Search Results

Overview

Uniprot IDQ7Z478
Protein NameATP-dependent RNA helicase DHX29
Gene NameDHX29
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
189 QQPKSRPKFQSPQIQ
26 AVSASRAKSAEAGIA
807 SKAGGIKKYQEYIPV
9 GGKNKKHKAPAAAVV

Function

ATP-binding RNA helicase involved in translation initiation. Part of the 43S pre-initiation complex that is required for efficient initiation on mRNAs of higher eukaryotes with structured 5'-UTRs by promoting efficient NTPase-dependent 48S complex formation. Specifically binds to the 40S ribosome near the mRNA entrance. Does not possess a processive helicase activity

Protein Sequence

10 MGGKNKKHKA 20 PAAAVVRAAV 30 SASRAKSAEA 40 GIAGEAQSKK 50 PVSRPATAAA 60 AAAGSREPRV 70 KQGPKIYSFN 80 STNDSSGPAN 90 LDKSILKVVI 100 NNKLEQRIIG 110 VINEHKKQNN 120 DKGMISGRLT 130 AKKLQDLYMA 140 LQAFSFKTKD 150 IEDAMTNTLL 160 YGGDLHSALD 170 WLCLNLSDDA 180 LPEGFSQEFE 190 EQQPKSRPKF 200 QSPQIQATIS 210 PPLQPKTKTY 220 EEDPKSKPKK 230 EEKNMEVNMK 240 EWILRYAEQQ 250 NEEEKNENSK 260 SLEEEEKFDP 270 NERYLHLAAK 280 LLDAKEQAAT 290 FKLEKNKQGQ 300 KEAQEKIRKF 310 QREMETLEDH 320 PVFNPAMKIS 330 HQQNERKKPP 340 VATEGESALN 350 FNLFEKSAAA 360 TEEEKDKKKE 370 PHDVRNFDYT 380 ARSWTGKSPK 390 QFLIDWVRKN 400 LPKSPNPSFE 410 KVPVGRYWKC 420 RVRVIKSEDD 430 VLVVCPTILT 440 EDGMQAQHLG 450 ATLALYRLVK 460 GQSVHQLLPP 470 TYRDVWLEWS 480 DAEKKREELN 490 KMETNKPRDL 500 FIAKLLNKLK 510 QQQQQQQQHS 520 ENKRENSEDP 530 EESWENLVSD 540 EDFSALSLES 550 ANVEDLEPVR 560 NLFRKLQSTP 570 KYQKLLKERQ 580 QLPVFKHRDS 590 IVETLKRHRV 600 VVVAGETGSG 610 KSTQVPHFLL 620 EDLLLNEWEA 630 SKCNIVCTQP 640 RRISAVSLAN 650 RVCDELGCEN 660 GPGGRNSLCG 670 YQIRMESRAC 680 ESTRLLYCTT 690 GVLLRKLQED 700 GLLSNVSHVI 710 VDEVHERSVQ 720 SDFLLIILKE 730 ILQKRSDLHL 740 ILMSATVDSE 750 KFSTYFTHCP 760 ILRISGRSYP 770 VEVFHLEDII 780 EETGFVLEKD 790 SEYCQKFLEE 800 EEEVTINVTS 810 KAGGIKKYQE 820 YIPVQTGAHA 830 DLNPFYQKYS 840 SRTQHAILYM 850 NPHKINLDLI 860 LELLAYLDKS 870 PQFRNIEGAV 880 LIFLPGLAHI 890 QQLYDLLSND 900 RRFYSERYKV 910 IALHSILSTQ 920 DQAAAFTLPP 930 PGVRKIVLAT 940 NIAETGITIP 950 DVVFVIDTGR 960 TKENKYHESS 970 QMSSLVETFV 980 SKASALQRQG 990 RAGRVRDGFC 1000 FRMYTRERFE 1010 GFMDYSVPEI 1020 LRVPLEELCL 1030 HIMKCNLGSP 1040 EDFLSKALDP 1050 PQLQVISNAM 1060 NLLRKIGACE 1070 LNEPKLTPLG 1080 QHLAALPVNV 1090 KIGKMLIFGA 1100 IFGCLDPVAT 1110 LAAVMTEKSP 1120 FTTPIGRKDE 1130 ADLAKSALAM 1140 ADSDHLTIYN 1150 AYLGWKKARQ 1160 EGGYRSEITY 1170 CRRNFLNRTS 1180 LLTLEDVKQE 1190 LIKLVKAAGF 1200 SSSTTSTSWE 1210 GNRASQTLSF 1220 QEIALLKAVL 1230 VAGLYDNVGK 1240 IIYTKSVDVT 1250 EKLACIVETA 1260 QGKAQVHPSS 1270 VNRDLQTHGW 1280 LLYQEKIRYA 1290 RVYLRETTLI 1300 TPFPVLLFGG 1310 DIEVQHRERL 1320 LSIDGWIYFQ 1330 APVKIAVIFK 1340 QLRVLIDSVL 1350 RKKLENPKMS 1360 LENDKILQII TELIKTENN

Gene Ontology

Classification GO ID Description
Cellular Component GO:0022627 cytosolic small ribosomal subunit
Cellular Component GO:0016282 eukaryotic 43S preinitiation complex
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0016887 ATP hydrolysis activity
Molecular Function GO:0045296 cadherin binding
Molecular Function GO:0004386 helicase activity
Molecular Function GO:0017111 ribonucleoside triphosphate phosphatase activity
Molecular Function GO:0043024 ribosomal small subunit binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0003724 RNA helicase activity
Molecular Function GO:0008494 translation activator activity
Molecular Function GO:0003743 translation initiation factor activity
Biological Process GO:0001731 formation of translation preinitiation complex
Biological Process GO:0045948 positive regulation of translational initiation
Biological Process GO:0042255 ribosome assembly

Reference

[1] 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.

[2] 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.

[3] 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.