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Overview

Uniprot IDQ15020
Protein NameSpliceosome associated factor 3, U4/U6 recycling protein
Gene NameSART3
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
586 QRMKAAEKEAALVQQ
643 DEEEQPSKRRRVENS
680 VDVEPPSKQKEKAAS
682 VEPPSKQKEKAASLK
790 KSKNPDFKVFRYSTS
958 MSNADFAKLFLRK**

Function

U6 snRNP-binding protein that functions as a recycling factor of the splicing machinery. Promotes the initial reassembly of U4 and U6 snRNPs following their ejection from the spliceosome during its maturation (PubMed:12032085). Also binds U6atac snRNPs and may function as a recycling factor for U4atac/U6atac spliceosomal snRNP, an initial step in the assembly of U12-type spliceosomal complex. The U12-type spliceosomal complex plays a role in the splicing of introns with non-canonical splice sites (PubMed:14749385). May also function as a substrate-targeting factor for deubiquitinases like USP4 and USP15. Recruits USP4 to ubiquitinated PRPF3 within the U4/U5/U6 tri-snRNP complex, promoting PRPF3 deubiquitination and thereby regulating the spliceosome U4/U5/U6 tri-snRNP spliceosomal complex disassembly (PubMed:20595234). May also recruit the deubiquitinase USP15 to histone H2B and mediate histone deubiquitination, thereby regulating gene expression and/or DNA repair (PubMed:24526689). May play a role in hematopoiesis probably through transcription regulation of specific genes including MYC (By similarity)

Protein Sequence

10 MATAAETSAS 20 EPEAESKAGP 30 KADGEEDEVK 40 AARTRRKVLS 50 RAVAAATYKT 60 MGPAWDQQEE 70 GVSESDGDEY 80 AMASSAESSP 90 GEYEWEYDEE 100 EEKNQLEIER 110 LEEQLSINVY 120 DYNCHVDLIR 130 LLRLEGELTK 140 VRMARQKMSE 150 IFPLTEELWL 160 EWLHDEISMA 170 QDGLDREHVY 180 DLFEKAVKDY 190 ICPNIWLEYG 200 QYSVGGIGQK 210 GGLEKVRSVF 220 ERALSSVGLH 230 MTKGLALWEA 240 YREFESAIVE 250 AARLEKVHSL 260 FRRQLAIPLY 270 DMEATFAEYE 280 EWSEDPIPES 290 VIQNYNKALQ 300 QLEKYKPYEE 310 ALLQAEAPRL 320 AEYQAYIDFE 330 MKIGDPARIQ 340 LIFERALVEN 350 CLVPDLWIRY 360 SQYLDRQLKV 370 KDLVLSVHNR 380 AIRNCPWTVA 390 LWSRYLLAME 400 RHGVDHQVIS 410 VTFEKALNAG 420 FIQATDYVEI 430 WQAYLDYLRR 440 RVDFKQDSSK 450 ELEELRAAFT 460 RALEYLKQEV 470 EERFNESGDP 480 SCVIMQNWAR 490 IEARLCNNMQ 500 KARELWDSIM 510 TRGNAKYANM 520 WLEYYNLERA 530 HGDTQHCRKA 540 LHRAVQCTSD 550 YPEHVCEVLL 560 TMERTEGSLE 570 DWDIAVQKTE 580 TRLARVNEQR 590 MKAAEKEAAL 600 VQQEEEKAEQ 610 RKRARAEKKA 620 LKKKKKIRGP 630 EKRGADEDDE 640 KEWGDDEEEQ 650 PSKRRRVENS 660 IPAAGETQNV 670 EVAAGPAGKC 680 AAVDVEPPSK 690 QKEKAASLKR 700 DMPKVLHDSS 710 KDSITVFVSN 720 LPYSMQEPDT 730 KLRPLFEACG 740 EVVQIRPIFS 750 NRGDFRGYCY 760 VEFKEEKSAL 770 QALEMDRKSV 780 EGRPMFVSPC 790 VDKSKNPDFK 800 VFRYSTSLEK 810 HKLFISGLPF 820 SCTKEELEEI 830 CKAHGTVKDL 840 RLVTNRAGKP 850 KGLAYVEYEN 860 ESQASQAVMK 870 MDGMTIKENI 880 IKVAISNPPQ 890 RKVPEKPETR 900 KAPGGPMLLP 910 QTYGARGKGR 920 TQLSLLPRAL 930 QRPSAAAPQA 940 ENGPAAAPAV 950 AAPAATEAPK 960 MSNADFAKLF LRK

Gene Ontology

Classification GO ID Description
Cellular Component GO:0061574 ASAP complex
Cellular Component GO:0015030 Cajal body
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0016607 nuclear speck
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0042393 histone binding
Molecular Function GO:0030674 protein-macromolecule adaptor activity
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0030621 U4 snRNA binding
Molecular Function GO:0017070 U6 snRNA binding
Molecular Function GO:0030624 U6atac snRNA binding
Molecular Function GO:1990381 ubiquitin-specific protease binding
Biological Process GO:0000398 mRNA splicing, via spliceosome
Biological Process GO:0006334 nucleosome assembly
Biological Process GO:0010468 regulation of gene expression
Biological Process GO:0051252 regulation of RNA metabolic process
Biological Process GO:0000387 spliceosomal snRNP assembly
Biological Process GO:0000244 spliceosomal tri-snRNP complex assembly
Biological Process GO:0140673 transcription elongation-coupled chromatin remodeling

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 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.

[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.