TRUB1_HUMAN
ID TRUB1_HUMAN Reviewed; 349 AA.
AC Q8WWH5; B2R716; Q53ES2;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Pseudouridylate synthase TRUB1 {ECO:0000305};
DE EC=5.4.99.- {ECO:0000269|PubMed:31477916, ECO:0000269|PubMed:32926445, ECO:0000305|PubMed:28073919};
DE AltName: Full=TruB pseudouridine synthase homolog 1 {ECO:0000303|PubMed:12736709};
DE AltName: Full=tRNA pseudouridine 55 synthase TRUB1 {ECO:0000305};
DE Short=Psi55 synthase TRUB1 {ECO:0000305};
DE EC=5.4.99.25 {ECO:0000269|PubMed:33023933};
GN Name=TRUB1 {ECO:0000303|PubMed:12736709, ECO:0000312|HGNC:HGNC:16060};
GN Synonyms=PUS4 {ECO:0000312|HGNC:HGNC:16060};
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], AND TISSUE SPECIFICITY.
RC TISSUE=Foreskin;
RX PubMed=12736709;
RA Zucchini C., Strippoli P., Biolchi A., Solmi R., Lenzi L., D'Addabbo P.,
RA Carinci P., Valvassori L.;
RT "The human TruB family of pseudouridine synthase genes, including the
RT Dyskeratosis Congenita 1 gene and the novel member TRUB1.";
RL Int. J. Mol. Med. 11:697-704(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Endometrial tumor;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LYS-167.
RC TISSUE=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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-11, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [9]
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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, 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 [12]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=28073919; DOI=10.1101/gr.207613.116;
RA Safra M., Nir R., Farouq D., Vainberg Slutskin I., Schwartz S.;
RT "TRUB1 is the predominant pseudouridine synthase acting on mammalian mRNA
RT via a predictable and conserved code.";
RL Genome Res. 27:393-406(2017).
RN [13]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=31477916; DOI=10.1038/s41589-019-0353-z;
RA Carlile T.M., Martinez N.M., Schaening C., Su A., Bell T.A., Zinshteyn B.,
RA Gilbert W.V.;
RT "mRNA structure determines modification by pseudouridine synthase 1.";
RL Nat. Chem. Biol. 15:966-974(2019).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF ASP-121;
RP LYS-147 AND ASP-163.
RX PubMed=32926445; DOI=10.15252/embj.2020104708;
RA Kurimoto R., Chiba T., Ito Y., Matsushima T., Yano Y., Miyata K.,
RA Yashiro Y., Suzuki T., Tomita K., Asahara H.;
RT "The tRNA pseudouridine synthase TruB1 regulates the maturation of let-7
RT miRNA.";
RL EMBO J. 39:e104708-e104708(2020).
RN [15]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=33023933; DOI=10.1261/rna.076810.120;
RA Mukhopadhyay S., Deogharia M., Gupta R.;
RT "Mammalian nuclear TRUB1, mitochondrial TRUB2, and cytoplasmic PUS10
RT produce conserved pseudouridine 55 in different sets of tRNA.";
RL RNA 27:66-79(2021).
CC -!- FUNCTION: Pseudouridine synthase that catalyzes pseudouridylation of
CC mRNAs and tRNAs (PubMed:28073919, PubMed:31477916, PubMed:32926445).
CC Mediates pseudouridylation of mRNAs with the consensus sequence 5'-
CC GUUCNANNC-3', harboring a stem-loop structure (PubMed:28073919,
CC PubMed:31477916). Constitutes the major pseudouridine synthase acting
CC on mRNAs (PubMed:28073919). Also catalyzes pseudouridylation of some
CC tRNAs, including synthesis of pseudouridine(55) from uracil-55, in the
CC psi GC loop of a subset of tRNAs (PubMed:32926445, PubMed:33023933).
CC Promotes the processing of pri-let-7 microRNAs (pri-miRNAs)
CC independently of its RNA pseudouridylate synthase activity
CC (PubMed:32926445). Acts by binding to the stem-loop structure on pri-
CC let-7, preventing LIN28-binding (LIN28A and/or LIN28B), thereby
CC enhancing the interaction between pri-let-7 and the microprocessor
CC DGCR8, which mediates miRNA maturation (PubMed:32926445).
CC {ECO:0000269|PubMed:28073919, ECO:0000269|PubMed:31477916,
CC ECO:0000269|PubMed:32926445, ECO:0000269|PubMed:33023933}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a uridine in mRNA = a pseudouridine in mRNA;
CC Xref=Rhea:RHEA:56644, Rhea:RHEA-COMP:14658, Rhea:RHEA-COMP:14659,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
CC Evidence={ECO:0000269|PubMed:31477916, ECO:0000305|PubMed:28073919};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a uridine in tRNA = a pseudouridine in tRNA;
CC Xref=Rhea:RHEA:54572, Rhea:RHEA-COMP:13339, Rhea:RHEA-COMP:13934,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
CC Evidence={ECO:0000269|PubMed:32926445};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(55) in tRNA = pseudouridine(55) in tRNA;
CC Xref=Rhea:RHEA:42532, Rhea:RHEA-COMP:10101, Rhea:RHEA-COMP:10102,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.25;
CC Evidence={ECO:0000269|PubMed:33023933};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42533;
CC Evidence={ECO:0000269|PubMed:33023933};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28073919,
CC ECO:0000269|PubMed:33023933}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:28073919}. Note=Catalyzes pseudouridylation of
CC mRNAs in the nucleus. {ECO:0000269|PubMed:28073919}.
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle and
CC liver. Expressed at lower levels in lung, small intestine, kidney and
CC spleen. {ECO:0000269|PubMed:12736709}.
CC -!- SIMILARITY: Belongs to the pseudouridine synthase TruB family.
CC {ECO:0000305}.
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DR EMBL; AF448144; AAL40350.1; -; mRNA.
DR EMBL; BX648709; CAH10560.1; -; mRNA.
DR EMBL; AK312805; BAG35663.1; -; mRNA.
DR EMBL; AK223567; BAD97287.1; -; mRNA.
DR EMBL; AL355340; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC030601; AAH30601.1; -; mRNA.
DR CCDS; CCDS7591.1; -.
DR RefSeq; NP_631908.1; NM_139169.4.
DR AlphaFoldDB; Q8WWH5; -.
DR SMR; Q8WWH5; -.
DR BioGRID; 126783; 28.
DR IntAct; Q8WWH5; 22.
DR MINT; Q8WWH5; -.
DR STRING; 9606.ENSP00000298746; -.
DR GlyGen; Q8WWH5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8WWH5; -.
DR PhosphoSitePlus; Q8WWH5; -.
DR BioMuta; TRUB1; -.
DR DMDM; 74751577; -.
DR EPD; Q8WWH5; -.
DR jPOST; Q8WWH5; -.
DR MassIVE; Q8WWH5; -.
DR MaxQB; Q8WWH5; -.
DR PaxDb; Q8WWH5; -.
DR PeptideAtlas; Q8WWH5; -.
DR PRIDE; Q8WWH5; -.
DR ProteomicsDB; 74887; -.
DR TopDownProteomics; Q8WWH5; -.
DR Antibodypedia; 31974; 126 antibodies from 22 providers.
DR DNASU; 142940; -.
DR Ensembl; ENST00000298746.5; ENSP00000298746.3; ENSG00000165832.6.
DR GeneID; 142940; -.
DR KEGG; hsa:142940; -.
DR MANE-Select; ENST00000298746.5; ENSP00000298746.3; NM_139169.5; NP_631908.1.
DR UCSC; uc001lcd.4; human.
DR CTD; 142940; -.
DR DisGeNET; 142940; -.
DR GeneCards; TRUB1; -.
DR HGNC; HGNC:16060; TRUB1.
DR HPA; ENSG00000165832; Low tissue specificity.
DR MIM; 610726; gene.
DR neXtProt; NX_Q8WWH5; -.
DR OpenTargets; ENSG00000165832; -.
DR PharmGKB; PA38086; -.
DR VEuPathDB; HostDB:ENSG00000165832; -.
DR eggNOG; KOG2529; Eukaryota.
DR GeneTree; ENSGT00940000158962; -.
DR HOGENOM; CLU_032087_1_0_1; -.
DR InParanoid; Q8WWH5; -.
DR OMA; ELQFIRW; -.
DR OrthoDB; 1535798at2759; -.
DR PhylomeDB; Q8WWH5; -.
DR TreeFam; TF320759; -.
DR PathwayCommons; Q8WWH5; -.
DR SignaLink; Q8WWH5; -.
DR BioGRID-ORCS; 142940; 11 hits in 1074 CRISPR screens.
DR ChiTaRS; TRUB1; human.
DR GenomeRNAi; 142940; -.
DR Pharos; Q8WWH5; Tbio.
DR PRO; PR:Q8WWH5; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q8WWH5; protein.
DR Bgee; ENSG00000165832; Expressed in adrenal tissue and 188 other tissues.
DR Genevisible; Q8WWH5; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0070883; F:pre-miRNA binding; IDA:UniProtKB.
DR GO; GO:0009982; F:pseudouridine synthase activity; IDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:1990481; P:mRNA pseudouridine synthesis; IDA:UniProtKB.
DR GO; GO:2000633; P:positive regulation of pre-miRNA processing; IDA:UniProtKB.
DR GO; GO:0006400; P:tRNA modification; IDA:UniProtKB.
DR HAMAP; MF_01080; TruB_bact; 1.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR002501; PsdUridine_synth_N.
DR InterPro; IPR014780; tRNA_psdUridine_synth_TruB.
DR PANTHER; PTHR13767; PTHR13767; 1.
DR Pfam; PF01509; TruB_N; 1.
DR SUPFAM; SSF55120; SSF55120; 1.
DR TIGRFAMs; TIGR00431; TruB; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Isomerase; mRNA processing; Nucleus;
KW Phosphoprotein; Reference proteome; tRNA processing.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22223895"
FT CHAIN 2..349
FT /note="Pseudouridylate synthase TRUB1"
FT /id="PRO_0000252087"
FT ACT_SITE 121
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:32926445"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22223895"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 103
FT /note="E -> A (in dbSNP:rs34393297)"
FT /id="VAR_051607"
FT VARIANT 167
FT /note="R -> K (in dbSNP:rs7099565)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_027748"
FT MUTAGEN 121
FT /note="D->A: Abolished pseudouridine synthase activity
FT without affecting ability to promote processing of let-7
FT miRNAs; when associated with A-163."
FT /evidence="ECO:0000269|PubMed:32926445"
FT MUTAGEN 147
FT /note="K->E: Abolished RNA-binding and ability to promote
FT processing of let-7 miRNAs."
FT /evidence="ECO:0000269|PubMed:32926445"
FT MUTAGEN 163
FT /note="D->A: Abolished pseudouridine synthase activity
FT without affecting ability to promote processing of let-7
FT miRNAs; when associated with A-121."
FT /evidence="ECO:0000269|PubMed:32926445"
FT CONFLICT 323
FT /note="E -> D (in Ref. 4; BAD97287)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 349 AA; 37253 MW; C3292D31EC60EE17 CRC64;
MAASEAAVVS SPSLKTDTSP VLETAGTVAA MAATPSARAA AAVVAAAART GSEARVSKAA
LATKLLSLSG VFAVHKPKGP TSAELLNRLK EKLLAEAGMP SPEWTKRKKQ TLKIGHGGTL
DSAARGVLVV GIGSGTKMLT SMLSGSKRYT AIGELGKATD TLDSTGRVTE EKPYDKITQE
DIEGILQKFT GNIMQVPPLY SALKKDGQRL STLMKRGEVV EAKPARPVTV YSISLQKFQP
PFFTLDVECG GGFYIRSLVS DIGKELSSCA NVLELTRTKQ GPFTLEEHAL PEDKWTIDDI
AQSLEHCSSL FPAELALKKS KPESNEQVLS CEYITLNEPK REDDVIKTC
