Search Results

Overview

Uniprot ID	Q9BRP8
Protein Name	Partner of Y14 and mago
Gene Name	PYM1
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
14	PAATETGKYIASTQR
33	WRKQRRVKEGYVPQE

Function

Key regulator of the exon junction complex (EJC), a multiprotein complex that associates immediately upstream of the exon-exon junction on mRNAs and serves as a positional landmark for the intron exon structure of genes and directs post-transcriptional processes in the cytoplasm such as mRNA export, nonsense-mediated mRNA decay (NMD) or translation. Acts as an EJC disassembly factor, allowing translation-dependent EJC removal and recycling by disrupting mature EJC from spliced mRNAs. Its association with the 40S ribosomal subunit probably prevents a translation-independent disassembly of the EJC from spliced mRNAs, by restricting its activity to mRNAs that have been translated. Interferes with NMD and enhances translation of spliced mRNAs, probably by antagonizing EJC functions. May bind RNA; the relevance of RNA-binding remains unclear in vivo, RNA-binding was detected by PubMed:14968132, while PubMed:19410547 did not detect RNA-binding activity independently of the EJC

Protein Sequence

10 MEAAGSPAAT 20 ETGKYIASTQ 30 RPDGTWRKQR 40 RVKEGYVPQE 50 EVPVYENKYV 60 KFFKSKPELP 70 PGLSPEATAP 80 VTPSRPEGGE 90 PGLSKTAKRN 100 LKRKEKRRQQ 110 QEKGEAEALS 120 RTLDKVSLEE 130 TAQLPSAPQG 140 SRAAPTAASD 150 QPDSAATTEK 160 AKKIKNLKKK 170 LRQVEELQQR 180 IQAGEVSQPS 190 KEQLEKLARR 200 RALEEELEDL ELGL

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0005737	cytoplasm
Cellular Component	GO:0005829	cytosol
Cellular Component	GO:0035145	exon-exon junction complex
Cellular Component	GO:0005730	nucleolus
Cellular Component	GO:0005654	nucleoplasm
Molecular Function	GO:0043022	ribosome binding
Molecular Function	GO:0003723	RNA binding
Biological Process	GO:1903259	exon-exon junction complex disassembly
Biological Process	GO:0000184	nuclear-transcribed mRNA catabolic process, nonsense-mediated decay
Biological Process	GO:0045727	positive regulation of translation

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] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.