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Q9NRR4

- RNC_HUMAN

UniProt

Q9NRR4 - RNC_HUMAN

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Protein

Ribonuclease 3

Gene

DROSHA

Organism
Homo sapiens (Human)
Status
Reviewed - 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.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. 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
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

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. nucleoplasm Source: Reactome
Complete GO annotation...

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

BgeeiQ9NRR4.
CleanExiHS_RNASEN.
ExpressionAtlasiQ9NRR4. baseline and differential.
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. 27 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.
GeneTreeiENSGT00730000111052.
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) [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 AAD29637.1 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. 27 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.
GeneTreei ENSGT00730000111052.
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

Bgeei Q9NRR4.
CleanExi HS_RNASEN.
ExpressionAtlasi Q9NRR4. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 133 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