Search Results

Overview

Uniprot IDQ13435
Protein NameSplicing factor 3B subunit 2
Gene NameSF3B2
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
182 HELLEQQKRAAVLLE
275 KIPQALEKILQLKES
280 LEKILQLKESRQEEM
320 EDTVSVSKKEKNRKR
321 DTVSVSKKEKNRKRR
352 ESSGDREKDSTRSRG
394 KRIFEAFKLTDDVKK
412 KEPEKLDKLENSAAP
420 LENSAAPKKKGFEEE
448 EKKPEAPKLSKKKLR
492 PKLLVHLKATRNSVP
563 KVRPKMGKIDIDYQK
570 KIDIDYQKLHDAFFK
577 KLHDAFFKWQTKPKL
770 LIELRKKKIEEAMDG
790 LFTVLPEKRTATVGG
870 MVAEHAAKQKQKKRK
872 AEHAAKQKQKKRKAQ
877 KQKQKKRKAQPQDSR

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:32494006, PubMed:34822310). 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:12234937, PubMed:32494006, PubMed:34822310). Within the 17S U2 SnRNP complex, SF3B2 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:27720643). 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)

Protein Sequence

10 MATEHPEPPK 20 AELQLPPPPP 30 PGHYGAWAAQ 40 ELQAKLAEIG 50 APIQGNREEL 60 VERLQSYTRQ 70 TGIVLNRPVL 80 RGEDGDKAAP 90 PPMSAQLPGI 100 PMPPPPLGLP 110 PLQPPPPPPP 120 PPPGLGLGFP 130 MAHPPNLGPP 140 PPLRVGEPVA 150 LSEEERLKLA 160 QQQAALLMQQ 170 EERAKQQGDH 180 SLKEHELLEQ 190 QKRAAVLLEQ 200 ERQQEIAKMG 210 TPVPRPPQDM 220 GQIGVRTPLG 230 PRVAAPVGPV 240 GPTPTVLPMG 250 APVPRPRGPP 260 PPPGDENREM 270 DDPSVGPKIP 280 QALEKILQLK 290 ESRQEEMNSQ 300 QEEEEMETDA 310 RSSLGQSASE 320 TEEDTVSVSK 330 KEKNRKRRNR 340 KKKKKPQRVR 350 GVSSESSGDR 360 EKDSTRSRGS 370 DSPAADVEIE 380 YVTEEPEIYE 390 PNFIFFKRIF 400 EAFKLTDDVK 410 KEKEKEPEKL 420 DKLENSAAPK 430 KKGFEEEHKD 440 SDDDSSDDEQ 450 EKKPEAPKLS 460 KKKLRRMNRF 470 TVAELKQLVA 480 RPDVVEMHDV 490 TAQDPKLLVH 500 LKATRNSVPV 510 PRHWCFKRKY 520 LQGKRGIEKP 530 PFELPDFIKR 540 TGIQEMREAL 550 QEKEEQKTMK 560 SKMREKVRPK 570 MGKIDIDYQK 580 LHDAFFKWQT 590 KPKLTIHGDL 600 YYEGKEFETR 610 LKEKKPGDLS 620 DELRISLGMP 630 VGPNAHKVPP 640 PWLIAMQRYG 650 PPPSYPNLKI 660 PGLNSPIPES 670 CSFGYHAGGW 680 GKPPVDETGK 690 PLYGDVFGTN 700 AAEFQTKTEE 710 EEIDRTPWGE 720 LEPSDEESSE 730 EEEEEESDED 740 KPDETGFITP 750 ADSGLITPGG 760 FSSVPAGMET 770 PELIELRKKK 780 IEEAMDGSET 790 PQLFTVLPEK 800 RTATVGGAMM 810 GSTHIYDMST 820 VMSRKGPAPE 830 LQGVEVALAP 840 EELELDPMAM 850 TQKYEEHVRE 860 QQAQVEKEDF 870 SDMVAEHAAK 880 QKQKKRKAQP 890 QDSRGGSKKY KEFKF

Gene Ontology

Classification GO ID Description
Cellular Component GO:0071013 catalytic step 2 spliceosome
Cellular Component GO:0016607 nuclear speck
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0071011 precatalytic spliceosome
Cellular Component GO:0005681 spliceosomal complex
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:0005684 U2-type spliceosomal complex
Molecular Function GO:0003723 RNA binding
Biological Process GO:0006397 mRNA processing
Biological Process GO:0000398 mRNA splicing, via spliceosome
Biological Process GO:0008380 RNA splicing
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] 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.

[5] 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.

[6] 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.

[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.