Search Results

Overview

Uniprot IDQ16630
Protein NameCleavage and polyadenylation specificity factor subunit 6
Gene NameCPSF6
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
138 VGSEASSKKLMDLLP
139 GSEASSKKLMDLLPK
185 GQMSGEGKAGPPGGS
483 CLHGIESKSYGSGSR
79 VVYTYTGKRIALYIG

Function

Component of the cleavage factor Im (CFIm) complex that functions as an activator of the pre-mRNA 3'-end cleavage and polyadenylation processing required for the maturation of pre-mRNA into functional mRNAs (PubMed:14690600, PubMed:29276085, PubMed:8626397, PubMed:9659921). CFIm contributes to the recruitment of multiprotein complexes on specific sequences on the pre-mRNA 3'-end, so called cleavage and polyadenylation signals (pA signals) (PubMed:14690600, PubMed:8626397, PubMed:9659921). Most pre-mRNAs contain multiple pA signals, resulting in alternative cleavage and polyadenylation (APA) producing mRNAs with variable 3'-end formation (PubMed:23187700, PubMed:29276085). The CFIm complex acts as a key regulator of cleavage and polyadenylation site choice during APA through its binding to 5'-UGUA-3' elements localized in the 3'-untranslated region (UTR) for a huge number of pre-mRNAs (PubMed:20695905, PubMed:29276085). CPSF6 enhances NUDT21/CPSF5 binding to 5'-UGUA-3' elements localized upstream of pA signals and promotes RNA looping, and hence activates directly the mRNA 3'-processing machinery (PubMed:15169763, PubMed:21295486, PubMed:29276085). Plays a role in mRNA export (PubMed:19864460)

Protein Sequence

10 MADGVDHIDI 20 YADVGEEFNQ 30 EAEYGGHDQI 40 DLYDDVISPS 50 ANNGDAPEDR 60 DYMDTLPPTV 70 GDDVGKGAAP 80 NVVYTYTGKR 90 IALYIGNLTW 100 WTTDEDLTEA 110 VHSLGVNDIL 120 EIKFFENRAN 130 GQSKGFALVG 140 VGSEASSKKL 150 MDLLPKRELH 160 GQNPVVTPCN 170 KQFLSQFEMQ 180 SRKTTQSGQM 190 SGEGKAGPPG 200 GSSRAAFPQG 210 GRGRGRFPGA 220 VPGGDRFPGP 230 AGPGGPPPPF 240 PAGQTPPRPP 250 LGPPGPPGPP 260 GPPPPGQVLP 270 PPLAGPPNRG 280 DRPPPPVLFP 290 GQPFGQPPLG 300 PLPPGPPPPV 310 PGYGPPPGPP 320 PPQQGPPPPP 330 GPFPPRPPGP 340 LGPPLTLAPP 350 PHLPGPPPGA 360 PPPAPHVNPA 370 FFPPPTNSGM 380 PTSDSRGPPP 390 TDPYGRPPPY 400 DRGDYGPPGR 410 EMDTARTPLS 420 EAEFEEIMNR 430 NRAISSSAIS 440 RAVSDASAGD 450 YGSAIETLVT 460 AISLIKQSKV 470 SADDRCKVLI 480 SSLQDCLHGI 490 ESKSYGSGSR 500 RERSRERDHS 510 RSREKSRRHK 520 SRSRDRHDDY 530 YRERSRERER 540 HRDRDRDRDR 550 ERDREREYRH R

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0035061 interchromatin granule
Cellular Component GO:0016020 membrane
Cellular Component GO:0005847 mRNA cleavage and polyadenylation specificity factor complex
Cellular Component GO:0005849 mRNA cleavage factor complex
Cellular Component GO:0016607 nuclear speck
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0042382 paraspeckles
Cellular Component GO:0005726 perichromatin fibrils
Cellular Component GO:1990904 ribonucleoprotein complex
Molecular Function GO:1990448 exon-exon junction complex binding
Molecular Function GO:0003729 mRNA binding
Molecular Function GO:0043023 ribosomal large subunit binding
Molecular Function GO:0003723 RNA binding
Biological Process GO:0180010 co-transcriptional mRNA 3'-end processing, cleavage and polyadenylation pathway
Biological Process GO:0031124 mRNA 3'-end processing
Biological Process GO:0110104 mRNA alternative polyadenylation
Biological Process GO:0006397 mRNA processing
Biological Process GO:0046833 positive regulation of RNA export from nucleus
Biological Process GO:0051290 protein heterotetramerization
Biological Process GO:0051262 protein tetramerization

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] 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.

[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] 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.

[5] 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.

[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.