PUS7_HUMAN
ID PUS7_HUMAN Reviewed; 661 AA.
AC Q96PZ0; Q75MG4; Q9NX19;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2003, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Pseudouridylate synthase 7 homolog {ECO:0000305};
DE EC=5.4.99.- {ECO:0000269|PubMed:29628141, ECO:0000269|PubMed:31477916, ECO:0000269|PubMed:34718722, ECO:0000269|PubMed:35051350, ECO:0000305|PubMed:28073919};
GN Name=PUS7 {ECO:0000303|PubMed:30526862, ECO:0000312|HGNC:HGNC:26033};
GN Synonyms=KIAA1897 {ECO:0000303|PubMed:11572484};
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=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, and Urinary bladder;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 23-661 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=11572484; DOI=10.1093/dnares/8.4.179;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXI. The
RT complete sequences of 60 new cDNA clones from brain which code for large
RT proteins.";
RL DNA Res. 8:179-187(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 420-661.
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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-610, AND IDENTIFICATION BY
RP 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 [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 ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-127 AND THR-610, AND
RP IDENTIFICATION BY 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 [10]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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 [11]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF ASP-294.
RX PubMed=29628141; DOI=10.1016/j.cell.2018.03.008;
RA Guzzi N., Ciesla M., Ngoc P.C.T., Lang S., Arora S., Dimitriou M.,
RA Pimkova K., Sommarin M.N.E., Munita R., Lubas M., Lim Y., Okuyama K.,
RA Soneji S., Karlsson G., Hansson J., Joensson G., Lund A.H., Sigvardsson M.,
RA Hellstroem-Lindberg E., Hsieh A.C., Bellodi C.;
RT "Pseudouridylation of tRNA-derived fragments steers translational control
RT in stem cells.";
RL Cell 0:0-0(2018).
RN [12]
RP INVOLVEMENT IN IDDABS, AND VARIANT IDDABS 450-ARG--ARG-661 DEL.
RX PubMed=30526862; DOI=10.1016/j.ajhg.2018.10.026;
RA de Brouwer A.P.M., Abou Jamra R., Koertel N., Soyris C., Polla D.L.,
RA Safra M., Zisso A., Powell C.A., Rebelo-Guiomar P., Dinges N., Morin V.,
RA Stock M., Hussain M., Shahzad M., Riazuddin S., Ahmed Z.M., Pfundt R.,
RA Schwarz F., de Boer L., Reis A., Grozeva D., Raymond F.L., Riazuddin S.,
RA Koolen D.A., Minczuk M., Roignant J.Y., van Bokhoven H., Schwartz S.;
RT "Variants in PUS7 cause intellectual disability with speech delay,
RT microcephaly, short stature, and aggressive behavior.";
RL Am. J. Hum. Genet. 103:1045-1052(2018).
RN [13]
RP INTERACTION WITH SIRT1.
RX PubMed=31451225; DOI=10.1016/j.bbrc.2019.08.097;
RA Dalal S., Deshmukh P., Unni S., Padavattan S., Padmanabhan B.;
RT "Biochemical insight into pseudouridine synthase 7 (PUS7) as a novel
RT interactor of sirtuin, SIRT1.";
RL Biochem. Biophys. Res. Commun. 518:598-604(2019).
RN [14]
RP FUNCTION, INVOLVEMENT IN IDDABS, VARIANT IDDABS TYR-503, AND
RP CHARACTERIZATION OF VARIANT IDDABS TYR-503.
RX PubMed=30778726; DOI=10.1007/s00439-019-01980-3;
RA Shaheen R., Tasak M., Maddirevula S., Abdel-Salam G.M.H., Sayed I.S.M.,
RA Alazami A.M., Al-Sheddi T., Alobeid E., Phizicky E.M., Alkuraya F.S.;
RT "PUS7 mutations impair pseudouridylation in humans and cause intellectual
RT disability and microcephaly.";
RL Hum. Genet. 138:231-239(2019).
RN [15]
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 [16]
RP VARIANT IDDABS ARG-128.
RX PubMed=31583274; DOI=10.1212/nxg.0000000000000356;
RA Darvish H., Azcona L.J., Alehabib E., Jamali F., Tafakhori A.,
RA Ranji-Burachaloo S., Jen J.C., Paisan-Ruiz C.;
RT "A novel PUS7 mutation causes intellectual disability with autistic and
RT aggressive behaviors.";
RL Neurol. Genet. 5:e356-e356(2019).
RN [17]
RP INVOLVEMENT IN IDDABS.
RX PubMed=33100873; DOI=10.1016/j.sjbs.2020.09.033;
RA Naseer M.I., Abdulkareem A.A., Jan M.M., Chaudhary A.G., Alharazy S.,
RA AlQahtani M.H.;
RT "Next generation sequencing reveals novel homozygous frameshift in PUS7 and
RT splice acceptor variants in AASS gene leading to intellectual disability,
RT developmental delay, dysmorphic feature and microcephaly.";
RL Saudi J. Biol. Sci. 27:3125-3131(2020).
RN [18]
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).
RN [19]
RP VARIANT IDDABS MET-387, AND SUBCELLULAR LOCATION.
RX PubMed=35144859; DOI=10.1016/j.ymgme.2022.01.103;
RA Han S.T., Kim A.C., Garcia K., Schimmenti L.A., Macnamara E., Network U.D.,
RA Gahl W.A., Malicdan M.C., Tifft C.J.;
RT "PUS7 deficiency in human patients causes profound neurodevelopmental
RT phenotype by dysregulating protein translation.";
RL Mol. Genet. Metab. 135:221-229(2022).
RN [20] {ECO:0007744|PDB:5KKP}
RP X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS) OF 99-661, FUNCTION, CATALYTIC
RP ACTIVITY, ACTIVE SITE, MUTAGENESIS OF ASP-294, AND CHARACTERIZATION OF
RP VARIANT IDDABS ARG-128.
RX PubMed=34718722; DOI=10.1093/nar/gkab934;
RA Guegueniat J., Halabelian L., Zeng H., Dong A., Li Y., Wu H.,
RA Arrowsmith C.H., Kothe U.;
RT "The human pseudouridine synthase PUS7 recognizes RNA with an extended
RT multi-domain binding surface.";
RL Nucleic Acids Res. 49:11810-11822(2021).
CC -!- FUNCTION: Pseudouridylate synthase that catalyzes pseudouridylation of
CC RNAs (PubMed:28073919, PubMed:29628141, PubMed:30778726,
CC PubMed:31477916, PubMed:35051350, PubMed:34718722). Acts as a regulator
CC of protein synthesis in embryonic stem cells by mediating
CC pseudouridylation of RNA fragments derived from tRNAs (tRFs):
CC pseudouridylated tRFs inhibit translation by targeting the translation
CC initiation complex (PubMed:29628141). Also catalyzes pseudouridylation
CC of mRNAs: mediates pseudouridylation of mRNAs with the consensus
CC sequence 5'-UGUAG-3' (PubMed:28073919, PubMed:31477916,
CC PubMed:35051350). Acts as a regulator of pre-mRNA splicing by mediating
CC pseudouridylation of pre-mRNAs at locations associated with
CC alternatively spliced regions (PubMed:35051350). Pseudouridylation of
CC pre-mRNAs near splice sites directly regulates mRNA splicing and mRNA
CC 3'-end processing (PubMed:35051350). In addition to mRNAs and tRNAs,
CC binds other types of RNAs, such as snRNAs, Y RNAs and vault RNAs,
CC suggesting that it can catalyze pseudouridylation of many RNA types
CC (PubMed:29628141). {ECO:0000269|PubMed:28073919,
CC ECO:0000269|PubMed:29628141, ECO:0000269|PubMed:30778726,
CC ECO:0000269|PubMed:31477916, ECO:0000269|PubMed:34718722,
CC ECO:0000269|PubMed:35051350}.
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:29628141, ECO:0000269|PubMed:34718722};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(13) in tRNA = pseudouridine(13) in tRNA;
CC Xref=Rhea:RHEA:42540, Rhea:RHEA-COMP:10105, Rhea:RHEA-COMP:10106,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
CC Evidence={ECO:0000269|PubMed:34718722};
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 ECO:0000305|PubMed:28073919};
CC -!- SUBUNIT: Interacts with SIRT1. {ECO:0000269|PubMed:31451225}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29628141,
CC ECO:0000269|PubMed:35144859}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96PZ0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96PZ0-2; Sequence=VSP_059620;
CC -!- DISEASE: Intellectual developmental disorder with abnormal behavior,
CC microcephaly, and short stature (IDDABS) [MIM:618342]: An autosomal
CC recessive disorder characterized by intellectual disability,
CC developmental delay with poor or absent speech, short stature,
CC progressive microcephaly, hyperactivity and aggressive behavior. Some
CC patients manifest sensorineural hearing loss.
CC {ECO:0000269|PubMed:30526862, ECO:0000269|PubMed:30778726,
CC ECO:0000269|PubMed:31583274, ECO:0000269|PubMed:33100873,
CC ECO:0000269|PubMed:34718722, ECO:0000269|PubMed:35144859}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the pseudouridine synthase TruD family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91203.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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; AC073138; AAS07447.1; -; Genomic_DNA.
DR EMBL; AC074013; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005209; AAH05209.3; -; mRNA.
DR EMBL; BC011396; AAH11396.2; -; mRNA.
DR EMBL; AB067484; BAB67790.1; -; mRNA.
DR EMBL; AK000492; BAA91203.1; ALT_INIT; mRNA.
DR CCDS; CCDS34725.1; -. [Q96PZ0-1]
DR RefSeq; NP_001305092.1; NM_001318163.1. [Q96PZ0-2]
DR RefSeq; NP_001305093.1; NM_001318164.1. [Q96PZ0-1]
DR RefSeq; NP_061915.2; NM_019042.4. [Q96PZ0-1]
DR RefSeq; XP_005250519.1; XM_005250462.3. [Q96PZ0-2]
DR RefSeq; XP_016867856.1; XM_017012367.1. [Q96PZ0-2]
DR PDB; 5KKP; X-ray; 2.26 A; A=99-661.
DR PDBsum; 5KKP; -.
DR AlphaFoldDB; Q96PZ0; -.
DR SMR; Q96PZ0; -.
DR BioGRID; 120011; 142.
DR IntAct; Q96PZ0; 6.
DR STRING; 9606.ENSP00000348722; -.
DR GlyGen; Q96PZ0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96PZ0; -.
DR MetOSite; Q96PZ0; -.
DR PhosphoSitePlus; Q96PZ0; -.
DR BioMuta; PUS7; -.
DR DMDM; 37090412; -.
DR EPD; Q96PZ0; -.
DR jPOST; Q96PZ0; -.
DR MassIVE; Q96PZ0; -.
DR MaxQB; Q96PZ0; -.
DR PaxDb; Q96PZ0; -.
DR PeptideAtlas; Q96PZ0; -.
DR PRIDE; Q96PZ0; -.
DR ProteomicsDB; 77793; -.
DR Antibodypedia; 17076; 133 antibodies from 17 providers.
DR DNASU; 54517; -.
DR Ensembl; ENST00000356362.6; ENSP00000348722.2; ENSG00000091127.14. [Q96PZ0-1]
DR Ensembl; ENST00000469408.6; ENSP00000417402.1; ENSG00000091127.14. [Q96PZ0-1]
DR GeneID; 54517; -.
DR KEGG; hsa:54517; -.
DR MANE-Select; ENST00000469408.6; ENSP00000417402.1; NM_019042.5; NP_061915.2.
DR UCSC; uc003vcx.5; human. [Q96PZ0-1]
DR CTD; 54517; -.
DR DisGeNET; 54517; -.
DR GeneCards; PUS7; -.
DR HGNC; HGNC:26033; PUS7.
DR HPA; ENSG00000091127; Low tissue specificity.
DR MalaCards; PUS7; -.
DR MIM; 616261; gene.
DR MIM; 618342; phenotype.
DR neXtProt; NX_Q96PZ0; -.
DR OpenTargets; ENSG00000091127; -.
DR Orphanet; 528084; Non-specific syndromic intellectual disability.
DR PharmGKB; PA143485587; -.
DR VEuPathDB; HostDB:ENSG00000091127; -.
DR eggNOG; KOG2339; Eukaryota.
DR GeneTree; ENSGT00530000063554; -.
DR HOGENOM; CLU_005281_0_1_1; -.
DR InParanoid; Q96PZ0; -.
DR OMA; ERGYFNY; -.
DR OrthoDB; 955294at2759; -.
DR PhylomeDB; Q96PZ0; -.
DR TreeFam; TF314278; -.
DR BRENDA; 5.4.99.27; 2681.
DR PathwayCommons; Q96PZ0; -.
DR Reactome; R-HSA-6782315; tRNA modification in the nucleus and cytosol.
DR SignaLink; Q96PZ0; -.
DR BioGRID-ORCS; 54517; 21 hits in 1078 CRISPR screens.
DR ChiTaRS; PUS7; human.
DR GenomeRNAi; 54517; -.
DR Pharos; Q96PZ0; Tbio.
DR PRO; PR:Q96PZ0; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q96PZ0; protein.
DR Bgee; ENSG00000091127; Expressed in buccal mucosa cell and 167 other tissues.
DR ExpressionAtlas; Q96PZ0; baseline and differential.
DR Genevisible; Q96PZ0; HS.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0009982; F:pseudouridine synthase activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:1990481; P:mRNA pseudouridine synthesis; IDA:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; IDA:UniProtKB.
DR GO; GO:0001522; P:pseudouridine synthesis; IBA:GO_Central.
DR GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; IMP:UniProtKB.
DR GO; GO:2000380; P:regulation of mesoderm development; IMP:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0031119; P:tRNA pseudouridine synthesis; IDA:UniProtKB.
DR Gene3D; 3.30.2350.20; -; 2.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR001656; PsdUridine_synth_TruD.
DR InterPro; IPR020119; PsdUridine_synth_TruD_CS.
DR InterPro; IPR011760; PsdUridine_synth_TruD_insert.
DR InterPro; IPR042214; TruD_catalytic.
DR PANTHER; PTHR13326; PTHR13326; 1.
DR Pfam; PF01142; TruD; 1.
DR PIRSF; PIRSF037016; Pseudouridin_synth_euk_prd; 1.
DR SUPFAM; SSF55120; SSF55120; 1.
DR TIGRFAMs; TIGR00094; tRNA_TruD_broad; 1.
DR PROSITE; PS50984; TRUD; 1.
DR PROSITE; PS01268; UPF0024; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Disease variant; Dwarfism;
KW Intellectual disability; Isomerase; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Reference proteome; tRNA processing.
FT CHAIN 1..661
FT /note="Pseudouridylate synthase 7 homolog"
FT /id="PRO_0000152558"
FT DOMAIN 370..580
FT /note="TRUD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00342"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..97
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 294
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:29628141,
FT ECO:0000305|PubMed:34718722"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 610
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 244
FT /note="N -> KVRTAAD (in isoform 2)"
FT /id="VSP_059620"
FT VARIANT 128
FT /note="G -> R (in IDDABS; unknown pathological
FT significance; mild phenotype; decreased pseudouridylate
FT synthase activity)"
FT /evidence="ECO:0000269|PubMed:31583274,
FT ECO:0000269|PubMed:34718722"
FT /id="VAR_086160"
FT VARIANT 387
FT /note="T -> M (in IDDABS; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:35144859"
FT /id="VAR_086161"
FT VARIANT 450..661
FT /note="Missing (in IDDABS)"
FT /evidence="ECO:0000269|PubMed:30526862"
FT /id="VAR_082041"
FT VARIANT 503
FT /note="D -> Y (in IDDABS; decreased pseudouridylate
FT synthase activity)"
FT /evidence="ECO:0000269|PubMed:30778726"
FT /id="VAR_082042"
FT MUTAGEN 294
FT /note="D->A: Loss of pseudouridylate synthase activity."
FT /evidence="ECO:0000269|PubMed:29628141,
FT ECO:0000269|PubMed:34718722"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:5KKP"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:5KKP"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:5KKP"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:5KKP"
FT HELIX 166..177
FT /evidence="ECO:0007829|PDB:5KKP"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:5KKP"
FT HELIX 201..213
FT /evidence="ECO:0007829|PDB:5KKP"
FT STRAND 219..225
FT /evidence="ECO:0007829|PDB:5KKP"
FT STRAND 228..234
FT /evidence="ECO:0007829|PDB:5KKP"
FT STRAND 256..266
FT /evidence="ECO:0007829|PDB:5KKP"
FT HELIX 269..280
FT /evidence="ECO:0007829|PDB:5KKP"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:5KKP"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:5KKP"
FT STRAND 295..306
FT /evidence="ECO:0007829|PDB:5KKP"
FT HELIX 310..315
FT /evidence="ECO:0007829|PDB:5KKP"
FT HELIX 316..319
FT /evidence="ECO:0007829|PDB:5KKP"
FT STRAND 321..333
FT /evidence="ECO:0007829|PDB:5KKP"
FT STRAND 342..351
FT /evidence="ECO:0007829|PDB:5KKP"
FT HELIX 356..368
FT /evidence="ECO:0007829|PDB:5KKP"
FT HELIX 377..380
FT /evidence="ECO:0007829|PDB:5KKP"
FT HELIX 387..395
FT /evidence="ECO:0007829|PDB:5KKP"
FT HELIX 399..407
FT /evidence="ECO:0007829|PDB:5KKP"
FT HELIX 416..428
FT /evidence="ECO:0007829|PDB:5KKP"
FT HELIX 431..435
FT /evidence="ECO:0007829|PDB:5KKP"
FT STRAND 441..443
FT /evidence="ECO:0007829|PDB:5KKP"
FT HELIX 444..455
FT /evidence="ECO:0007829|PDB:5KKP"
FT HELIX 460..464
FT /evidence="ECO:0007829|PDB:5KKP"
FT HELIX 469..495
FT /evidence="ECO:0007829|PDB:5KKP"
FT STRAND 504..507
FT /evidence="ECO:0007829|PDB:5KKP"
FT STRAND 510..513
FT /evidence="ECO:0007829|PDB:5KKP"
FT STRAND 516..518
FT /evidence="ECO:0007829|PDB:5KKP"
FT HELIX 519..521
FT /evidence="ECO:0007829|PDB:5KKP"
FT HELIX 524..526
FT /evidence="ECO:0007829|PDB:5KKP"
FT STRAND 527..531
FT /evidence="ECO:0007829|PDB:5KKP"
FT STRAND 533..535
FT /evidence="ECO:0007829|PDB:5KKP"
FT HELIX 543..553
FT /evidence="ECO:0007829|PDB:5KKP"
FT HELIX 566..568
FT /evidence="ECO:0007829|PDB:5KKP"
FT STRAND 573..579
FT /evidence="ECO:0007829|PDB:5KKP"
FT STRAND 582..592
FT /evidence="ECO:0007829|PDB:5KKP"
FT HELIX 602..607
FT /evidence="ECO:0007829|PDB:5KKP"
FT STRAND 619..629
FT /evidence="ECO:0007829|PDB:5KKP"
FT HELIX 635..643
FT /evidence="ECO:0007829|PDB:5KKP"
SQ SEQUENCE 661 AA; 75035 MW; 6F6A05A9B57B1560 CRC64;
MEMTEMTGVS LKRGALVVED NDSGVPVEET KKQKLSECSL TKGQDGLQND FLSISEDVPR
PPDTVSTGKG GKNSEAQLED EEEEEEDGLS EECEEEESES FADMMKHGLT EADVGITKFV
SSHQGFSGIL KERYSDFVVH EIGKDGRISH LNDLSIPVDE EDPSEDIFTV LTAEEKQRLE
ELQLFKNKET SVAIEVIEDT KEKRTIIHQA IKSLFPGLET KTEDREGKKY IVAYHAAGKK
ALANPRKHSW PKSRGSYCHF VLYKENKDTM DAINVLSKYL RVKPNIFSYM GTKDKRAITV
QEIAVLKITA QRLAHLNKCL MNFKLGNFSY QKNPLKLGEL QGNHFTVVLR NITGTDDQVQ
QAMNSLKEIG FINYYGMQRF GTTAVPTYQV GRAILQNSWT EVMDLILKPR SGAEKGYLVK
CREEWAKTKD PTAALRKLPV KRCVEGQLLR GLSKYGMKNI VSAFGIIPRN NRLMYIHSYQ
SYVWNNMVSK RIEDYGLKPV PGDLVLKGAT ATYIEEDDVN NYSIHDVVMP LPGFDVIYPK
HKIQEAYREM LTADNLDIDN MRHKIRDYSL SGAYRKIIIR PQNVSWEVVA YDDPKIPLFN
TDVDNLEGKT PPVFASEGKY RALKMDFSLP PSTYATMAIR EVLKMDTSIK NQTQLNTTWL
R
