Search Results

Overview

Uniprot IDO00541
Protein NamePescadillo homolog
Gene NamePES1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
152 STFPRTGKCHVQTIQ
26 TRNKARKKLQLSLAD
441 YVPPEKLKLLALQRG
517 RVMAGTLKLEDKQRL
521 GTLKLEDKQRLAQEE
533 QEEESEAKRLAIMMM
56 KHKKKVNKGSTAART
564 RKIREANKLAEKRKA
98 KLRKAYGKSEWNTVE

Function

Component of the PeBoW complex, which is required for maturation of 28S and 5.8S ribosomal RNAs and formation of the 60S ribosome

Protein Sequence

10 MGGLEKKKYE 20 RGSATNYITR 30 NKARKKLQLS 40 LADFRRLCIL 50 KGIYPHEPKH 60 KKKVNKGSTA 70 ARTFYLIKDI 80 RFLLHEPIVN 90 KFREYKVFVR 100 KLRKAYGKSE 110 WNTVERLKDN 120 KPNYKLDHII 130 KERYPTFIDA 140 LRDLDDALSM 150 CFLFSTFPRT 160 GKCHVQTIQL 170 CRRLTVEFMH 180 YIIAARALRK 190 VFLSIKGIYY 200 QAEVLGQPIV 210 WITPYAFSHD 220 HPTDVDYRVM 230 ATFTEFYTTL 240 LGFVNFRLYQ 250 LLNLHYPPKL 260 EGQAQAEAKA 270 GEGTYALDSE 280 SCMEKLAALS 290 ASLARVVVPA 300 TEEEAEVDEF 310 PTDGEMSAQE 320 EDRRKELEAQ 330 EKHKKLFEGL 340 KFFLNREVPR 350 EALAFIIRSF 360 GGEVSWDKSL 370 CIGATYDVTD 380 SRITHQIVDR 390 PGQQTSVIGR 400 CYVQPQWVFD 410 SVNARLLLPV 420 AEYFSGVQLP 430 PHLSPFVTEK 440 EGDYVPPEKL 450 KLLALQRGED 460 PGNLNESEEE 470 EEEDDNNEGD 480 GDEEGENEEE 490 EEDAEAGSEK 500 EEEARLAALE 510 EQRMEGKKPR 520 VMAGTLKLED 530 KQRLAQEEES 540 EAKRLAIMMM 550 KKREKYLYQK 560 IMFGKRRKIR 570 EANKLAEKRK 580 AHDEAVRSEK KAKKARPE

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005694 chromosome
Cellular Component GO:0016020 membrane
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0070545 PeBoW complex
Cellular Component GO:0030687 preribosome, large subunit precursor
Molecular Function GO:0043021 ribonucleoprotein complex binding
Molecular Function GO:0003723 RNA binding
Biological Process GO:0008283 cell population proliferation
Biological Process GO:0000466 maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
Biological Process GO:0000463 maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
Biological Process GO:0051726 regulation of cell cycle
Biological Process GO:0042273 ribosomal large subunit biogenesis
Biological Process GO:0006364 rRNA processing

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] 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.

[3] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[4] 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.

[5] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[6] 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.

[7] 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.