Search Results

Overview

Uniprot IDQ6P2Q9
Protein NamePre-mRNA-processing-splicing factor 8
Gene NamePRPF8
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
1831 TSVWAGQKRLGQLAK
2049 TQTRTVNKHGDEIIT
36 KLQEKARKWQQLQAK
50 KRYAEKRKFGFVDAQ
670 RHSKGVAKTVTKQRV

Function

Plays a role in pre-mRNA splicing as core component of precatalytic, catalytic and postcatalytic spliceosomal complexes, both of the predominant U2-type spliceosome and the minor U12-type spliceosome (PubMed:10411133, PubMed:11971955, PubMed:28076346, PubMed:28502770, PubMed:28781166, PubMed:29301961, PubMed:29360106, PubMed:29361316, PubMed:30315277, PubMed:30705154, PubMed:30728453). Functions as a scaffold that mediates the ordered assembly of spliceosomal proteins and snRNAs. Required for the assembly of the U4/U6-U5 tri-snRNP complex, a building block of the spliceosome. Functions as a scaffold that positions spliceosomal U2, U5 and U6 snRNAs at splice sites on pre-mRNA substrates, so that splicing can occur. Interacts with both the 5' and the 3' splice site

Protein Sequence

10 MAGVFPYRGP 20 GNPVPGPLAP 30 LPDYMSEEKL 40 QEKARKWQQL 50 QAKRYAEKRK 60 FGFVDAQKED 70 MPPEHVRKII 80 RDHGDMTNRK 90 FRHDKRVYLG 100 ALKYMPHAVL 110 KLLENMPMPW 120 EQIRDVPVLY 130 HITGAISFVN 140 EIPWVIEPVY 150 ISQWGSMWIM 160 MRREKRDRRH 170 FKRMRFPPFD 180 DEEPPLDYAD 190 NILDVEPLEA 200 IQLELDPEED 210 APVLDWFYDH 220 QPLRDSRKYV 230 NGSTYQRWQF 240 TLPMMSTLYR 250 LANQLLTDLV 260 DDNYFYLFDL 270 KAFFTSKALN 280 MAIPGGPKFE 290 PLVRDINLQD 300 EDWNEFNDIN 310 KIIIRQPIRT 320 EYKIAFPYLY 330 NNLPHHVHLT 340 WYHTPNVVFI 350 KTEDPDLPAF 360 YFDPLINPIS 370 HRHSVKSQEP 380 LPDDDEEFEL 390 PEFVEPFLKD 400 TPLYTDNTAN 410 GIALLWAPRP 420 FNLRSGRTRR 430 ALDIPLVKNW 440 YREHCPAGQP 450 VKVRVSYQKL 460 LKYYVLNALK 470 HRPPKAQKKR 480 YLFRSFKATK 490 FFQSTKLDWV 500 EVGLQVCRQG 510 YNMLNLLIHR 520 KNLNYLHLDY 530 NFNLKPVKTL 540 TTKERKKSRF 550 GNAFHLCREV 560 LRLTKLVVDS 570 HVQYRLGNVD 580 AFQLADGLQY 590 IFAHVGQLTG 600 MYRYKYKLMR 610 QIRMCKDLKH 620 LIYYRFNTGP 630 VGKGPGCGFW 640 AAGWRVWLFF 650 MRGITPLLER 660 WLGNLLARQF 670 EGRHSKGVAK 680 TVTKQRVESH 690 FDLELRAAVM 700 HDILDMMPEG 710 IKQNKARTIL 720 QHLSEAWRCW 730 KANIPWKVPG 740 LPTPIENMIL 750 RYVKAKADWW 760 TNTAHYNRER 770 IRRGATVDKT 780 VCKKNLGRLT 790 RLYLKAEQER 800 QHNYLKDGPY 810 ITAEEAVAVY 820 TTTVHWLESR 830 RFSPIPFPPL 840 SYKHDTKLLI 850 LALERLKEAY 860 SVKSRLNQSQ 870 REELGLIEQA 880 YDNPHEALSR 890 IKRHLLTQRA 900 FKEVGIEFMD 910 LYSHLVPVYD 920 VEPLEKITDA 930 YLDQYLWYEA 940 DKRRLFPPWI 950 KPADTEPPPL 960 LVYKWCQGIN 970 NLQDVWETSE 980 GECNVMLESR 990 FEKMYEKIDL 1000 TLLNRLLRLI 1010 VDHNIADYMT 1020 AKNNVVINYK 1030 DMNHTNSYGI 1040 IRGLQFASFI 1050 VQYYGLVMDL 1060 LVLGLHRASE 1070 MAGPPQMPND 1080 FLSFQDIATE 1090 AAHPIRLFCR 1100 YIDRIHIFFR 1110 FTADEARDLI 1120 QRYLTEHPDP 1130 NNENIVGYNN 1140 KKCWPRDARM 1150 RLMKHDVNLG 1160 RAVFWDIKNR 1170 LPRSVTTVQW 1180 ENSFVSVYSK 1190 DNPNLLFNMC 1200 GFECRILPKC 1210 RTSYEEFTHK 1220 DGVWNLQNEV 1230 TKERTAQCFL 1240 RVDDESMQRF 1250 HNRVRQILMA 1260 SGSTTFTKIV 1270 NKWNTALIGL 1280 MTYFREAVVN 1290 TQELLDLLVK 1300 CENKIQTRIK 1310 IGLNSKMPSR 1320 FPPVVFYTPK 1330 ELGGLGMLSM 1340 GHVLIPQSDL 1350 RWSKQTDVGI 1360 THFRSGMSHE 1370 EDQLIPNLYR 1380 YIQPWESEFI 1390 DSQRVWAEYA 1400 LKRQEAIAQN 1410 RRLTLEDLED 1420 SWDRGIPRIN 1430 TLFQKDRHTL 1440 AYDKGWRVRT 1450 DFKQYQVLKQ 1460 NPFWWTHQRH 1470 DGKLWNLNNY 1480 RTDMIQALGG 1490 VEGILEHTLF 1500 KGTYFPTWEG 1510 LFWEKASGFE 1520 ESMKWKKLTN 1530 AQRSGLNQIP 1540 NRRFTLWWSP 1550 TINRANVYVG 1560 FQVQLDLTGI 1570 FMHGKIPTLK 1580 ISLIQIFRAH 1590 LWQKIHESIV 1600 MDLCQVFDQE 1610 LDALEIETVQ 1620 KETIHPRKSY 1630 KMNSSCADIL 1640 LFASYKWNVS 1650 RPSLLADSKD 1660 VMDSTTTQKY 1670 WIDIQLRWGD 1680 YDSHDIERYA 1690 RAKFLDYTTD 1700 NMSIYPSPTG 1710 VLIAIDLAYN 1720 LHSAYGNWFP 1730 GSKPLIQQAM 1740 AKIMKANPAL 1750 YVLRERIRKG 1760 LQLYSSEPTE 1770 PYLSSQNYGE 1780 LFSNQIIWFV 1790 DDTNVYRVTI 1800 HKTFEGNLTT 1810 KPINGAIFIF 1820 NPRTGQLFLK 1830 IIHTSVWAGQ 1840 KRLGQLAKWK 1850 TAEEVAALIR 1860 SLPVEEQPKQ 1870 IIVTRKGMLD 1880 PLEVHLLDFP 1890 NIVIKGSELQ 1900 LPFQACLKVE 1910 KFGDLILKAT 1920 EPQMVLFNLY 1930 DDWLKTISSY 1940 TAFSRLILIL 1950 RALHVNNDRA 1960 KVILKPDKTT 1970 ITEPHHIWPT 1980 LTDEEWIKVE 1990 VQLKDLILAD 2000 YGKKNNVNVA 2010 SLTQSEIRDI 2020 ILGMEISAPS 2030 QQRQQIAEIE 2040 KQTKEQSQLT 2050 ATQTRTVNKH 2060 GDEIITSTTS 2070 NYETQTFSSK 2080 TEWRVRAISA 2090 ANLHLRTNHI 2100 YVSSDDIKET 2110 GYTYILPKNV 2120 LKKFICISDL 2130 RAQIAGYLYG 2140 VSPPDNPQVK 2150 EIRCIVMVPQ 2160 WGTHQTVHLP 2170 GQLPQHEYLK 2180 EMEPLGWIHT 2190 QPNESPQLSP 2200 QDVTTHAKIM 2210 ADNPSWDGEK 2220 TIIITCSFTP 2230 GSCTLTAYKL 2240 TPSGYEWGRQ 2250 NTDKGNNPKG 2260 YLPSHYERVQ 2270 MLLSDRFLGF 2280 FMVPAQSSWN 2290 YNFMGVRHDP 2300 NMKYELQLAN 2310 PKEFYHEVHR 2320 PSHFLNFALL 2330 QEGEVYSADR EDLYA

Gene Ontology

Classification GO ID Description
Cellular Component GO:0071013 catalytic step 2 spliceosome
Cellular Component GO:0016020 membrane
Cellular Component GO:0016607 nuclear speck
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0071006 U2-type catalytic step 1 spliceosome
Cellular Component GO:0071007 U2-type catalytic step 2 spliceosome
Cellular Component GO:0071005 U2-type precatalytic spliceosome
Cellular Component GO:0046540 U4/U6 x U5 tri-snRNP complex
Cellular Component GO:0005682 U5 snRNP
Molecular Function GO:0070530 K63-linked polyubiquitin modification-dependent protein binding
Molecular Function GO:0097157 pre-mRNA intronic binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0030619 U1 snRNA binding
Molecular Function GO:0030620 U2 snRNA binding
Molecular Function GO:0030623 U5 snRNA binding
Molecular Function GO:0017070 U6 snRNA binding
Biological Process GO:0071222 cellular response to lipopolysaccharide
Biological Process GO:0071356 cellular response to tumor necrosis factor
Biological Process GO:0006397 mRNA processing
Biological Process GO:0000398 mRNA splicing, via spliceosome
Biological Process GO:0048025 negative regulation of mRNA splicing, via spliceosome
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] 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] 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] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.

[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.