CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022086
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ribonuclease 3 
Protein Synonyms/Alias
 Protein Drosha; Ribonuclease III; RNase III; p241 
Gene Name
 DROSHA 
Gene Synonyms/Alias
 RN3; RNASE3L; RNASEN 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
738QKYAEECKGMIVTNPubiquitination[1]
748IVTNPGTKPSSVRIDubiquitination[2]
795PQYQKLWKSYVKLRHubiquitination[2]
827QREEALQKIRQKNTMubiquitination[2]
1205EYAITNDKTKRPVALubiquitination[2]
1207AITNDKTKRPVALRTubiquitination[2]
1250VCFFPRLKEFILNQDubiquitination[3, 4]
1277LTLRTEGKEPDIPLYubiquitination[2]
1285EPDIPLYKTLQTVGPubiquitination[2]
1313GERIGCGKGPSIQQAubiquitination[2]
Reference
 [1] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [2] 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]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 
Functional Description
 Ribonuclease III double-stranded (ds) RNA-specific endoribonuclease 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, DROSHA cleaves the 3' and 5' strands of a stem-loop in pri-miRNAs (processing center 11 bp from the dsRNA- ssRNA junction) to release hairpin-shaped pre-miRNAs that are subsequently cut by the cytoplasmic DICER to generate mature miRNAs. Involved also in pre-rRNA processing. Cleaves double- strand RNA and does not cleave single-strand RNA. Involved in the formation of GW bodies. 
Sequence Annotation
 DOMAIN 876 1056 RNase III 1.
 DOMAIN 1107 1233 RNase III 2.
 DOMAIN 1260 1334 DRBM.
 REGION 490 1374 Necessary for interaction with DGCR8 and
 METAL 1147 1147 Magnesium or manganese (By similarity).
 METAL 1219 1219 Magnesium or manganese (By similarity).
 METAL 1222 1222 Magnesium or manganese (By similarity).
 MOD_RES 373 373 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Endonuclease; Hydrolase; Magnesium; Manganese; Metal-binding; Nuclease; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Ribosome biogenesis; RNA-binding; RNA-mediated gene silencing. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1374 AA 
Protein Sequence
MMQGNTCHRM SFHPGRGCPR GRGGHGARPS APSFRPQNLR LLHPQQPPVQ YQYEPPSAPS 60
TTFSNSPAPN FLPPRPDFVP FPPPMPPSAQ GPLPPCPIRP PFPNHQMRHP FPVPPCFPPM 120
PPPMPCPNNP PVPGAPPGQG TFPFMMPPPS MPHPPPPPVM PQQVNYQYPP GYSHHNFPPP 180
SFNSFQNNPS SFLPSANNSS SPHFRHLPPY PLPKAPSERR SPERLKHYDD HRHRDHSHGR 240
GERHRSLDRR ERGRSPDRRR QDSRYRSDYD RGRTPSRHRS YERSRERERE RHRHRDNRRS 300
PSLERSYKKE YKRSGRSYGL SVVPEPAGCT PELPGEIIKN TDSWAPPLEI VNHRSPSREK 360
KRARWEEEKD RWSDNQSSGK DKNYTSIKEK EPEETMPDKN EEEEEELLKP VWIRCTHSEN 420
YYSSDPMDQV GDSTVVGTSR LRDLYDKFEE ELGSRQEKAK AARPPWEPPK TKLDEDLESS 480
SESECESDED STCSSSSDSE VFDVIAEIKR KKAHPDRLHD ELWYNDPGQM NDGPLCKCSA 540
KARRTGIRHS IYPGEEAIKP CRPMTNNAGR LFHYRITVSP PTNFLTDRPT VIEYDDHEYI 600
FEGFSMFAHA PLTNIPLCKV IRFNIDYTIH FIEEMMPENF CVKGLELFSL FLFRDILELY 660
DWNLKGPLFE DSPPCCPRFH FMPRFVRFLP DGGKEVLSMH QILLYLLRCS KALVPEEEIA 720
NMLQWEELEW QKYAEECKGM IVTNPGTKPS SVRIDQLDRE QFNPDVITFP IIVHFGIRPA 780
QLSYAGDPQY QKLWKSYVKL RHLLANSPKV KQTDKQKLAQ REEALQKIRQ KNTMRREVTV 840
ELSSQGFWKT GIRSDVCQHA MMLPVLTHHI RYHQCLMHLD KLIGYTFQDR CLLQLAMTHP 900
SHHLNFGMNP DHARNSLSNC GIRQPKYGDR KVHHMHMRKK GINTLINIMS RLGQDDPTPS 960
RINHNERLEF LGDAVVEFLT SVHLYYLFPS LEEGGLATYR TAIVQNQHLA MLAKKLELDR 1020
FMLYAHGPDL CRESDLRHAM ANCFEALIGA VYLEGSLEEA KQLFGRLLFN DPDLREVWLN 1080
YPLHPLQLQE PNTDRQLIET SPVLQKLTEF EEAIGVIFTH VRLLARAFTL RTVGFNHLTL 1140
GHNQRMEFLG DSIMQLVATE YLFIHFPDHH EGHLTLLRSS LVNNRTQAKV AEELGMQEYA 1200
ITNDKTKRPV ALRTKTLADL LESFIAALYI DKDLEYVHTF MNVCFFPRLK EFILNQDWND 1260
PKSQLQQCCL TLRTEGKEPD IPLYKTLQTV GPSHARTYTV AVYFKGERIG CGKGPSIQQA 1320
EMGAAMDALE KYNFPQMAHQ KRFIERKYRQ ELKEMRWERE HQEREPDETE DIKK 1374 
Gene Ontology
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004525; F:ribonuclease III activity; IEA:EC.
 GO:0010467; P:gene expression; TAS:Reactome.
 GO:0010586; P:miRNA metabolic process; IEA:Compara.
 GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
 GO:0031054; P:pre-miRNA processing; IEA:Compara.
 GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
 GO:0016075; P:rRNA catabolic process; IEA:InterPro. 
Interpro
 IPR001159; Ds-RNA-bd.
 IPR014720; dsRNA-bd-like_dom.
 IPR011907; RNase_III.
 IPR000999; RNase_III_dom. 
Pfam
 PF00035; dsrm
 PF00636; Ribonuclease_3 
SMART
 SM00358; DSRM
 SM00535; RIBOc 
PROSITE
 PS50137; DS_RBD
 PS00517; RNASE_3_1
 PS50142; RNASE_3_2 
PRINTS