Search Results

Overview

Uniprot IDQ9NZ63
Protein NameSplicing factor C9orf78
Gene NameC9orf78
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
124 KYIETELKKRKGIVE
125 YIETELKKRKGIVEH
127 ETELKKRKGIVEHEE
138 EHEEQKVKPKNAEDC
140 EEQKVKPKNAEDCLY
185 LGIDAKIKNIISTED
194 IISTEDAKARLLAEQ
204 LLAEQQNKKKDSETS
205 LAEQQNKKKDSETSF
281 TDDYHYEKFKKMNRR
283 DYHYEKFKKMNRRY*
284 YHYEKFKKMNRRY**
30 DSEEVRLKLEETREV
81 GGMVDMKKLKERGKD

Function

Plays a role in pre-mRNA splicing by promoting usage of the upstream 3'-splice site at alternative NAGNAG splice sites; these are sites featuring alternative acceptor motifs separated by only a few nucleotides (PubMed:35241646). May also modulate exon inclusion events (PubMed:35241646). Plays a role in spliceosomal remodeling by displacing WBP4 from SNRNP200 and may act to inhibit SNRNP200 helicase activity (PubMed:35241646). Binds U5 snRNA (PubMed:35241646). Required for proper chromosome segregation (PubMed:35167828). Not required for splicing of shelterin components (PubMed:35167828)

Protein Sequence

10 MPVVRKIFRR 20 RRGDSESEED 30 EQDSEEVRLK 40 LEETREVQNL 50 RKRPNGVSAV 60 ALLVGEKVQE 70 ETTLVDDPFQ 80 MKTGGMVDMK 90 KLKERGKDKI 100 SEEEDLHLGT 110 SFSAETNRRD 120 EDADMMKYIE 130 TELKKRKGIV 140 EHEEQKVKPK 150 NAEDCLYELP 160 ENIRVSSAKK 170 TEEMLSNQML 180 SGIPEVDLGI 190 DAKIKNIIST 200 EDAKARLLAE 210 QQNKKKDSET 220 SFVPTNMAVN 230 YVQHNRFYHE 240 ELNAPIRRNK 250 EEPKARPLRV 260 GDTEKPEPER 270 SPPNRKRPAN 280 EKATDDYHYE KFKKMNRRY

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000775 chromosome, centromeric region
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005681 spliceosomal complex
Molecular Function GO:0030623 U5 snRNA binding
Biological Process GO:0007059 chromosome segregation
Biological Process GO:0045292 mRNA cis splicing, via spliceosome
Biological Process GO:0000398 mRNA splicing, via spliceosome
Biological Process GO:0060629 regulation of homologous chromosome segregation

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] 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.

[4] 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.

[5] 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.