TSR3_HUMAN
ID TSR3_HUMAN Reviewed; 312 AA.
AC Q9UJK0; Q6PJT8;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=18S rRNA aminocarboxypropyltransferase {ECO:0000305};
DE EC=2.5.1.- {ECO:0000305|PubMed:27084949};
DE AltName: Full=20S S rRNA accumulation protein 3 homolog {ECO:0000303|PubMed:27084949};
DE Short=HsTsr3 {ECO:0000303|PubMed:27084949};
GN Name=TSR3 {ECO:0000303|PubMed:27084949, ECO:0000312|HGNC:HGNC:14175};
GN Synonyms=C16orf42 {ECO:0000312|HGNC:HGNC:14175},
GN UND313L {ECO:0000303|PubMed:11157797};
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 GENOMIC DNA].
RX PubMed=11157797; DOI=10.1093/hmg/10.4.339;
RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C.,
RA Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.;
RT "Sequence, structure and pathology of the fully annotated terminal 2 Mb of
RT the short arm of human chromosome 16.";
RL Hum. Mol. Genet. 10:339-352(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow, Lung, and Ovary;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282, AND IDENTIFICATION BY
RP 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259; THR-261 AND SER-264, AND
RP IDENTIFICATION BY MASS 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 [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, AND CATALYTIC ACTIVITY.
RX PubMed=27084949; DOI=10.1093/nar/gkw244;
RA Meyer B., Wurm J.P., Sharma S., Immer C., Pogoryelov D., Koetter P.,
RA Lafontaine D.L., Woehnert J., Entian K.D.;
RT "Ribosome biogenesis factor Tsr3 is the aminocarboxypropyl transferase
RT responsible for 18S rRNA hypermodification in yeast and humans.";
RL Nucleic Acids Res. 44:4304-4316(2016).
CC -!- FUNCTION: Aminocarboxypropyltransferase that catalyzes the
CC aminocarboxypropyl transfer on pseudouridine at position 1248 (Psi1248)
CC in 18S rRNA (Probable). It constitutes the last step in biosynthesis of
CC the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine
CC (m1acp3-Psi) conserved in eukaryotic 18S rRNA (Probable).
CC {ECO:0000305|PubMed:27084949}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(1)-methylpseudouridine(1248) in human 18S rRNA + S-adenosyl-
CC L-methionine = H(+) + N(1)-methyl-N(3)-[(3S)-3-amino-3-
CC carboxypropyl]pseudouridine(1248) in human 18S rRNA + S-methyl-5'-
CC thioadenosine; Xref=Rhea:RHEA:63292, Rhea:RHEA-COMP:11639, Rhea:RHEA-
CC COMP:16308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74890, ChEBI:CHEBI:146234; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03146, ECO:0000305|PubMed:27084949};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63293;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03146,
CC ECO:0000305|PubMed:27084949};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q12094,
CC ECO:0000255|HAMAP-Rule:MF_03146}.
CC -!- SIMILARITY: Belongs to the TDD superfamily. TSR3 family.
CC {ECO:0000255|HAMAP-Rule:MF_03146}.
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; AE006467; AAK61276.1; -; Genomic_DNA.
DR EMBL; AL031709; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC013943; AAH13943.1; -; mRNA.
DR EMBL; BC016699; AAH16699.1; -; mRNA.
DR EMBL; BC017325; AAH17325.1; -; mRNA.
DR CCDS; CCDS10435.1; -.
DR PIR; T45061; T45061.
DR RefSeq; NP_001001410.1; NM_001001410.2.
DR AlphaFoldDB; Q9UJK0; -.
DR SMR; Q9UJK0; -.
DR BioGRID; 125462; 58.
DR IntAct; Q9UJK0; 23.
DR STRING; 9606.ENSP00000007390; -.
DR iPTMnet; Q9UJK0; -.
DR PhosphoSitePlus; Q9UJK0; -.
DR BioMuta; TSR3; -.
DR DMDM; 74753359; -.
DR EPD; Q9UJK0; -.
DR jPOST; Q9UJK0; -.
DR MassIVE; Q9UJK0; -.
DR MaxQB; Q9UJK0; -.
DR PaxDb; Q9UJK0; -.
DR PeptideAtlas; Q9UJK0; -.
DR PRIDE; Q9UJK0; -.
DR ProteomicsDB; 84629; -.
DR Antibodypedia; 52454; 22 antibodies from 11 providers.
DR DNASU; 115939; -.
DR Ensembl; ENST00000007390.3; ENSP00000007390.2; ENSG00000007520.4.
DR GeneID; 115939; -.
DR KEGG; hsa:115939; -.
DR MANE-Select; ENST00000007390.3; ENSP00000007390.2; NM_001001410.3; NP_001001410.1.
DR UCSC; uc002cll.4; human.
DR CTD; 115939; -.
DR DisGeNET; 115939; -.
DR GeneCards; TSR3; -.
DR HGNC; HGNC:14175; TSR3.
DR HPA; ENSG00000007520; Low tissue specificity.
DR neXtProt; NX_Q9UJK0; -.
DR OpenTargets; ENSG00000007520; -.
DR PharmGKB; PA25558; -.
DR VEuPathDB; HostDB:ENSG00000007520; -.
DR eggNOG; KOG3154; Eukaryota.
DR GeneTree; ENSGT00390000014665; -.
DR HOGENOM; CLU_035060_2_0_1; -.
DR InParanoid; Q9UJK0; -.
DR OMA; GRECMNL; -.
DR OrthoDB; 1222562at2759; -.
DR PhylomeDB; Q9UJK0; -.
DR TreeFam; TF105862; -.
DR PathwayCommons; Q9UJK0; -.
DR Reactome; R-HSA-6790901; rRNA modification in the nucleus and cytosol.
DR SignaLink; Q9UJK0; -.
DR BioGRID-ORCS; 115939; 59 hits in 1083 CRISPR screens.
DR ChiTaRS; TSR3; human.
DR GeneWiki; C16orf42; -.
DR GenomeRNAi; 115939; -.
DR Pharos; Q9UJK0; Tdark.
DR PRO; PR:Q9UJK0; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9UJK0; protein.
DR Bgee; ENSG00000007520; Expressed in tendon of biceps brachii and 203 other tissues.
DR ExpressionAtlas; Q9UJK0; baseline and differential.
DR Genevisible; Q9UJK0; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0106388; F:18S rRNA aminocarboxypropyltransferase activity; IMP:UniProtKB.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016740; F:transferase activity; EXP:Reactome.
DR GO; GO:0000455; P:enzyme-directed rRNA pseudouridine synthesis; IMP:UniProtKB.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IBA:GO_Central.
DR GO; GO:0000154; P:rRNA modification; TAS:Reactome.
DR HAMAP; MF_01116; TSR3; 1.
DR InterPro; IPR007209; RNaseL-inhib-like_metal-bd_dom.
DR InterPro; IPR022968; Tsr3-like.
DR InterPro; IPR007177; Tsr3_C.
DR PANTHER; PTHR20426; PTHR20426; 1.
DR Pfam; PF04034; Ribo_biogen_C; 1.
DR Pfam; PF04068; RLI; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome; Ribosome biogenesis;
KW rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..312
FT /note="18S rRNA aminocarboxypropyltransferase"
FT /id="PRO_0000278669"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 74
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:E1QU22"
FT BINDING 122
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:E1QU22"
FT BINDING 145
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:E1QU22"
FT BINDING 160
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:E1QU22"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5HZH2"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 261
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
SQ SEQUENCE 312 AA; 33596 MW; 47D33346832145BB CRC64;
MGRRRAARGP GAEGGRPRHL PTRSLEAFAE EVGAALQASV EPGAADGEGG PGPAALPCTL
AMWELGHCDP RRCTGRKLAR LGLVRCLRLG HRFGGLVLSP VGKQYASPAD RQLVAQSGVA
VIDCSWARLD ETPFGKMRGS HLRLLPYLVA ANPVNYGRPY RLSCVEAFAA TFCIVGFPDL
AVILLRKFKW GKGFLDLNRQ LLDKYAACGS PEEVLQAEQE FLANAKESPQ EEEIDPFDVD
SGREFGNPNR PVASTRLPSD TDDSDASEDP GPGAERGGAS SSCCEEEQTQ GRGAEARAPA
EVWKGIKKRQ RD
