NSUN5_HUMAN
ID NSUN5_HUMAN Reviewed; 429 AA.
AC Q96P11; B3KX04; B4DP79; G3V0G9; Q6ZUI8; Q96HT9; Q9NW70;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=28S rRNA (cytosine-C(5))-methyltransferase {ECO:0000305};
DE EC=2.1.1.- {ECO:0000269|PubMed:31722427};
DE AltName: Full=NOL1-related protein {ECO:0000312|HGNC:HGNC:16385};
DE Short=NOL1R {ECO:0000312|HGNC:HGNC:16385};
DE AltName: Full=NOL1/NOP2/Sun domain family member 5 {ECO:0000303|PubMed:23913415};
DE AltName: Full=Williams-Beuren syndrome chromosomal region 20A protein {ECO:0000303|PubMed:12073013};
GN Name=NSUN5 {ECO:0000303|PubMed:23913415, ECO:0000312|HGNC:HGNC:16385};
GN Synonyms=NSUN5A {ECO:0000312|HGNC:HGNC:16385},
GN WBSCR20 {ECO:0000303|PubMed:11978965},
GN WBSCR20A {ECO:0000303|PubMed:12073013};
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=11978965; DOI=10.1159/000057012;
RA Doll A., Grzeschik K.-H.;
RT "Characterization of two novel genes, WBSCR20 and WBSCR22, deleted in
RT Williams-Beuren syndrome.";
RL Cytogenet. Cell Genet. 95:20-27(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RX PubMed=12073013; DOI=10.1007/s00439-002-0710-x;
RA Merla G., Ucla C., Guipponi M., Reymond A.;
RT "Identification of additional transcripts in the Williams-Beuren syndrome
RT critical region.";
RL Hum. Genet. 110:429-438(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 4 AND 5).
RC TISSUE=Embryo, Mammary tumor, and Uterus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung;
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 [7]
RP PROTEIN SEQUENCE OF 2-17; 46-61 AND 73-82, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT GLY-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Hepatoma;
RA Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.;
RL Submitted (JUL-2007) to UniProtKB.
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167, AND IDENTIFICATION BY
RP 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.
RX PubMed=23913415; DOI=10.1093/nar/gkt679;
RA Sharma S., Yang J., Watzinger P., Kotter P., Entian K.D.;
RT "Yeast Nop2 and Rcm1 methylate C2870 and C2278 of the 25S rRNA,
RT respectively.";
RL Nucleic Acids Res. 41:9062-9076(2013).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RX PubMed=31428936; DOI=10.1007/s00401-019-02062-4;
RA Janin M., Ortiz-Barahona V., de Moura M.C., Martinez-Cardus A.,
RA Llinas-Arias P., Soler M., Nachmani D., Pelletier J., Schumann U.,
RA Calleja-Cervantes M.E., Moran S., Guil S., Bueno-Costa A., Pineyro D.,
RA Perez-Salvia M., Rossello-Tortella M., Pique L., Bech-Serra J.J.,
RA De La Torre C., Vidal A., Martinez-Iniesta M., Martin-Tejera J.F.,
RA Villanueva A., Arias A., Cuartas I., Aransay A.M., La Madrid A.M.,
RA Carcaboso A.M., Santa-Maria V., Mora J., Fernandez A.F., Fraga M.F.,
RA Aldecoa I., Pedrosa L., Graus F., Vidal N., Martinez-Soler F., Tortosa A.,
RA Carrato C., Balana C., Boudreau M.W., Hergenrother P.J., Koetter P.,
RA Entian K.D., Hench J., Frank S., Mansouri S., Zadeh G., Dans P.D.,
RA Orozco M., Thomas G., Blanco S., Seoane J., Preiss T., Pandolfi P.P.,
RA Esteller M.;
RT "Epigenetic loss of RNA-methyltransferase NSUN5 in glioma targets ribosomes
RT to drive a stress adaptive translational program.";
RL Acta Neuropathol. 138:1053-1074(2019).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF CYS-308 AND CYS-359.
RX PubMed=31722427; DOI=10.1093/nar/gkz1043;
RA Heissenberger C., Liendl L., Nagelreiter F., Gonskikh Y., Yang G.,
RA Stelzer E.M., Krammer T.L., Micutkova L., Vogt S., Kreil D.P., Sekot G.,
RA Siena E., Poser I., Harreither E., Linder A., Ehret V., Helbich T.H.,
RA Grillari-Voglauer R., Jansen-Duerr P., Kos M., Polacek N., Grillari J.,
RA Schosserer M.;
RT "Loss of the ribosomal RNA methyltransferase NSUN5 impairs global protein
RT synthesis and normal growth.";
RL Nucleic Acids Res. 47:11807-11825(2019).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 127-429 IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE.
RG Structural genomics consortium (SGC);
RT "The crystal structure of human NSUN5 protein in complex with S-adenosyl-L-
RT methionine.";
RL Submitted (MAR-2006) to the PDB data bank.
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC specifically methylates the C(5) position of cytosine 3782 (m5C3782) in
CC 28S rRNA (PubMed:23913415, PubMed:31428936, PubMed:31722427). m5C3782
CC promotes protein translation without affecting ribosome biogenesis and
CC fidelity (PubMed:31428936, PubMed:31722427). Required for corpus
CC callosum and cerebral cortex development (By similarity).
CC {ECO:0000250|UniProtKB:Q8K4F6, ECO:0000269|PubMed:23913415,
CC ECO:0000269|PubMed:31428936, ECO:0000269|PubMed:31722427}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(3782) in 28S rRNA + S-adenosyl-L-methionine = 5-
CC methylcytidine(3782) in 28S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:47784, Rhea:RHEA-COMP:11913, Rhea:RHEA-COMP:11914,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748;
CC Evidence={ECO:0000269|PubMed:31428936, ECO:0000269|PubMed:31722427};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47785;
CC Evidence={ECO:0000269|PubMed:31428936, ECO:0000269|PubMed:31722427};
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:31722427}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q96P11-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96P11-2; Sequence=VSP_021756;
CC Name=3;
CC IsoId=Q96P11-3; Sequence=VSP_021752, VSP_021753, VSP_021754,
CC VSP_021755;
CC Name=4;
CC IsoId=Q96P11-4; Sequence=VSP_043352;
CC Name=5;
CC IsoId=Q96P11-5; Sequence=VSP_045492;
CC -!- TISSUE SPECIFICITY: Ubiquitous (PubMed:11978965, PubMed:12073013).
CC Detected in placenta, heart and skeletal muscle (PubMed:11978965,
CC PubMed:12073013). {ECO:0000269|PubMed:11978965,
CC ECO:0000269|PubMed:12073013}.
CC -!- INDUCTION: Down-regulated in some glioma; epigenetic inactivation is a
CC hallmark of glioma patients with long-term survival.
CC {ECO:0000269|PubMed:31428936}.
CC -!- DISEASE: Note=NSUN5 is located in the Williams-Beuren syndrome (WBS)
CC critical region (PubMed:11978965, PubMed:12073013). WBS results from a
CC hemizygous deletion of several genes on chromosome 7q11.23, thought to
CC arise as a consequence of unequal crossing over between highly
CC homologous low-copy repeat sequences flanking the deleted region
CC (PubMed:11978965, PubMed:12073013). Its deletion in WBS results in
CC decreased methylation of the C(5) position of cytosine 3782 (m5C3782)
CC in 28S rRNA (PubMed:31722427). {ECO:0000269|PubMed:11978965,
CC ECO:0000269|PubMed:12073013, ECO:0000269|PubMed:31722427}.
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; AF420249; AAL16067.1; -; mRNA.
DR EMBL; AF412028; AAM62310.1; -; mRNA.
DR EMBL; AK001129; BAA91515.1; -; mRNA.
DR EMBL; AK125667; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK126375; BAG54316.1; -; mRNA.
DR EMBL; AK298221; BAG60491.1; -; mRNA.
DR EMBL; AC073841; AAQ96838.1; -; Genomic_DNA.
DR EMBL; AC073841; AAQ96839.1; -; Genomic_DNA.
DR EMBL; CH471200; EAW69694.1; -; Genomic_DNA.
DR EMBL; BC008084; AAH08084.1; -; mRNA.
DR CCDS; CCDS55118.1; -. [Q96P11-5]
DR CCDS; CCDS55119.1; -. [Q96P11-4]
DR CCDS; CCDS5546.1; -. [Q96P11-2]
DR CCDS; CCDS5547.1; -. [Q96P11-1]
DR RefSeq; NP_001161819.1; NM_001168347.2. [Q96P11-4]
DR RefSeq; NP_001161820.1; NM_001168348.2. [Q96P11-5]
DR RefSeq; NP_060514.1; NM_018044.4. [Q96P11-1]
DR RefSeq; NP_683759.1; NM_148956.3. [Q96P11-2]
DR PDB; 2B9E; X-ray; 1.65 A; A=127-429.
DR PDBsum; 2B9E; -.
DR AlphaFoldDB; Q96P11; -.
DR SMR; Q96P11; -.
DR BioGRID; 120820; 41.
DR IntAct; Q96P11; 17.
DR MINT; Q96P11; -.
DR STRING; 9606.ENSP00000309126; -.
DR ChEMBL; CHEMBL4802014; -.
DR GlyGen; Q96P11; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96P11; -.
DR PhosphoSitePlus; Q96P11; -.
DR BioMuta; NSUN5; -.
DR DMDM; 118573085; -.
DR EPD; Q96P11; -.
DR jPOST; Q96P11; -.
DR MassIVE; Q96P11; -.
DR MaxQB; Q96P11; -.
DR PaxDb; Q96P11; -.
DR PeptideAtlas; Q96P11; -.
DR PRIDE; Q96P11; -.
DR ProteomicsDB; 32194; -.
DR ProteomicsDB; 77590; -. [Q96P11-1]
DR ProteomicsDB; 77591; -. [Q96P11-2]
DR ProteomicsDB; 77592; -. [Q96P11-3]
DR ProteomicsDB; 77593; -. [Q96P11-4]
DR Antibodypedia; 14275; 91 antibodies from 22 providers.
DR DNASU; 55695; -.
DR Ensembl; ENST00000252594.10; ENSP00000252594.6; ENSG00000130305.17. [Q96P11-1]
DR Ensembl; ENST00000310326.8; ENSP00000309126.8; ENSG00000130305.17. [Q96P11-4]
DR Ensembl; ENST00000428206.5; ENSP00000393081.1; ENSG00000130305.17. [Q96P11-5]
DR Ensembl; ENST00000438747.7; ENSP00000388464.2; ENSG00000130305.17. [Q96P11-2]
DR GeneID; 55695; -.
DR KEGG; hsa:55695; -.
DR MANE-Select; ENST00000438747.7; ENSP00000388464.2; NM_148956.4; NP_683759.1. [Q96P11-2]
DR UCSC; uc003txv.5; human. [Q96P11-1]
DR CTD; 55695; -.
DR DisGeNET; 55695; -.
DR GeneCards; NSUN5; -.
DR HGNC; HGNC:16385; NSUN5.
DR HPA; ENSG00000130305; Low tissue specificity.
DR MIM; 615732; gene.
DR neXtProt; NX_Q96P11; -.
DR OpenTargets; ENSG00000130305; -.
DR PharmGKB; PA134993779; -.
DR VEuPathDB; HostDB:ENSG00000130305; -.
DR eggNOG; KOG2360; Eukaryota.
DR GeneTree; ENSGT00940000155974; -.
DR HOGENOM; CLU_005316_7_4_1; -.
DR InParanoid; Q96P11; -.
DR OMA; IQMGKHP; -.
DR OrthoDB; 1128973at2759; -.
DR PhylomeDB; Q96P11; -.
DR TreeFam; TF314285; -.
DR PathwayCommons; Q96P11; -.
DR SignaLink; Q96P11; -.
DR BioGRID-ORCS; 55695; 28 hits in 1075 CRISPR screens.
DR ChiTaRS; NSUN5; human.
DR EvolutionaryTrace; Q96P11; -.
DR GeneWiki; NSUN5; -.
DR GenomeRNAi; 55695; -.
DR Pharos; Q96P11; Tbio.
DR PRO; PR:Q96P11; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q96P11; protein.
DR Bgee; ENSG00000130305; Expressed in granulocyte and 94 other tissues.
DR ExpressionAtlas; Q96P11; baseline and differential.
DR Genevisible; Q96P11; HS.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0009383; F:rRNA (cytosine-C5-)-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0021987; P:cerebral cortex development; ISS:UniProtKB.
DR GO; GO:0050890; P:cognition; ISS:UniProtKB.
DR GO; GO:0022038; P:corpus callosum development; ISS:UniProtKB.
DR GO; GO:0014003; P:oligodendrocyte development; ISS:UniProtKB.
DR GO; GO:0045727; P:positive regulation of translation; IMP:UniProtKB.
DR GO; GO:0031641; P:regulation of myelination; ISS:UniProtKB.
DR GO; GO:0001510; P:RNA methylation; IBA:GO_Central.
DR GO; GO:0070475; P:rRNA base 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; PTHR22807; PTHR22807; 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; Acetylation; Alternative splicing; Direct protein sequencing;
KW Methyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding; rRNA processing; S-adenosyl-L-methionine; Transferase;
KW Williams-Beuren syndrome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.7"
FT CHAIN 2..429
FT /note="28S rRNA (cytosine-C(5))-methyltransferase"
FT /id="PRO_0000261669"
FT ACT_SITE 359
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023,
FT ECO:0000305|PubMed:31722427"
FT BINDING 234..240
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 258
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023,
FT ECO:0000269|Ref.14"
FT BINDING 263
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023,
FT ECO:0000269|Ref.14"
FT BINDING 305
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023,
FT ECO:0000269|Ref.14"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000269|Ref.7"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..57
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_021752"
FT VAR_SEQ 58..72
FT /note="GLLRAEKKLRPHLAK -> MLRAFLFLSLFPHSQ (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_021753"
FT VAR_SEQ 72..109
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045492"
FT VAR_SEQ 253..381
FT /note="KIFAFDLDAKRLASMATLLARAGVSCCELAEEDFLAVSPSDPRYHEVHYILL
FT DPSCSGSGMPSRQLEEPGAGTPSPVRLHALAGFQQRALCHALTFPSLQRLVYSTCSLCQ
FT EENEDVVRDALQQNPGAF -> SLPLTWMPSGWHPWPRCWPGLASLAVNWLRRTSWRSP
FT PRIHATMRSTTSCWILPAVARVCRADSWRSPGQAHLARCVCMPWQGSSSEPCATRSLSL
FT PCSGSSTPRAPSARRRMKTWCEMRCSRTRAPSG (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_021754"
FT VAR_SEQ 382..429
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_021755"
FT VAR_SEQ 429
FT /note="R -> SSASQAKASAPERTPSPAPKRKKRQQRAAAGACTPPCT (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:12073013,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_021756"
FT VAR_SEQ 429
FT /note="R -> SLTGQSISTRTHTQPSPKEKEETAKSRSRCLHTALHIAEAPG (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043352"
FT VARIANT 183
FT /note="P -> S (in dbSNP:rs34913552)"
FT /id="VAR_051889"
FT MUTAGEN 308
FT /note="C->S: Abolished methyltransferase activity without
FT affecting nucleolar localization; when associated with S-
FT 359."
FT /evidence="ECO:0000269|PubMed:31722427"
FT MUTAGEN 359
FT /note="C->S: Abolished methyltransferase activity without
FT affecting nucleolar localization; when associated with S-
FT 308."
FT /evidence="ECO:0000269|PubMed:31722427"
FT CONFLICT 42
FT /note="E -> G (in Ref. 1; AAL16067)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="A -> P (in Ref. 1; AAL16067)"
FT /evidence="ECO:0000305"
FT CONFLICT 425
FT /note="V -> A (in Ref. 3; BAG54316)"
FT /evidence="ECO:0000305"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:2B9E"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:2B9E"
FT HELIX 147..156
FT /evidence="ECO:0007829|PDB:2B9E"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:2B9E"
FT HELIX 168..172
FT /evidence="ECO:0007829|PDB:2B9E"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:2B9E"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:2B9E"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:2B9E"
FT HELIX 201..204
FT /evidence="ECO:0007829|PDB:2B9E"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:2B9E"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:2B9E"
FT HELIX 217..222
FT /evidence="ECO:0007829|PDB:2B9E"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:2B9E"
FT HELIX 239..248
FT /evidence="ECO:0007829|PDB:2B9E"
FT STRAND 252..259
FT /evidence="ECO:0007829|PDB:2B9E"
FT HELIX 261..273
FT /evidence="ECO:0007829|PDB:2B9E"
FT STRAND 278..283
FT /evidence="ECO:0007829|PDB:2B9E"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:2B9E"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:2B9E"
FT STRAND 299..304
FT /evidence="ECO:0007829|PDB:2B9E"
FT HELIX 331..345
FT /evidence="ECO:0007829|PDB:2B9E"
FT STRAND 353..359
FT /evidence="ECO:0007829|PDB:2B9E"
FT HELIX 363..365
FT /evidence="ECO:0007829|PDB:2B9E"
FT HELIX 367..374
FT /evidence="ECO:0007829|PDB:2B9E"
FT TURN 378..380
FT /evidence="ECO:0007829|PDB:2B9E"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:2B9E"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:2B9E"
FT HELIX 401..403
FT /evidence="ECO:0007829|PDB:2B9E"
FT STRAND 404..407
FT /evidence="ECO:0007829|PDB:2B9E"
FT HELIX 409..412
FT /evidence="ECO:0007829|PDB:2B9E"
FT STRAND 416..424
FT /evidence="ECO:0007829|PDB:2B9E"
SQ SEQUENCE 429 AA; 46692 MW; E4DA635C6135298B CRC64;
MGLYAAAAGV LAGVESRQGS IKGLVYSSNF QNVKQLYALV CETQRYSAVL DAVIASAGLL
RAEKKLRPHL AKVLVYELLL GKGFRGGGGR WKALLGRHQA RLKAELARLK VHRGVSRNED
LLEVGSRPGP ASQLPRFVRV NTLKTCSDDV VDYFKRQGFS YQGRASSLDD LRALKGKHFL
LDPLMPELLV FPAQTDLHEH PLYRAGHLIL QDRASCLPAM LLDPPPGSHV IDACAAPGNK
TSHLAALLKN QGKIFAFDLD AKRLASMATL LARAGVSCCE LAEEDFLAVS PSDPRYHEVH
YILLDPSCSG SGMPSRQLEE PGAGTPSPVR LHALAGFQQR ALCHALTFPS LQRLVYSTCS
LCQEENEDVV RDALQQNPGA FRLAPALPAW PHRGLSTFPG AEHCLRASPE TTLSSGFFVA
VIERVEVPR
