Search Results

Overview

Uniprot IDO60306
Protein NameRNA helicase aquarius
Gene NameAQR
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
762 SGKGKKRKDADVEDE
9 AAPAQPKKIVAPTVS

Function

Involved in pre-mRNA splicing as component of the spliceosome (PubMed:11991638, PubMed:25599396, PubMed:28076346, PubMed:28502770). Intron-binding spliceosomal protein required to link pre-mRNA splicing and snoRNP (small nucleolar ribonucleoprotein) biogenesis (PubMed:16949364). Plays a key role in position-dependent assembly of intron-encoded box C/D small snoRNP, splicing being required for snoRNP assembly (PubMed:16949364). May act by helping the folding of the snoRNA sequence. Binds to intron of pre-mRNAs in a sequence-independent manner, contacting the region between snoRNA and the branchpoint of introns (40 nucleotides upstream of the branchpoint) during the late stages of splicing (PubMed:16949364). Has ATP-dependent RNA helicase activity and can unwind double-stranded RNA molecules with a 3' overhang (in vitro) (PubMed:25599396)

Protein Sequence

10 MAAPAQPKKI 20 VAPTVSQINA 30 EFVTQLACKY 40 WAPHIKKKSP 50 FDIKVIEDIY 60 EKEIVKSRFA 70 IRKIMLLEFS 80 QYLENYLWMN 90 YSPEVSSKAY 100 LMSICCMVNE 110 KFRENVPAWE 120 IFKKKPDHFP 130 FFFKHILKAA 140 LAETDGEFSL 150 HEQTVLLLFL 160 DHCFNSLEVD 170 LIRSQVQQLI 180 SLPMWMGLQL 190 ARLELELKKT 200 PKLRKFWNLI 210 KKNDEKMDPE 220 AREQAYQERR 230 FLSQLIQKFI 240 SVLKSVPLSE 250 PVTMDKVHYC 260 ERFIELMIDL 270 EALLPTRRWF 280 NTILDDSHLL 290 VHCYLSNLVR 300 REEDGHLFSQ 310 LLDMLKFYTG 320 FEINDQTGNA 330 LTENEMTTIH 340 YDRITSLQRA 350 AFAHFPELYD 360 FALSNVAEVD 370 TRESLVKFFG 380 PLSSNTLHQV 390 ASYLCLLPTL 400 PKNEDTTFDK 410 EFLLELLVSR 420 HERRISQIQQ 430 LNQMPLYPTE 440 KIIWDENIVP 450 TEYYSGEGCL 460 ALPKLNLQFL 470 TLHDYLLRNF 480 NLFRLESTYE 490 IRQDIEDSVS 500 RMKPWQSEYG 510 GVVFGGWARM 520 AQPIVAFTVV 530 EVAKPNIGEN 540 WPTRVRADVT 550 INLNVRDHIK 560 DEWEGLRKHD 570 VCFLITVRPT 580 KPYGTKFDRR 590 RPFIEQVGLV 600 YVRGCEIQGM 610 LDDKGRVIED 620 GPEPRPNLRG 630 ESRTFRVFLD 640 PNQYQQDMTN 650 TIQNGAEDVY 660 ETFNIIMRRK 670 PKENNFKAVL 680 ETIRNLMNTD 690 CVVPDWLHDI 700 ILGYGDPSSA 710 HYSKMPNQIA 720 TLDFNDTFLS 730 IEHLKASFPG 740 HNVKVTVEDP 750 ALQIPPFRIT 760 FPVRSGKGKK 770 RKDADVEDED 780 TEEAKTLIVE 790 PHVIPNRGPY 800 PYNQPKRNTI 810 QFTHTQIEAI 820 RAGMQPGLTM 830 VVGPPGTGKT 840 DVAVQIISNI 850 YHNFPEQRTL 860 IVTHSNQALN 870 QLFEKIMALD 880 IDERHLLRLG 890 HGEEELETEK 900 DFSRYGRVNY 910 VLARRIELLE 920 EVKRLQKSLG 930 VPGDASYTCE 940 TAGYFFLYQV 950 MSRWEEYISK 960 VKNKGSTLPD 970 VTEVSTFFPF 980 HEYFANAPQP 990 IFKGRSYEED 1000 MEIAEGCFRH 1010 IKKIFTQLEE 1020 FRASELLRSG 1030 LDRSKYLLVK 1040 EAKIIAMTCT 1050 HAALKRHDLV 1060 KLGFKYDNIL 1070 MEEAAQILEI 1080 ETFIPLLLQN 1090 PQDGFSRLKR 1100 WIMIGDHHQL 1110 PPVIKNMAFQ 1120 KYSNMEQSLF 1130 TRFVRVGVPT 1140 VDLDAQGRAR 1150 ASLCNLYNWR 1160 YKNLGNLPHV 1170 QLLPEFSTAN 1180 AGLLYDFQLI 1190 NVEDFQGVGE 1200 SEPNPYFYQN 1210 LGEAEYVVAL 1220 FMYMCLLGYP 1230 ADKISILTTY 1240 NGQKHLIRDI 1250 INRRCGNNPL 1260 IGRPNKVTTV 1270 DRFQGQQNDY 1280 ILLSLVRTRA 1290 VGHLRDVRRL 1300 VVAMSRARLG 1310 LYIFARVSLF 1320 QNCFELTPAF 1330 SQLTARPLHL 1340 HIIPTEPFPT 1350 TRKNGERPSH 1360 EVQIIKNMPQ 1370 MANFVYNMYM 1380 HLIQTTHHYH 1390 QTLLQLPPAM 1400 VEEGEEVQNQ 1410 ETELETEEEA 1420 MTVQADIIPS 1430 PTDTSCRQET 1440 PAFQTDTTPS 1450 ETGATSTPEA 1460 IPALSETTPT 1470 VVGAVSAPAE 1480 ANTPQDATSA PEETK

Gene Ontology

Classification GO ID Description
Cellular Component GO:0071013 catalytic step 2 spliceosome
Cellular Component GO:0016020 membrane
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0071007 U2-type catalytic step 2 spliceosome
Molecular Function GO:0034458 3'-5' RNA helicase activity
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0016887 ATP hydrolysis activity
Molecular Function GO:0003729 mRNA binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0003727 single-stranded RNA binding
Biological Process GO:0000398 mRNA splicing, via spliceosome

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 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.

[3] 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.

[4] 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.

[5] 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.