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Overview

Uniprot IDP17844
Protein NameProbable ATP-dependent RNA helicase DDX5
Gene NameDDX5
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
197 YCRACRLKSTCIYGG
207 CIYGGAPKGPQIRDL
32 RAGPLSGKKFGNPGE
33 AGPLSGKKFGNPGEK
340 MEEIMSEKENKTIVF
351 TIVFVETKRRCDELT
40 KFGNPGEKLVKKKWN
43 NPGEKLVKKKWNLDE
45 GEKLVKKKWNLDELP
523 RGYSSLLKRDFGAKT

Function

Involved in the alternative regulation of pre-mRNA splicing; its RNA helicase activity is necessary for increasing tau exon 10 inclusion and occurs in a RBM4-dependent manner. Binds to the tau pre-mRNA in the stem-loop region downstream of exon 10. The rate of ATP hydrolysis is highly stimulated by single-stranded RNA. Involved in transcriptional regulation; the function is independent of the RNA helicase activity. Transcriptional coactivator for androgen receptor AR but probably not ESR1. Synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and involved in skeletal muscle differentiation. Transcriptional coactivator for p53/TP53 and involved in p53/TP53 transcriptional response to DNA damage and p53/TP53-dependent apoptosis. Transcriptional coactivator for RUNX2 and involved in regulation of osteoblast differentiation. Acts as a transcriptional repressor in a promoter-specific manner; the function probably involves association with histone deacetylases, such as HDAC1. As component of a large PER complex is involved in the inhibition of 3' transcriptional termination of circadian target genes such as PER1 and NR1D1 and the control of the circadian rhythms

Protein Sequence

10 MSGYSSDRDR 20 GRDRGFGAPR 30 FGGSRAGPLS 40 GKKFGNPGEK 50 LVKKKWNLDE 60 LPKFEKNFYQ 70 EHPDLARRTA 80 QEVETYRRSK 90 EITVRGHNCP 100 KPVLNFYEAN 110 FPANVMDVIA 120 RQNFTEPTAI 130 QAQGWPVALS 140 GLDMVGVAQT 150 GSGKTLSYLL 160 PAIVHINHQP 170 FLERGDGPIC 180 LVLAPTRELA 190 QQVQQVAAEY 200 CRACRLKSTC 210 IYGGAPKGPQ 220 IRDLERGVEI 230 CIATPGRLID 240 FLECGKTNLR 250 RTTYLVLDEA 260 DRMLDMGFEP 270 QIRKIVDQIR 280 PDRQTLMWSA 290 TWPKEVRQLA 300 EDFLKDYIHI 310 NIGALELSAN 320 HNILQIVDVC 330 HDVEKDEKLI 340 RLMEEIMSEK 350 ENKTIVFVET 360 KRRCDELTRK 370 MRRDGWPAMG 380 IHGDKSQQER 390 DWVLNEFKHG 400 KAPILIATDV 410 ASRGLDVEDV 420 KFVINYDYPN 430 SSEDYIHRIG 440 RTARSTKTGT 450 AYTFFTPNNI 460 KQVSDLISVL 470 REANQAINPK 480 LLQLVEDRGS 490 GRSRGRGGMK 500 DDRRDRYSAG 510 KRGGFNTFRD 520 RENYDRGYSS 530 LLKRDFGAKT 540 QNGVYSAANY 550 TNGSFGSNFV 560 SAGIQTSFRT 570 GNPTGTYQNG 580 YDSTQQYGSN 590 VPNMHNGMNQ 600 QAYAYPATAA 610 APMIGYPMPT GYSQ

Gene Ontology

Classification GO ID Description
Cellular Component GO:0071013 catalytic step 2 spliceosome
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0016020 membrane
Cellular Component GO:0016607 nuclear speck
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:1990904 ribonucleoprotein complex
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0016887 ATP hydrolysis activity
Molecular Function GO:0048306 calcium-dependent protein binding
Molecular Function GO:0005516 calmodulin binding
Molecular Function GO:0019899 enzyme binding
Molecular Function GO:0035500 MH2 domain binding
Molecular Function GO:0003730 mRNA 3'-UTR binding
Molecular Function GO:0003729 mRNA binding
Molecular Function GO:0050681 nuclear androgen receptor binding
Molecular Function GO:0036002 pre-mRNA binding
Molecular Function GO:0070878 primary miRNA binding
Molecular Function GO:1990841 promoter-specific chromatin binding
Molecular Function GO:0070412 R-SMAD binding
Molecular Function GO:0043021 ribonucleoprotein complex binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0003724 RNA helicase activity
Molecular Function GO:0046332 SMAD binding
Biological Process GO:0000380 alternative mRNA splicing, via spliceosome
Biological Process GO:0030521 androgen receptor signaling pathway
Biological Process GO:0030509 BMP signaling pathway
Biological Process GO:0001837 epithelial to mesenchymal transition
Biological Process GO:0030520 estrogen receptor signaling pathway
Biological Process GO:0072332 intrinsic apoptotic signaling pathway by p53 class mediator
Biological Process GO:0061614 miRNA transcription
Biological Process GO:0000398 mRNA splicing, via spliceosome
Biological Process GO:0009299 mRNA transcription
Biological Process GO:0045445 myoblast differentiation
Biological Process GO:0000122 negative regulation of transcription by RNA polymerase II
Biological Process GO:0000956 nuclear-transcribed mRNA catabolic process
Biological Process GO:0043517 positive regulation of DNA damage response, signal transduction by p53 class mediator
Biological Process GO:0031053 primary miRNA processing
Biological Process GO:0000381 regulation of alternative mRNA splicing, via spliceosome
Biological Process GO:0060765 regulation of androgen receptor signaling pathway
Biological Process GO:0045667 regulation of osteoblast differentiation
Biological Process GO:2001014 regulation of skeletal muscle cell differentiation
Biological Process GO:0006357 regulation of transcription by RNA polymerase II
Biological Process GO:0045069 regulation of viral genome replication
Biological Process GO:0048511 rhythmic process

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] 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.