Search Results

Overview

Uniprot ID	P42285
Protein Name	Exosome RNA helicase MTR4
Gene Name	MTREX
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
126	EEDYLPLKPRVGKAA
35	EKDKGKWKGPPGSAD
358	RDAGDLAKGDQKGRK
369	KGRKGGTKGPSNVFK
43	GPPGSADKAGKRFDG
51	AGKRFDGKLQSESTN
61	SESTNNGKNKRDVDF
63	STNNGKNKRDVDFEG
761	DNRQSVLKSIQEVQK
78	TDEPIFGKKPRIEES
79	DEPIFGKKPRIEESI

Function

Catalyzes the ATP-dependent unwinding of RNA duplexes with a single-stranded 3' RNA extension (PubMed:27871484, PubMed:29844170, PubMed:29906447). Central subunit of many protein complexes, namely TRAMP-like, nuclear exosome targeting (NEXT) and poly(A) tail exosome targeting (PAXT) (PubMed:21855801, PubMed:27871484, PubMed:29844170). NEXT functions as an RNA exosome cofactor that directs a subset of non-coding short-lived RNAs for exosomal degradation. NEXT is involved in surveillance and turnover of aberrant transcripts and non-coding RNAs (PubMed:27871484, PubMed:29844170). PAXT directs a subset of long and polyadenylated poly(A) RNAs for exosomal degradation. The RNA exosome is fundamental for the degradation of RNA in eukaryotic nuclei. Substrate targeting is facilitated by its cofactor ZCCHC8, which links to RNA-binding protein adapters (PubMed:27871484). Associated with the RNA exosome complex and involved in the 3'-processing of the 7S pre-RNA to the mature 5.8S rRNA (PubMed:17412707, PubMed:29107693). May be involved in pre-mRNA splicing. In the context of NEXT complex can also in vitro unwind DNA:RNA heteroduplexes with a 3' poly (A) RNA tracking strand (PubMed:29844170). Can promote unwinding and degradation of structured RNA substrates when associated with the nuclear exosome and its cofactors. Can displace a DNA strand while translocating on RNA to ultimately degrade the RNA within a DNA/RNA heteroduplex (PubMed:29906447). Plays a role in DNA damage response (PubMed:29902117)

Protein Sequence

10 MADAFGDELF 20 SVFEGDSTTA 30 AGTKKDKEKD 40 KGKWKGPPGS 50 ADKAGKRFDG 60 KLQSESTNNG 70 KNKRDVDFEG 80 TDEPIFGKKP 90 RIEESITEDL 100 SLADLMPRVK 110 VQSVETVEGC 120 THEVALPAEE 130 DYLPLKPRVG 140 KAAKEYPFIL 150 DAFQREAIQC 160 VDNNQSVLVS 170 AHTSAGKTVC 180 AEYAIALALR 190 EKQRVIFTSP 200 IKALSNQKYR 210 EMYEEFQDVG 220 LMTGDVTINP 230 TASCLVMTTE 240 ILRSMLYRGS 250 EVMREVAWVI 260 FDEIHYMRDS 270 ERGVVWEETI 280 ILLPDNVHYV 290 FLSATIPNAR 300 QFAEWICHLH 310 KQPCHVIYTD 320 YRPTPLQHYI 330 FPAGGDGLHL 340 VVDENGDFRE 350 DNFNTAMQVL 360 RDAGDLAKGD 370 QKGRKGGTKG 380 PSNVFKIVKM 390 IMERNFQPVI 400 IFSFSKKDCE 410 AYALQMTKLD 420 FNTDEEKKMV 430 EEVFSNAIDC 440 LSDEDKKLPQ 450 VEHVLPLLKR 460 GIGIHHGGLL 470 PILKETIEIL 480 FSEGLIKALF 490 ATETFAMGIN 500 MPARTVLFTN 510 ARKFDGKDFR 520 WISSGEYIQM 530 SGRAGRRGMD 540 DRGIVILMVD 550 EKMSPTIGKQ 560 LLKGSADPLN 570 SAFHLTYNMV 580 LNLLRVEEIN 590 PEYMLEKSFY 600 QFQHYRAIPG 610 VVEKVKNSEE 620 QYNKIVIPNE 630 ESVVIYYKIR 640 QQLAKLGKEI 650 EEYIHKPKYC 660 LPFLQPGRLV 670 KVKNEGDDFG 680 WGVVVNFSKK 690 SNVKPNSGEL 700 DPLYVVEVLL 710 RCSKESLKNS 720 ATEAAKPAKP 730 DEKGEMQVVP 740 VLVHLLSAIS 750 SVRLYIPKDL 760 RPVDNRQSVL 770 KSIQEVQKRF 780 PDGIPLLDPI 790 DDMGIQDQGL 800 KKVIQKVEAF 810 EHRMYSHPLH 820 NDPNLETVYT 830 LCEKKAQIAI 840 DIKSAKRELK 850 KARTVLQMDE 860 LKCRKRVLRR 870 LGFATSSDVI 880 EMKGRVACEI 890 SSADELLLTE 900 MMFNGLFNDL 910 SAEQATALLS 920 CFVFQENSSE 930 MPKLTEQLAG 940 PLRQMQECAK 950 RIAKVSAEAK 960 LEIDEETYLS 970 SFKPHLMDVV 980 YTWATGATFA 990 HICKMTDVFE 1000 GSIIRCMRRL 1010 EELLRQMCQA 1020 AKAIGNTELE 1030 NKFAEGITKI 1040 KRDIVFAASL YL

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0071013	catalytic step 2 spliceosome
Biological Process	GO:0000460	maturation of 5.8S rRNA
Biological Process	GO:0000398	mRNA splicing, via spliceosome
Biological Process	GO:0006401	RNA catabolic process
Biological Process	GO:0006364	rRNA processing
Biological Process	GO:0016076	snRNA catabolic process
Cellular Component	GO:0016607	nuclear speck
Cellular Component	GO:0005730	nucleolus
Cellular Component	GO:0005654	nucleoplasm
Cellular Component	GO:0005634	nucleus
Cellular Component	GO:0031499	TRAMP 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:0006974	DNA damage response

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.