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Q9NRR4 (RNC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribonuclease 3

EC=3.1.26.3
Alternative name(s):
Protein Drosha
Ribonuclease III
Short name=RNase III
p241
Gene names
Name:DROSHA
Synonyms:RN3, RNASE3L, RNASEN
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1374 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15

Catalytic activity

Endonucleolytic cleavage to 5'-phosphomonoester. HAMAP-Rule MF_00104

Cofactor

Magnesium or manganese By similarity. HAMAP-Rule MF_00104

Subunit structure

Component of the microprocessor complex, or pri-miRNA processing protein complex, which is composed of DROSHA and DGCR8. The microprocessor complex may contain multiple subunit of DGCR8 and DROSHA. Interacts with DGCR8, SP1 and SNIP1. Interacts with SRRT/ARS2. Ref.4 Ref.9 Ref.10 Ref.11 Ref.13 Ref.16

Subcellular location

Nucleus. Nucleusnucleolus. Note: A fraction is translocated to the nucleolus during the S phase of the cell cycle. Localized in GW bodies (GWBs), also known as P-bodies. Ref.1 Ref.14

Tissue specificity

Ubiquitous. Ref.1

Domain

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. HAMAP-Rule MF_00104

Sequence similarities

Contains 1 DRBM (double-stranded RNA-binding) domain.

Contains 2 RNase III domains.

Sequence caution

The sequence AAD29637.1 differs from that shown. Reason: Frameshift at position 775.

The sequence BAA91511.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processRibosome biogenesis
RNA-mediated gene silencing
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   LigandMagnesium
Manganese
Metal-binding
RNA-binding
   Molecular functionEndonuclease
Hydrolase
Nuclease
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA phosphodiester bond hydrolysis

Inferred from direct assay Ref.8. Source: GOC

RNA phosphodiester bond hydrolysis, endonucleolytic

Inferred from direct assay Ref.8. Source: GOC

gene expression

Traceable author statement. Source: Reactome

miRNA metabolic process

Inferred from electronic annotation. Source: Ensembl

pre-miRNA processing

Inferred from electronic annotation. Source: Ensembl

primary miRNA processing

Inferred from direct assay Ref.8. Source: WormBase

rRNA catabolic process

Inferred from electronic annotation. Source: InterPro

ribosome biogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.10PubMed 22222205PubMed 23232809. Source: IntAct

ribonuclease III activity

Inferred from direct assay Ref.8. Source: WormBase

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NRR4-1)

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.
Isoform 2 (identifier: Q9NRR4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     285-353: RERERERHRHRDNRRSPSLERSYKKEYKRSGRSYGLSVVPEPAGCTPELPGEIIKNTDSWAPPLEIVNH → S
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9NRR4-3)

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.
Isoform 4 (identifier: Q9NRR4-4)

The sequence of this isoform differs from the canonical sequence as follows:
     316-352: Missing.
     353-353: H → S
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13741374Ribonuclease 3 HAMAP-Rule MF_00104
PRO_0000180468

Regions

Domain876 – 1056181RNase III 1
Domain1107 – 1233127RNase III 2
Domain1260 – 133475DRBM
Region490 – 1374885Necessary for interaction with DGCR8 and pri-miRNA processing activity HAMAP-Rule MF_00104
Compositional bias1 – 212212Pro-rich HAMAP-Rule MF_00104
Compositional bias219 – 31698Arg-rich HAMAP-Rule MF_00104

Sites

Metal binding11471Magnesium or manganese By similarity
Metal binding12191Magnesium or manganese By similarity
Metal binding12221Magnesium or manganese By similarity
Site12151Important for activity By similarity

Amino acid modifications

Modified residue3731Phosphoserine Ref.18

Natural variations

Alternative sequence285 – 35369RERER…EIVNH → S in isoform 2.
VSP_005777
Alternative sequence316 – 35237Missing in isoform 3 and isoform 4.
VSP_012450
Alternative sequence3531H → S in isoform 3 and isoform 4.
VSP_012451
Alternative sequence1198 – 122932EYAIT…IAALY → VWSIYLLSNCDCCLLRPSLV FLQTMNEVCSLK in isoform 3.
VSP_012452
Alternative sequence1230 – 1374145Missing in isoform 3.
VSP_012453
Natural variant671P → T.
Corresponds to variant rs35342496 [ dbSNP | Ensembl ].
VAR_051866
Natural variant3211S → L.
Corresponds to variant rs55656741 [ dbSNP | Ensembl ].
VAR_061778

Experimental info

Mutagenesis9931E → A or Q: Does not reduce pri-miRNA processing activity. Ref.10
Mutagenesis10451E → Q: Reduces pri-miRNA processing activity. Ref.10
Mutagenesis11711E → A or Q: Does not reduce pri-miRNA processing activity. Ref.10
Mutagenesis12221E → Q: Reduces pri-miRNA processing activity. Ref.10
Sequence conflict166 – 1749YQYPPGYSH → RERERTSLE in CAB45133. Ref.4
Sequence conflict6121L → P in CAB45133. Ref.4
Sequence conflict10201R → P in AAF80558. Ref.1
Sequence conflict12301I → T in AAF80558. Ref.1
Sequence conflict12721L → R in BX647724. Ref.2

Secondary structure

.............. 1374
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2002. Version 2.
Checksum: ED6FDEA09F3B8092

FASTA1,374159,316
        10         20         30         40         50         60 
MMQGNTCHRM SFHPGRGCPR GRGGHGARPS APSFRPQNLR LLHPQQPPVQ YQYEPPSAPS 

        70         80         90        100        110        120 
TTFSNSPAPN FLPPRPDFVP FPPPMPPSAQ GPLPPCPIRP PFPNHQMRHP FPVPPCFPPM 

       130        140        150        160        170        180 
PPPMPCPNNP PVPGAPPGQG TFPFMMPPPS MPHPPPPPVM PQQVNYQYPP GYSHHNFPPP 

       190        200        210        220        230        240 
SFNSFQNNPS SFLPSANNSS SPHFRHLPPY PLPKAPSERR SPERLKHYDD HRHRDHSHGR 

       250        260        270        280        290        300 
GERHRSLDRR ERGRSPDRRR QDSRYRSDYD RGRTPSRHRS YERSRERERE RHRHRDNRRS 

       310        320        330        340        350        360 
PSLERSYKKE YKRSGRSYGL SVVPEPAGCT PELPGEIIKN TDSWAPPLEI VNHRSPSREK 

       370        380        390        400        410        420 
KRARWEEEKD RWSDNQSSGK DKNYTSIKEK EPEETMPDKN EEEEEELLKP VWIRCTHSEN 

       430        440        450        460        470        480 
YYSSDPMDQV GDSTVVGTSR LRDLYDKFEE ELGSRQEKAK AARPPWEPPK TKLDEDLESS 

       490        500        510        520        530        540 
SESECESDED STCSSSSDSE VFDVIAEIKR KKAHPDRLHD ELWYNDPGQM NDGPLCKCSA 

       550        560        570        580        590        600 
KARRTGIRHS IYPGEEAIKP CRPMTNNAGR LFHYRITVSP PTNFLTDRPT VIEYDDHEYI 

       610        620        630        640        650        660 
FEGFSMFAHA PLTNIPLCKV IRFNIDYTIH FIEEMMPENF CVKGLELFSL FLFRDILELY 

       670        680        690        700        710        720 
DWNLKGPLFE DSPPCCPRFH FMPRFVRFLP DGGKEVLSMH QILLYLLRCS KALVPEEEIA 

       730        740        750        760        770        780 
NMLQWEELEW QKYAEECKGM IVTNPGTKPS SVRIDQLDRE QFNPDVITFP IIVHFGIRPA 

       790        800        810        820        830        840 
QLSYAGDPQY QKLWKSYVKL RHLLANSPKV KQTDKQKLAQ REEALQKIRQ KNTMRREVTV 

       850        860        870        880        890        900 
ELSSQGFWKT GIRSDVCQHA MMLPVLTHHI RYHQCLMHLD KLIGYTFQDR CLLQLAMTHP 

       910        920        930        940        950        960 
SHHLNFGMNP DHARNSLSNC GIRQPKYGDR KVHHMHMRKK GINTLINIMS RLGQDDPTPS 

       970        980        990       1000       1010       1020 
RINHNERLEF LGDAVVEFLT SVHLYYLFPS LEEGGLATYR TAIVQNQHLA MLAKKLELDR 

      1030       1040       1050       1060       1070       1080 
FMLYAHGPDL CRESDLRHAM ANCFEALIGA VYLEGSLEEA KQLFGRLLFN DPDLREVWLN 

      1090       1100       1110       1120       1130       1140 
YPLHPLQLQE PNTDRQLIET SPVLQKLTEF EEAIGVIFTH VRLLARAFTL RTVGFNHLTL 

      1150       1160       1170       1180       1190       1200 
GHNQRMEFLG DSIMQLVATE YLFIHFPDHH EGHLTLLRSS LVNNRTQAKV AEELGMQEYA 

      1210       1220       1230       1240       1250       1260 
ITNDKTKRPV ALRTKTLADL LESFIAALYI DKDLEYVHTF MNVCFFPRLK EFILNQDWND 

      1270       1280       1290       1300       1310       1320 
PKSQLQQCCL TLRTEGKEPD IPLYKTLQTV GPSHARTYTV AVYFKGERIG CGKGPSIQQA 

      1330       1340       1350       1360       1370 
EMGAAMDALE KYNFPQMAHQ KRFIERKYRQ ELKEMRWERE HQEREPDETE DIKK 

« Hide

Isoform 2 [UniParc].

Checksum: E2A0A46BE0E0A692
Show »

FASTA1,306151,296
Isoform 3 [UniParc].

Checksum: 18479E41CFD76BAC
Show »

FASTA1,192138,157
Isoform 4 [UniParc].

Checksum: 834B12891D1DB08D
Show »

FASTA1,337155,333

References

« Hide 'large scale' references
[1]"Human RNase III is a 160-kDa protein involved in preribosomal RNA processing."
Wu H., Xu H., Miraglia L.J., Crooke S.T.
J. Biol. Chem. 275:36957-36965(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[2]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Cerebellum.
[3]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"A set of proteins interacting with transcription factor Sp1 identified in a two-hybrid screening."
Gunther M., Laithier M., Brison O.
Mol. Cell. Biochem. 210:131-142(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 166-613 (ISOFORM 2), INTERACTION WITH SP1.
Tissue: Colon.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 603-1374.
Tissue: Embryo.
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 653-1374 (ISOFORM 1).
Tissue: Cervix and Skin.
[7]Wei Y.J., Ding J.F., Xiong H., Zhou Y., Liew C.C.
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 706-1374.
Tissue: Aorta.
[8]"The nuclear RNase III Drosha initiates microRNA processing."
Lee Y., Ahn C., Han J., Choi H., Kim J., Yim J., Lee J., Provost P., Raadmark O., Kim S., Kim V.N.
Nature 425:415-419(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"The human DiGeorge syndrome critical region gene 8 and its D. melanogaster homolog are required for miRNA biogenesis."
Landthaler M., Yalcin A., Tuschl T.
Curr. Biol. 14:2162-2167(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH DGCR8.
[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, MUTAGENESIS OF GLU-993; GLU-1045; GLU-1171 AND GLU-1222.
[11]"The microprocessor complex mediates the genesis of microRNAs."
Gregory R.I., Yan K.-P., Amuthan G., Chendrimada T., Doratotaj B., Cooch N., Shiekhattar R.
Nature 432:235-240(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE MICROPROCESSOR COMPLEX.
[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.
[13]"Molecular basis for the recognition of primary microRNAs by the Drosha-DGCR8 complex."
Han J., Lee Y., Yeom K.-H., Nam J.-W., Heo I., Rhee J.-K., Sohn S.Y., Cho Y., Zhang B.-T., Kim V.N.
Cell 125:887-901(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE MICROPROCESSOR COMPLEX.
[14]"Formation of GW bodies is a consequence of microRNA genesis."
Pauley K.M., Eystathioy T., Jakymiw A., Hamel J.C., Fritzler M.J., Chan E.K.L.
EMBO Rep. 7:904-910(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[15]"Heme is involved in microRNA processing."
Faller M., Matsunaga M., Yin S., Loo J.A., Guo F.
Nat. Struct. Mol. Biol. 14:23-29(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[16]"The FHA domain proteins DAWDLE in Arabidopsis and SNIP1 in humans act in small RNA biogenesis."
Yu B., Bi L., Zheng B., Ji L., Chevalier D., Agarwal M., Ramachandran V., Li W., Lagrange T., Walker J.C., Chen X.
Proc. Natl. Acad. Sci. U.S.A. 105:10073-10078(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SNIP1.
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Solution structure of the Drosha double-stranded RNA-binding domain."
Mueller G.A., Miller M.T., Derose E.F., Ghosh M., London R.E., Hall T.M.
Silence 1:2-2(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1259-1337.
+Additional computationally mapped references.

Web resources

Protein Spotlight

The dark side of RNA - Issue 87 of October 2007

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS47194.1. [Q9NRR4-4]
CCDS47195.1. [Q9NRR4-1]
RefSeqNP_001093882.1. NM_001100412.1. [Q9NRR4-4]
NP_037367.3. NM_013235.4. [Q9NRR4-1]
XP_005248348.1. XM_005248291.1. [Q9NRR4-1]
XP_005248351.1. XM_005248294.1. [Q9NRR4-2]
UniGeneHs.97997.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KHXNMR-A1259-1337[»]
ProteinModelPortalQ9NRR4.
SMRQ9NRR4. Positions 962-1337.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118870. 10 interactions.
DIPDIP-33300N.
IntActQ9NRR4. 16 interactions.
MINTMINT-1184869.

PTM databases

PhosphoSiteQ9NRR4.

Polymorphism databases

DMDM20139357.

Proteomic databases

MaxQBQ9NRR4.
PaxDbQ9NRR4.
PRIDEQ9NRR4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000344624; ENSP00000339845; ENSG00000113360. [Q9NRR4-1]
ENST00000442743; ENSP00000409335; ENSG00000113360. [Q9NRR4-4]
ENST00000511367; ENSP00000425979; ENSG00000113360. [Q9NRR4-1]
ENST00000513349; ENSP00000424161; ENSG00000113360. [Q9NRR4-4]
GeneID29102.
KEGGhsa:29102.
UCSCuc003jhg.2. human. [Q9NRR4-1]
uc003jhh.2. human.

Organism-specific databases

CTD29102.
GeneCardsGC05M031401.
H-InvDBHIX0004780.
HGNCHGNC:17904. DROSHA.
MIM608828. gene.
neXtProtNX_Q9NRR4.
PharmGKBPA142671060.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0571.
HOGENOMHOG000122291.
HOVERGENHBG023130.
InParanoidQ9NRR4.
KOK03685.
OMAESYYSND.
OrthoDBEOG773XF7.
PhylomeDBQ9NRR4.
TreeFamTF314734.

Enzyme and pathway databases

BRENDA3.1.26.3. 2681.
ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ9NRR4.
BgeeQ9NRR4.
CleanExHS_RNASEN.
GenevestigatorQ9NRR4.

Family and domain databases

Gene3D1.10.1520.10. 3 hits.
3.30.160.20. 1 hit.
HAMAPMF_00104. RNase_III.
InterProIPR014720. dsRNA-bd_dom.
IPR011907. RNase_III.
IPR000999. RNase_III_dom.
[Graphical view]
PANTHERPTHR11207. PTHR11207. 1 hit.
PfamPF00035. dsrm. 1 hit.
PF14622. Ribonucleas_3_3. 1 hit.
PF00636. Ribonuclease_3. 1 hit.
[Graphical view]
SMARTSM00358. DSRM. 1 hit.
SM00535. RIBOc. 2 hits.
[Graphical view]
SUPFAMSSF69065. SSF69065. 3 hits.
PROSITEPS50137. DS_RBD. 1 hit.
PS00517. RNASE_3_1. 2 hits.
PS50142. RNASE_3_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDROSHA. human.
EvolutionaryTraceQ9NRR4.
GeneWikiRNASEN.
GenomeRNAi29102.
NextBio52141.
PROQ9NRR4.
SOURCESearch...

Entry information

Entry nameRNC_HUMAN
AccessionPrimary (citable) accession number: Q9NRR4
Secondary accession number(s): E7EMP9 expand/collapse secondary AC list , Q7Z5V2, Q86YH0, Q9NW73, Q9Y2V9, Q9Y4Y0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: January 23, 2002
Last modified: July 9, 2014
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM