Search Results

Overview

Uniprot IDQ9Y2L1
Protein NameExosome complex exonuclease RRP44
Gene NameDIS3
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
18 TRAGGVMKIVREHYL

Function

Putative catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. DIS3 has both 3'-5' exonuclease and endonuclease activities

Protein Sequence

10 MLKSKTFLKK 20 TRAGGVMKIV 30 REHYLRDDIG 40 CGAPGCAACG 50 GAHEGPALEP 60 QPQDPASSVC 70 PQPHYLLPDT 80 NVLLHQIDVL 90 EDPAIRNVIV 100 LQTVLQEVRN 110 RSAPVYKRIR 120 DVTNNQEKHF 130 YTFTNEHHRE 140 TYVEQEQGEN 150 ANDRNDRAIR 160 VAAKWYNEHL 170 KKMSADNQLQ 180 VIFITNDRRN 190 KEKAIEEGIP 200 AFTCEEYVKS 210 LTANPELIDR 220 LACLSEEGNE 230 IESGKIIFSE 240 HLPLSKLQQG 250 IKSGTYLQGT 260 FRASRENYLE 270 ATVWIHGDNE 280 ENKEIILQGL 290 KHLNRAVHED 300 IVAVELLPKS 310 QWVAPSSVVL 320 HDEGQNEEDV 330 EKEEETERML 340 KTAVSEKMLK 350 PTGRVVGIIK 360 RNWRPYCGML 370 SKSDIKESRR 380 HLFTPADKRI 390 PRIRIETRQA 400 STLEGRRIIV 410 AIDGWPRNSR 420 YPNGHFVRNL 430 GDVGEKETET 440 EVLLLEHDVP 450 HQPFSQAVLS 460 FLPKMPWSIT 470 EKDMKNREDL 480 RHLCICSVDP 490 PGCTDIDDAL 500 HCRELENGNL 510 EVGVHIADVS 520 HFIRPGNALD 530 QESARRGTTV 540 YLCEKRIDMV 550 PELLSSNLCS 560 LKCDVDRLAF 570 SCIWEMNHNA 580 EILKTKFTKS 590 VINSKASLTY 600 AEAQLRIDSA 610 NMNDDITTSL 620 RGLNKLAKIL 630 KKRRIEKGAL 640 TLSSPEVRFH 650 MDSETHDPID 660 LQTKELRETN 670 SMVEEFMLLA 680 NISVAKKIHE 690 EFSEHALLRK 700 HPAPPPSNYE 710 ILVKAARSRN 720 LEIKTDTAKS 730 LAESLDQAES 740 PTFPYLNTLL 750 RILATRCMMQ 760 AVYFCSGMDN 770 DFHHYGLASP 780 IYTHFTSPIR 790 RYADVIVHRL 800 LAVAIGADCT 810 YPELTDKHKL 820 ADICKNLNFR 830 HKMAQYAQRA 840 SVAFHTQLFF 850 KSKGIVSEEA 860 YILFVRKNAI 870 VVLIPKYGLE 880 GTVFFEEKDK 890 PNPQLIYDDE 900 IPSLKIEDTV 910 FHVFDKVKVK 920 IMLDSSNLQH 930 QKIRMSLVEP 940 QIPGISIPTD 950 TSNMDLNGPK KKKMKLGK

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000177 cytoplasmic exosome (RNase complex)
Cellular Component GO:0005829 cytosol
Cellular Component GO:0000178 exosome (RNase complex)
Cellular Component GO:0016020 membrane
Cellular Component GO:0000176 nuclear exosome (RNase complex)
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0000175 3'-5'-RNA exonuclease activity
Molecular Function GO:0004519 endonuclease activity
Molecular Function GO:0005085 guanyl-nucleotide exchange factor activity
Molecular Function GO:0003723 RNA binding
Biological Process GO:0071034 CUT catabolic process
Biological Process GO:0071031 nuclear mRNA surveillance of mRNA 3'-end processing
Biological Process GO:0000288 nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay
Biological Process GO:0006401 RNA catabolic process
Biological Process GO:0006396 RNA processing
Biological Process GO:0016075 rRNA catabolic process
Biological Process GO:0006364 rRNA processing

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] 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.