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Overview

Uniprot IDQ12996
Protein NameCleavage stimulation factor subunit 3
Gene NameCSTF3
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
114 YVRETKGKLPSYKEK
682 ESNAVLTKAVKRPNE

Function

One of the multiple factors required for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs

Protein Sequence

10 MSGDGATEQA 20 AEYVPEKVKK 30 AEKKLEENPY 40 DLDAWSILIR 50 EAQNQPIDKA 60 RKTYERLVAQ 70 FPSSGRFWKL 80 YIEAEIKAKN 90 YDKVEKLFQR 100 CLMKVLHIDL 110 WKCYLSYVRE 120 TKGKLPSYKE 130 KMAQAYDFAL 140 DKIGMEIMSY 150 QIWVDYINFL 160 KGVEAVGSYA 170 ENQRITAVRR 180 VYQRGCVNPM 190 INIEQLWRDY 200 NKYEEGINIH 210 LAKKMIEDRS 220 RDYMNARRVA 230 KEYETVMKGL 240 DRNAPSVPPQ 250 NTPQEAQQVD 260 MWKKYIQWEK 270 SNPLRTEDQT 280 LITKRVMFAY 290 EQCLLVLGHH 300 PDIWYEAAQY 310 LEQSSKLLAE 320 KGDMNNAKLF 330 SDEAANIYER 340 AISTLLKKNM 350 LLYFAYADYE 360 ESRMKYEKVH 370 SIYNRLLAIE 380 DIDPTLVYIQ 390 YMKFARRAEG 400 IKSGRMIFKK 410 AREDTRTRHH 420 VYVTAALMEY 430 YCSKDKSVAF 440 KIFELGLKKY 450 GDIPEYVLAY 460 IDYLSHLNED 470 NNTRVLFERV 480 LTSGSLPPEK 490 SGEIWARFLA 500 FESNIGDLAS 510 ILKVEKRRFT 520 AFKEEYEGKE 530 TALLVDRYKF 540 MDLYPCSASE 550 LKALGYKDVS 560 RAKLAAIIPD 570 PVVAPSIVPV 580 LKDEVDRKPE 590 YPKPDTQQMI 600 PFQPRHLAPP 610 GLHPVPGGVF 620 PVPPAAVVLM 630 KLLPPPICFQ 640 GPFVQVDELM 650 EIFRRCKIPN 660 TVEEAVRIIT 670 GGAPELAVEG 680 NGPVESNAVL 690 TKAVKRPNED 700 SDEDEEKGAV 710 VPPVHDIYRA RQQKRIR

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005848 mRNA cleavage stimulating factor complex
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0003729 mRNA binding
Molecular Function GO:0003723 RNA binding
Biological Process GO:0180010 co-transcriptional mRNA 3'-end processing, cleavage and polyadenylation pathway
Biological Process GO:0031440 regulation of mRNA 3'-end processing
Biological Process GO:0031123 RNA 3'-end processing

Reference

[1] 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.

[2] 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.

[3] 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.

[4] 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.