SPB1_HUMAN
ID SPB1_HUMAN Reviewed; 847 AA.
AC Q8IY81; B2RCA5; D3DU22; Q8N3A3; Q8WXX1; Q9BWM4; Q9NXT6;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=pre-rRNA 2'-O-ribose RNA methyltransferase FTSJ3 {ECO:0000255|HAMAP-Rule:MF_03163};
DE EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_03163, ECO:0000269|PubMed:30626973};
DE AltName: Full=Protein ftsJ homolog 3 {ECO:0000255|HAMAP-Rule:MF_03163};
DE AltName: Full=Putative rRNA methyltransferase 3 {ECO:0000255|HAMAP-Rule:MF_03163};
GN Name=FTSJ3 {ECO:0000255|HAMAP-Rule:MF_03163}; ORFNames=SB92;
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], AND VARIANTS GLU-91 AND CYS-424.
RA Zhang W., Li N., Wan T., Chen T., Cao T.;
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLU-91 AND CYS-424.
RC TISSUE=Colon, and Placenta;
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=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLU-91 AND CYS-424.
RC TISSUE=Placenta, and Skin;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 157-847, AND VARIANT CYS-424.
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333; SER-335; SER-336 AND
RP SER-347, AND 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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333; SER-335; SER-336;
RP SER-356; SER-549; SER-584 AND SER-644, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-336; SER-584; SER-644;
RP SER-676 AND SER-688, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
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 [17]
RP FUNCTION, INTERACTION WITH NIP7, AND SUBCELLULAR LOCATION.
RX PubMed=22195017; DOI=10.1371/journal.pone.0029174;
RA Morello L.G., Coltri P.P., Quaresma A.J., Simabuco F.M., Silva T.C.,
RA Singh G., Nickerson J.A., Oliveira C.C., Moore M.J., Zanchin N.I.;
RT "The human nucleolar protein FTSJ3 associates with NIP7 and functions in
RT pre-rRNA processing.";
RL PLoS ONE 6:E29174-E29174(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333; SER-335; SER-336;
RP SER-584 AND SER-644, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-573; SER-584; SER-644;
RP SER-676 AND SER-688, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333 AND SER-335, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [22]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-357; LYS-579; LYS-643; LYS-659;
RP LYS-678 AND LYS-710, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [23]
RP FUNCTION (MICROBIAL INFECTION), CATALYTIC ACTIVITY, INTERACTION WITH
RP TARBP2, ACTIVE SITE, AND MUTAGENESIS OF LYS-31; ASP-117 AND LYS-157.
RX PubMed=30626973; DOI=10.1038/s41586-018-0841-4;
RA Ringeard M., Marchand V., Decroly E., Motorin Y., Bennasser Y.;
RT "FTSJ3 is an RNA 2'-O-methyltransferase recruited by HIV to avoid innate
RT immune sensing.";
RL Nature 565:500-504(2019).
CC -!- FUNCTION: RNA 2'-O-methyltransferase involved in the processing of the
CC 34S pre-rRNA to 18S rRNA and in 40S ribosomal subunit formation.
CC {ECO:0000255|HAMAP-Rule:MF_03163, ECO:0000269|PubMed:22195017}.
CC -!- FUNCTION: (Microbial infection) In case of infection by HIV-1 virus,
CC recruited to HIV-1 RNA and catalyzes 2'-O-methylation of the viral
CC genome, allowing HIV-1 virus to escape the innate immune system
CC (PubMed:30626973). RNA 2'-O-methylation provides a molecular signature
CC for discrimination of self from non-self and is used by HIV-1 to evade
CC innate immune recognition by IFIH1/MDA5 (PubMed:30626973). Mediates
CC methylation of internal residues of HIV-1 RNA, with a strong preference
CC for adenosine (PubMed:30626973). Recruited to HIV-1 RNA via interaction
CC with TARBP2/TRBP (PubMed:30626973). {ECO:0000269|PubMed:30626973}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleotide in rRNA + S-adenosyl-L-methionine = a 2'-O-
CC methylribonucleotide in rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:48628, Rhea:RHEA-COMP:12164, Rhea:RHEA-COMP:12165,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:90675, ChEBI:CHEBI:90676; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03163};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleotide in RNA + S-adenosyl-L-methionine = a 2'-O-
CC methylribonucleotide in RNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:58956, Rhea:RHEA-COMP:15261, Rhea:RHEA-COMP:15262,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:90675, ChEBI:CHEBI:90676;
CC Evidence={ECO:0000269|PubMed:30626973};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58957;
CC Evidence={ECO:0000269|PubMed:30626973};
CC -!- SUBUNIT: Interacts with NIP7. {ECO:0000255|HAMAP-Rule:MF_03163,
CC ECO:0000269|PubMed:22195017}.
CC -!- SUBUNIT: (Microbial infection) Interacts with TARBP2/TRBP in case of
CC infection by HIV-1; leading to recruitment to HIV-1 TAR RNA
CC (PubMed:30626973). The complex formed with TARBP2/TRBP is independent
CC of DICER (PubMed:30626973). {ECO:0000269|PubMed:30626973}.
CC -!- INTERACTION:
CC Q8IY81; P19525: EIF2AK2; NbExp=3; IntAct=EBI-744088, EBI-640775;
CC Q8IY81; P10412: H1-4; NbExp=2; IntAct=EBI-744088, EBI-358163;
CC Q8IY81; Q9Y6K5: OAS3; NbExp=2; IntAct=EBI-744088, EBI-6115729;
CC Q8IY81; Q16385-2: SSX2B; NbExp=3; IntAct=EBI-744088, EBI-17564583;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-
CC Rule:MF_03163, ECO:0000269|PubMed:12429849,
CC ECO:0000269|PubMed:22195017}.
CC -!- PTM: Citrullinated by PADI4. {ECO:0000250|UniProtKB:Q9DBE9}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase RlmE family. SPB1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03163}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA90924.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF327355; AAL56015.1; -; mRNA.
DR EMBL; AK000069; BAA90924.1; ALT_INIT; mRNA.
DR EMBL; AK315010; BAG37502.1; -; mRNA.
DR EMBL; AC015651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471109; EAW94273.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94274.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94275.1; -; Genomic_DNA.
DR EMBL; BC000131; AAH00131.2; -; mRNA.
DR EMBL; BC036710; AAH36710.1; -; mRNA.
DR EMBL; AL834482; CAD39141.1; -; mRNA.
DR CCDS; CCDS11644.1; -.
DR RefSeq; NP_060117.3; NM_017647.3.
DR AlphaFoldDB; Q8IY81; -.
DR BioGRID; 125581; 354.
DR IntAct; Q8IY81; 104.
DR MINT; Q8IY81; -.
DR STRING; 9606.ENSP00000396673; -.
DR GlyGen; Q8IY81; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8IY81; -.
DR PhosphoSitePlus; Q8IY81; -.
DR SwissPalm; Q8IY81; -.
DR BioMuta; FTSJ3; -.
DR DMDM; 296452883; -.
DR SWISS-2DPAGE; Q8IY81; -.
DR EPD; Q8IY81; -.
DR jPOST; Q8IY81; -.
DR MassIVE; Q8IY81; -.
DR MaxQB; Q8IY81; -.
DR PaxDb; Q8IY81; -.
DR PeptideAtlas; Q8IY81; -.
DR PRIDE; Q8IY81; -.
DR ProteomicsDB; 71121; -.
DR Antibodypedia; 31352; 118 antibodies from 23 providers.
DR DNASU; 117246; -.
DR Ensembl; ENST00000427159.7; ENSP00000396673.2; ENSG00000108592.17.
DR GeneID; 117246; -.
DR KEGG; hsa:117246; -.
DR MANE-Select; ENST00000427159.7; ENSP00000396673.2; NM_017647.4; NP_060117.3.
DR UCSC; uc002jca.3; human.
DR CTD; 117246; -.
DR DisGeNET; 117246; -.
DR GeneCards; FTSJ3; -.
DR HGNC; HGNC:17136; FTSJ3.
DR HPA; ENSG00000108592; Low tissue specificity.
DR MIM; 618411; gene.
DR neXtProt; NX_Q8IY81; -.
DR OpenTargets; ENSG00000108592; -.
DR PharmGKB; PA28419; -.
DR VEuPathDB; HostDB:ENSG00000108592; -.
DR eggNOG; KOG1098; Eukaryota.
DR GeneTree; ENSGT00550000075004; -.
DR HOGENOM; CLU_009422_8_1_1; -.
DR InParanoid; Q8IY81; -.
DR OMA; LMWVFQQ; -.
DR OrthoDB; 1362679at2759; -.
DR PhylomeDB; Q8IY81; -.
DR TreeFam; TF106102; -.
DR PathwayCommons; Q8IY81; -.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR SignaLink; Q8IY81; -.
DR BioGRID-ORCS; 117246; 509 hits in 1089 CRISPR screens.
DR ChiTaRS; FTSJ3; human.
DR GeneWiki; FTSJ3; -.
DR GenomeRNAi; 117246; -.
DR Pharos; Q8IY81; Tbio.
DR PRO; PR:Q8IY81; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q8IY81; protein.
DR Bgee; ENSG00000108592; Expressed in metanephros cortex and 176 other tissues.
DR ExpressionAtlas; Q8IY81; baseline and differential.
DR Genevisible; Q8IY81; HS.
DR GO; GO:0005694; C:chromosome; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IBA:GO_Central.
DR GO; GO:0030688; C:preribosome, small subunit precursor; IEA:UniProtKB-UniRule.
DR GO; GO:0062105; F:RNA 2'-O-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0008173; F:RNA methyltransferase activity; IBA:GO_Central.
DR GO; GO:0016435; F:rRNA (guanine) methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008650; F:rRNA (uridine-2'-O-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0000453; P:enzyme-directed rRNA 2'-O-methylation; IEA:UniProtKB-UniRule.
DR GO; GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0001510; P:RNA methylation; IDA:UniProtKB.
DR GO; GO:0031167; P:rRNA methylation; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_01547; RNA_methyltr_E; 1.
DR HAMAP; MF_03163; RNA_methyltr_E_SPB1; 1.
DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR015507; rRNA-MeTfrase_E.
DR InterPro; IPR012920; rRNA_MeTfrase_SPB1-like_C.
DR InterPro; IPR024576; rRNA_MeTfrase_Spb1_DUF3381.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR028589; SPB1-like.
DR Pfam; PF11861; DUF3381; 1.
DR Pfam; PF01728; FtsJ; 1.
DR Pfam; PF07780; Spb1_C; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Citrullination; Coiled coil; Isopeptide bond; Methyltransferase; Nucleus;
KW Phosphoprotein; Reference proteome; Ribosome biogenesis; rRNA processing;
KW S-adenosyl-L-methionine; Transferase; Ubl conjugation.
FT CHAIN 1..847
FT /note="pre-rRNA 2'-O-ribose RNA methyltransferase FTSJ3"
FT /id="PRO_0000155577"
FT REGION 332..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 355..407
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT COILED 739..777
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT COMPBIAS 457..473
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..499
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..653
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..835
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 157
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163,
FT ECO:0000269|PubMed:30626973"
FT BINDING 56
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT BINDING 58
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT BINDING 76
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT BINDING 92
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT BINDING 117
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163,
FT ECO:0000269|PubMed:30626973"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 392
FT /note="Citrulline"
FT /evidence="ECO:0000250|UniProtKB:Q9DBE9"
FT MOD_RES 549
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 573
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 584
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 644
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 676
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 783
FT /note="Citrulline"
FT /evidence="ECO:0000250|UniProtKB:Q9DBE9"
FT CROSSLNK 357
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 579
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 643
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 659
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 678
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 710
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 91
FT /note="Q -> E (in dbSNP:rs2584625)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1"
FT /id="VAR_023284"
FT VARIANT 424
FT /note="S -> C (in dbSNP:rs2727288)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005,
FT ECO:0000269|Ref.1"
FT /id="VAR_023285"
FT MUTAGEN 31
FT /note="K->A: Abolishes RNA 2'-O-methyltransferase activity;
FT when associated with A-117 and A-157."
FT /evidence="ECO:0000269|PubMed:30626973"
FT MUTAGEN 117
FT /note="D->A: Abolishes RNA 2'-O-methyltransferase activity;
FT when associated with A-31 and A-157."
FT /evidence="ECO:0000269|PubMed:30626973"
FT MUTAGEN 157
FT /note="K->A: Abolishes RNA 2'-O-methyltransferase activity;
FT when associated with A-31 and A-117."
FT /evidence="ECO:0000269|PubMed:30626973"
FT CONFLICT 278
FT /note="E -> I (in Ref. 1; AAL56015 and 2; BAA90924)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 847 AA; 96558 MW; 06B2F4D28A48026F CRC64;
MGKKGKVGKS RRDKFYHLAK ETGYRSRSAF KLIQLNRRFQ FLQKARALLD LCAAPGGWLQ
VAAKFMPVSS LIVGVDLVPI KPLPNVVTLQ QDITTERCRQ ALRKELKTWK VDVVLNDGAP
NVGASWVHDA YSQAHLTLMA LRLACDFLAR GGSFITKVFR SRDYQPLLWI FQQLFRRVQA
TKPQASRHES AEIFVVCQGF LAPDKVDSKF FDPKFAFKEV EVQAKTVTEL VTKKKPKAEG
YAEGDLTLYH RTSVTDFLRA ANPVDFLSKA SEIMVDDEEL AQHPATTEDI RVCCQDIRVL
GRKELRSLLN WRTKLRRYVA KKLKEQAKAL DISLSSGEED EGDEEDSTAG TTKQPSKEEE
EEEEEEQLNQ TLAEMKAQEV AELKRKKKKL LREQRKQRER VELKMDLPGV SIADEGETGM
FSLSTIRGHQ LLEEVTQGDM SAADTFLSDL PRDDIYVSDV EDDGDDTSLD SDLDPEELAG
VRGHQGLRDQ KRMRLTEVQD DKEEEEEENP LLVPLEEKAV LQEEQANLWF SKGSFAGIED
DADEALEISQ AQLLFENRRK GRQQQQKQQL PQTPPSCLKT EIMSPLYQDE APKGTEASSG
TEAATGLEGE EKDGISDSDS STSSEEEESW EPLRGKKRSR GPKSDDDGFE IVPIEDPAKH
RILDPEGLAL GAVIASSKKA KRDLIDNSFN RYTFNEDEGE LPEWFVQEEK QHRIRQLPVG
KKEVEHYRKR WREINARPIK KVAEAKARKK RRMLKRLEQT RKKAEAVVNT VDISEREKVA
QLRSLYKKAG LGKEKRHVTY VVAKKGVGRK VRRPAGVRGH FKVVDSRMKK DQRAQQRKEQ
KKKHKRK
