Search Results

Overview

Uniprot IDQ7L014
Protein NameProbable ATP-dependent RNA helicase DDX46
Gene NameDDX46
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
1025 NSYQPTNKGRYKVL*
177 WREEQRKKAMENIGE
193 KKEIEEMKQGKKWSL
248 KFNMRSVKGGGGNEK
263 KSGPTVTKVVTVVTT
271 VVTVVTTKKAVVDSD
272 VTVVTTKKAVVDSDK
316 GYQTKQRKLLEPVDH
765 DQQKAEGKIIKKSSG
769 AEGKIIKKSSGFSGK
776 KSSGFSGKGFKFDET
779 GFSGKGFKFDETEQA
848 PTAGNAEKLEIAKRL
903 IAEQLAEKINAKLNY
907 LAEKINAKLNYVPLE

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, PubMed:36797247). 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). Within the 17S U2 SnRNP complex, DDX46 plays essential roles during assembly of pre-spliceosome and proofreading of the branch site (PubMed:34822310)

Protein Sequence

10 MGRESRHYRK 20 RSASRGRSGS 30 RSRSRSPSDK 40 RSKRGDDRRS 50 RSRDRDRRRE 60 RSRSRDKRRS 70 RSRDRKRLRR 80 SRSRERDRSR 90 ERRRSRSRDR 100 RRSRSRSRGR 110 RSRSSSPGNK 120 SKKTENRSRS 130 KEKTDGGESS 140 KEKKKDKDDK 150 EDEKEKDAGN 160 FDQNKLEEEM 170 RKRKERVEKW 180 REEQRKKAME 190 NIGELKKEIE 200 EMKQGKKWSL 210 EDDDDDEDDP 220 AEAEKEGNEM 230 EGEELDPLDA 240 YMEEVKEEVK 250 KFNMRSVKGG 260 GGNEKKSGPT 270 VTKVVTVVTT 280 KKAVVDSDKK 290 KGELMENDQD 300 AMEYSSEEEE 310 VDLQTALTGY 320 QTKQRKLLEP 330 VDHGKIEYEP 340 FRKNFYVEVP 350 ELAKMSQEEV 360 NVFRLEMEGI 370 TVKGKGCPKP 380 IKSWVQCGIS 390 MKILNSLKKH 400 GYEKPTPIQT 410 QAIPAIMSGR 420 DLIGIAKTGS 430 GKTIAFLLPM 440 FRHIMDQRSL 450 EEGEGPIAVI 460 MTPTRELALQ 470 ITKECKKFSK 480 TLGLRVVCVY 490 GGTGISEQIA 500 ELKRGAEIIV 510 CTPGRMIDML 520 AANSGRVTNL 530 RRVTYVVLDE 540 ADRMFDMGFE 550 PQVMRIVDNV 560 RPDRQTVMFS 570 ATFPRAMEAL 580 ARRILSKPIE 590 VQVGGRSVVC 600 SDVEQQVIVI 610 EEEKKFLKLL 620 ELLGHYQESG 630 SVIIFVDKQE 640 HADGLLKDLM 650 RASYPCMSLH 660 GGIDQYDRDS 670 IINDFKNGTC 680 KLLVATSVAA 690 RGLDVKHLIL 700 VVNYSCPNHY 710 EDYVHRAGRT 720 GRAGNKGYAY 730 TFITEDQARY 740 AGDIIKALEL 750 SGTAVPPDLE 760 KLWSDFKDQQ 770 KAEGKIIKKS 780 SGFSGKGFKF 790 DETEQALANE 800 RKKLQKAALG 810 LQDSDDEDAA 820 VDIDEQIESM 830 FNSKKRVKDM 840 AAPGTSSVPA 850 PTAGNAEKLE 860 IAKRLALRIN 870 AQKNLGIESQ 880 DVMQQATNAI 890 LRGGTILAPT 900 VSAKTIAEQL 910 AEKINAKLNY 920 VPLEKQEEER 930 QDGGQNESFK 940 RYEEELEIND 950 FPQTARWKVT 960 SKEALQRISE 970 YSEAAITIRG 980 TYFPPGKEPK 990 EGERKIYLAI 1000 ESANELAVQK 1010 AKAEITRLIK 1020 EELIRLQNSY 1030 QPTNKGRYKV L

Gene Ontology

Classification GO ID Description
Cellular Component GO:0015030 Cajal body
Cellular Component GO:0016607 nuclear speck
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005684 U2-type spliceosomal complex
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0016887 ATP hydrolysis activity
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0003724 RNA helicase activity
Biological Process GO:0000398 mRNA splicing, via spliceosome
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] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.

[5] 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.

[6] 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.

[7] 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.

[8] 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.

[9] 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.

[10] 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.

[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.