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 Publications

Catalytic activityⁱ

Endonucleolytic cleavage to 5'-phosphomonoester.
4 Publications
Manual assertion based on experiment inⁱ
- Ref.10
  "The Drosha-DGCR8 complex in primary microRNA processing."
  Han J., Lee Y., Yeom K.-H., Kim Y.-K., Jin H., Kim V.N.
  Genes Dev. 18:3016-3027(2004) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, IDENTIFICATION IN THE MICROPROCESSOR COMPLEX, INTERACTION WITH DGCR8, CATALYTIC ACTIVITY, COFACTOR, DOMAIN, MUTAGENESIS OF GLU-993; GLU-1045; GLU-1171 AND GLU-1222.
- Ref.12
  "Recognition and cleavage of primary microRNA precursors by the nuclear processing enzyme Drosha."
  Zeng Y., Yi R., Cullen B.R.
  EMBO J. 24:138-148(2005) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY.
- Ref.21
  "Functional anatomy of the human microprocessor."
  Nguyen T.A., Jo M.H., Choi Y.G., Park J., Kwon S.C., Hohng S., Kim V.N., Woo J.S.
  Cell 161:1374-1387(2015) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, SUBUNIT, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-1045 AND GLU-1222.
- Ref.23
  "Structure of human DROSHA."
  Kwon S.C., Nguyen T.A., Choi Y.G., Jo M.H., Hohng S., Kim V.N., Woo J.S.
  Cell 164:81-90(2016) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 411-1365 OF MUTANT GLN-1045/GLN-1222 IN COMPLEX WITH DGCR8 AND ZINC IONS, FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH DGCR8, SUBUNIT, MUTAGENESIS OF CYS-536; CYS-538; CYS-561; 622-ARG-PHE-623; CYS-676; 835-ARG-ARG-836; ARG-914; ARG-923; TYR-927; 938-ARG--LYS-940; VAL-1077; LEU-1194 AND VAL-1243, REGION.
EC:3.1.26.3

Cofactorⁱ

Mg²⁺1 Publication, Mn²⁺1 PublicationNote: Each RNase III domain binds at least one Mg²⁺ or Mn²⁺ ion.Curated

Sites

Feature key	Position(s)	DescriptionActions	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 or manganese 1By similarity	1
Metal bindingⁱ	1026	Zinc 11 Publication	1
Metal bindingⁱ	1042	Magnesium or manganese 1By similarity	1
Metal bindingⁱ	1045	Magnesium or manganese 1By similarity1 Publication	1
Metal bindingⁱ	1147	Magnesium or manganese 2By similarity	1
Siteⁱ	1215	Important for activityBy similarity	1
Metal bindingⁱ	1219	Magnesium or manganese 2By similarity	1
Metal bindingⁱ	1222	Magnesium or manganese 2By similarity1 Publication	1

GO - Molecular functionⁱ

DEAD/H-box RNA helicase binding
Source: BHF-UCL
Inferred from physical interactionⁱ
- 18548003
double-stranded RNA binding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
lipopolysaccharide binding
Source: UniProtKB
Inferred from direct assayⁱ
- 20180804
metal ion binding Source: UniProtKB-KW
primary miRNA binding
Source: BHF-UCL
Inferred from physical interactionⁱ
- 18548003
protein homodimerization activity
Source: BHF-UCL
Inferred from direct assayⁱ
- 15574589
ribonuclease III activity
Source: WormBase
Inferred from direct assayⁱ
- 14508493
RNA binding
Source: UniProtKB
Inferred from high throughput direct assayⁱ
- 22658674
- 22681889
R-SMAD binding
Source: BHF-UCL
Inferred from physical interactionⁱ
- 18548003
SMAD binding
Source: BHF-UCL
Inferred from physical interactionⁱ
- 18548003

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

defense response to Gram-negative bacterium
Source: UniProtKB
Inferred from direct assayⁱ
- 20180804
defense response to Gram-positive bacterium
Source: UniProtKB
Inferred from direct assayⁱ
- 20180804
miRNA metabolic process Source: Ensembl
positive regulation of gene expression Source: Ensembl
pre-miRNA processing
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
primary miRNA processing
Source: WormBase
Inferred from direct assayⁱ
- 14508493
production of siRNA involved in RNA interference
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
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
Inferred from biological aspect of ancestorⁱ
- 21873635
rRNA catabolic process Source: InterPro

View the complete GO annotation on QuickGO ...

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
Reactomeⁱ	R-HSA-203927 MicroRNA (miRNA) biogenesis

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	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 5

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000113360.16
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:17904 DROSHA
MIMⁱ	608828 gene
neXtProtⁱ	NX_Q9NRR4

Keywords - Cellular componentⁱ

Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	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

DisGeNET More...DisGeNETⁱ	29102
Open Targets More...OpenTargetsⁱ	ENSG00000113360
PharmGKBⁱ	PA142671060

Polymorphism and mutation 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

Phosphoprotein

Proteomic databases

EPDⁱ	Q9NRR4
jPOSTⁱ	Q9NRR4
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q9NRR4
PaxDbⁱ	Q9NRR4
PeptideAtlas More...PeptideAtlasⁱ	Q9NRR4
PRIDEⁱ	Q9NRR4
ProteomicsDBⁱ	82409 82410 [Q9NRR4-2] 82411 [Q9NRR4-3]

PTM databases

iPTMnetⁱ	Q9NRR4
PhosphoSitePlusⁱ	Q9NRR4

Expressionⁱ

Tissue specificityⁱ

Ubiquitous.1 Publication

Gene expression databases

Bgeeⁱ	ENSG00000113360 Expressed in 221 organ(s), highest expression level in endothelial cell
ExpressionAtlasⁱ	Q9NRR4 baseline and differential
Genevisibleⁱ	Q9NRR4 HS

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).By similarity8 Publications

Binary interactionsⁱ

With	Entry	#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
Inferred from physical interactionⁱ
- 18548003
protein homodimerization activity
Source: BHF-UCL
Inferred from direct assayⁱ
- 15574589
R-SMAD binding
Source: BHF-UCL
Inferred from physical interactionⁱ
- 18548003
SMAD binding
Source: BHF-UCL
Inferred from physical interactionⁱ
- 18548003

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	118870, 44 interactors
ComplexPortalⁱ	CPX-3080 Microprocessor complex
CORUMⁱ	Q9NRR4
Database of interacting proteins More...DIPⁱ	DIP-33300N
IntActⁱ	Q9NRR4, 31 interactors
Molecular INTeraction database More...MINTⁱ	Q9NRR4
STRINGⁱ	9606.ENSP00000339845

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	413 – 415	Combined sources	3
Beta strandⁱ	420 – 423	Combined sources	4
Helixⁱ	441 – 451	Combined sources	11
Turnⁱ	455 – 457	Combined sources	3
Helixⁱ	506 – 510	Combined sources	5
Beta strandⁱ	531 – 535	Combined sources	5
Turnⁱ	547 – 550	Combined sources	4
Beta strandⁱ	563 – 565	Combined sources	3
Turnⁱ	568 – 570	Combined sources	3
Beta strandⁱ	572 – 580	Combined sources	9
Beta strandⁱ	582 – 584	Combined sources	3
Beta strandⁱ	591 – 593	Combined sources	3
Beta strandⁱ	595 – 610	Combined sources	16
Beta strandⁱ	618 – 632	Combined sources	15
Helixⁱ	642 – 652	Combined sources	11
Turnⁱ	653 – 656	Combined sources	4
Beta strandⁱ	678 – 686	Combined sources	9
Beta strandⁱ	694 – 696	Combined sources	3
Helixⁱ	699 – 708	Combined sources	10
Beta strandⁱ	737 – 743	Combined sources	7
Beta strandⁱ	751 – 754	Combined sources	4
Helixⁱ	856 – 860	Combined sources	5
Helixⁱ	863 – 875	Combined sources	13
Helixⁱ	876 – 878	Combined sources	3
Helixⁱ	880 – 883	Combined sources	4
Helixⁱ	890 – 897	Combined sources	8
Helixⁱ	910 – 919	Combined sources	10
Helixⁱ	966 – 986	Combined sources	21
Helixⁱ	993 – 1004	Combined sources	12
Helixⁱ	1006 – 1013	Combined sources	8
Helixⁱ	1014 – 1016	Combined sources	3
Helixⁱ	1018 – 1021	Combined sources	4
Helixⁱ	1033 – 1054	Combined sources	22
Helixⁱ	1057 – 1068	Combined sources	12
Helixⁱ	1072 – 1079	Combined sources	8
Helixⁱ	1085 – 1088	Combined sources	4
Helixⁱ	1095 – 1098	Combined sources	4
Helixⁱ	1104 – 1114	Combined sources	11
Helixⁱ	1121 – 1127	Combined sources	7
Helixⁱ	1144 – 1164	Combined sources	21
Helixⁱ	1171 – 1181	Combined sources	11
Helixⁱ	1184 – 1194	Combined sources	11
Beta strandⁱ	1203 – 1205	Combined sources	3
Helixⁱ	1214 – 1231	Combined sources	18
Helixⁱ	1234 – 1244	Combined sources	11
Helixⁱ	1246 – 1248	Combined sources	3
Helixⁱ	1249 – 1254	Combined sources	6
Helixⁱ	1261 – 1269	Combined sources	9
Beta strandⁱ	1275 – 1277	Combined sources	3
Beta strandⁱ	1283 – 1291	Combined sources	9
Beta strandⁱ	1292 – 1294	Combined sources	3
Beta strandⁱ	1297 – 1304	Combined sources	8
Beta strandⁱ	1307 – 1316	Combined sources	10
Helixⁱ	1317 – 1330	Combined sources	14

Show more details

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...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	[»]
ProteinModelPortalⁱ	Q9NRR4
SMRⁱ	Q9NRR4
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	Q9NRR4

EvolutionaryTraceⁱ

Q9NRR4

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	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	390 – 1365	Necessary for interaction with DGCR8 and pri-miRNA processing activity2 PublicationsAdd BLAST		976

Compositional bias

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Compositional biasⁱ	1 – 212	Pro-richAdd BLAST		212
Compositional biasⁱ	219 – 316	Arg-richAdd BLAST		98

Domainⁱ

The 2 RNase III domains form an intramolecular dimer where the domain 1 cuts the 3'strand while the domain 2 cleaves the 5'strand of pri-miRNAs, independently of each other.1 Publication

Sequence similaritiesⁱ

Belongs to the ribonuclease III family.Curated

Keywords - Domainⁱ

Repeat

Phylogenomic databases

eggNOGⁱ	KOG1817 Eukaryota COG0571 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00730000111052
HOGENOMⁱ	HOG000122291
HOVERGENⁱ	HBG023130
InParanoidⁱ	Q9NRR4
KEGG Orthology (KO) More...KOⁱ	K03685
OMAⁱ	EYLYRHF
Database of Orthologous Groups More...OrthoDBⁱ	935825at2759
PhylomeDBⁱ	Q9NRR4
TreeFamⁱ	TF314734

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00048 DSRM, 1 hit cd00593 RIBOc, 2 hits
Gene3Dⁱ	1.10.1520.10, 1 hit
HAMAPⁱ	MF_00104 RNase_III, 1 hit
InterProⁱ	View protein in InterPro IPR014720 dsRBD_dom IPR011907 RNase_III IPR000999 RNase_III_dom IPR036389 RNase_III_sf
Pfam protein domain database More...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

Sequences (4+)ⁱ

Sequence statusⁱ: Complete.

This entry describes 4 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 4 described isoforms and 3 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: Q9NRR4-1) [UniParc]FASTA Add to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        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

Length:1,374

Mass (Da):159,316

Last modified:January 23, 2002 - v2

Checksum:ⁱED6FDEA09F3B8092

GO

Isoform 2 (identifier: Q9NRR4-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
285-353: RERERERHRHRDNRRSPSLERSYKKEYKRSGRSYGLSVVPEPAGCTPELPGEIIKNTDSWAPPLEIVNH → S

« Hide

        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 YERSSRSPSR EKKRARWEEE 
       310        320        330        340        350
KDRWSDNQSS GKDKNYTSIK EKEPEETMPD KNEEEEEELL KPVWIRCTHS 
       360        370        380        390        400
ENYYSSDPMD QVGDSTVVGT SRLRDLYDKF EEELGSRQEK AKAARPPWEP 
       410        420        430        440        450
PKTKLDEDLE SSSESECESD EDSTCSSSSD SEVFDVIAEI KRKKAHPDRL 
       460        470        480        490        500
HDELWYNDPG QMNDGPLCKC SAKARRTGIR HSIYPGEEAI KPCRPMTNNA 
       510        520        530        540        550
GRLFHYRITV SPPTNFLTDR PTVIEYDDHE YIFEGFSMFA HAPLTNIPLC 
       560        570        580        590        600
KVIRFNIDYT IHFIEEMMPE NFCVKGLELF SLFLFRDILE LYDWNLKGPL 
       610        620        630        640        650
FEDSPPCCPR FHFMPRFVRF LPDGGKEVLS MHQILLYLLR CSKALVPEEE 
       660        670        680        690        700
IANMLQWEEL EWQKYAEECK GMIVTNPGTK PSSVRIDQLD REQFNPDVIT 
       710        720        730        740        750
FPIIVHFGIR PAQLSYAGDP QYQKLWKSYV KLRHLLANSP KVKQTDKQKL 
       760        770        780        790        800
AQREEALQKI RQKNTMRREV TVELSSQGFW KTGIRSDVCQ HAMMLPVLTH 
       810        820        830        840        850
HIRYHQCLMH LDKLIGYTFQ DRCLLQLAMT HPSHHLNFGM NPDHARNSLS 
       860        870        880        890        900
NCGIRQPKYG DRKVHHMHMR KKGINTLINI MSRLGQDDPT PSRINHNERL 
       910        920        930        940        950
EFLGDAVVEF LTSVHLYYLF PSLEEGGLAT YRTAIVQNQH LAMLAKKLEL 
       960        970        980        990       1000
DRFMLYAHGP DLCRESDLRH AMANCFEALI GAVYLEGSLE EAKQLFGRLL 
      1010       1020       1030       1040       1050
FNDPDLREVW LNYPLHPLQL QEPNTDRQLI ETSPVLQKLT EFEEAIGVIF 
      1060       1070       1080       1090       1100
THVRLLARAF TLRTVGFNHL TLGHNQRMEF LGDSIMQLVA TEYLFIHFPD 
      1110       1120       1130       1140       1150
HHEGHLTLLR SSLVNNRTQA KVAEELGMQE YAITNDKTKR PVALRTKTLA 
      1160       1170       1180       1190       1200
DLLESFIAAL YIDKDLEYVH TFMNVCFFPR LKEFILNQDW NDPKSQLQQC 
      1210       1220       1230       1240       1250
CLTLRTEGKE PDIPLYKTLQ TVGPSHARTY TVAVYFKGER IGCGKGPSIQ 
      1260       1270       1280       1290       1300
QAEMGAAMDA LEKYNFPQMA HQKRFIERKY RQELKEMRWE REHQEREPDE 

TEDIKK

Note: No experimental confirmation available.

Show »

Length:1,306

Mass (Da):151,296

Checksum:ⁱE2A0A46BE0E0A692

GO

Isoform 3 (identifier: Q9NRR4-3) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
     316-352: Missing.
     353-353: H → S
     1198-1229: EYAITNDKTKRPVALRTKTLADLLESFIAALY → VWSIYLLSNCDCCLLRPSLVFLQTMNEVCSLK
     1230-1374: Missing.

« Hide

        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 YKRSGSRSPS REKKRARWEE EKDRWSDNQS SGKDKNYTSI 
       360        370        380        390        400
KEKEPEETMP DKNEEEEEEL LKPVWIRCTH SENYYSSDPM DQVGDSTVVG 
       410        420        430        440        450
TSRLRDLYDK FEEELGSRQE KAKAARPPWE PPKTKLDEDL ESSSESECES 
       460        470        480        490        500
DEDSTCSSSS DSEVFDVIAE IKRKKAHPDR LHDELWYNDP GQMNDGPLCK 
       510        520        530        540        550
CSAKARRTGI RHSIYPGEEA IKPCRPMTNN AGRLFHYRIT VSPPTNFLTD 
       560        570        580        590        600
RPTVIEYDDH EYIFEGFSMF AHAPLTNIPL CKVIRFNIDY TIHFIEEMMP 
       610        620        630        640        650
ENFCVKGLEL FSLFLFRDIL ELYDWNLKGP LFEDSPPCCP RFHFMPRFVR 
       660        670        680        690        700
FLPDGGKEVL SMHQILLYLL RCSKALVPEE EIANMLQWEE LEWQKYAEEC 
       710        720        730        740        750
KGMIVTNPGT KPSSVRIDQL DREQFNPDVI TFPIIVHFGI RPAQLSYAGD 
       760        770        780        790        800
PQYQKLWKSY VKLRHLLANS PKVKQTDKQK LAQREEALQK IRQKNTMRRE 
       810        820        830        840        850
VTVELSSQGF WKTGIRSDVC QHAMMLPVLT HHIRYHQCLM HLDKLIGYTF 
       860        870        880        890        900
QDRCLLQLAM THPSHHLNFG MNPDHARNSL SNCGIRQPKY GDRKVHHMHM 
       910        920        930        940        950
RKKGINTLIN IMSRLGQDDP TPSRINHNER LEFLGDAVVE FLTSVHLYYL 
       960        970        980        990       1000
FPSLEEGGLA TYRTAIVQNQ HLAMLAKKLE LDRFMLYAHG PDLCRESDLR 
      1010       1020       1030       1040       1050
HAMANCFEAL IGAVYLEGSL EEAKQLFGRL LFNDPDLREV WLNYPLHPLQ 
      1060       1070       1080       1090       1100
LQEPNTDRQL IETSPVLQKL TEFEEAIGVI FTHVRLLARA FTLRTVGFNH 
      1110       1120       1130       1140       1150
LTLGHNQRME FLGDSIMQLV ATEYLFIHFP DHHEGHLTLL RSSLVNNRTQ 
      1160       1170       1180       1190 
AKVAEELGMQ VWSIYLLSNC DCCLLRPSLV FLQTMNEVCS LK

Note: No experimental confirmation available.

Show »

Length:1,192

Mass (Da):138,157

Checksum:ⁱ18479E41CFD76BAC

GO

Isoform 4 (identifier: Q9NRR4-4) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
316-352: Missing.
353-353: H → S

« Hide

        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 YKRSGSRSPS REKKRARWEE EKDRWSDNQS SGKDKNYTSI 
       360        370        380        390        400
KEKEPEETMP DKNEEEEEEL LKPVWIRCTH SENYYSSDPM DQVGDSTVVG 
       410        420        430        440        450
TSRLRDLYDK FEEELGSRQE KAKAARPPWE PPKTKLDEDL ESSSESECES 
       460        470        480        490        500
DEDSTCSSSS DSEVFDVIAE IKRKKAHPDR LHDELWYNDP GQMNDGPLCK 
       510        520        530        540        550
CSAKARRTGI RHSIYPGEEA IKPCRPMTNN AGRLFHYRIT VSPPTNFLTD 
       560        570        580        590        600
RPTVIEYDDH EYIFEGFSMF AHAPLTNIPL CKVIRFNIDY TIHFIEEMMP 
       610        620        630        640        650
ENFCVKGLEL FSLFLFRDIL ELYDWNLKGP LFEDSPPCCP RFHFMPRFVR 
       660        670        680        690        700
FLPDGGKEVL SMHQILLYLL RCSKALVPEE EIANMLQWEE LEWQKYAEEC 
       710        720        730        740        750
KGMIVTNPGT KPSSVRIDQL DREQFNPDVI TFPIIVHFGI RPAQLSYAGD 
       760        770        780        790        800
PQYQKLWKSY VKLRHLLANS PKVKQTDKQK LAQREEALQK IRQKNTMRRE 
       810        820        830        840        850
VTVELSSQGF WKTGIRSDVC QHAMMLPVLT HHIRYHQCLM HLDKLIGYTF 
       860        870        880        890        900
QDRCLLQLAM THPSHHLNFG MNPDHARNSL SNCGIRQPKY GDRKVHHMHM 
       910        920        930        940        950
RKKGINTLIN IMSRLGQDDP TPSRINHNER LEFLGDAVVE FLTSVHLYYL 
       960        970        980        990       1000
FPSLEEGGLA TYRTAIVQNQ HLAMLAKKLE LDRFMLYAHG PDLCRESDLR 
      1010       1020       1030       1040       1050
HAMANCFEAL IGAVYLEGSL EEAKQLFGRL LFNDPDLREV WLNYPLHPLQ 
      1060       1070       1080       1090       1100
LQEPNTDRQL IETSPVLQKL TEFEEAIGVI FTHVRLLARA FTLRTVGFNH 
      1110       1120       1130       1140       1150
LTLGHNQRME FLGDSIMQLV ATEYLFIHFP DHHEGHLTLL RSSLVNNRTQ 
      1160       1170       1180       1190       1200
AKVAEELGMQ EYAITNDKTK RPVALRTKTL ADLLESFIAA LYIDKDLEYV 
      1210       1220       1230       1240       1250
HTFMNVCFFP RLKEFILNQD WNDPKSQLQQ CCLTLRTEGK EPDIPLYKTL 
      1260       1270       1280       1290       1300
QTVGPSHART YTVAVYFKGE RIGCGKGPSI QQAEMGAAMD ALEKYNFPQM 
      1310       1320       1330 
AHQKRFIERK YRQELKEMRW EREHQEREPD ETEDIKK

Note: No experimental confirmation available.

Show »

Length:1,337

Mass (Da):155,333

Checksum:ⁱ834B12891D1DB08D

GO

Computationally mapped potential isoform sequencesⁱ

There are 3 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

H0YB67	H0YB67_HUMAN	Ribonuclease 3 Ribonuclease 3	DROSHA	195	Annotation score:
H7C5U6	H7C5U6_HUMAN	Ribonuclease 3 Ribonuclease 3	DROSHA	375	Annotation score:
E5RHD1	E5RHD1_HUMAN	Ribonuclease 3 Ribonuclease 3	DROSHA	201	Annotation score:

Sequence cautionⁱ

The sequence AAD29637 differs from that shown. Reason: Frameshift at position 775.Curated

The sequence BAA91511 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature key	Position(s)	DescriptionActions	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:rs35342496Ensembl.		1
Natural variantⁱVAR_061778	321	S → L. Corresponds to variant dbSNP:rs55656741Ensembl.		1

Alternative sequence

Feature key	Position(s)	DescriptionActions	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.
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS47194.1 [Q9NRR4-4] CCDS47195.1 [Q9NRR4-1]
NCBI Reference Sequences More...RefSeqⁱ	NP_001093882.1, NM_001100412.1 [Q9NRR4-4] NP_037367.3, NM_013235.4 [Q9NRR4-1] XP_005248348.1, XM_005248291.3 [Q9NRR4-1] XP_005248351.1, XM_005248294.3 [Q9NRR4-2]
UniGeneⁱ	Hs.97997

Genome annotation databases

Ensemblⁱ	ENST00000344624; ENSP00000339845; ENSG00000113360 [Q9NRR4-1] ENST00000442743; ENSP00000409335; ENSG00000113360 [Q9NRR4-4] ENST00000511367; ENSP00000425979; ENSG00000113360 [Q9NRR4-1] ENST00000513349; ENSP00000424161; ENSG00000113360 [Q9NRR4-4]
GeneIDⁱ	29102
KEGGⁱ	hsa:29102
UCSC genome browser More...UCSCⁱ	uc003jhg.3 human [Q9NRR4-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q9NRR4	Drosha ribonuclease III		GORGO		1374	UniRef100_Q9NRR4
Q9NRR4-2	Drosha ribonuclease III		PANTR		1306	UniRef100_A0A2I3RXI8
DROSHA isoform 18 (Fragment)		PONAB		374
DROSHA isoform 9 (Fragment)		PANTR		374
Q9NRR4-4	DROSHA isoform 2		PANTR		1337	UniRef100_K7DD05
Drosha ribonuclease III		GORGO		1337

Protein	Similar proteins		Species	Score	Length	Source
Q9NRR4	Drosha ribonuclease III		GORGO		1374	UniRef90_Q9NRR4
ribonuclease 3 isoform X1		MESAU		1418
Ribonuclease (Fragment)		BUBBU		194
Drosha ribonuclease III		CALJA		1401
Ribonuclease type III, nuclear (Fragment)		MUSPF		593
+199
Q9NRR4-2	Drosha ribonuclease III		FELCA		1306	UniRef90_M3VUL7
Drosha ribonuclease III		PAPAN		1348
Drosha ribonuclease III		MACFA		1348
Drosha ribonuclease III		MACNE		1348
Drosha ribonuclease III		RHIRO		1331
+25
Q9NRR4-3	Uncharacterized protein		MACMU		195	UniRef90_Q9NRR4-3
UPI0004F20EF8		PAPAN		1382
UPI0003AB9221		MACFA		1376
UPI0004F22D86		PAPAN		1376
UPI0003AB88BB		MACFA		1382
Q9NRR4-4	Drosha ribonuclease III		PIG		1336	UniRef90_F1SP38
Drosha ribonuclease III		PAPAN		1379
Drosha ribonuclease III		ICTTR		541
Drosha ribonuclease III		CHLSB		1379
Drosha ribonuclease III		MACFA		1379
+113

Protein	Similar proteins		Species	Score	Length	Source
Q9NRR4	Drosha ribonuclease III		GORGO		1374	UniRef50_Q9NRR4
ribonuclease 3 isoform X1		MESAU		1418
Ribonuclease (Fragment)		BUBBU		194
Drosha ribonuclease III		CALJA		1401
Ribonuclease type III, nuclear (Fragment)		MUSPF		593
+598
Q9NRR4-3	Uncharacterized protein		MACMU		195	UniRef50_Q9NRR4-3
Uncharacterized protein		ONCMY		1188
Ribonuclease type III, nuclear		ORYLA		1020
Ribonuclease type III, nuclear		LEPOC		1373
Ribonuclease 3		HETGA		1388
+57

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 [Q9NRR4-1] XP_005248351.1, XM_005248294.3 [Q9NRR4-2]
UniGeneⁱ	Hs.97997

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	[»]
ProteinModelPortalⁱ	Q9NRR4
SMRⁱ	Q9NRR4
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	118870, 44 interactors
ComplexPortalⁱ	CPX-3080 Microprocessor complex
CORUMⁱ	Q9NRR4
DIPⁱ	DIP-33300N
IntActⁱ	Q9NRR4, 31 interactors
MINTⁱ	Q9NRR4
STRINGⁱ	9606.ENSP00000339845

PTM databases

iPTMnetⁱ	Q9NRR4
PhosphoSitePlusⁱ	Q9NRR4

Polymorphism and mutation databases

BioMutaⁱ	DROSHA
DMDMⁱ	20139357

Proteomic databases

EPDⁱ	Q9NRR4
jPOSTⁱ	Q9NRR4
MaxQBⁱ	Q9NRR4
PaxDbⁱ	Q9NRR4
PeptideAtlasⁱ	Q9NRR4
PRIDEⁱ	Q9NRR4
ProteomicsDBⁱ	82409 82410 [Q9NRR4-2] 82411 [Q9NRR4-3]

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENST00000344624; ENSP00000339845; ENSG00000113360 [Q9NRR4-1] ENST00000442743; ENSP00000409335; ENSG00000113360 [Q9NRR4-4] ENST00000511367; ENSP00000425979; ENSG00000113360 [Q9NRR4-1] ENST00000513349; ENSP00000424161; ENSG00000113360 [Q9NRR4-4]
GeneIDⁱ	29102
KEGGⁱ	hsa:29102
UCSCⁱ	uc003jhg.3 human [Q9NRR4-1]

Organism-specific databases

CTDⁱ	29102
DisGeNETⁱ	29102
EuPathDBⁱ	HostDB:ENSG00000113360.16
GeneCardsⁱ	DROSHA
H-InvDBⁱ	HIX0004780
HGNCⁱ	HGNC:17904 DROSHA
MIMⁱ	608828 gene
neXtProtⁱ	NX_Q9NRR4
OpenTargetsⁱ	ENSG00000113360
PharmGKBⁱ	PA142671060
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG1817 Eukaryota COG0571 LUCA
GeneTreeⁱ	ENSGT00730000111052
HOGENOMⁱ	HOG000122291
HOVERGENⁱ	HBG023130
InParanoidⁱ	Q9NRR4
KOⁱ	K03685
OMAⁱ	EYLYRHF
OrthoDBⁱ	935825at2759
PhylomeDBⁱ	Q9NRR4
TreeFamⁱ	TF314734

Enzyme and pathway databases

BRENDAⁱ	3.1.26.3 2681
Reactomeⁱ	R-HSA-203927 MicroRNA (miRNA) biogenesis

Miscellaneous databases

ChiTaRSⁱ	DROSHA human
EvolutionaryTraceⁱ	Q9NRR4
GeneWikiⁱ	RNASEN
GenomeRNAiⁱ	29102
Protein Ontology More...PROⁱ	PR:Q9NRR4
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000113360 Expressed in 221 organ(s), highest expression level in endothelial cell
ExpressionAtlasⁱ	Q9NRR4 baseline and differential
Genevisibleⁱ	Q9NRR4 HS

Family and domain databases

CDDⁱ	cd00048 DSRM, 1 hit cd00593 RIBOc, 2 hits
Gene3Dⁱ	1.10.1520.10, 1 hit
HAMAPⁱ	MF_00104 RNase_III, 1 hit
InterProⁱ	View protein in InterPro IPR014720 dsRBD_dom IPR011907 RNase_III IPR000999 RNase_III_dom IPR036389 RNase_III_sf
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
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	RNC_HUMAN
Accessionⁱ	Q9NRR4Primary (citable) accession number: Q9NRR4 Secondary accession number(s): E7EMP9 , Q7Z5V2, Q86YH0, Q9NW73, Q9Y2V9, Q9Y4Y0
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	January 23, 2002
	Last sequence update:	January 23, 2002
	Last modified:	February 13, 2019
	This is version 174 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, Complete proteome, Reference proteome

Documents

PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families
Human chromosome 5
Human chromosome 5: entries, gene names and cross-references to MIM
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
Protein Spotlight
Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

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UniProtKB - Q9NRR4 (RNC_HUMAN)

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Ribonuclease 3

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<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

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<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

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Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

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Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

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Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

Compositional bias

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

Catalytic activityⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Sequence cautionⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ