PUS10_HUMAN
ID PUS10_HUMAN Reviewed; 529 AA.
AC Q3MIT2; Q5JPJ5; Q96MI8;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=tRNA pseudouridine synthase Pus10;
DE Short=Hup10 {ECO:0000303|PubMed:28981101};
DE EC=5.4.99.25 {ECO:0000269|PubMed:31819270, ECO:0000269|PubMed:33023933};
DE AltName: Full=Coiled-coil domain-containing protein 139 {ECO:0000312|HGNC:HGNC:26505};
DE AltName: Full=tRNA pseudouridine 55 synthase;
DE Short=Psi55 synthase;
DE AltName: Full=tRNA pseudouridylate synthase;
DE AltName: Full=tRNA-uridine isomerase;
GN Name=PUS10 {ECO:0000312|HGNC:HGNC:26505};
GN Synonyms=CCDC139 {ECO:0000312|HGNC:HGNC:26505},
GN DOBI {ECO:0000303|PubMed:19712588};
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].
RC TISSUE=Prostate;
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 MRNA].
RC TISSUE=Cervix;
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 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 (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 FUNCTION.
RX PubMed=14527409; DOI=10.1016/s1097-2765(03)00348-4;
RA Aza-Blanc P., Cooper C.L., Wagner K., Batalov S., Deveraux Q.L.,
RA Cooke M.P.;
RT "Identification of modulators of TRAIL-induced apoptosis via RNAi-based
RT phenotypic screening.";
RL Mol. Cell 12:627-637(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79 AND SER-84, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [7]
RP PROTEOLYTIC CLEAVAGE, AND FUNCTION.
RX PubMed=19712588; DOI=10.5483/bmbrep.2009.42.8.511;
RA Park S.Y., Shin J.N., Woo H.N., Piya S., Moon A.R., Seo Y.W., Seol D.W.,
RA Kim T.H.;
RT "DOBI is cleaved by caspases during TRAIL-induced apoptotic cell death.";
RL BMB Rep. 42:511-515(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84, 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 [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=28981101; DOI=10.1038/cddis.2017.476;
RA Jana S., Hsieh A.C., Gupta R.;
RT "Reciprocal amplification of caspase-3 activity by nuclear export of a
RT putative human RNA-modifying protein, PUS10 during TRAIL-induced
RT apoptosis.";
RL Cell Death Dis. 8:E3093-E3093(2017).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH DROSHA
RP AND DGCR8, ACTIVE SITE, AND MUTAGENESIS OF ASP-344.
RX PubMed=31819270; DOI=10.1038/s41589-019-0420-5;
RA Song J., Zhuang Y., Zhu C., Meng H., Lu B., Xie B., Peng J., Li M., Yi C.;
RT "Differential roles of human PUS10 in miRNA processing and tRNA
RT pseudouridylation.";
RL Nat. Chem. Biol. 16:160-169(2020).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF ASP-344.
RX PubMed=30530625; DOI=10.1261/rna.068114.118;
RA Deogharia M., Mukhopadhyay S., Joardar A., Gupta R.;
RT "The human ortholog of archaeal Pus10 produces pseudouridine 54 in select
RT tRNAs where its recognition sequence contains a modified residue.";
RL RNA 25:336-351(2019).
RN [12]
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).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ZINC.
RX PubMed=17900615; DOI=10.1016/j.jmb.2007.08.053;
RA McCleverty C.J., Hornsby M., Spraggon G., Kreusch A.;
RT "Crystal structure of human Pus10, a novel pseudouridine synthase.";
RL J. Mol. Biol. 373:1243-1254(2007).
RN [14]
RP VARIANT [LARGE SCALE ANALYSIS] ILE-484.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Protein with different functions depending on its subcellular
CC location: involved in miRNA processing in the nucleus and acts as a
CC tRNA pseudouridylate synthase in the cytoplasm (PubMed:31819270,
CC PubMed:33023933). In the cytoplasm, acts as a pseudouridylate synthase
CC by catalyzing synthesis of pseudouridine(54) and pseudouridine(55) from
CC uracil-54 and uracil-55, respectively, in the psi GC loop of a subset
CC of tRNAs (PubMed:30530625, PubMed:31819270, PubMed:33023933). tRNA
CC pseudouridylate synthase activity is enhanced by the presence of 1-
CC methyladenosine at position 53-61 of tRNAs (PubMed:30530625). Does not
CC show tRNA pseudouridylate synthase activity in the nucleus
CC (PubMed:33023933). In the nucleus, promotes primary microRNAs (pri-
CC miRNAs) processing independently of its RNA pseudouridylate synthase
CC activity (PubMed:31819270). Binds pri-miRNAs (PubMed:31819270).
CC Modulator of TRAIL/TNFSF10-induced cell death via activation of
CC procaspase-8 and BID cleavage (PubMed:14527409, PubMed:19712588).
CC Required for the progression of the apoptotic signal through intrinsic
CC mitochondrial cell death (PubMed:19712588).
CC {ECO:0000269|PubMed:14527409, ECO:0000269|PubMed:19712588,
CC ECO:0000269|PubMed:30530625, ECO:0000269|PubMed:31819270,
CC ECO:0000269|PubMed:33023933}.
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:31819270, ECO:0000269|PubMed:33023933};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42533;
CC Evidence={ECO:0000269|PubMed:31819270};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(54) in tRNA = pseudouridine(54) in tRNA;
CC Xref=Rhea:RHEA:57876, Rhea:RHEA-COMP:10193, Rhea:RHEA-COMP:14141,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
CC Evidence={ECO:0000269|PubMed:30530625, ECO:0000269|PubMed:31819270,
CC ECO:0000269|PubMed:33023933};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57877;
CC Evidence={ECO:0000269|PubMed:31819270};
CC -!- SUBUNIT: Interacts with components of the microprocessor complex DROSHA
CC and DGCR8. {ECO:0000269|PubMed:31819270}.
CC -!- INTERACTION:
CC Q3MIT2; Q9NX38: ABITRAM; NbExp=7; IntAct=EBI-11983583, EBI-9105722;
CC Q3MIT2; Q04760: GLO1; NbExp=3; IntAct=EBI-11983583, EBI-1055525;
CC Q3MIT2; P02533: KRT14; NbExp=3; IntAct=EBI-11983583, EBI-702178;
CC Q3MIT2; P08779: KRT16; NbExp=3; IntAct=EBI-11983583, EBI-356410;
CC Q3MIT2; Q7Z6G3-2: NECAB2; NbExp=3; IntAct=EBI-11983583, EBI-10172876;
CC Q3MIT2; Q9UHP3: USP25; NbExp=3; IntAct=EBI-11983583, EBI-2513462;
CC Q3MIT2; Q6GMQ7: VPS16; NbExp=3; IntAct=EBI-11983583, EBI-17974829;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28981101,
CC ECO:0000269|PubMed:30530625, ECO:0000269|PubMed:31819270,
CC ECO:0000269|PubMed:33023933}. Cytoplasm {ECO:0000269|PubMed:31819270,
CC ECO:0000269|PubMed:33023933, ECO:0000305|PubMed:30530625}.
CC Mitochondrion {ECO:0000269|PubMed:28981101}. Note=Localizes mainly in
CC the nucleus (Probable) (PubMed:31819270). tRNA pseudouridylate synthase
CC activity is restricted to the cytoplasm (PubMed:31819270). Translocates
CC from nucleus to mitochondria during TRAIL-induced apoptosis
CC (PubMed:28981101). {ECO:0000269|PubMed:28981101,
CC ECO:0000269|PubMed:31819270, ECO:0000305|PubMed:30530625}.
CC -!- PTM: Proteolytically cleaved during TRAIL-induced cell death
CC (PubMed:19712588). Cleaved, in vitro, either by caspase-3 (CASP3) or
CC caspase-8 (CASP8) (PubMed:19712588). {ECO:0000269|PubMed:19712588}.
CC -!- SIMILARITY: Belongs to the pseudouridine synthase Pus10 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI46123.1; Type=Miscellaneous discrepancy; Note=Partially unspliced pre-RNA.; Evidence={ECO:0000305};
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DR EMBL; AK056874; BAB71300.1; -; mRNA.
DR EMBL; AL832208; CAI46123.1; ALT_SEQ; Transcribed_RNA.
DR EMBL; CH471053; EAX00024.1; -; Genomic_DNA.
DR EMBL; BC101680; AAI01681.1; -; mRNA.
DR EMBL; BC101706; AAI01707.1; -; mRNA.
DR CCDS; CCDS1865.1; -.
DR RefSeq; NP_001309052.1; NM_001322123.1.
DR RefSeq; NP_001309053.1; NM_001322124.1.
DR RefSeq; NP_653310.2; NM_144709.3.
DR RefSeq; XP_011530870.1; XM_011532568.2.
DR RefSeq; XP_011530872.1; XM_011532570.1.
DR RefSeq; XP_011530873.1; XM_011532571.1.
DR RefSeq; XP_011530874.1; XM_011532572.1.
DR RefSeq; XP_011530875.1; XM_011532573.2.
DR RefSeq; XP_011530876.1; XM_011532574.2.
DR RefSeq; XP_011530878.1; XM_011532576.2.
DR PDB; 2V9K; X-ray; 2.00 A; A=1-529.
DR PDBsum; 2V9K; -.
DR AlphaFoldDB; Q3MIT2; -.
DR SMR; Q3MIT2; -.
DR BioGRID; 127335; 6.
DR IntAct; Q3MIT2; 7.
DR STRING; 9606.ENSP00000326003; -.
DR iPTMnet; Q3MIT2; -.
DR PhosphoSitePlus; Q3MIT2; -.
DR BioMuta; PUS10; -.
DR DMDM; 121942830; -.
DR EPD; Q3MIT2; -.
DR jPOST; Q3MIT2; -.
DR MassIVE; Q3MIT2; -.
DR MaxQB; Q3MIT2; -.
DR PaxDb; Q3MIT2; -.
DR PeptideAtlas; Q3MIT2; -.
DR PRIDE; Q3MIT2; -.
DR ProteomicsDB; 61794; -.
DR Antibodypedia; 47429; 114 antibodies from 16 providers.
DR DNASU; 150962; -.
DR Ensembl; ENST00000316752.11; ENSP00000326003.6; ENSG00000162927.14.
DR Ensembl; ENST00000407787.5; ENSP00000386074.1; ENSG00000162927.14.
DR GeneID; 150962; -.
DR KEGG; hsa:150962; -.
DR MANE-Select; ENST00000316752.11; ENSP00000326003.6; NM_144709.4; NP_653310.2.
DR UCSC; uc002sao.4; human.
DR CTD; 150962; -.
DR DisGeNET; 150962; -.
DR GeneCards; PUS10; -.
DR HGNC; HGNC:26505; PUS10.
DR HPA; ENSG00000162927; Low tissue specificity.
DR MIM; 612787; gene.
DR neXtProt; NX_Q3MIT2; -.
DR OpenTargets; ENSG00000162927; -.
DR PharmGKB; PA162400393; -.
DR VEuPathDB; HostDB:ENSG00000162927; -.
DR eggNOG; KOG2364; Eukaryota.
DR GeneTree; ENSGT00390000007529; -.
DR HOGENOM; CLU_028780_2_0_1; -.
DR InParanoid; Q3MIT2; -.
DR OMA; INIDVRH; -.
DR OrthoDB; 1067006at2759; -.
DR PhylomeDB; Q3MIT2; -.
DR TreeFam; TF106109; -.
DR BRENDA; 5.4.99.25; 2681.
DR BRENDA; 5.4.99.B22; 2681.
DR BRENDA; 5.4.99.B25; 2681.
DR PathwayCommons; Q3MIT2; -.
DR SignaLink; Q3MIT2; -.
DR BioGRID-ORCS; 150962; 12 hits in 1078 CRISPR screens.
DR ChiTaRS; PUS10; human.
DR EvolutionaryTrace; Q3MIT2; -.
DR GenomeRNAi; 150962; -.
DR Pharos; Q3MIT2; Tbio.
DR PRO; PR:Q3MIT2; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q3MIT2; protein.
DR Bgee; ENSG00000162927; Expressed in jejunal mucosa and 128 other tissues.
DR ExpressionAtlas; Q3MIT2; baseline and differential.
DR Genevisible; Q3MIT2; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070878; F:primary miRNA binding; IDA:UniProtKB.
DR GO; GO:0009982; F:pseudouridine synthase activity; IDA:UniProtKB.
DR GO; GO:0106029; F:tRNA pseudouridine synthase activity; IDA:UniProtKB.
DR GO; GO:0031053; P:primary miRNA processing; IDA:UniProtKB.
DR GO; GO:0031119; P:tRNA pseudouridine synthesis; IDA:UniProtKB.
DR DisProt; DP02614; -.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR039894; Pus10-like.
DR PANTHER; PTHR21568; PTHR21568; 1.
DR SUPFAM; SSF55120; SSF55120; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; Isomerase; Metal-binding;
KW Mitochondrion; Nucleus; Phosphoprotein; Reference proteome;
KW tRNA processing; Zinc.
FT CHAIN 1..529
FT /note="tRNA pseudouridine synthase Pus10"
FT /id="PRO_0000299022"
FT REGION 304..317
FT /note="RNA binding forefinger loop"
FT /evidence="ECO:0000255"
FT REGION 442..457
FT /note="RNA binding thumb loop"
FT /evidence="ECO:0000255"
FT COILED 42..89
FT /evidence="ECO:0000255"
FT ACT_SITE 344
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:30530625,
FT ECO:0000269|PubMed:31819270"
FT BINDING 21
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:17900615,
FT ECO:0007744|PDB:2V9K"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:17900615,
FT ECO:0007744|PDB:2V9K"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:17900615,
FT ECO:0007744|PDB:2V9K"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:17900615,
FT ECO:0007744|PDB:2V9K"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 484
FT /note="T -> I (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs1486089321)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035617"
FT MUTAGEN 344
FT /note="D->A: Abolished tRNA pseudouridine synthase without
FT affecting ability to promote miRNA processing."
FT /evidence="ECO:0000269|PubMed:30530625,
FT ECO:0000269|PubMed:31819270"
FT CONFLICT 208
FT /note="F -> L (in Ref. 1; BAB71300)"
FT /evidence="ECO:0000305"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:2V9K"
FT HELIX 9..18
FT /evidence="ECO:0007829|PDB:2V9K"
FT HELIX 22..28
FT /evidence="ECO:0007829|PDB:2V9K"
FT HELIX 35..38
FT /evidence="ECO:0007829|PDB:2V9K"
FT HELIX 41..52
FT /evidence="ECO:0007829|PDB:2V9K"
FT TURN 110..117
FT /evidence="ECO:0007829|PDB:2V9K"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:2V9K"
FT HELIX 122..134
FT /evidence="ECO:0007829|PDB:2V9K"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:2V9K"
FT HELIX 152..169
FT /evidence="ECO:0007829|PDB:2V9K"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:2V9K"
FT HELIX 182..198
FT /evidence="ECO:0007829|PDB:2V9K"
FT STRAND 207..215
FT /evidence="ECO:0007829|PDB:2V9K"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:2V9K"
FT HELIX 221..227
FT /evidence="ECO:0007829|PDB:2V9K"
FT HELIX 246..255
FT /evidence="ECO:0007829|PDB:2V9K"
FT HELIX 258..264
FT /evidence="ECO:0007829|PDB:2V9K"
FT STRAND 277..285
FT /evidence="ECO:0007829|PDB:2V9K"
FT STRAND 288..296
FT /evidence="ECO:0007829|PDB:2V9K"
FT STRAND 307..315
FT /evidence="ECO:0007829|PDB:2V9K"
FT HELIX 318..323
FT /evidence="ECO:0007829|PDB:2V9K"
FT HELIX 326..330
FT /evidence="ECO:0007829|PDB:2V9K"
FT STRAND 333..341
FT /evidence="ECO:0007829|PDB:2V9K"
FT STRAND 348..362
FT /evidence="ECO:0007829|PDB:2V9K"
FT HELIX 370..381
FT /evidence="ECO:0007829|PDB:2V9K"
FT STRAND 385..395
FT /evidence="ECO:0007829|PDB:2V9K"
FT HELIX 398..409
FT /evidence="ECO:0007829|PDB:2V9K"
FT STRAND 412..422
FT /evidence="ECO:0007829|PDB:2V9K"
FT HELIX 426..429
FT /evidence="ECO:0007829|PDB:2V9K"
FT HELIX 430..434
FT /evidence="ECO:0007829|PDB:2V9K"
FT STRAND 437..443
FT /evidence="ECO:0007829|PDB:2V9K"
FT HELIX 446..448
FT /evidence="ECO:0007829|PDB:2V9K"
FT TURN 449..451
FT /evidence="ECO:0007829|PDB:2V9K"
FT STRAND 456..470
FT /evidence="ECO:0007829|PDB:2V9K"
FT STRAND 473..480
FT /evidence="ECO:0007829|PDB:2V9K"
FT HELIX 486..491
FT /evidence="ECO:0007829|PDB:2V9K"
FT TURN 493..496
FT /evidence="ECO:0007829|PDB:2V9K"
FT STRAND 497..499
FT /evidence="ECO:0007829|PDB:2V9K"
FT HELIX 501..505
FT /evidence="ECO:0007829|PDB:2V9K"
FT STRAND 509..519
FT /evidence="ECO:0007829|PDB:2V9K"
SQ SEQUENCE 529 AA; 60244 MW; 44E7BD6ED9C9864E CRC64;
MFPLTEENKH VAQLLLNTGT CPRCIFRFCG VDFHAPYKLP YKELLNELQK FLETEKDELI
LEVMNPPPKK IRLQELEDSI DNLSQNGEGR ISVSHVGSTA SKNSNLNVCN VCLGILQEFC
EKDFIKKVCQ KVEASGFEFT SLVFSVSFPP QLSVREHAAW LLVKQEMGKQ SLSLGRDDIV
QLKEAYKWIT HPLFSEELGV PIDGKSLFEV SVVFAHPETV EDCHFLAAIC PDCFKPAKNK
QSVFTRMAVM KALNKIKEED FLKQFPCPPN SPKAVCAVLE IECAHGAVFV AGRYNKYSRN
LPQTPWIIDG ERKLESSVEE LISDHLLAVF KAESFNFSSS GREDVDVRTL GNGRPFAIEL
VNPHRVHFTS QEIKELQQKI NNSSNKIQVR DLQLVTREAI GHMKEGEEEK TKTYSALIWT
NKAIQKKDIE FLNDIKDLKI DQKTPLRVLH RRPLAVRARV IHFMETQYVD EHHFRLHLKT
QAGTYIKEFV HGDFGRTKPN IGSLMNVTAD ILELDVESVD VDWPPALDD
