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Protein

Ribonuclease 3

Gene

DROSHA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi536Zinc 11 Publication1
Metal bindingi538Zinc 11 Publication1
Metal bindingi549Zinc 11 Publication1
Metal bindingi561Zinc 21 Publication1
Metal bindingi609Zinc 21 Publication1
Metal bindingi676Zinc 21 Publication1
Metal bindingi680Zinc 21 Publication1
Metal bindingi969Magnesium or manganese 1By similarity1
Metal bindingi1026Zinc 11 Publication1
Metal bindingi1042Magnesium or manganese 1By similarity1
Metal bindingi1045Magnesium or manganese 1By similarity1 Publication1
Metal bindingi1147Magnesium or manganese 2By similarity1
Sitei1215Important for activityBy similarity1
Metal bindingi1219Magnesium or manganese 2By similarity1
Metal bindingi1222Magnesium or manganese 2By similarity1 Publication1

GO - Molecular functioni

  • double-stranded RNA binding Source: GO_Central
  • lipopolysaccharide binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • poly(A) RNA binding Source: UniProtKB
  • primary miRNA binding Source: BHF-UCL
  • protein homodimerization activity Source: BHF-UCL
  • ribonuclease III activity Source: WormBase

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

Ribosome biogenesis, RNA-mediated gene silencing

Keywords - Ligandi

Magnesium, Manganese, Metal-binding, RNA-binding

Enzyme and pathway databases

BioCyciZFISH:HS03674-MONOMER.
BRENDAi3.1.26.3. 2681.
ReactomeiR-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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:17904. DROSHA.

Subcellular locationi

GO - Cellular componenti

  • microprocessor complex Source: BHF-UCL
  • nucleolus Source: UniProtKB-SubCell
  • nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi536C → A: Impairs protein folding and stability; when associated with A-538. 1 Publication1
Mutagenesisi538C → A: Impairs protein folding and stability; when associated with A-536. 1 Publication1
Mutagenesisi561C → A: Impairs protein folding and stability. 1 Publication1
Mutagenesisi622 – 623RF → AA: Abolishes RNase activity. 1 Publication2
Mutagenesisi676C → A: Impairs protein folding and stability. 1 Publication1
Mutagenesisi835 – 836RR → AA: Abolishes RNase activity. 1 Publication2
Mutagenesisi914R → M: Impairs RNase activity. 1 Publication1
Mutagenesisi923R → A: Abolishes RNase activity; when associated with A-927. 1 Publication1
Mutagenesisi927Y → A: Abolishes RNase activity; when associated with A-923. 1 Publication1
Mutagenesisi938 – 940RKK → QQQ: Abolishes RNase activity. 1 Publication3
Mutagenesisi993E → A or Q: No effect on pri-miRNA processing activity. 1 Publication1
Mutagenesisi1045E → Q: Impairs pri-miRNA processing activity. Abolishes cleavage of the 3' strand. Abolishes enzyme activity; when associated with Q-1222. 2 Publications1
Mutagenesisi1077V → E: Loss of one DGCR8 interaction site; no effect on the second DGCR8 interaction site. 1 Publication1
Mutagenesisi1171E → A or Q: No effect on pri-miRNA processing activity. 1 Publication1
Mutagenesisi1194L → R: Abolishes interaction with DGCR8. 1 Publication1
Mutagenesisi1222E → Q: Impairs pri-miRNA processing activity. Abolishes cleavage of the 5' strand. Abolishes enzyme activity; when associated with Q-1045. 2 Publications1
Mutagenesisi1243V → D: Abolishes interaction with DGCR8. 1 Publication1

Organism-specific databases

DisGeNETi29102.
OpenTargetsiENSG00000113360.
PharmGKBiPA142671060.

Polymorphism and mutation databases

BioMutaiDROSHA.
DMDMi20139357.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001804681 – 1374Ribonuclease 3Add BLAST1374

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei355PhosphoserineCombined sources1
Modified residuei373PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9NRR4.
MaxQBiQ9NRR4.
PaxDbiQ9NRR4.
PeptideAtlasiQ9NRR4.
PRIDEiQ9NRR4.

PTM databases

iPTMnetiQ9NRR4.
PhosphoSitePlusiQ9NRR4.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiENSG00000113360.
CleanExiHS_RNASEN.
ExpressionAtlasiQ9NRR4. baseline and differential.
GenevisibleiQ9NRR4. HS.

Organism-specific databases

HPAiCAB026471.

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

WithEntry#Exp.IntActNotes
DGCR8Q8WYQ58EBI-528367,EBI-528411
FUSP356372EBI-528367,EBI-400434

GO - Molecular functioni

  • protein homodimerization activity Source: BHF-UCL

Protein-protein interaction databases

BioGridi118870. 40 interactors.
DIPiDIP-33300N.
IntActiQ9NRR4. 27 interactors.
MINTiMINT-1184869.
STRINGi9606.ENSP00000339845.

Structurei

Secondary structure

11374
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi413 – 415Combined sources3
Beta strandi420 – 423Combined sources4
Helixi441 – 451Combined sources11
Turni455 – 457Combined sources3
Beta strandi531 – 535Combined sources5
Turni547 – 550Combined sources4
Beta strandi563 – 565Combined sources3
Turni568 – 570Combined sources3
Beta strandi572 – 580Combined sources9
Beta strandi582 – 584Combined sources3
Beta strandi591 – 593Combined sources3
Beta strandi595 – 610Combined sources16
Beta strandi618 – 632Combined sources15
Helixi642 – 652Combined sources11
Turni653 – 656Combined sources4
Beta strandi678 – 686Combined sources9
Beta strandi694 – 696Combined sources3
Helixi699 – 708Combined sources10
Helixi856 – 860Combined sources5
Helixi863 – 875Combined sources13
Helixi876 – 878Combined sources3
Helixi880 – 883Combined sources4
Helixi890 – 897Combined sources8
Helixi910 – 919Combined sources10
Helixi966 – 986Combined sources21
Helixi993 – 1004Combined sources12
Helixi1006 – 1013Combined sources8
Helixi1014 – 1016Combined sources3
Helixi1018 – 1021Combined sources4
Helixi1033 – 1054Combined sources22
Helixi1057 – 1068Combined sources12
Helixi1072 – 1079Combined sources8
Helixi1085 – 1088Combined sources4
Helixi1095 – 1098Combined sources4
Helixi1104 – 1114Combined sources11
Helixi1121 – 1127Combined sources7
Helixi1144 – 1164Combined sources21
Helixi1171 – 1181Combined sources11
Helixi1184 – 1194Combined sources11
Beta strandi1203 – 1205Combined sources3
Helixi1214 – 1231Combined sources18
Helixi1234 – 1244Combined sources11
Helixi1246 – 1248Combined sources3
Helixi1249 – 1254Combined sources6
Helixi1261 – 1269Combined sources9
Beta strandi1275 – 1277Combined sources3
Beta strandi1283 – 1291Combined sources9
Beta strandi1292 – 1294Combined sources3
Beta strandi1297 – 1304Combined sources8
Beta strandi1307 – 1316Combined sources10
Helixi1317 – 1330Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KHXNMR-A1259-1337[»]
5B16X-ray3.20A411-458[»]
A522-711[»]
A850-1365[»]
ProteinModelPortaliQ9NRR4.
SMRiQ9NRR4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NRR4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini876 – 1056RNase III 1Add BLAST181
Domaini1107 – 1233RNase III 2Add BLAST127
Domaini1260 – 1334DRBMAdd BLAST75

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni390 – 1365Necessary for interaction with DGCR8 and pri-miRNA processing activity2 PublicationsAdd BLAST976

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1 – 212Pro-richAdd BLAST212
Compositional biasi219 – 316Arg-richAdd BLAST98

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

Contains 2 RNase III domains.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1817. Eukaryota.
COG0571. LUCA.
GeneTreeiENSGT00730000111052.
HOGENOMiHOG000122291.
HOVERGENiHBG023130.
InParanoidiQ9NRR4.
KOiK03685.
OMAiLSRKVQH.
OrthoDBiEOG091G02A9.
PhylomeDBiQ9NRR4.
TreeFamiTF314734.

Family and domain databases

CDDicd00593. RIBOc. 2 hits.
Gene3Di1.10.1520.10. 3 hits.
3.30.160.20. 1 hit.
HAMAPiMF_00104. RNase_III. 1 hit.
InterProiIPR014720. dsRBD_dom.
IPR011907. RNase_III.
IPR000999. RNase_III_dom.
[Graphical view]
PfamiPF00035. dsrm. 1 hit.
PF14622. Ribonucleas_3_3. 1 hit.
PF00636. Ribonuclease_3. 1 hit.
[Graphical view]
SMARTiSM00358. DSRM. 1 hit.
SM00535. RIBOc. 2 hits.
[Graphical view]
SUPFAMiSSF69065. SSF69065. 3 hits.
PROSITEiPS50137. DS_RBD. 1 hit.
PS00517. RNASE_3_1. 2 hits.
PS50142. RNASE_3_2. 2 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

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

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

Note: No experimental confirmation available.
Show »
Length:1,306
Mass (Da):151,296
Checksum:iE2A0A46BE0E0A692
GO
Isoform 3 (identifier: Q9NRR4-3) [UniParc]FASTAAdd 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.

Note: No experimental confirmation available.
Show »
Length:1,192
Mass (Da):138,157
Checksum:i18479E41CFD76BAC
GO
Isoform 4 (identifier: Q9NRR4-4) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:1,337
Mass (Da):155,333
Checksum:i834B12891D1DB08D
GO

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 keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti166 – 174YQYPPGYSH → RERERTSLE in CAB45133 (PubMed:10976766).Curated9
Sequence conflicti612L → P in CAB45133 (PubMed:10976766).Curated1
Sequence conflicti1020R → P in AAF80558 (PubMed:10948199).Curated1
Sequence conflicti1230I → T in AAF80558 (PubMed:10948199).Curated1
Sequence conflicti1272L → R in BX647724 (PubMed:17974005).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05186667P → T.Corresponds to variant rs35342496dbSNPEnsembl.1
Natural variantiVAR_061778321S → L.Corresponds to variant rs55656741dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_005777285 – 353RERER…EIVNH → S in isoform 2. 1 PublicationAdd BLAST69
Alternative sequenceiVSP_012450316 – 352Missing in isoform 3 and isoform 4. 2 PublicationsAdd BLAST37
Alternative sequenceiVSP_012451353H → S in isoform 3 and isoform 4. 2 Publications1
Alternative sequenceiVSP_0124521198 – 1229EYAIT…IAALY → VWSIYLLSNCDCCLLRPSLV FLQTMNEVCSLK in isoform 3. 1 PublicationAdd BLAST32
Alternative sequenceiVSP_0124531230 – 1374Missing in isoform 3. 1 PublicationAdd BLAST145

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.
CCDSiCCDS47194.1. [Q9NRR4-4]
CCDS47195.1. [Q9NRR4-1]
RefSeqiNP_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]
UniGeneiHs.97997.

Genome annotation databases

EnsembliENST00000344624; ENSP00000339845; ENSG00000113360. [Q9NRR4-1]
ENST00000442743; ENSP00000409335; ENSG00000113360. [Q9NRR4-4]
ENST00000511367; ENSP00000425979; ENSG00000113360. [Q9NRR4-1]
ENST00000513349; ENSP00000424161; ENSG00000113360. [Q9NRR4-4]
GeneIDi29102.
KEGGihsa:29102.
UCSCiuc003jhg.3. human. [Q9NRR4-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

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.
CCDSiCCDS47194.1. [Q9NRR4-4]
CCDS47195.1. [Q9NRR4-1]
RefSeqiNP_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]
UniGeneiHs.97997.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KHXNMR-A1259-1337[»]
5B16X-ray3.20A411-458[»]
A522-711[»]
A850-1365[»]
ProteinModelPortaliQ9NRR4.
SMRiQ9NRR4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118870. 40 interactors.
DIPiDIP-33300N.
IntActiQ9NRR4. 27 interactors.
MINTiMINT-1184869.
STRINGi9606.ENSP00000339845.

PTM databases

iPTMnetiQ9NRR4.
PhosphoSitePlusiQ9NRR4.

Polymorphism and mutation databases

BioMutaiDROSHA.
DMDMi20139357.

Proteomic databases

EPDiQ9NRR4.
MaxQBiQ9NRR4.
PaxDbiQ9NRR4.
PeptideAtlasiQ9NRR4.
PRIDEiQ9NRR4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000344624; ENSP00000339845; ENSG00000113360. [Q9NRR4-1]
ENST00000442743; ENSP00000409335; ENSG00000113360. [Q9NRR4-4]
ENST00000511367; ENSP00000425979; ENSG00000113360. [Q9NRR4-1]
ENST00000513349; ENSP00000424161; ENSG00000113360. [Q9NRR4-4]
GeneIDi29102.
KEGGihsa:29102.
UCSCiuc003jhg.3. human. [Q9NRR4-1]

Organism-specific databases

CTDi29102.
DisGeNETi29102.
GeneCardsiDROSHA.
H-InvDBHIX0004780.
HGNCiHGNC:17904. DROSHA.
HPAiCAB026471.
MIMi608828. gene.
neXtProtiNX_Q9NRR4.
OpenTargetsiENSG00000113360.
PharmGKBiPA142671060.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1817. Eukaryota.
COG0571. LUCA.
GeneTreeiENSGT00730000111052.
HOGENOMiHOG000122291.
HOVERGENiHBG023130.
InParanoidiQ9NRR4.
KOiK03685.
OMAiLSRKVQH.
OrthoDBiEOG091G02A9.
PhylomeDBiQ9NRR4.
TreeFamiTF314734.

Enzyme and pathway databases

BioCyciZFISH:HS03674-MONOMER.
BRENDAi3.1.26.3. 2681.
ReactomeiR-HSA-203927. MicroRNA (miRNA) biogenesis.

Miscellaneous databases

ChiTaRSiDROSHA. human.
EvolutionaryTraceiQ9NRR4.
GeneWikiiRNASEN.
GenomeRNAii29102.
PROiQ9NRR4.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000113360.
CleanExiHS_RNASEN.
ExpressionAtlasiQ9NRR4. baseline and differential.
GenevisibleiQ9NRR4. HS.

Family and domain databases

CDDicd00593. RIBOc. 2 hits.
Gene3Di1.10.1520.10. 3 hits.
3.30.160.20. 1 hit.
HAMAPiMF_00104. RNase_III. 1 hit.
InterProiIPR014720. dsRBD_dom.
IPR011907. RNase_III.
IPR000999. RNase_III_dom.
[Graphical view]
PfamiPF00035. dsrm. 1 hit.
PF14622. Ribonucleas_3_3. 1 hit.
PF00636. Ribonuclease_3. 1 hit.
[Graphical view]
SMARTiSM00358. DSRM. 1 hit.
SM00535. RIBOc. 2 hits.
[Graphical view]
SUPFAMiSSF69065. SSF69065. 3 hits.
PROSITEiPS50137. DS_RBD. 1 hit.
PS00517. RNASE_3_1. 2 hits.
PS50142. RNASE_3_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRNC_HUMAN
AccessioniPrimary (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: November 30, 2016
This is version 156 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.