Search Results

Overview

Uniprot IDQ96DI7
Protein NameU5 small nuclear ribonucleoprotein 40 kDa protein
Gene NameSNRNP40
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
18 ELPLVPVKRQRHELL
270 DVRPFAPKERCVKIF
6 **MIEQQKRKGPELP
8 MIEQQKRKGPELPLV

Function

Required for pre-mRNA splicing as component of the activated spliceosome (PubMed:11991638, PubMed:28076346, PubMed:28502770, PubMed:28781166, PubMed:29301961, PubMed:29360106, PubMed:30315277, PubMed:30705154). Component of the U5 small nuclear ribonucleoprotein (snRNP) complex and the U4/U6-U5 tri-snRNP complex, building blocks of the spliceosome (PubMed:16723661, PubMed:26912367, PubMed:9774689). As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable)

Protein Sequence

10 MIEQQKRKGP 20 ELPLVPVKRQ 30 RHELLLGAGS 40 GPGAGQQQAT 50 PGALLQAGPP 60 RCSSLQAPIM 70 LLSGHEGEVY 80 CCKFHPNGST 90 LASAGFDRLI 100 LLWNVYGDCD 110 NYATLKGHSG 120 AVMELHYNTD 130 GSMLFSASTD 140 KTVAVWDSET 150 GERVKRLKGH 160 TSFVNSCYPA 170 RRGPQLVCTG 180 SDDGTVKLWD 190 IRKKAAIQTF 200 QNTYQVLAVT 210 FNDTSDQIIS 220 GGIDNDIKVW 230 DLRQNKLTYT 240 MRGHADSVTG 250 LSLSSEGSYL 260 LSNAMDNTVR 270 VWDVRPFAPK 280 ERCVKIFQGN 290 VHNFEKNLLR 300 CSWSPDGSKI 310 AAGSADRFVY 320 VWDTTSRRIL 330 YKLPGHAGSI 340 NEVAFHPDEP 350 IIISASSDKR LYMGEIQ

Gene Ontology

Classification GO ID Description
Cellular Component GO:0071013 catalytic step 2 spliceosome
Cellular Component GO:0016607 nuclear speck
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005732 sno(s)RNA-containing ribonucleoprotein complex
Cellular Component GO:0071007 U2-type catalytic step 2 spliceosome
Cellular Component GO:0005682 U5 snRNP
Molecular Function GO:0003723 RNA binding
Biological Process GO:0000398 mRNA splicing, via spliceosome
Biological Process GO:0006396 RNA processing
Biological Process GO:0008380 RNA splicing
Biological Process GO:0000375 RNA splicing, via transesterification reactions
Biological Process GO:0000387 spliceosomal snRNP assembly
Biological Process GO:0000244 spliceosomal tri-snRNP complex assembly
Biological Process GO:0000388 spliceosome conformational change to release U4 (or U4atac) and U1 (or U11)

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] 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.

[4] 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.

[5] 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.

[6] 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.