| Tag | Content |
|---|
| CPLM ID | CPLM-018379 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Microprocessor complex subunit DGCR8 |
Protein Synonyms/Alias | DiGeorge syndrome critical region 8 |
Gene Name | DGCR8 |
Gene Synonyms/Alias | C22orf12; DGCRK6; LP4941 |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 501 | VQDAPTKKEFVINPN | ubiquitination | [1] |
|
Reference | [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments. Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA. Mol Cell Proteomics. 2013 Mar;12(3):825-31. [ PMID: 23266961] |
Functional Description | 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. 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. Involved in the silencing of embryonic stem cells self- renewal. |
Sequence Annotation | DOMAIN 301 334 WW.
DOMAIN 511 578 DRBM 1.
DOMAIN 620 685 DRBM 2.
REGION 1 342 Necessary for interaction with NCL.
REGION 1 275 Necessary for nuclear localization and
REGION 276 751 Necessary for heme-binding and pri-miRNA
REGION 484 773 Necessary for interaction with DROSHA.
METAL 352 352 Iron (heme axial ligand) (Probable).
MOD_RES 95 95 Phosphoserine.
MOD_RES 271 271 Phosphoserine.
MOD_RES 275 275 Phosphoserine.
MOD_RES 371 371 Phosphothreonine.
MOD_RES 377 377 Phosphoserine. |
Keyword | 3D-structure; Alternative splicing; Complete proteome; Heme; Iron; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; RNA-binding. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 773 AA |
Protein Sequence | METDESPSPL PCGPAGEAVM ESRARPFQAL PREQSPPPPL QTSSGAEVMD VGSGGDGQSE 60
LPAEDPFNFY GASLLSKGSF SKGRLLIDPN CSGHSPRTAR HAPAVRKFSP DLKLLKDVKI 120
SVSFTESCRS KDRKVLYTGA ERDVRAECGL LLSPVSGDVH ACPFGGSVGD GVGIGGESAD 180
KKDEENELDQ EKRVEYAVLD ELEDFTDNLE LDEEGAGGFT AKAIVQRDRV DEEALNFPYE 240
DDFDNDVDAL LEEGLCAPKK RRTEEKYGGD SDHPSDGETS VQPMMTKIKT VLKSRGRPPT 300
EPLPDGWIMT FHNSGVPVYL HRESRVVTWS RPYFLGTGSI RKHDPPLSSI PCLHYKKMKD 360
NEEREQSSDL TPSGDVSPVK PLSRSAELEF PLDEPDSMGA DPGPPDEKDP LGAEAAPGAL 420
GQVKAKVEVC KDESVDLEEF RSYLEKRFDF EQVTVKKFRT WAERRQFNRE MKRKQAESER 480
PILPANQKLI TLSVQDAPTK KEFVINPNGK SEVCILHEYM QRVLKVRPVY NFFECENPSE 540
PFGASVTIDG VTYGSGTASS KKLAKNKAAR ATLEILIPDF VKQTSEEKPK DSEELEYFNH 600
ISIEDSRVYE LTSKAGLLSP YQILHECLKR NHGMGDTSIK FEVVPGKNQK SEYVMACGKH 660
TVRGWCKNKR VGKQLASQKI LQLLHPHVKN WGSLLRMYGR ESSKMVKQET SDKSVIELQQ 720
YAKKNKPNLH ILSKLQEEMK RLAEEREETR KKPKMSIVAS AQPGGEPLCT VDV 773 |
Gene Ontology | |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |