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Protein

Ribonuclease 3

Gene

DROSHA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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

GO - Biological processi

Keywordsi

Molecular functionEndonuclease, Hydrolase, Nuclease, RNA-binding
Biological processRibosome biogenesis, RNA-mediated gene silencing
LigandMagnesium, Manganese, Metal-binding

Enzyme and pathway databases

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

EuPathDBiHostDB:ENSG00000113360.16
HGNCiHGNC:17904 DROSHA
MIMi608828 gene
neXtProtiNX_Q9NRR4

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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
ProteomicsDBi82409
82410 [Q9NRR4-2]
82411 [Q9NRR4-3]

PTM databases

iPTMnetiQ9NRR4
PhosphoSitePlusiQ9NRR4

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiENSG00000113360 Expressed in 221 organ(s), highest expression level in endothelial cell
CleanExiHS_RNASEN
ExpressionAtlasiQ9NRR4 baseline and differential
GenevisibleiQ9NRR4 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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi118870, 43 interactors
ComplexPortaliCPX-3080 Microprocessor complex
CORUMiQ9NRR4
DIPiDIP-33300N
IntActiQ9NRR4, 31 interactors
MINTiQ9NRR4
STRINGi9606.ENSP00000339845

Structurei

Secondary structure

11374
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

Belongs to the ribonuclease III family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

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

Family and domain databases

CDDicd00048 DSRM, 1 hit
cd00593 RIBOc, 2 hits
Gene3Di1.10.1520.10, 1 hit
HAMAPiMF_00104 RNase_III, 1 hit
InterProiView protein in InterPro
IPR014720 dsRBD_dom
IPR011907 RNase_III
IPR000999 RNase_III_dom
IPR036389 RNase_III_sf
PfamiView protein in Pfam
PF00035 dsrm, 1 hit
PF14622 Ribonucleas_3_3, 1 hit
PF00636 Ribonuclease_3, 1 hit
SMARTiView protein in SMART
SM00358 DSRM, 1 hit
SM00535 RIBOc, 2 hits
SUPFAMiSSF69065 SSF69065, 3 hits
PROSITEiView 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. AlignAdd to basket

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

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

Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H0YB67H0YB67_HUMAN
Ribonuclease 3
DROSHA
195Annotation score:
H7C5U6H7C5U6_HUMAN
Ribonuclease 3
DROSHA
375Annotation score:
E5RHD1E5RHD1_HUMAN
Ribonuclease 3
DROSHA
201Annotation 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 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 dbSNP:rs35342496Ensembl.1
Natural variantiVAR_061778321S → L. Corresponds to variant dbSNP:rs55656741Ensembl.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

Similar 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.
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[»]
2NA2NMR-A1259-1337[»]
5B16X-ray3.20A411-458[»]
A522-711[»]
A850-1365[»]
ProteinModelPortaliQ9NRR4
SMRiQ9NRR4
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118870, 43 interactors
ComplexPortaliCPX-3080 Microprocessor complex
CORUMiQ9NRR4
DIPiDIP-33300N
IntActiQ9NRR4, 31 interactors
MINTiQ9NRR4
STRINGi9606.ENSP00000339845

PTM databases

iPTMnetiQ9NRR4
PhosphoSitePlusiQ9NRR4

Polymorphism and mutation databases

BioMutaiDROSHA
DMDMi20139357

Proteomic databases

EPDiQ9NRR4
MaxQBiQ9NRR4
PaxDbiQ9NRR4
PeptideAtlasiQ9NRR4
PRIDEiQ9NRR4
ProteomicsDBi82409
82410 [Q9NRR4-2]
82411 [Q9NRR4-3]

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
EuPathDBiHostDB:ENSG00000113360.16
GeneCardsiDROSHA
H-InvDBiHIX0004780
HGNCiHGNC:17904 DROSHA
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

BRENDAi3.1.26.3 2681
ReactomeiR-HSA-203927 MicroRNA (miRNA) biogenesis

Miscellaneous databases

ChiTaRSiDROSHA human
EvolutionaryTraceiQ9NRR4
GeneWikiiRNASEN
GenomeRNAii29102
PROiPR:Q9NRR4
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000113360 Expressed in 221 organ(s), highest expression level in endothelial cell
CleanExiHS_RNASEN
ExpressionAtlasiQ9NRR4 baseline and differential
GenevisibleiQ9NRR4 HS

Family and domain databases

CDDicd00048 DSRM, 1 hit
cd00593 RIBOc, 2 hits
Gene3Di1.10.1520.10, 1 hit
HAMAPiMF_00104 RNase_III, 1 hit
InterProiView protein in InterPro
IPR014720 dsRBD_dom
IPR011907 RNase_III
IPR000999 RNase_III_dom
IPR036389 RNase_III_sf
PfamiView protein in Pfam
PF00035 dsrm, 1 hit
PF14622 Ribonucleas_3_3, 1 hit
PF00636 Ribonuclease_3, 1 hit
SMARTiView protein in SMART
SM00358 DSRM, 1 hit
SM00535 RIBOc, 2 hits
SUPFAMiSSF69065 SSF69065, 3 hits
PROSITEiView protein in PROSITE
PS50137 DS_RBD, 1 hit
PS00517 RNASE_3_1, 2 hits
PS50142 RNASE_3_2, 2 hits
ProtoNetiSearch...

Entry informationi

Entry nameiRNC_HUMAN
AccessioniPrimary (citable) accession number: Q9NRR4
Secondary accession number(s): E7EMP9
, Q7Z5V2, Q86YH0, Q9NW73, Q9Y2V9, Q9Y4Y0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: January 23, 2002
Last modified: September 12, 2018
This is version 170 of the entry and version 2 of the sequence. See 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  7. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
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