Search Results

Overview

Uniprot ID	Q8WYQ5
Protein Name	Microprocessor complex subunit DGCR8
Gene Name	DGCR8
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
107	RHAPAVRKFSPDLKL
647	KFEVVPGKNQKSEYV

Function

Component of the microprocessor complex that acts as a RNA- and heme-binding protein that is involved in the initial step of microRNA (miRNA) biogenesis. Component of the microprocessor complex that is required to process primary miRNA transcripts (pri-miRNAs) to release precursor miRNA (pre-miRNA) in the nucleus. Within the microprocessor complex, DGCR8 function as a molecular anchor necessary for the recognition of pri-miRNA at dsRNA-ssRNA junction and directs DROSHA to cleave 11 bp away form the junction to release hairpin-shaped pre-miRNAs that are subsequently cut by the cytoplasmic DICER to generate mature miRNAs (PubMed:26027739, PubMed:26748718). The heme-bound DGCR8 dimer binds pri-miRNAs as a cooperative trimer (of dimers) and is active in triggering pri-miRNA cleavage, whereas the heme-free DGCR8 monomer binds pri-miRNAs as a dimer and is much less active. Both double-stranded and single-stranded regions of a pri-miRNA are required for its binding (PubMed:15531877, PubMed:15574589, PubMed:15589161, PubMed:16751099, PubMed:16906129, PubMed:16963499, PubMed:17159994). Specifically recognizes and binds N6-methyladenosine (m6A)-containing pri-miRNAs, a modification required for pri-miRNAs processing (PubMed:25799998). Involved in the silencing of embryonic stem cell self-renewal (By similarity). Also plays a role in DNA repair by promoting the recruitment of RNF168 to RNF8 and MDC1 at DNA double-strand breaks and subsequently the clearance of DNA breaks (PubMed:34188037)

Protein Sequence

10 METDESPSPL 20 PCGPAGEAVM 30 ESRARPFQAL 40 PREQSPPPPL 50 QTSSGAEVMD 60 VGSGGDGQSE 70 LPAEDPFNFY 80 GASLLSKGSF 90 SKGRLLIDPN 100 CSGHSPRTAR 110 HAPAVRKFSP 120 DLKLLKDVKI 130 SVSFTESCRS 140 KDRKVLYTGA 150 ERDVRAECGL 160 LLSPVSGDVH 170 ACPFGGSVGD 180 GVGIGGESAD 190 KKDEENELDQ 200 EKRVEYAVLD 210 ELEDFTDNLE 220 LDEEGAGGFT 230 AKAIVQRDRV 240 DEEALNFPYE 250 DDFDNDVDAL 260 LEEGLCAPKK 270 RRTEEKYGGD 280 SDHPSDGETS 290 VQPMMTKIKT 300 VLKSRGRPPT 310 EPLPDGWIMT 320 FHNSGVPVYL 330 HRESRVVTWS 340 RPYFLGTGSI 350 RKHDPPLSSI 360 PCLHYKKMKD 370 NEEREQSSDL 380 TPSGDVSPVK 390 PLSRSAELEF 400 PLDEPDSMGA 410 DPGPPDEKDP 420 LGAEAAPGAL 430 GQVKAKVEVC 440 KDESVDLEEF 450 RSYLEKRFDF 460 EQVTVKKFRT 470 WAERRQFNRE 480 MKRKQAESER 490 PILPANQKLI 500 TLSVQDAPTK 510 KEFVINPNGK 520 SEVCILHEYM 530 QRVLKVRPVY 540 NFFECENPSE 550 PFGASVTIDG 560 VTYGSGTASS 570 KKLAKNKAAR 580 ATLEILIPDF 590 VKQTSEEKPK 600 DSEELEYFNH 610 ISIEDSRVYE 620 LTSKAGLLSP 630 YQILHECLKR 640 NHGMGDTSIK 650 FEVVPGKNQK 660 SEYVMACGKH 670 TVRGWCKNKR 680 VGKQLASQKI 690 LQLLHPHVKN 700 WGSLLRMYGR 710 ESSKMVKQET 720 SDKSVIELQQ 730 YAKKNKPNLH 740 ILSKLQEEMK 750 RLAEEREETR 760 KKPKMSIVAS 770 AQPGGEPLCT VDV

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0005737	cytoplasm
Cellular Component	GO:0098978	glutamatergic synapse
Cellular Component	GO:0070877	microprocessor complex
Cellular Component	GO:0016604	nuclear body
Cellular Component	GO:0005730	nucleolus
Cellular Component	GO:0005654	nucleoplasm
Cellular Component	GO:0005634	nucleus
Cellular Component	GO:0014069	postsynaptic density
Cellular Component	GO:0035861	site of double-strand break
Molecular Function	GO:0003725	double-stranded RNA binding
Molecular Function	GO:0020037	heme binding
Molecular Function	GO:0042802	identical protein binding
Molecular Function	GO:0046872	metal ion binding
Molecular Function	GO:0070878	primary miRNA binding
Molecular Function	GO:0042803	protein homodimerization activity
Molecular Function	GO:0030674	protein-macromolecule adaptor activity
Molecular Function	GO:0140517	protein-RNA adaptor activity
Biological Process	GO:0006974	DNA damage response
Biological Process	GO:2000633	positive regulation of pre-miRNA processing
Biological Process	GO:0031053	primary miRNA processing

Reference

[1] 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.

[2] 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.