Search Results

Overview

Uniprot IDQ96PZ0
Protein NamePseudouridylate synthase 7 homolog
Gene NamePUS7
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
186 LEELQLFKNKETSVA
188 ELQLFKNKETSVAIE
31 GVPVEETKKQKLSEC
32 VPVEETKKQKLSECS
34 VEETKKQKLSECSLT

Function

Pseudouridylate synthase that catalyzes pseudouridylation of RNAs (PubMed:28073919, PubMed:29628141, PubMed:30778726, PubMed:31477916, PubMed:34718722, PubMed:35051350). Acts as a regulator of protein synthesis in embryonic stem cells by mediating pseudouridylation of RNA fragments derived from tRNAs (tRFs): pseudouridylated tRFs inhibit translation by targeting the translation initiation complex (PubMed:29628141). Also catalyzes pseudouridylation of mRNAs: mediates pseudouridylation of mRNAs with the consensus sequence 5'-UGUAG-3' (PubMed:28073919, PubMed:31477916, PubMed:35051350). Acts as a regulator of pre-mRNA splicing by mediating pseudouridylation of pre-mRNAs at locations associated with alternatively spliced regions (PubMed:35051350). Pseudouridylation of pre-mRNAs near splice sites directly regulates mRNA splicing and mRNA 3'-end processing (PubMed:35051350). In addition to mRNAs and tRNAs, binds other types of RNAs, such as snRNAs, Y RNAs and vault RNAs, suggesting that it can catalyze pseudouridylation of many RNA types (PubMed:29628141)

Protein Sequence

10 MEMTEMTGVS 20 LKRGALVVED 30 NDSGVPVEET 40 KKQKLSECSL 50 TKGQDGLQND 60 FLSISEDVPR 70 PPDTVSTGKG 80 GKNSEAQLED 90 EEEEEEDGLS 100 EECEEEESES 110 FADMMKHGLT 120 EADVGITKFV 130 SSHQGFSGIL 140 KERYSDFVVH 150 EIGKDGRISH 160 LNDLSIPVDE 170 EDPSEDIFTV 180 LTAEEKQRLE 190 ELQLFKNKET 200 SVAIEVIEDT 210 KEKRTIIHQA 220 IKSLFPGLET 230 KTEDREGKKY 240 IVAYHAAGKK 250 ALANPRKHSW 260 PKSRGSYCHF 270 VLYKENKDTM 280 DAINVLSKYL 290 RVKPNIFSYM 300 GTKDKRAITV 310 QEIAVLKITA 320 QRLAHLNKCL 330 MNFKLGNFSY 340 QKNPLKLGEL 350 QGNHFTVVLR 360 NITGTDDQVQ 370 QAMNSLKEIG 380 FINYYGMQRF 390 GTTAVPTYQV 400 GRAILQNSWT 410 EVMDLILKPR 420 SGAEKGYLVK 430 CREEWAKTKD 440 PTAALRKLPV 450 KRCVEGQLLR 460 GLSKYGMKNI 470 VSAFGIIPRN 480 NRLMYIHSYQ 490 SYVWNNMVSK 500 RIEDYGLKPV 510 PGDLVLKGAT 520 ATYIEEDDVN 530 NYSIHDVVMP 540 LPGFDVIYPK 550 HKIQEAYREM 560 LTADNLDIDN 570 MRHKIRDYSL 580 SGAYRKIIIR 590 PQNVSWEVVA 600 YDDPKIPLFN 610 TDVDNLEGKT 620 PPVFASEGKY 630 RALKMDFSLP 640 PSTYATMAIR 650 EVLKMDTSIK 660 NQTQLNTTWL R

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005634 nucleus
Molecular Function GO:0019899 enzyme binding
Molecular Function GO:0009982 pseudouridine synthase activity
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0160150 tRNA pseudouridine(13) synthase activity
Biological Process GO:0006397 mRNA processing
Biological Process GO:1990481 mRNA pseudouridine synthesis
Biological Process GO:0017148 negative regulation of translation
Biological Process GO:0001522 pseudouridine synthesis
Biological Process GO:1902036 regulation of hematopoietic stem cell differentiation
Biological Process GO:2000380 regulation of mesoderm development
Biological Process GO:0008380 RNA splicing
Biological Process GO:0031119 tRNA pseudouridine synthesis

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[3] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[4] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.