NSUN4_HUMAN
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 03-AUG-2022, entry version 143.
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}.
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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 SMR; Q96CB9; -.
DR BioGRID; 132288; 177.
DR DIP; DIP-58104N; -.
DR IntAct; Q96CB9; 31.
DR MINT; Q96CB9; -.
DR STRING; 9606.ENSP00000419740; -.
DR iPTMnet; Q96CB9; -.
DR PhosphoSitePlus; Q96CB9; -.
DR BioMuta; NSUN4; -.
DR DMDM; 152125805; -.
DR EPD; Q96CB9; -.
DR jPOST; Q96CB9; -.
DR MassIVE; Q96CB9; -.
DR MaxQB; Q96CB9; -.
DR PaxDb; Q96CB9; -.
DR PeptideAtlas; Q96CB9; -.
DR PRIDE; Q96CB9; -.
DR ProteomicsDB; 4205; -.
DR ProteomicsDB; 76175; -. [Q96CB9-1]
DR ProteomicsDB; 76176; -. [Q96CB9-2]
DR ProteomicsDB; 76177; -. [Q96CB9-3]
DR Antibodypedia; 32791; 71 antibodies from 19 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 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; 1239772at2759; -.
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; 262 hits in 1082 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 182 other tissues.
DR ExpressionAtlas; Q96CB9; baseline and differential.
DR Genevisible; Q96CB9; HS.
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; IDA:UniProtKB.
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:0001510; P:RNA methylation; IBA:GO_Central.
DR GO; GO:0031167; P:rRNA methylation; IDA:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR001678; MeTrfase_RsmB/NOP2.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22808; PTHR22808; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
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
