DGCR8_MOUSE - dbPTM
DGCR8_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DGCR8_MOUSE
UniProt AC Q9EQM6
Protein Name Microprocessor complex subunit DGCR8
Gene Name Dgcr8
Organism Mus musculus (Mouse).
Sequence Length 773
Subcellular Localization Nucleus . Nucleus, nucleolus . Colocalizes with nucleolin and DROSHA in the nucleolus. Mostly detected in the nucleolus as electron-dense granular patches around the fibrillar center (FC) and granular component (GC). Also detected in the nucleoplasm
Protein 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. [PubMed: 17259983 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. Specifically recognizes and binds N6-methyladenosine (m6A)-containing pri-miRNAs, a modification required for pri-miRNAs processing (By similarity Involved in the silencing of embryonic stem cell self-renewal]
Protein Sequence METYESPSPLPREPAGEAMMENRACPFQVLPHEQSPPPPLQTSSDAEVMDVGSGGDGQSEPPADDPFNFYGASLLSKGSFSKGRLLIDPNCSGHSPRTARHAPAVRKFSPDLKLLKDVKISVSFTESCRSKDRKVLYTGVERSTRPECGQLLSPVSGDVHACPFGGSVGNGVGLGGESADKKDEENELDQEKRVEYAVLDELEDFTDNLELDEEGTGGFTAKAIVQRDRVDEEALNFSYEDDFDNDVDALLEEGLCAPKKRRMEEKYGGDSDHPSDGETSVQPMMTKIKTVLKSRGRPPTEPLPDGWIMTFHNSGVPVYLHRESRVVTWSRPYFLGTGSIRKHDPPLSSIPCLHYKKMKDNEEREQNCDLAPSGEVSPVKPLGRSAELDFPLEEPDSMGGDSGSMDEKDPLGAEAAAGALGQVKAKVEVCKDESVDLEEFRNYLEKRFDFEQVTVKKFRTWAERRQFNREMKRKQAESERPILPANQKLITLSVQDAPTKKEFVINPNGKSEVCILHEYMQRVLKVRPVYNFFECENPSEPFGASVTIDGVTYGSGTASSKKLAKNKAARATLEILIPDFVKQTSEEKPKDSEELEYFNHISIEDSRVYELTSKAGLLSPYQILHECLKRNHGMGDTSIKFEVVPGKNQKSEYVMACGKHTVRGWCKNKRVGKQLASQKILQLLHPHVKNWGSLLRMYGRESSKMVKQETSDKSVIELQQYAKKNRPNLHILSKLQEEMKRLAAEREETRKKPKMSIVASAQPGGEPLCTVDV
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
3Phosphorylation-----METYESPSPL
-----CCCCCCCCCC		31.1529472430
4Phosphorylation----METYESPSPLP
----CCCCCCCCCCC		10.9126643407
6Phosphorylation--METYESPSPLPRE
--CCCCCCCCCCCCC		21.9225266776
8PhosphorylationMETYESPSPLPREPA
CCCCCCCCCCCCCCC		48.6326824392
35PhosphorylationQVLPHEQSPPPPLQT
CCCCCCCCCCCCCCC		36.07-
92PhosphorylationLLIDPNCSGHSPRTA
EEECCCCCCCCCCHH		46.2926824392
95PhosphorylationDPNCSGHSPRTARHA
CCCCCCCCCCHHHCC		21.4327087446
109PhosphorylationAPAVRKFSPDLKLLK
CHHHHHCCCCCHHHC		22.1222942356
267PhosphorylationKRRMEEKYGGDSDHP
HHHHHHHHCCCCCCC		29.6227087446
271PhosphorylationEEKYGGDSDHPSDGE
HHHHCCCCCCCCCCC		40.8825521595
275PhosphorylationGGDSDHPSDGETSVQ
CCCCCCCCCCCCCHH		55.6225521595
279PhosphorylationDHPSDGETSVQPMMT
CCCCCCCCCHHHHHH		39.4623684622
280PhosphorylationHPSDGETSVQPMMTK
CCCCCCCCHHHHHHH		17.9125159016
286PhosphorylationTSVQPMMTKIKTVLK
CCHHHHHHHHHHHHH		24.3025777480
294PhosphorylationKIKTVLKSRGRPPTE
HHHHHHHHCCCCCCC		35.4924704852
373PhosphorylationQNCDLAPSGEVSPVK
HCCCCCCCCCCCCCC		41.8127742792
377PhosphorylationLAPSGEVSPVKPLGR
CCCCCCCCCCCCCCC		21.4825521595
385PhosphorylationPVKPLGRSAELDFPL
CCCCCCCEEECCCCC		25.0523984901
397PhosphorylationFPLEEPDSMGGDSGS
CCCCCCCCCCCCCCC		30.0026239621
402PhosphorylationPDSMGGDSGSMDEKD
CCCCCCCCCCCCCCC		35.7226239621
404PhosphorylationSMGGDSGSMDEKDPL
CCCCCCCCCCCCCCC		27.3226239621
426AcetylationALGQVKAKVEVCKDE
HHCHHHEEEEECCCC		32.9619861685
434PhosphorylationVEVCKDESVDLEEFR
EEECCCCCCCHHHHH		30.9429550500
491PhosphorylationPANQKLITLSVQDAP
CCCCEEEEEEECCCC		24.34-
493PhosphorylationNQKLITLSVQDAPTK
CCEEEEEEECCCCCC		14.75-
619PhosphorylationTSKAGLLSPYQILHE
HCCCCCCCHHHHHHH		26.9726745281
621PhosphorylationKAGLLSPYQILHECL
CCCCCCHHHHHHHHH		12.5726745281
714PhosphorylationKQETSDKSVIELQQY
CCCCCCCHHHHHHHH		33.0627841257
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of DGCR8_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DGCR8_MOUSE !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of DGCR8_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of DGCR8_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DGCR8_MOUSE

loading...

Related Literatures of Post-Translational Modification

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory