Search Results

Overview

Uniprot IDQ6UN15
Protein NamePre-mRNA 3'-end-processing factor FIP1
Gene NameFIP1L1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
123 APVNLNIKTGGRVYG
135 VYGTTGTKVKGVDLD
137 GTTGTKVKGVDLDAP
235 DGRFNLFKVQQGRTG
265 TSPPSLFKTGLPPSR
294 KANSSVGKWQDRYGR

Function

Component of the cleavage and polyadenylation specificity factor (CPSF) complex that plays a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. FIP1L1 contributes to poly(A) site recognition and stimulates poly(A) addition. Binds to U-rich RNA sequence elements surrounding the poly(A) site. May act to tether poly(A) polymerase to the CPSF complex

Protein Sequence

10 MSAGEVERLV 20 SELSGGTGGD 30 EEEEWLYGGP 40 WDVHVHSDLA 50 KDLDENEVER 60 PEEENASANP 70 PSGIEDETAE 80 NGVPKPKVTE 90 TEDDSDSDSD 100 DDEDDVHVTI 110 GDIKTGAPQY 120 GSYGTAPVNL 130 NIKTGGRVYG 140 TTGTKVKGVD 150 LDAPGSINGV 160 PLLEVDLDSF 170 EDKPWRKPGA 180 DLSDYFNYGF 190 NEDTWKAYCE 200 KQKRIRMGLE 210 VIPVTSTTNK 220 ITAEDCTMEV 230 TPGAEIQDGR 240 FNLFKVQQGR 250 TGNSEKETAL 260 PSTKAEFTSP 270 PSLFKTGLPP 280 SRNSTSSQSQ 290 TSTASRKANS 300 SVGKWQDRYG 310 RAESPDLRRL 320 PGAIDVIGQT 330 ITISRVEGRR 340 RANENSNIQV 350 LSERSATEVD 360 NNFSKPPPFF 370 PPGAPPTHLP 380 PPPFLPPPPT 390 VSTAPPLIPP 400 PGFPPPPGAP 410 PPSLIPTIES 420 GHSSGYDSRS 430 ARAFPYGNVA 440 FPHLPGSAPS 450 WPSLVDTSKQ 460 WDYYARREKD 470 RDRERDRDRE 480 RDRDRDRERE 490 RTRERERERD 500 HSPTPSVFNS 510 DEERYRYREY 520 AERGYERHRA 530 SREKEERHRE 540 RRHREKEETR 550 HKSSRSNSRR 560 RHESEEGDSH 570 RRHKHKKSKR 580 SKEGKEAGSE 590 PAPEQESTEA TPAE

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005847 mRNA cleavage and polyadenylation specificity factor complex
Cellular Component GO:0005654 nucleoplasm
Molecular Function GO:0003723 RNA binding
Biological Process GO:0031124 mRNA 3'-end processing
Biological Process GO:0006398 mRNA 3'-end processing by stem-loop binding and cleavage

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] 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.

[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] 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.