RUSD2_HUMAN
ID RUSD2_HUMAN Reviewed; 545 AA.
AC Q8IZ73; B4DDD1; Q7L989; Q92939; Q96IA7; Q96N50;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Pseudouridylate synthase RPUSD2 {ECO:0000305};
DE EC=5.4.99.- {ECO:0000269|PubMed:31477916, ECO:0000269|PubMed:35051350};
DE AltName: Full=RNA pseudouridylate synthase domain-containing protein 2 {ECO:0000305};
GN Name=RPUSD2 {ECO:0000303|PubMed:31477916, ECO:0000312|HGNC:HGNC:24180};
GN Synonyms=C15orf19 {ECO:0000312|HGNC:HGNC:24180};
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] (ISOFORMS 1 AND 2).
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 GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymph;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 334-545.
RC TISSUE=Lung;
RA Sampson M., McClendon D., Wiley K., Barlow C.;
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND IDENTIFICATION BY
RP 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 [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, 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 [9]
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 [10]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=35051350; DOI=10.1016/j.molcel.2021.12.023;
RA Martinez N.M., Su A., Burns M.C., Nussbacher J.K., Schaening C., Sathe S.,
RA Yeo G.W., Gilbert W.V.;
RT "Pseudouridine synthases modify human pre-mRNA co-transcriptionally and
RT affect pre-mRNA processing.";
RL Mol. Cell 82:645-659(2022).
CC -!- FUNCTION: Pseudouridine synthase that catalyzes pseudouridylation of
CC mRNAs. {ECO:0000269|PubMed:31477916, ECO:0000269|PubMed:35051350}.
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:0000269|PubMed:35051350};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8IZ73-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IZ73-2; Sequence=VSP_055372;
CC -!- SIMILARITY: Belongs to the pseudouridine synthase RluA family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB07777.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK055971; BAB71059.1; -; mRNA.
DR EMBL; AK293145; BAG56692.1; -; mRNA.
DR EMBL; AC091045; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007697; AAH07697.1; -; mRNA.
DR EMBL; BC016967; AAH16967.2; -; mRNA.
DR EMBL; U67934; AAB07777.1; ALT_FRAME; Genomic_DNA.
DR CCDS; CCDS10061.1; -. [Q8IZ73-1]
DR CCDS; CCDS66737.1; -. [Q8IZ73-2]
DR RefSeq; NP_001273336.1; NM_001286407.1. [Q8IZ73-2]
DR RefSeq; NP_689473.1; NM_152260.2. [Q8IZ73-1]
DR AlphaFoldDB; Q8IZ73; -.
DR SMR; Q8IZ73; -.
DR BioGRID; 117987; 32.
DR IntAct; Q8IZ73; 9.
DR MINT; Q8IZ73; -.
DR STRING; 9606.ENSP00000323288; -.
DR GlyGen; Q8IZ73; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8IZ73; -.
DR MetOSite; Q8IZ73; -.
DR PhosphoSitePlus; Q8IZ73; -.
DR BioMuta; RPUSD2; -.
DR DMDM; 158563848; -.
DR EPD; Q8IZ73; -.
DR jPOST; Q8IZ73; -.
DR MassIVE; Q8IZ73; -.
DR MaxQB; Q8IZ73; -.
DR PaxDb; Q8IZ73; -.
DR PeptideAtlas; Q8IZ73; -.
DR PRIDE; Q8IZ73; -.
DR ProteomicsDB; 3846; -.
DR ProteomicsDB; 71285; -. [Q8IZ73-1]
DR Antibodypedia; 10143; 152 antibodies from 21 providers.
DR DNASU; 27079; -.
DR Ensembl; ENST00000315616.12; ENSP00000323288.7; ENSG00000166133.18. [Q8IZ73-1]
DR Ensembl; ENST00000559271.1; ENSP00000453036.1; ENSG00000166133.18. [Q8IZ73-2]
DR GeneID; 27079; -.
DR KEGG; hsa:27079; -.
DR MANE-Select; ENST00000315616.12; ENSP00000323288.7; NM_152260.3; NP_689473.1.
DR UCSC; uc001zmd.3; human. [Q8IZ73-1]
DR CTD; 27079; -.
DR DisGeNET; 27079; -.
DR GeneCards; RPUSD2; -.
DR HGNC; HGNC:24180; RPUSD2.
DR HPA; ENSG00000166133; Low tissue specificity.
DR MIM; 617488; gene.
DR neXtProt; NX_Q8IZ73; -.
DR OpenTargets; ENSG00000166133; -.
DR PharmGKB; PA134866412; -.
DR VEuPathDB; HostDB:ENSG00000166133; -.
DR eggNOG; KOG1919; Eukaryota.
DR GeneTree; ENSGT00420000029802; -.
DR HOGENOM; CLU_016902_12_5_1; -.
DR InParanoid; Q8IZ73; -.
DR OMA; VAYHDEM; -.
DR OrthoDB; 821308at2759; -.
DR PhylomeDB; Q8IZ73; -.
DR TreeFam; TF323255; -.
DR PathwayCommons; Q8IZ73; -.
DR SignaLink; Q8IZ73; -.
DR BioGRID-ORCS; 27079; 11 hits in 1078 CRISPR screens.
DR ChiTaRS; RPUSD2; human.
DR GenomeRNAi; 27079; -.
DR Pharos; Q8IZ73; Tdark.
DR PRO; PR:Q8IZ73; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q8IZ73; protein.
DR Bgee; ENSG00000166133; Expressed in endometrium epithelium and 132 other tissues.
DR ExpressionAtlas; Q8IZ73; baseline and differential.
DR Genevisible; Q8IZ73; HS.
DR GO; GO:0009982; F:pseudouridine synthase activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000455; P:enzyme-directed rRNA pseudouridine synthesis; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:1990481; P:mRNA pseudouridine synthesis; IDA:UniProtKB.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR006225; PsdUridine_synth_RluC/D.
DR InterPro; IPR006224; PsdUridine_synth_RluC/D_CS.
DR InterPro; IPR006145; PsdUridine_synth_RsuA/RluA.
DR Pfam; PF00849; PseudoU_synth_2; 1.
DR SUPFAM; SSF55120; SSF55120; 1.
DR TIGRFAMs; TIGR00005; rluA_subfam; 1.
DR PROSITE; PS01129; PSI_RLU; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Isomerase; mRNA processing; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..545
FT /note="Pseudouridylate synthase RPUSD2"
FT /id="PRO_0000300819"
FT REGION 48..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 274
FT /evidence="ECO:0000250|UniProtKB:P0AA37"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 477
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q149F1"
FT VAR_SEQ 141..201
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055372"
FT CONFLICT 336
FT /note="R -> L (in Ref. 4; AAB07777)"
FT /evidence="ECO:0000305"
FT CONFLICT 492
FT /note="N -> H (in Ref. 4; AAB07777)"
FT /evidence="ECO:0000305"
FT CONFLICT 499
FT /note="C -> S (in Ref. 4; AAB07777)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 545 AA; 61311 MW; 16E8B71918A6E0B7 CRC64;
MWLDRRGWLR VLGHWRYDLR RPSFTRTWSG DKGPMAETVS TQVGTEGGLR ASHQQNGDAG
GDAKVELSPG PPKPAGREVE PAPVGGEHPS AAAPGPGKHK KRRGATRERV VPPPKKRRTG
VSFGDEHFAE TSYYFEGGLR KVRPYYFDFR TYCKGRWVGH SLLHVFSTEF RAQPLAYYEA
AVRAGRLQLN EKPVQDLNIV LKDNDFLRNT VHRHEPPVTA EPIRLLAENE DVVVVDKPSS
IPVHPCGRFR HNTVIFILGK EHQLKELHPL HRLDRLTSGV LMFAKTAAVS ERIHEQVRDR
QLEKEYVCRV EGEFPTEEVT CKEPILVVSY KVGVCRVDPR GKPCETVFQR LSYNGQSSVV
RCRPLTGRTH QIRVHLQFLG HPILNDPIYN SVAWGPSRGR GGYIPKTNEE LLRDLVAEHQ
AKQSLDVLDL CEGDLSPGLT DSTAPSSELG KDDLEELAAA AQKMEEVAEA APQELDTIAL
ASEKAVETDV MNQETDPLCA ECRLVRQDPL PQDLVMFLHA LRYKGPGFEY FSPMPAWAQD
DWQKD
