Search Results

Overview

Uniprot IDQ8IY37
Protein NameProbable ATP-dependent RNA helicase DHX37
Gene NameDHX37
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
118 RLFYTTSKLGTGNRM
142 VVAPGQEKISSLSGA
397 RIVTLRAKRNLPLKL
403 AKRNLPLKLLIMSAT
54 NALVLPGKKKKKTKA
55 ALVLPGKKKKKTKAP
60 GKKKKKTKAPPLSKK
757 PQKAERVKQLQENRL
82 KEKKVLQKILEQKEK

Function

ATP-binding RNA helicase that plays a role in maturation of the small ribosomal subunit in ribosome biogenesis (PubMed:30582406). Required for the release of the U3 snoRNP from pre-ribosomal particles (PubMed:30582406). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797). Plays a role in early testis development (PubMed:31287541, PubMed:31337883). Probably also plays a role in brain development (PubMed:31256877)

Protein Sequence

10 MGKLRRRYNI 20 KGRQQAGPGP 30 SKGPPEPPPV 40 QLELEDKDTL 50 KGVDASNALV 60 LPGKKKKKTK 70 APPLSKKEKK 80 PLTKKEKKVL 90 QKILEQKEKK 100 SQRAEMLQKL 110 SEVQASEAEM 120 RLFYTTSKLG 130 TGNRMYHTKE 140 KADEVVAPGQ 150 EKISSLSGAH 160 RKRRRWPSAE 170 EEEEEEEESE 180 SELEEESELD 190 EDPAAEPAEA 200 GVGTTVAPLP 210 PAPAPSSQPV 220 PAGMTVPPPP 230 AAAPPLPRAL 240 AKPAVFIPVN 250 RSPEMQEERL 260 KLPILSEEQV 270 IMEAVAEHPI 280 VIVCGETGSG 290 KTTQVPQFLY 300 EAGFSSEDSI 310 IGVTEPRRVA 320 AVAMSQRVAK 330 EMNLSQRVVS 340 YQIRYEGNVT 350 EETRIKFMTD 360 GVLLKEIQKD 370 FLLLRYKVVI 380 IDEAHERSVY 390 TDILIGLLSR 400 IVTLRAKRNL 410 PLKLLIMSAT 420 LRVEDFTQNP 430 RLFAKPPPVI 440 KVESRQFPVT 450 VHFNKRTPLE 460 DYSGECFRKV 470 CKIHRMLPAG 480 GILVFLTGQA 490 EVHALCRRLR 500 KAFPPSRARP 510 QEKDDDQKDS 520 VEEMRKFKKS 530 RARAKKARAE 540 VLPQINLDHY 550 SVLPAGEGDE 560 DREAEVDEEE 570 GALDSDLDLD 580 LGDGGQDGGE 590 QPDASLPLHV 600 LPLYSLLAPE 610 KQAQVFKPPP 620 EGTRLCVVAT 630 NVAETSLTIP 640 GIKYVVDCGK 650 VKKRYYDRVT 660 GVSSFRVTWV 670 SQASADQRAG 680 RAGRTEPGHC 690 YRLYSSAVFG 700 DFEQFPPPEI 710 TRRPVEDLIL 720 QMKALNVEKV 730 INFPFPTPPS 740 VEALLAAEEL 750 LIALGALQPP 760 QKAERVKQLQ 770 ENRLSCPITA 780 LGRTMATFPV 790 APRYAKMLAL 800 SRQHGCLPYA 810 ITIVASMTVR 820 ELFEELDRPA 830 ASDEELTRLK 840 SKRARVAQMK 850 RTWAGQGASL 860 KLGDLMVLLG 870 AVGACEYASC 880 TPQFCEANGL 890 RYKAMMEIRR 900 LRGQLTTAVN 910 AVCPEAELFV 920 DPKMQPPTES 930 QVTYLRQIVT 940 AGLGDHLARR 950 VQSEEMLEDK 960 WRNAYKTPLL 970 DDPVFIHPSS 980 VLFKELPEFV 990 VYQEIVETTK 1000 MYMKGVSSVE 1010 VQWIPALLPS 1020 YCQFDKPLEE 1030 PAPTYCPERG 1040 RVLCHRASVF 1050 YRVGWPLPAI 1060 EVDFPEGIDR 1070 YKHFARFLLE 1080 GQVFRKLASY 1090 RSCLLSSPGT 1100 MLKTWARLQP 1110 RTESLLRALV 1120 AEKADCHEAL 1130 LAAWKKNPKY 1140 LLAEYCEWLP 1150 QAMHPDIEKA WPPTTVH

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0031965 nuclear membrane
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0032040 small-subunit processome
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0016887 ATP hydrolysis activity
Molecular Function GO:0004386 helicase activity
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0003724 RNA helicase activity
Molecular Function GO:0034511 U3 snoRNA binding
Biological Process GO:0007420 brain development
Biological Process GO:0000462 maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
Biological Process GO:2000020 positive regulation of male gonad development
Biological Process GO:0042274 ribosomal small subunit biogenesis
Biological Process GO:0042255 ribosome assembly
Biological Process GO:0042254 ribosome biogenesis

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] 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.

[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.