Search Results

Overview

Uniprot IDO75533
Protein NameSplicing factor 3B subunit 1
Gene NameSF3B1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
120 ADREDEYKKHRRTMI
141 DPFADGGKTPDPKMN
146 GGKTPDPKMNARTYM
163 MREQHLTKEEREIRQ
182 KAKAGELKVVNGAAA
195 AASQPPSKRKRRWDQ
213 QTPGATPKKLSSWDQ
214 TPGATPKKLSSWDQA
240 DETPGRAKGSETPGA
252 PGATPGSKIWDPTPS
290 GATSSARKNRWDETP
3 *****MAKIAKTHED
333 TPTPGASKRKSRWDE
430 PIRTPARKLTATPTP
6 **MAKIAKTHEDIEA

Function

Component of the 17S U2 SnRNP complex of the spliceosome, a large ribonucleoprotein complex that removes introns from transcribed pre-mRNAs (PubMed:12234937, PubMed:27720643, PubMed:32494006, PubMed:34822310, PubMed:36104565). The 17S U2 SnRNP complex (1) directly participates in early spliceosome assembly and (2) mediates recognition of the intron branch site during pre-mRNA splicing by promoting the selection of the pre-mRNA branch-site adenosine, the nucleophile for the first step of splicing (PubMed:32494006, PubMed:34822310, PubMed:36104565). Within the 17S U2 SnRNP complex, SF3B1 is part of the SF3B subcomplex, which is required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence in pre-mRNA (PubMed:12234937, PubMed:36104565). Sequence independent binding of SF3A and SF3B subcomplexes upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA (PubMed:12234937). May also be involved in the assembly of the 'E' complex (PubMed:10882114). Also acts as a component of the minor spliceosome, which is involved in the splicing of U12-type introns in pre-mRNAs (PubMed:15146077, PubMed:33509932). Together with other U2 snRNP complex components may also play a role in the selective processing of microRNAs (miRNAs) from the long primary miRNA transcript, pri-miR-17-92 (By similarity)

Protein Sequence

10 MAKIAKTHED 20 IEAQIREIQG 30 KKAALDEAQG 40 VGLDSTGYYD 50 QEIYGGSDSR 60 FAGYVTSIAA 70 TELEDDDDDY 80 SSSTSLLGQK 90 KPGYHAPVAL 100 LNDIPQSTEQ 110 YDPFAEHRPP 120 KIADREDEYK 130 KHRRTMIISP 140 ERLDPFADGG 150 KTPDPKMNAR 160 TYMDVMREQH 170 LTKEEREIRQ 180 QLAEKAKAGE 190 LKVVNGAAAS 200 QPPSKRKRRW 210 DQTADQTPGA 220 TPKKLSSWDQ 230 AETPGHTPSL 240 RWDETPGRAK 250 GSETPGATPG 260 SKIWDPTPSH 270 TPAGAATPGR 280 GDTPGHATPG 290 HGGATSSARK 300 NRWDETPKTE 310 RDTPGHGSGW 320 AETPRTDRGG 330 DSIGETPTPG 340 ASKRKSRWDE 350 TPASQMGGST 360 PVLTPGKTPI 370 GTPAMNMATP 380 TPGHIMSMTP 390 EQLQAWRWER 400 EIDERNRPLS 410 DEELDAMFPE 420 GYKVLPPPAG 430 YVPIRTPARK 440 LTATPTPLGG 450 MTGFHMQTED 460 RTMKSVNDQP 470 SGNLPFLKPD 480 DIQYFDKLLV 490 DVDESTLSPE 500 EQKERKIMKL 510 LLKIKNGTPP 520 MRKAALRQIT 530 DKAREFGAGP 540 LFNQILPLLM 550 SPTLEDQERH 560 LLVKVIDRIL 570 YKLDDLVRPY 580 VHKILVVIEP 590 LLIDEDYYAR 600 VEGREIISNL 610 AKAAGLATMI 620 STMRPDIDNM 630 DEYVRNTTAR 640 AFAVVASALG 650 IPSLLPFLKA 660 VCKSKKSWQA 670 RHTGIKIVQQ 680 IAILMGCAIL 690 PHLRSLVEII 700 EHGLVDEQQK 710 VRTISALAIA 720 ALAEAATPYG 730 IESFDSVLKP 740 LWKGIRQHRG 750 KGLAAFLKAI 760 GYLIPLMDAE 770 YANYYTREVM 780 LILIREFQSP 790 DEEMKKIVLK 800 VVKQCCGTDG 810 VEANYIKTEI 820 LPPFFKHFWQ 830 HRMALDRRNY 840 RQLVDTTVEL 850 ANKVGAAEII 860 SRIVDDLKDE 870 AEQYRKMVME 880 TIEKIMGNLG 890 AADIDHKLEE 900 QLIDGILYAF 910 QEQTTEDSVM 920 LNGFGTVVNA 930 LGKRVKPYLP 940 QICGTVLWRL 950 NNKSAKVRQQ 960 AADLISRTAV 970 VMKTCQEEKL 980 MGHLGVVLYE 990 YLGEEYPEVL 1000 GSILGALKAI 1010 VNVIGMHKMT 1020 PPIKDLLPRL 1030 TPILKNRHEK 1040 VQENCIDLVG 1050 RIADRGAEYV 1060 SAREWMRICF 1070 ELLELLKAHK 1080 KAIRRATVNT 1090 FGYIAKAIGP 1100 HDVLATLLNN 1110 LKVQERQNRV 1120 CTTVAIAIVA 1130 ETCSPFTVLP 1140 ALMNEYRVPE 1150 LNVQNGVLKS 1160 LSFLFEYIGE 1170 MGKDYIYAVT 1180 PLLEDALMDR 1190 DLVHRQTASA 1200 VVQHMSLGVY 1210 GFGCEDSLNH 1220 LLNYVWPNVF 1230 ETSPHVIQAV 1240 MGALEGLRVA 1250 IGPCRMLQYC 1260 LQGLFHPARK 1270 VRDVYWKIYN 1280 SIYIGSQDAL 1290 IAHYPRIYND 1300 DKNTYIRYEL DYIL

Gene Ontology

Classification GO ID Description
Cellular Component GO:0071013 catalytic step 2 spliceosome
Cellular Component GO:0000785 chromatin
Cellular Component GO:0016607 nuclear speck
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005681 spliceosomal complex
Cellular Component GO:0034693 U11/U12 snRNP
Cellular Component GO:0005689 U12-type spliceosomal complex
Cellular Component GO:0005686 U2 snRNP
Cellular Component GO:0071005 U2-type precatalytic spliceosome
Cellular Component GO:0071004 U2-type prespliceosome
Cellular Component GO:0005684 U2-type spliceosomal complex
Molecular Function GO:0003729 mRNA binding
Molecular Function GO:0036002 pre-mRNA binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:1990935 splicing factor binding
Biological Process GO:0006338 chromatin remodeling
Biological Process GO:0000398 mRNA splicing, via spliceosome
Biological Process GO:0045943 positive regulation of transcription by RNA polymerase I
Biological Process GO:0045944 positive regulation of transcription by RNA polymerase II
Biological Process GO:0045945 positive regulation of transcription by RNA polymerase III
Biological Process GO:0008380 RNA splicing
Biological Process GO:0000375 RNA splicing, via transesterification reactions
Biological Process GO:0000245 spliceosomal complex assembly
Biological Process GO:0000387 spliceosomal snRNP assembly
Biological Process GO:0000388 spliceosome conformational change to release U4 (or U4atac) and U1 (or U11)
Biological Process GO:1903241 U2-type prespliceosome assembly

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] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.

[5] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.

[6] 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.

[7] 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.

[8] 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.

[9] 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.

[10] 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.

[11] 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.