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 10-JUN-2026, entry version 178. 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:34718722, PubMed:35051350). 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_001318164.2. [Q96PZ0-1] DR RefSeq; NP_061915.2; NM_019042.4. [Q96PZ0-1] DR RefSeq; XP_005250519.1; XM_005250462.5. [Q96PZ0-2] DR RefSeq; XP_016867856.1; XM_017012367.3. [Q96PZ0-2] DR RefSeq; XP_054214480.1; XM_054358505.1. [Q96PZ0-2] DR RefSeq; XP_054214481.1; XM_054358506.1. [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; 153. DR FunCoup; Q96PZ0; 2257. DR IntAct; Q96PZ0; 80. DR NDEx; IQUERY-CP-PUS7; 1 NDEx IQuery Curated Pathway. DR STRING; 9606.ENSP00000417402; -. 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 jPOST; Q96PZ0; -. DR MassIVE; Q96PZ0; -. DR PaxDb; 9606-ENSP00000417402; -. DR PeptideAtlas; Q96PZ0; -. DR ProteomicsDB; 77793; -. DR Pumba; Q96PZ0; -. DR Antibodypedia; 17076; 135 antibodies from 19 providers. DR DNASU; 54517; -. DR Ensembl; ENST00000356362.6; ENSP00000348722.2; ENSG00000091127.15. [Q96PZ0-1] DR Ensembl; ENST00000469408.6; ENSP00000417402.1; ENSG00000091127.15. [Q96PZ0-1] DR Ensembl; ENST00000929037.1; ENSP00000599096.1; ENSG00000091127.15. [Q96PZ0-1] DR Ensembl; ENST00000929039.1; ENSP00000599098.1; ENSG00000091127.15. [Q96PZ0-1] DR Ensembl; ENST00000947300.1; ENSP00000617359.1; ENSG00000091127.15. [Q96PZ0-2] DR Ensembl; ENST00000947301.1; ENSP00000617360.1; ENSG00000091127.15. [Q96PZ0-2] 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 AGR; HGNC:26033; -. DR ClinPGx; PA143485587; -. 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 OpenTargets; ENSG00000091127; -. DR Orphanet; 528084; Non-specific syndromic intellectual disability. DR VEuPathDB; HostDB:ENSG00000091127; -. DR eggNOG; KOG2339; Eukaryota. DR GeneTree; ENSGT00530000063554; -. DR HOGENOM; CLU_005281_0_1_1; -. DR InParanoid; Q96PZ0; -. DR OMA; WINYFGH; -. DR OrthoDB; 447290at2759; -. DR PAN-GO; Q96PZ0; 3 GO annotations based on evolutionary models. DR PhylomeDB; Q96PZ0; -. DR BRENDA; 4.2.1.70; 2681. 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 Agora; ENSG00000091127; -. DR BioGRID-ORCS; 54517; 23 hits in 1159 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 169 other cell types or tissues. DR ExpressionAtlas; Q96PZ0; baseline and differential. 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:0160150; F:tRNA pseudouridine(13) 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: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 CDD; cd02576; PseudoU_synth_ScPUS7; 1. DR FunFam; 3.30.2350.20:FF:000002; Pseudouridylate synthase 7 homolog; 1. DR FunFam; 3.30.2350.20:FF:000003; Pseudouridylate synthase 7 homolog; 1. DR Gene3D; 3.30.2350.20; TruD, catalytic domain; 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 NCBIfam; TIGR00094; tRNA_TruD_broad; 1. DR PANTHER; PTHR13326:SF31; PSEUDOURIDYLATE SYNTHASE 7 HOMOLOG; 1. DR PANTHER; PTHR13326; TRNA PSEUDOURIDINE SYNTHASE D; 1. DR Pfam; PF01142; TruD; 1. DR PIRSF; PIRSF037016; Pseudouridin_synth_euk_prd; 1. DR SUPFAM; SSF55120; Pseudouridine synthase; 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; Proteomics identification; Reference proteome; KW 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 36..52 FT /note="Polar 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; uncertain significance; mild FT phenotype; decreased pseudouridylate 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; uncertain 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 155..157 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 HELIX 609..612 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 //