Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9NRR4

- RNC_HUMAN

UniProt

Q9NRR4 - RNC_HUMAN

Protein

Ribonuclease 3

Gene

DROSHA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 2 (23 Jan 2002)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.9 Publications

    Catalytic activityi

    Endonucleolytic cleavage to 5'-phosphomonoester.

    Cofactori

    Magnesium or manganese.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi1147 – 11471Magnesium or manganeseBy similarity
    Sitei1215 – 12151Important for activityBy similarity
    Metal bindingi1219 – 12191Magnesium or manganeseBy similarity
    Metal bindingi1222 – 12221Magnesium or manganeseBy similarity

    GO - Molecular functioni

    1. lipopolysaccharide binding Source: UniProt
    2. metal ion binding Source: UniProtKB-KW
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: IntAct
    5. ribonuclease III activity Source: WormBase

    GO - Biological processi

    1. defense response to Gram-negative bacterium Source: UniProt
    2. defense response to Gram-positive bacterium Source: UniProt
    3. gene expression Source: Reactome
    4. miRNA metabolic process Source: Ensembl
    5. pre-miRNA processing Source: Ensembl
    6. primary miRNA processing Source: WormBase
    7. ribosome biogenesis Source: UniProtKB-KW
    8. RNA phosphodiester bond hydrolysis Source: GOC
    9. RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
    10. rRNA catabolic process Source: InterPro

    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

    BRENDAi3.1.26.3. 2681.
    ReactomeiREACT_12417. MicroRNA (miRNA) biogenesis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribonuclease 3 (EC:3.1.26.3)
    Alternative name(s):
    Protein Drosha
    Ribonuclease III
    Short name:
    RNase III
    p241
    Gene namesi
    Name:DROSHA
    Synonyms:RN3, RNASE3L, RNASEN
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:17904. DROSHA.

    Subcellular locationi

    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.

    GO - Cellular componenti

    1. nucleolus Source: UniProtKB-SubCell
    2. nucleoplasm Source: Reactome

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi993 – 9931E → A or Q: Does not reduce pri-miRNA processing activity. 1 Publication
    Mutagenesisi1045 – 10451E → Q: Reduces pri-miRNA processing activity. 1 Publication
    Mutagenesisi1171 – 11711E → A or Q: Does not reduce pri-miRNA processing activity. 1 Publication
    Mutagenesisi1222 – 12221E → Q: Reduces pri-miRNA processing activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA142671060.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13741374Ribonuclease 3PRO_0000180468Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei373 – 3731Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9NRR4.
    PaxDbiQ9NRR4.
    PRIDEiQ9NRR4.

    PTM databases

    PhosphoSiteiQ9NRR4.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    ArrayExpressiQ9NRR4.
    BgeeiQ9NRR4.
    CleanExiHS_RNASEN.
    GenevestigatoriQ9NRR4.

    Interactioni

    Subunit structurei

    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/ARS2.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DGCR8Q8WYQ57EBI-528367,EBI-528411
    FUSP356372EBI-528367,EBI-400434

    Protein-protein interaction databases

    BioGridi118870. 26 interactions.
    DIPiDIP-33300N.
    IntActiQ9NRR4. 16 interactions.
    MINTiMINT-1184869.

    Structurei

    Secondary structure

    1
    1374
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi1263 – 12719
    Beta strandi1275 – 12773
    Beta strandi1284 – 12863
    Beta strandi1292 – 12943
    Beta strandi1298 – 13047
    Beta strandi1312 – 13165
    Helixi1317 – 132913

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KHXNMR-A1259-1337[»]
    ProteinModelPortaliQ9NRR4.
    SMRiQ9NRR4. Positions 962-1337.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NRR4.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini876 – 1056181RNase III 1Add
    BLAST
    Domaini1107 – 1233127RNase III 2Add
    BLAST
    Domaini1260 – 133475DRBMAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni490 – 1374885Necessary for interaction with DGCR8 and pri-miRNA processing activityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1 – 212212Pro-richAdd
    BLAST
    Compositional biasi219 – 31698Arg-richAdd
    BLAST

    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.

    Sequence similaritiesi

    Contains 2 RNase III domains.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0571.
    HOGENOMiHOG000122291.
    HOVERGENiHBG023130.
    InParanoidiQ9NRR4.
    KOiK03685.
    OMAiESYYSND.
    OrthoDBiEOG773XF7.
    PhylomeDBiQ9NRR4.
    TreeFamiTF314734.

    Family and domain databases

    Gene3Di1.10.1520.10. 3 hits.
    3.30.160.20. 1 hit.
    HAMAPiMF_00104. RNase_III.
    InterProiIPR014720. dsRNA-bd_dom.
    IPR011907. RNase_III.
    IPR000999. RNase_III_dom.
    [Graphical view]
    PANTHERiPTHR11207. PTHR11207. 1 hit.
    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. Align

    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

    MMQGNTCHRM SFHPGRGCPR GRGGHGARPS APSFRPQNLR LLHPQQPPVQ     50
    YQYEPPSAPS TTFSNSPAPN FLPPRPDFVP FPPPMPPSAQ GPLPPCPIRP 100
    PFPNHQMRHP FPVPPCFPPM PPPMPCPNNP PVPGAPPGQG TFPFMMPPPS 150
    MPHPPPPPVM PQQVNYQYPP GYSHHNFPPP SFNSFQNNPS SFLPSANNSS 200
    SPHFRHLPPY PLPKAPSERR SPERLKHYDD HRHRDHSHGR GERHRSLDRR 250
    ERGRSPDRRR QDSRYRSDYD RGRTPSRHRS YERSRERERE RHRHRDNRRS 300
    PSLERSYKKE YKRSGRSYGL SVVPEPAGCT PELPGEIIKN TDSWAPPLEI 350
    VNHRSPSREK KRARWEEEKD RWSDNQSSGK DKNYTSIKEK EPEETMPDKN 400
    EEEEEELLKP VWIRCTHSEN YYSSDPMDQV GDSTVVGTSR LRDLYDKFEE 450
    ELGSRQEKAK AARPPWEPPK TKLDEDLESS SESECESDED STCSSSSDSE 500
    VFDVIAEIKR KKAHPDRLHD ELWYNDPGQM NDGPLCKCSA KARRTGIRHS 550
    IYPGEEAIKP CRPMTNNAGR LFHYRITVSP PTNFLTDRPT VIEYDDHEYI 600
    FEGFSMFAHA PLTNIPLCKV IRFNIDYTIH FIEEMMPENF CVKGLELFSL 650
    FLFRDILELY DWNLKGPLFE DSPPCCPRFH FMPRFVRFLP DGGKEVLSMH 700
    QILLYLLRCS KALVPEEEIA NMLQWEELEW QKYAEECKGM IVTNPGTKPS 750
    SVRIDQLDRE QFNPDVITFP IIVHFGIRPA QLSYAGDPQY QKLWKSYVKL 800
    RHLLANSPKV KQTDKQKLAQ REEALQKIRQ KNTMRREVTV ELSSQGFWKT 850
    GIRSDVCQHA MMLPVLTHHI RYHQCLMHLD KLIGYTFQDR CLLQLAMTHP 900
    SHHLNFGMNP DHARNSLSNC GIRQPKYGDR KVHHMHMRKK GINTLINIMS 950
    RLGQDDPTPS RINHNERLEF LGDAVVEFLT SVHLYYLFPS LEEGGLATYR 1000
    TAIVQNQHLA MLAKKLELDR FMLYAHGPDL CRESDLRHAM ANCFEALIGA 1050
    VYLEGSLEEA KQLFGRLLFN DPDLREVWLN YPLHPLQLQE PNTDRQLIET 1100
    SPVLQKLTEF EEAIGVIFTH VRLLARAFTL RTVGFNHLTL GHNQRMEFLG 1150
    DSIMQLVATE YLFIHFPDHH EGHLTLLRSS LVNNRTQAKV AEELGMQEYA 1200
    ITNDKTKRPV ALRTKTLADL LESFIAALYI DKDLEYVHTF MNVCFFPRLK 1250
    EFILNQDWND PKSQLQQCCL TLRTEGKEPD IPLYKTLQTV GPSHARTYTV 1300
    AVYFKGERIG CGKGPSIQQA EMGAAMDALE KYNFPQMAHQ KRFIERKYRQ 1350
    ELKEMRWERE HQEREPDETE DIKK 1374
    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 AAD29637.1 differs from that shown. Reason: Frameshift at position 775.
    The sequence BAA91511.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti166 – 1749YQYPPGYSH → RERERTSLE in CAB45133. (PubMed:10976766)Curated
    Sequence conflicti612 – 6121L → P in CAB45133. (PubMed:10976766)Curated
    Sequence conflicti1020 – 10201R → P in AAF80558. (PubMed:10948199)Curated
    Sequence conflicti1230 – 12301I → T in AAF80558. (PubMed:10948199)Curated
    Sequence conflicti1272 – 12721L → R in BX647724. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti67 – 671P → T.
    Corresponds to variant rs35342496 [ dbSNP | Ensembl ].
    VAR_051866
    Natural varianti321 – 3211S → L.
    Corresponds to variant rs55656741 [ dbSNP | Ensembl ].
    VAR_061778

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei285 – 35369RERER…EIVNH → S in isoform 2. 1 PublicationVSP_005777Add
    BLAST
    Alternative sequencei316 – 35237Missing in isoform 3 and isoform 4. 2 PublicationsVSP_012450Add
    BLAST
    Alternative sequencei353 – 3531H → S in isoform 3 and isoform 4. 2 PublicationsVSP_012451
    Alternative sequencei1198 – 122932EYAIT…IAALY → VWSIYLLSNCDCCLLRPSLV FLQTMNEVCSLK in isoform 3. 1 PublicationVSP_012452Add
    BLAST
    Alternative sequencei1230 – 1374145Missing in isoform 3. 1 PublicationVSP_012453Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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_005248291.1. [Q9NRR4-1]
    XP_005248351.1. XM_005248294.1. [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.2. human. [Q9NRR4-1]
    uc003jhh.2. human.

    Polymorphism databases

    DMDMi20139357.

    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:
    EMBL
    GenBank
    DDBJ
    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_005248291.1. [Q9NRR4-1 ]
    XP_005248351.1. XM_005248294.1. [Q9NRR4-2 ]
    UniGenei Hs.97997.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KHX NMR - A 1259-1337 [» ]
    ProteinModelPortali Q9NRR4.
    SMRi Q9NRR4. Positions 962-1337.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118870. 26 interactions.
    DIPi DIP-33300N.
    IntActi Q9NRR4. 16 interactions.
    MINTi MINT-1184869.

    PTM databases

    PhosphoSitei Q9NRR4.

    Polymorphism databases

    DMDMi 20139357.

    Proteomic databases

    MaxQBi Q9NRR4.
    PaxDbi Q9NRR4.
    PRIDEi Q9NRR4.

    Protocols and materials databases

    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.2. human. [Q9NRR4-1 ]
    uc003jhh.2. human.

    Organism-specific databases

    CTDi 29102.
    GeneCardsi GC05M031401.
    H-InvDB HIX0004780.
    HGNCi HGNC:17904. DROSHA.
    MIMi 608828. gene.
    neXtProti NX_Q9NRR4.
    PharmGKBi PA142671060.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0571.
    HOGENOMi HOG000122291.
    HOVERGENi HBG023130.
    InParanoidi Q9NRR4.
    KOi K03685.
    OMAi ESYYSND.
    OrthoDBi EOG773XF7.
    PhylomeDBi Q9NRR4.
    TreeFami TF314734.

    Enzyme and pathway databases

    BRENDAi 3.1.26.3. 2681.
    Reactomei REACT_12417. MicroRNA (miRNA) biogenesis.

    Miscellaneous databases

    ChiTaRSi DROSHA. human.
    EvolutionaryTracei Q9NRR4.
    GeneWikii RNASEN.
    GenomeRNAii 29102.
    NextBioi 52141.
    PROi Q9NRR4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NRR4.
    Bgeei Q9NRR4.
    CleanExi HS_RNASEN.
    Genevestigatori Q9NRR4.

    Family and domain databases

    Gene3Di 1.10.1520.10. 3 hits.
    3.30.160.20. 1 hit.
    HAMAPi MF_00104. RNase_III.
    InterProi IPR014720. dsRNA-bd_dom.
    IPR011907. RNase_III.
    IPR000999. RNase_III_dom.
    [Graphical view ]
    PANTHERi PTHR11207. PTHR11207. 1 hit.
    Pfami PF00035. dsrm. 1 hit.
    PF14622. Ribonucleas_3_3. 1 hit.
    PF00636. Ribonuclease_3. 1 hit.
    [Graphical view ]
    SMARTi SM00358. DSRM. 1 hit.
    SM00535. RIBOc. 2 hits.
    [Graphical view ]
    SUPFAMi SSF69065. SSF69065. 3 hits.
    PROSITEi PS50137. DS_RBD. 1 hit.
    PS00517. RNASE_3_1. 2 hits.
    PS50142. RNASE_3_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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.
      , 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.
      , 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. 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. 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. 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.

    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: October 1, 2014
    This is version 132 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

    External Data

    Dasty 3