.10 A; A1=1-384. DR PDB; 7O9M; EM; 2.50 A; A1=1-384. DR PDB; 7ODR; EM; 2.90 A; x=1-384. DR PDB; 7ODS; EM; 3.10 A; x=1-384. DR PDB; 7ODT; EM; 3.10 A; x=1-384. DR PDB; 7OF0; EM; 2.20 A; C=1-384. DR PDB; 7OF3; EM; 2.70 A; C=1-384. DR PDB; 7OF5; EM; 2.90 A; C=1-384. DR PDB; 7OF7; EM; 2.50 A; C=1-384. DR PDB; 7OIC; EM; 3.10 A; x=1-384. DR PDB; 7PD3; EM; 3.40 A; x=1-384. DR PDBsum; 4FP9; -. DR PDBsum; 4FZV; -. DR PDBsum; 7O9K; -. DR PDBsum; 7O9M; -. DR PDBsum; 7ODR; -. DR PDBsum; 7ODS; -. DR PDBsum; 7ODT; -. DR PDBsum; 7OF0; -. DR PDBsum; 7OF3; -. DR PDBsum; 7OF5; -. DR PDBsum; 7OF7; -. DR PDBsum; 7OIC; -. DR PDBsum; 7PD3; -. DR AlphaFoldDB; Q96CB9; -. DR EMDB; EMD-12763; -. DR EMDB; EMD-12764; -. DR EMDB; EMD-12845; -. DR EMDB; EMD-12846; -. DR EMDB; EMD-12847; -. DR EMDB; EMD-12865; -. DR EMDB; EMD-12868; -. DR EMDB; EMD-12870; -. DR EMDB; EMD-12872; -. DR EMDB; EMD-12925; -. DR EMDB; EMD-13329; -. DR SMR; Q96CB9; -. DR BioGRID; 132288; 185. DR ComplexPortal; CPX-885; MTERF4-NSUN4 mitochondiral ribosomal assembly complex. DR DIP; DIP-58104N; -. DR IntAct; Q96CB9; 32. DR MINT; Q96CB9; -. DR STRING; 9606.ENSP00000419740; -. DR iPTMnet; Q96CB9; -. DR PhosphoSitePlus; Q96CB9; -. DR SwissPalm; Q96CB9; -. DR BioMuta; NSUN4; -. DR DMDM; 152125805; -. DR EPD; Q96CB9; -. DR jPOST; Q96CB9; -. DR MassIVE; Q96CB9; -. DR MaxQB; Q96CB9; -. DR PaxDb; 9606-ENSP00000419740; -. DR PeptideAtlas; Q96CB9; -. DR ProteomicsDB; 4205; -. DR ProteomicsDB; 76175; -. [Q96CB9-1] DR ProteomicsDB; 76176; -. [Q96CB9-2] DR ProteomicsDB; 76177; -. [Q96CB9-3] DR Pumba; Q96CB9; -. DR Antibodypedia; 32791; 91 antibodies from 20 providers. DR DNASU; 387338; -. DR Ensembl; ENST00000474844.6; ENSP00000419740.1; ENSG00000117481.11. [Q96CB9-1] DR Ensembl; ENST00000537428.2; ENSP00000437758.1; ENSG00000117481.11. [Q96CB9-4] DR GeneID; 387338; -. DR KEGG; hsa:387338; -. DR MANE-Select; ENST00000474844.6; ENSP00000419740.1; NM_199044.4; NP_950245.2. DR UCSC; uc001cpr.3; human. [Q96CB9-1] DR AGR; HGNC:31802; -. DR CTD; 387338; -. DR DisGeNET; 387338; -. DR GeneCards; NSUN4; -. DR HGNC; HGNC:31802; NSUN4. DR HPA; ENSG00000117481; Tissue enriched (testis). DR MIM; 615394; gene. DR neXtProt; NX_Q96CB9; -. DR OpenTargets; ENSG00000117481; -. DR PharmGKB; PA134953046; -. DR VEuPathDB; HostDB:ENSG00000117481; -. DR eggNOG; KOG2198; Eukaryota. DR GeneTree; ENSGT00940000153665; -. DR HOGENOM; CLU_041061_3_1_1; -. DR InParanoid; Q96CB9; -. DR OrthoDB; 317522at2759; -. DR PhylomeDB; Q96CB9; -. DR TreeFam; TF321304; -. DR PathwayCommons; Q96CB9; -. DR Reactome; R-HSA-6793080; rRNA modification in the mitochondrion. DR SignaLink; Q96CB9; -. DR BioGRID-ORCS; 387338; 286 hits in 1162 CRISPR screens. DR GenomeRNAi; 387338; -. DR Pharos; Q96CB9; Tbio. DR PRO; PR:Q96CB9; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q96CB9; Protein. DR Bgee; ENSG00000117481; Expressed in sperm and 184 other cell types or tissues. DR ExpressionAtlas; Q96CB9; baseline and differential. DR GO; GO:0005762; C:mitochondrial large ribosomal subunit; IDA:MGI. DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome. DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central. DR GO; GO:0009383; F:rRNA (cytosine-C5-)-methyltransferase activity; EXP:Reactome. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW. DR GO; GO:0008649; F:rRNA methyltransferase activity; IDA:UniProtKB. DR GO; GO:0016428; F:tRNA (cytidine-5-)-methyltransferase activity; IEA:RHEA. DR GO; GO:0031167; P:rRNA methylation; IDA:UniProtKB. DR CDD; cd02440; AdoMet_MTases; 1. DR Gene3D; 6.20.240.40; -; 1. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat. DR InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom. DR InterPro; IPR023267; RCMT. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR PANTHER; PTHR46955:SF6; 5-METHYLCYTOSINE RRNA METHYLTRANSFERASE NSUN-4; 1. DR PANTHER; PTHR46955; PROTEIN CBG01349-RELATED; 1. DR Pfam; PF01189; Methyltr_RsmB-F; 1. DR PRINTS; PR02008; RCMTFAMILY. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1. DR Genevisible; Q96CB9; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Methyltransferase; Mitochondrion; KW Phosphoprotein; Reference proteome; Ribosome biogenesis; RNA-binding; KW rRNA processing; rRNA-binding; S-adenosyl-L-methionine; Transferase; KW Transit peptide. FT TRANSIT 1..25 FT /note="Mitochondrion" FT /evidence="ECO:0000269|PubMed:22949673, FT ECO:0000269|PubMed:23022348" FT CHAIN 26..384 FT /note="5-methylcytosine rRNA methyltransferase NSUN4" FT /id="PRO_0000289234" FT ACT_SITE 310 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023, FT ECO:0000269|PubMed:22949673" FT BINDING 181..187 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT BINDING 237 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023, FT ECO:0000269|PubMed:23022348" FT BINDING 255 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023, FT ECO:0000269|PubMed:23022348" FT MOD_RES 206 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..198 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_025971" FT VAR_SEQ 1..49 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045053" FT VAR_SEQ 147..384 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_025972" FT VAR_SEQ 199..219 FT /note="NLAANDLSPSRIARLQKILHS -> MLPPCCLFWPSACSLGTSCLT (in FT isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_025973" FT VARIANT 51 FT /note="T -> A (in dbSNP:rs3737744)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334" FT /id="VAR_032606" FT VARIANT 128 FT /note="N -> K (in dbSNP:rs17102152)" FT /id="VAR_032607" FT VARIANT 325 FT /note="I -> T (in dbSNP:rs13374337)" FT /id="VAR_032608" FT VARIANT 365 FT /note="I -> V (in dbSNP:rs9865)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_032609" FT MUTAGEN 65 FT /note="V->R: Disrupts complex with MTERFD2; when associated FT with A-136, R-139 and A-141." FT /evidence="ECO:0000269|PubMed:22949673" FT MUTAGEN 136 FT /note="R->A: Disrupts complex with MTERFD2; when associated FT with R-65, R-139 and A-141." FT /evidence="ECO:0000269|PubMed:22949673" FT MUTAGEN 139 FT /note="I->R: Disrupts complex with MTERFD2; when associated FT with R-65, A-136, and A-141." FT /evidence="ECO:0000269|PubMed:22949673" FT MUTAGEN 141 FT /note="R->A: Disrupts complex with MTERFD2; when associated FT with R-65, A-136 and R-139." FT /evidence="ECO:0000269|PubMed:22949673" FT CONFLICT 282 FT /note="Q -> R (in Ref. 1; BAG51912)" FT /evidence="ECO:0000305" FT HELIX 40..56 FT /evidence="ECO:0007829|PDB:4FZV" FT HELIX 57..59 FT /evidence="ECO:0007829|PDB:4FZV" FT HELIX 60..67 FT /evidence="ECO:0007829|PDB:4FZV" FT STRAND 74..77 FT /evidence="ECO:0007829|PDB:4FZV" FT HELIX 79..81 FT /evidence="ECO:0007829|PDB:4FP9" FT HELIX 83..92 FT /evidence="ECO:0007829|PDB:4FZV" FT HELIX 98..104 FT /evidence="ECO:0007829|PDB:4FZV" FT TURN 105..107 FT /evidence="ECO:0007829|PDB:4FZV" FT HELIX 121..124 FT /evidence="ECO:0007829|PDB:4FZV" FT STRAND 131..133 FT /evidence="ECO:0007829|PDB:4FZV" FT STRAND 151..158 FT /evidence="ECO:0007829|PDB:4FZV" FT HELIX 160..162 FT /evidence="ECO:0007829|PDB:4FZV" FT HELIX 163..169 FT /evidence="ECO:0007829|PDB:4FZV" FT STRAND 175..181 FT /evidence="ECO:0007829|PDB:4FZV" FT HELIX 186..193 FT /evidence="ECO:0007829|PDB:4FZV" FT STRAND 197..203 FT /evidence="ECO:0007829|PDB:4FZV" FT HELIX 207..220 FT /evidence="ECO:0007829|PDB:4FZV" FT TURN 223..227 FT /evidence="ECO:0007829|PDB:4FZV" FT STRAND 228..234 FT /evidence="ECO:0007829|PDB:4FZV" FT HELIX 238..240 FT /evidence="ECO:0007829|PDB:4FZV" FT HELIX 241..244 FT /evidence="ECO:0007829|PDB:4FZV" FT STRAND 249..255 FT /evidence="ECO:0007829|PDB:4FZV" FT HELIX 261..264 FT /evidence="ECO:0007829|PDB:4FZV" FT HELIX 275..277 FT /evidence="ECO:0007829|PDB:4FZV" FT HELIX 278..282 FT /evidence="ECO:0007829|PDB:4FZV" FT HELIX 284..297 FT /evidence="ECO:0007829|PDB:4FZV" FT STRAND 299..310 FT /evidence="ECO:0007829|PDB:4FZV" FT TURN 314..317 FT /evidence="ECO:0007829|PDB:4FZV" FT HELIX 318..332 FT /evidence="ECO:0007829|PDB:4FZV" FT STRAND 336..338 FT /evidence="ECO:0007829|PDB:4FZV" FT HELIX 342..348 FT /evidence="ECO:0007829|PDB:4FZV" FT TURN 349..351 FT /evidence="ECO:0007829|PDB:4FZV" FT STRAND 353..356 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 359..365 FT /evidence="ECO:0007829|PDB:4FZV" FT STRAND 368..370 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 375..382 FT /evidence="ECO:0007829|PDB:4FZV" SQ SEQUENCE 384 AA; 43089 MW; 4D83B6D55D65C27F CRC64; MAALTLRGVR ELLKRVDLAT VPRRHRYKKK WAATEPKFPA VRLALQNFDM TYSVQFGDLW PSIRVSLLSE QKYGALVNNF AAWDHVSAKL EQLSAKDFVN EAISHWELQS EGGQSAAPSP ASWACSPNLR CFTFDRGDIS RFPPARPGSL GVMEYYLMDA ASLLPVLALG LQPGDIVLDL CAAPGGKTLA LLQTGCCRNL AANDLSPSRI ARLQKILHSY VPEEIRDGNQ VRVTSWDGRK WGELEGDTYD RVLVDVPCTT DRHSLHEEEN NIFKRSRKKE RQILPVLQVQ LLAAGLLATK PGGHVVYSTC SLSHLQNEYV VQGAIELLAN QYSIQVQVED LTHFRRVFMD TFCFFSSCQV GELVIPNLMA NFGPMYFCKM RRLT //