UniProtKB - Q9NRR4 (RNC_HUMAN)
Ribonuclease 3
DROSHA
Functioni
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.
11 PublicationsCatalytic activityi
- Endonucleolytic cleavage to 5'-phosphomonoester.4 Publications EC:3.1.26.3
Cofactori
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 536 | Zinc 11 Publication | 1 | |
Metal bindingi | 538 | Zinc 11 Publication | 1 | |
Metal bindingi | 549 | Zinc 11 Publication | 1 | |
Metal bindingi | 561 | Zinc 21 Publication | 1 | |
Metal bindingi | 609 | Zinc 21 Publication | 1 | |
Metal bindingi | 676 | Zinc 21 Publication | 1 | |
Metal bindingi | 680 | Zinc 21 Publication | 1 | |
Metal bindingi | 969 | Magnesium 1By similarity | 1 | |
Metal bindingi | 1026 | Zinc 11 Publication | 1 | |
Metal bindingi | 1042 | Magnesium 1By similarity | 1 | |
Metal bindingi | 1045 | Magnesium 1By similarity1 Publication | 1 | |
Metal bindingi | 1147 | Magnesium 2By similarity | 1 | |
Sitei | 1215 | Important for activityBy similarity | 1 | |
Metal bindingi | 1219 | Magnesium 2By similarity | 1 | |
Metal bindingi | 1222 | Magnesium 2By similarity1 Publication | 1 |
GO - Molecular functioni
- DEAD/H-box RNA helicase binding Source: BHF-UCL
- double-stranded RNA binding Source: GO_Central
- lipopolysaccharide binding Source: UniProtKB
- metal ion binding Source: UniProtKB-KW
- primary miRNA binding Source: ARUK-UCL
- protein homodimerization activity Source: BHF-UCL
- ribonuclease III activity Source: WormBase
- RNA binding Source: UniProtKB
- R-SMAD binding Source: BHF-UCL
- SMAD binding Source: BHF-UCL
GO - Biological processi
- defense response to Gram-negative bacterium Source: UniProtKB
- defense response to Gram-positive bacterium Source: UniProtKB
- miRNA metabolic process Source: Ensembl
- positive regulation of gene expression Source: Ensembl
- pre-miRNA processing Source: Ensembl
- primary miRNA processing Source: WormBase
- regulation of gene expression Source: GO_Central
- regulation of inflammatory response Source: Ensembl
- regulation of miRNA metabolic process Source: Ensembl
- regulation of regulatory T cell differentiation Source: Ensembl
- ribosome biogenesis Source: UniProtKB-KW
- RNA processing Source: GO_Central
- rRNA catabolic process Source: InterPro
Keywordsi
Molecular function | Endonuclease, Hydrolase, Nuclease, RNA-binding |
Biological process | Ribosome biogenesis, RNA-mediated gene silencing |
Ligand | Magnesium, Manganese, Metal-binding |
Enzyme and pathway databases
BRENDAi | 3.1.26.3, 2681 |
PathwayCommonsi | Q9NRR4 |
Reactomei | R-HSA-203927, MicroRNA (miRNA) biogenesis |
SignaLinki | Q9NRR4 |
SIGNORi | Q9NRR4 |
Names & Taxonomyi
Protein namesi | Recommended name: Ribonuclease 3 (EC:3.1.26.34 Publications)Alternative name(s): Protein Drosha1 Publication Ribonuclease III Short name: RNase III p241 |
Gene namesi | Name:DROSHA Synonyms:RN3, RNASE3L, RNASEN |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:17904, DROSHA |
MIMi | 608828, gene |
neXtProti | NX_Q9NRR4 |
VEuPathDBi | HostDB:ENSG00000113360 |
Subcellular locationi
Cytosol
- cytosol Source: HPA
Nucleus
- microprocessor complex Source: BHF-UCL
- nucleolus Source: UniProtKB-SubCell
- nucleoplasm Source: HPA
- nucleus Source: GO_Central
Other locations
- postsynaptic density Source: Ensembl
Keywords - Cellular componenti
NucleusPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 536 | C → A: Impairs protein folding and stability; when associated with A-538. 1 Publication | 1 | |
Mutagenesisi | 538 | C → A: Impairs protein folding and stability; when associated with A-536. 1 Publication | 1 | |
Mutagenesisi | 561 | C → A: Impairs protein folding and stability. 1 Publication | 1 | |
Mutagenesisi | 622 – 623 | RF → AA: Abolishes RNase activity. 1 Publication | 2 | |
Mutagenesisi | 676 | C → A: Impairs protein folding and stability. 1 Publication | 1 | |
Mutagenesisi | 835 – 836 | RR → AA: Abolishes RNase activity. 1 Publication | 2 | |
Mutagenesisi | 914 | R → M: Impairs RNase activity. 1 Publication | 1 | |
Mutagenesisi | 923 | R → A: Abolishes RNase activity; when associated with A-927. 1 Publication | 1 | |
Mutagenesisi | 927 | Y → A: Abolishes RNase activity; when associated with A-923. 1 Publication | 1 | |
Mutagenesisi | 938 – 940 | RKK → QQQ: Abolishes RNase activity. 1 Publication | 3 | |
Mutagenesisi | 993 | E → A or Q: No effect on pri-miRNA processing activity. 1 Publication | 1 | |
Mutagenesisi | 1045 | E → Q: Impairs pri-miRNA processing activity. Abolishes cleavage of the 3' strand. Abolishes enzyme activity; when associated with Q-1222. 2 Publications | 1 | |
Mutagenesisi | 1077 | V → E: Loss of one DGCR8 interaction site; no effect on the second DGCR8 interaction site. 1 Publication | 1 | |
Mutagenesisi | 1171 | E → A or Q: No effect on pri-miRNA processing activity. 1 Publication | 1 | |
Mutagenesisi | 1194 | L → R: Abolishes interaction with DGCR8. 1 Publication | 1 | |
Mutagenesisi | 1222 | E → Q: Impairs pri-miRNA processing activity. Abolishes cleavage of the 5' strand. Abolishes enzyme activity; when associated with Q-1045. 2 Publications | 1 | |
Mutagenesisi | 1243 | V → D: Abolishes interaction with DGCR8. 1 Publication | 1 |
Organism-specific databases
DisGeNETi | 29102 |
OpenTargetsi | ENSG00000113360 |
PharmGKBi | PA142671060 |
Miscellaneous databases
Pharosi | Q9NRR4, Tbio |
Genetic variation databases
BioMutai | DROSHA |
DMDMi | 20139357 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000180468 | 1 – 1374 | Ribonuclease 3Add BLAST | 1374 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 355 | PhosphoserineCombined sources | 1 | |
Modified residuei | 373 | PhosphoserineCombined sources | 1 |
Keywords - PTMi
PhosphoproteinProteomic databases
EPDi | Q9NRR4 |
jPOSTi | Q9NRR4 |
MassIVEi | Q9NRR4 |
MaxQBi | Q9NRR4 |
PaxDbi | Q9NRR4 |
PeptideAtlasi | Q9NRR4 |
PRIDEi | Q9NRR4 |
ProteomicsDBi | 16990 82409 [Q9NRR4-1] 82410 [Q9NRR4-2] 82411 [Q9NRR4-3] |
PTM databases
iPTMneti | Q9NRR4 |
PhosphoSitePlusi | Q9NRR4 |
Expressioni
Tissue specificityi
Gene expression databases
Bgeei | ENSG00000113360, Expressed in ventricular zone and 231 other tissues |
ExpressionAtlasi | Q9NRR4, baseline and differential |
Genevisiblei | Q9NRR4, HS |
Organism-specific databases
HPAi | ENSG00000113360, Low tissue specificity |
Interactioni
Subunit structurei
Component of the microprocessor complex, or pri-miRNA processing protein complex, which is composed of DROSHA and DGCR8 (PubMed:15589161, PubMed:15574589, PubMed:15531877, PubMed:16751099, PubMed:26027739, PubMed:26748718). The microprocessor complex is a heterotrimer; each of the two DROSHA RNase III domains binds one DGCR8 (via C-terminal region) (PubMed:26027739, PubMed:26748718).
Interacts with SP1 and SNIP1 (PubMed:10976766, PubMed:18632581).
Interacts with SRRT/ARS2 (By similarity).
Interacts with CPSF3 and ISY1; this interaction is in an RNA dependent manner (By similarity).
Interacts with PUS10; interaction promotes pri-miRNAs processing (PubMed:31819270).
By similarity9 PublicationsBinary interactionsi
Q9NRR4
With | #Exp. | IntAct |
---|---|---|
DDX5 [P17844] | 6 | EBI-528367,EBI-351962 |
DGCR8 [Q8WYQ5] | 13 | EBI-528367,EBI-528411 |
FUS [P35637] | 2 | EBI-528367,EBI-400434 |
SMAD1 [Q15797] | 3 | EBI-528367,EBI-1567153 |
TP53 [P04637] | 5 | EBI-528367,EBI-366083 |
GO - Molecular functioni
- DEAD/H-box RNA helicase binding Source: BHF-UCL
- protein homodimerization activity Source: BHF-UCL
- R-SMAD binding Source: BHF-UCL
- SMAD binding Source: BHF-UCL
Protein-protein interaction databases
BioGRIDi | 118870, 67 interactors |
ComplexPortali | CPX-3080, Microprocessor complex |
CORUMi | Q9NRR4 |
DIPi | DIP-33300N |
IntActi | Q9NRR4, 35 interactors |
MINTi | Q9NRR4 |
STRINGi | 9606.ENSP00000425979 |
Miscellaneous databases
RNActi | Q9NRR4, protein |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | Q9NRR4 |
BMRBi | Q9NRR4 |
SMRi | Q9NRR4 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q9NRR4 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 876 – 1056 | RNase III 1Add BLAST | 181 | |
Domaini | 1107 – 1233 | RNase III 2Add BLAST | 127 | |
Domaini | 1260 – 1334 | DRBMAdd BLAST | 75 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 95 | DisorderedSequence analysisAdd BLAST | 95 | |
Regioni | 130 – 406 | DisorderedSequence analysisAdd BLAST | 277 | |
Regioni | 390 – 1365 | Necessary for interaction with DGCR8 and pri-miRNA processing activity2 PublicationsAdd BLAST | 976 | |
Regioni | 452 – 497 | DisorderedSequence analysisAdd BLAST | 46 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 69 – 95 | Pro residuesSequence analysisAdd BLAST | 27 | |
Compositional biasi | 130 – 164 | Pro residuesSequence analysisAdd BLAST | 35 | |
Compositional biasi | 177 – 204 | Polar residuesSequence analysisAdd BLAST | 28 | |
Compositional biasi | 217 – 315 | Basic and acidic residuesSequence analysisAdd BLAST | 99 | |
Compositional biasi | 353 – 395 | Basic and acidic residuesSequence analysisAdd BLAST | 43 | |
Compositional biasi | 452 – 478 | Basic and acidic residuesSequence analysisAdd BLAST | 27 | |
Compositional biasi | 479 – 493 | Acidic residuesSequence analysisAdd BLAST | 15 |
Domaini
Sequence similaritiesi
Keywords - Domaini
RepeatPhylogenomic databases
eggNOGi | KOG1817, Eukaryota |
GeneTreei | ENSGT00730000111052 |
HOGENOMi | CLU_004383_0_0_1 |
InParanoidi | Q9NRR4 |
OMAi | CSNFCEK |
OrthoDBi | 935825at2759 |
PhylomeDBi | Q9NRR4 |
TreeFami | TF314734 |
Family and domain databases
CDDi | cd19877, DSRM_RNAse_III_meta_like, 1 hit cd00593, RIBOc, 2 hits |
DisProti | DP02463 |
Gene3Di | 1.10.1520.10, 2 hits |
HAMAPi | MF_00104, RNase_III, 1 hit |
InterProi | View protein in InterPro IPR014720, dsRBD_dom IPR011907, RNase_III IPR000999, RNase_III_dom IPR044442, RNAse_III_DSRM__animal IPR036389, RNase_III_sf |
PANTHERi | PTHR11207, PTHR11207, 1 hit |
Pfami | View protein in Pfam PF00035, dsrm, 1 hit PF14622, Ribonucleas_3_3, 1 hit PF00636, Ribonuclease_3, 1 hit |
SMARTi | View protein in SMART SM00358, DSRM, 1 hit SM00535, RIBOc, 2 hits |
SUPFAMi | SSF69065, SSF69065, 2 hits |
PROSITEi | View protein in PROSITE PS50137, DS_RBD, 1 hit PS00517, RNASE_3_1, 2 hits PS50142, RNASE_3_2, 2 hits |
s (4+)i Sequence
Sequence statusi: Complete.
This entry describes 4 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 4 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MMQGNTCHRM SFHPGRGCPR GRGGHGARPS APSFRPQNLR LLHPQQPPVQ
60 70 80 90 100
YQYEPPSAPS TTFSNSPAPN FLPPRPDFVP FPPPMPPSAQ GPLPPCPIRP
110 120 130 140 150
PFPNHQMRHP FPVPPCFPPM PPPMPCPNNP PVPGAPPGQG TFPFMMPPPS
160 170 180 190 200
MPHPPPPPVM PQQVNYQYPP GYSHHNFPPP SFNSFQNNPS SFLPSANNSS
210 220 230 240 250
SPHFRHLPPY PLPKAPSERR SPERLKHYDD HRHRDHSHGR GERHRSLDRR
260 270 280 290 300
ERGRSPDRRR QDSRYRSDYD RGRTPSRHRS YERSRERERE RHRHRDNRRS
310 320 330 340 350
PSLERSYKKE YKRSGRSYGL SVVPEPAGCT PELPGEIIKN TDSWAPPLEI
360 370 380 390 400
VNHRSPSREK KRARWEEEKD RWSDNQSSGK DKNYTSIKEK EPEETMPDKN
410 420 430 440 450
EEEEEELLKP VWIRCTHSEN YYSSDPMDQV GDSTVVGTSR LRDLYDKFEE
460 470 480 490 500
ELGSRQEKAK AARPPWEPPK TKLDEDLESS SESECESDED STCSSSSDSE
510 520 530 540 550
VFDVIAEIKR KKAHPDRLHD ELWYNDPGQM NDGPLCKCSA KARRTGIRHS
560 570 580 590 600
IYPGEEAIKP CRPMTNNAGR LFHYRITVSP PTNFLTDRPT VIEYDDHEYI
610 620 630 640 650
FEGFSMFAHA PLTNIPLCKV IRFNIDYTIH FIEEMMPENF CVKGLELFSL
660 670 680 690 700
FLFRDILELY DWNLKGPLFE DSPPCCPRFH FMPRFVRFLP DGGKEVLSMH
710 720 730 740 750
QILLYLLRCS KALVPEEEIA NMLQWEELEW QKYAEECKGM IVTNPGTKPS
760 770 780 790 800
SVRIDQLDRE QFNPDVITFP IIVHFGIRPA QLSYAGDPQY QKLWKSYVKL
810 820 830 840 850
RHLLANSPKV KQTDKQKLAQ REEALQKIRQ KNTMRREVTV ELSSQGFWKT
860 870 880 890 900
GIRSDVCQHA MMLPVLTHHI RYHQCLMHLD KLIGYTFQDR CLLQLAMTHP
910 920 930 940 950
SHHLNFGMNP DHARNSLSNC GIRQPKYGDR KVHHMHMRKK GINTLINIMS
960 970 980 990 1000
RLGQDDPTPS RINHNERLEF LGDAVVEFLT SVHLYYLFPS LEEGGLATYR
1010 1020 1030 1040 1050
TAIVQNQHLA MLAKKLELDR FMLYAHGPDL CRESDLRHAM ANCFEALIGA
1060 1070 1080 1090 1100
VYLEGSLEEA KQLFGRLLFN DPDLREVWLN YPLHPLQLQE PNTDRQLIET
1110 1120 1130 1140 1150
SPVLQKLTEF EEAIGVIFTH VRLLARAFTL RTVGFNHLTL GHNQRMEFLG
1160 1170 1180 1190 1200
DSIMQLVATE YLFIHFPDHH EGHLTLLRSS LVNNRTQAKV AEELGMQEYA
1210 1220 1230 1240 1250
ITNDKTKRPV ALRTKTLADL LESFIAALYI DKDLEYVHTF MNVCFFPRLK
1260 1270 1280 1290 1300
EFILNQDWND PKSQLQQCCL TLRTEGKEPD IPLYKTLQTV GPSHARTYTV
1310 1320 1330 1340 1350
AVYFKGERIG CGKGPSIQQA EMGAAMDALE KYNFPQMAHQ KRFIERKYRQ
1360 1370
ELKEMRWERE HQEREPDETE DIKK
Computationally mapped potential isoform sequencesi
There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketH7C5U6 | H7C5U6_HUMAN | Ribonuclease 3 | DROSHA | 375 | Annotation score: | ||
H0YB67 | H0YB67_HUMAN | Ribonuclease 3 | DROSHA | 195 | Annotation score: | ||
E5RHD1 | E5RHD1_HUMAN | Ribonuclease 3 | DROSHA | 201 | Annotation score: |
Sequence cautioni
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 166 – 174 | YQYPPGYSH → RERERTSLE in CAB45133 (PubMed:10976766).Curated | 9 | |
Sequence conflicti | 612 | L → P in CAB45133 (PubMed:10976766).Curated | 1 | |
Sequence conflicti | 1020 | R → P in AAF80558 (PubMed:10948199).Curated | 1 | |
Sequence conflicti | 1230 | I → T in AAF80558 (PubMed:10948199).Curated | 1 | |
Sequence conflicti | 1272 | L → R in BX647724 (PubMed:17974005).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_051866 | 67 | P → T. Corresponds to variant dbSNP:rs35342496EnsemblClinVar. | 1 | |
Natural variantiVAR_061778 | 321 | S → L. Corresponds to variant dbSNP:rs55656741Ensembl. | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_005777 | 285 – 353 | RERER…EIVNH → S in isoform 2. 1 PublicationAdd BLAST | 69 | |
Alternative sequenceiVSP_012450 | 316 – 352 | Missing in isoform 3 and isoform 4. 2 PublicationsAdd BLAST | 37 | |
Alternative sequenceiVSP_012451 | 353 | H → S in isoform 3 and isoform 4. 2 Publications | 1 | |
Alternative sequenceiVSP_012452 | 1198 – 1229 | EYAIT…IAALY → VWSIYLLSNCDCCLLRPSLV FLQTMNEVCSLK in isoform 3. 1 PublicationAdd BLAST | 32 | |
Alternative sequenceiVSP_012453 | 1230 – 1374 | Missing in isoform 3. 1 PublicationAdd BLAST | 145 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF189011 mRNA Translation: AAF80558.1 BX647724 mRNA No translation available. AC008768 Genomic DNA No translation available. AC022417 Genomic DNA No translation available. AC106802 Genomic DNA No translation available. AJ242976 mRNA Translation: CAB45133.1 AK001121 mRNA Translation: BAA91511.1 Different initiation. BC041162 mRNA Translation: AAH41162.1 BC054003 mRNA Translation: AAH54003.1 AF116910 mRNA Translation: AAD29637.1 Frameshift. |
CCDSi | CCDS47194.1 [Q9NRR4-4] CCDS47195.1 [Q9NRR4-1] |
RefSeqi | NP_001093882.1, NM_001100412.1 [Q9NRR4-4] NP_037367.3, NM_013235.4 [Q9NRR4-1] XP_005248348.1, XM_005248291.3 XP_005248351.1, XM_005248294.3 [Q9NRR4-2] |
Genome annotation databases
Ensembli | ENST00000344624.8; ENSP00000339845.3; ENSG00000113360.17 ENST00000511367.6; ENSP00000425979.2; ENSG00000113360.17 ENST00000513349.5; ENSP00000424161.1; ENSG00000113360.17 [Q9NRR4-4] |
GeneIDi | 29102 |
KEGGi | hsa:29102 |
MANE-Selecti | ENST00000344624.8; ENSP00000339845.3; NM_001382508.1; NP_001369437.1 |
UCSCi | uc003jhg.3, human [Q9NRR4-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Web resourcesi
Protein Spotlight The dark side of RNA - Issue 87 of October 2007 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF189011 mRNA Translation: AAF80558.1 BX647724 mRNA No translation available. AC008768 Genomic DNA No translation available. AC022417 Genomic DNA No translation available. AC106802 Genomic DNA No translation available. AJ242976 mRNA Translation: CAB45133.1 AK001121 mRNA Translation: BAA91511.1 Different initiation. BC041162 mRNA Translation: AAH41162.1 BC054003 mRNA Translation: AAH54003.1 AF116910 mRNA Translation: AAD29637.1 Frameshift. |
CCDSi | CCDS47194.1 [Q9NRR4-4] CCDS47195.1 [Q9NRR4-1] |
RefSeqi | NP_001093882.1, NM_001100412.1 [Q9NRR4-4] NP_037367.3, NM_013235.4 [Q9NRR4-1] XP_005248348.1, XM_005248291.3 XP_005248351.1, XM_005248294.3 [Q9NRR4-2] |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2KHX | NMR | - | A | 1259-1337 | [»] | |
2NA2 | NMR | - | A | 1259-1337 | [»] | |
5B16 | X-ray | 3.20 | A | 411-458 | [»] | |
A | 522-711 | [»] | ||||
A | 850-1365 | [»] | ||||
6LXD | electron microscopy | 3.90 | A | 391-1374 | [»] | |
6LXE | electron microscopy | 4.20 | A | 391-1374 | [»] | |
6V5B | electron microscopy | 3.70 | A | 353-1365 | [»] | |
6V5C | electron microscopy | 4.40 | A | 353-1365 | [»] | |
AlphaFoldDBi | Q9NRR4 | |||||
BMRBi | Q9NRR4 | |||||
SMRi | Q9NRR4 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 118870, 67 interactors |
ComplexPortali | CPX-3080, Microprocessor complex |
CORUMi | Q9NRR4 |
DIPi | DIP-33300N |
IntActi | Q9NRR4, 35 interactors |
MINTi | Q9NRR4 |
STRINGi | 9606.ENSP00000425979 |
PTM databases
iPTMneti | Q9NRR4 |
PhosphoSitePlusi | Q9NRR4 |
Genetic variation databases
BioMutai | DROSHA |
DMDMi | 20139357 |
Proteomic databases
EPDi | Q9NRR4 |
jPOSTi | Q9NRR4 |
MassIVEi | Q9NRR4 |
MaxQBi | Q9NRR4 |
PaxDbi | Q9NRR4 |
PeptideAtlasi | Q9NRR4 |
PRIDEi | Q9NRR4 |
ProteomicsDBi | 16990 82409 [Q9NRR4-1] 82410 [Q9NRR4-2] 82411 [Q9NRR4-3] |
Protocols and materials databases
Antibodypediai | 22652, 283 antibodies from 37 providers |
DNASUi | 29102 |
Genome annotation databases
Ensembli | ENST00000344624.8; ENSP00000339845.3; ENSG00000113360.17 ENST00000511367.6; ENSP00000425979.2; ENSG00000113360.17 ENST00000513349.5; ENSP00000424161.1; ENSG00000113360.17 [Q9NRR4-4] |
GeneIDi | 29102 |
KEGGi | hsa:29102 |
MANE-Selecti | ENST00000344624.8; ENSP00000339845.3; NM_001382508.1; NP_001369437.1 |
UCSCi | uc003jhg.3, human [Q9NRR4-1] |
Organism-specific databases
CTDi | 29102 |
DisGeNETi | 29102 |
GeneCardsi | DROSHA |
HGNCi | HGNC:17904, DROSHA |
HPAi | ENSG00000113360, Low tissue specificity |
MIMi | 608828, gene |
neXtProti | NX_Q9NRR4 |
OpenTargetsi | ENSG00000113360 |
PharmGKBi | PA142671060 |
VEuPathDBi | HostDB:ENSG00000113360 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG1817, Eukaryota |
GeneTreei | ENSGT00730000111052 |
HOGENOMi | CLU_004383_0_0_1 |
InParanoidi | Q9NRR4 |
OMAi | CSNFCEK |
OrthoDBi | 935825at2759 |
PhylomeDBi | Q9NRR4 |
TreeFami | TF314734 |
Enzyme and pathway databases
BRENDAi | 3.1.26.3, 2681 |
PathwayCommonsi | Q9NRR4 |
Reactomei | R-HSA-203927, MicroRNA (miRNA) biogenesis |
SignaLinki | Q9NRR4 |
SIGNORi | Q9NRR4 |
Miscellaneous databases
BioGRID-ORCSi | 29102, 303 hits in 1081 CRISPR screens |
ChiTaRSi | DROSHA, human |
EvolutionaryTracei | Q9NRR4 |
GeneWikii | RNASEN |
GenomeRNAii | 29102 |
Pharosi | Q9NRR4, Tbio |
PROi | PR:Q9NRR4 |
RNActi | Q9NRR4, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000113360, Expressed in ventricular zone and 231 other tissues |
ExpressionAtlasi | Q9NRR4, baseline and differential |
Genevisiblei | Q9NRR4, HS |
Family and domain databases
CDDi | cd19877, DSRM_RNAse_III_meta_like, 1 hit cd00593, RIBOc, 2 hits |
DisProti | DP02463 |
Gene3Di | 1.10.1520.10, 2 hits |
HAMAPi | MF_00104, RNase_III, 1 hit |
InterProi | View protein in InterPro IPR014720, dsRBD_dom IPR011907, RNase_III IPR000999, RNase_III_dom IPR044442, RNAse_III_DSRM__animal IPR036389, RNase_III_sf |
PANTHERi | PTHR11207, PTHR11207, 1 hit |
Pfami | View protein in Pfam PF00035, dsrm, 1 hit PF14622, Ribonucleas_3_3, 1 hit PF00636, Ribonuclease_3, 1 hit |
SMARTi | View protein in SMART SM00358, DSRM, 1 hit SM00535, RIBOc, 2 hits |
SUPFAMi | SSF69065, SSF69065, 2 hits |
PROSITEi | View protein in PROSITE PS50137, DS_RBD, 1 hit PS00517, RNASE_3_1, 2 hits PS50142, RNASE_3_2, 2 hits |
MobiDBi | Search... |
Entry informationi
Entry namei | RNC_HUMAN | |
Accessioni | Q9NRR4Primary (citable) accession number: Q9NRR4 Secondary accession number(s): E7EMP9 Q9Y4Y0 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | January 23, 2002 |
Last sequence update: | January 23, 2002 | |
Last modified: | May 25, 2022 | |
This is version 192 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- Human chromosome 5
Human chromosome 5: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families - Protein Spotlight
Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries