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Ribonuclease 3 (EC 3.1.26.3) (Protein Drosha) (Ribonuclease III) (RNase III) (p241)

 RNC_HUMAN               Reviewed;        1374 AA.
Q9NRR4; E7EMP9; Q7Z5V2; Q86YH0; Q9NW73; Q9Y2V9; Q9Y4Y0;
23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
23-JAN-2002, sequence version 2.
27-SEP-2017, entry version 164.
RecName: Full=Ribonuclease 3;
EC=3.1.26.3 {ECO:0000269|PubMed:15565168, ECO:0000269|PubMed:15574589, ECO:0000269|PubMed:26027739, ECO:0000269|PubMed:26748718};
AltName: Full=Protein Drosha {ECO:0000303|PubMed:14508493};
AltName: Full=Ribonuclease III;
Short=RNase III;
AltName: Full=p241;
Name=DROSHA; Synonyms=RN3, RNASE3L, RNASEN;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
AND SUBCELLULAR LOCATION.
PubMed=10948199; DOI=10.1074/jbc.M005494200;
Wu H., Xu H., Miraglia L.J., Crooke S.T.;
"Human RNase III is a 160-kDa protein involved in preribosomal RNA
processing.";
J. Biol. Chem. 275:36957-36965(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Cerebellum;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
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.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
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.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 166-613 (ISOFORM 2), AND INTERACTION
WITH SP1.
TISSUE=Colon;
PubMed=10976766; DOI=10.1023/A:1007177623283;
Gunther M., Laithier M., Brison O.;
"A set of proteins interacting with transcription factor Sp1
identified in a two-hybrid screening.";
Mol. Cell. Biochem. 210:131-142(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 603-1374.
TISSUE=Embryo;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 653-1374 (ISOFORM 1).
TISSUE=Cervix, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 706-1374.
TISSUE=Aorta;
Wei Y.J., Ding J.F., Xiong H., Zhou Y., Liew C.C.;
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
[8]
FUNCTION.
PubMed=14508493; DOI=10.1038/nature01957;
Lee Y., Ahn C., Han J., Choi H., Kim J., Yim J., Lee J., Provost P.,
Raadmark O., Kim S., Kim V.N.;
"The nuclear RNase III Drosha initiates microRNA processing.";
Nature 425:415-419(2003).
[9]
FUNCTION, AND INTERACTION WITH DGCR8.
PubMed=15589161; DOI=10.1016/j.cub.2004.11.001;
Landthaler M., Yalcin A., Tuschl T.;
"The human DiGeorge syndrome critical region gene 8 and its D.
melanogaster homolog are required for miRNA biogenesis.";
Curr. Biol. 14:2162-2167(2004).
[10]
FUNCTION, IDENTIFICATION IN THE MICROPROCESSOR COMPLEX, INTERACTION
WITH DGCR8, CATALYTIC ACTIVITY, COFACTOR, DOMAIN, AND MUTAGENESIS OF
GLU-993; GLU-1045; GLU-1171 AND GLU-1222.
PubMed=15574589; DOI=10.1101/gad.1262504;
Han J., Lee Y., Yeom K.-H., Kim Y.-K., Jin H., Kim V.N.;
"The Drosha-DGCR8 complex in primary microRNA processing.";
Genes Dev. 18:3016-3027(2004).
[11]
FUNCTION, AND IDENTIFICATION IN THE MICROPROCESSOR COMPLEX.
PubMed=15531877; DOI=10.1038/nature03120;
Gregory R.I., Yan K.-P., Amuthan G., Chendrimada T., Doratotaj B.,
Cooch N., Shiekhattar R.;
"The microprocessor complex mediates the genesis of microRNAs.";
Nature 432:235-240(2004).
[12]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=15565168; DOI=10.1038/sj.emboj.7600491;
Zeng Y., Yi R., Cullen B.R.;
"Recognition and cleavage of primary microRNA precursors by the
nuclear processing enzyme Drosha.";
EMBO J. 24:138-148(2005).
[13]
FUNCTION, AND IDENTIFICATION IN THE MICROPROCESSOR COMPLEX.
PubMed=16751099; DOI=10.1016/j.cell.2006.03.043;
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.;
"Molecular basis for the recognition of primary microRNAs by the
Drosha-DGCR8 complex.";
Cell 125:887-901(2006).
[14]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16906129; DOI=10.1038/sj.embor.7400783;
Pauley K.M., Eystathioy T., Jakymiw A., Hamel J.C., Fritzler M.J.,
Chan E.K.L.;
"Formation of GW bodies is a consequence of microRNA genesis.";
EMBO Rep. 7:904-910(2006).
[15]
FUNCTION.
PubMed=17159994; DOI=10.1038/nsmb1182;
Faller M., Matsunaga M., Yin S., Loo J.A., Guo F.;
"Heme is involved in microRNA processing.";
Nat. Struct. Mol. Biol. 14:23-29(2007).
[16]
INTERACTION WITH SNIP1.
PubMed=18632581; DOI=10.1073/pnas.0804218105;
Yu B., Bi L., Zheng B., Ji L., Chevalier D., Agarwal M.,
Ramachandran V., Li W., Lagrange T., Walker J.C., Chen X.;
"The FHA domain proteins DAWDLE in Arabidopsis and SNIP1 in humans act
in small RNA biogenesis.";
Proc. Natl. Acad. Sci. U.S.A. 105:10073-10078(2008).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
SUBCELLULAR LOCATION.
PubMed=22118463; DOI=10.1016/j.cell.2011.10.039;
Piskounova E., Polytarchou C., Thornton J.E., LaPierre R.J.,
Pothoulakis C., Hagan J.P., Iliopoulos D., Gregory R.I.;
"Lin28A and Lin28B inhibit let-7 microRNA biogenesis by distinct
mechanisms.";
Cell 147:1066-1079(2011).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355 AND SER-373, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[21]
FUNCTION, SUBUNIT, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLU-1045 AND
GLU-1222.
PubMed=26027739; DOI=10.1016/j.cell.2015.05.010;
Nguyen T.A., Jo M.H., Choi Y.G., Park J., Kwon S.C., Hohng S.,
Kim V.N., Woo J.S.;
"Functional anatomy of the human microprocessor.";
Cell 161:1374-1387(2015).
[22]
STRUCTURE BY NMR OF 1259-1337.
PubMed=20226070; DOI=10.1186/1758-907X-1-2;
Mueller G.A., Miller M.T., Derose E.F., Ghosh M., London R.E.,
Hall T.M.;
"Solution structure of the Drosha double-stranded RNA-binding
domain.";
Silence 1:2-2(2010).
[23]
X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 411-1365 OF MUTANT
GLN-1045/GLN-1222 IN COMPLEX WITH DGCR8 AND ZINC IONS, FUNCTION,
CATALYTIC ACTIVITY, INTERACTION WITH DGCR8, SUBUNIT, MUTAGENESIS OF
CYS-536; CYS-538; CYS-561; 622-ARG-PHE-623; CYS-676; 835-ARG-ARG-836;
ARG-914; ARG-923; TYR-927; 938-ARG--LYS-940; VAL-1077; LEU-1194 AND
VAL-1243, AND REGION.
PubMed=26748718; DOI=10.1016/j.cell.2015.12.019;
Kwon S.C., Nguyen T.A., Choi Y.G., Jo M.H., Hohng S., Kim V.N.,
Woo J.S.;
"Structure of human DROSHA.";
Cell 164:81-90(2016).
-!- 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. {ECO:0000269|PubMed:10948199,
ECO:0000269|PubMed:14508493, ECO:0000269|PubMed:15531877,
ECO:0000269|PubMed:15565168, ECO:0000269|PubMed:15574589,
ECO:0000269|PubMed:15589161, ECO:0000269|PubMed:16751099,
ECO:0000269|PubMed:16906129, ECO:0000269|PubMed:17159994,
ECO:0000269|PubMed:26027739, ECO:0000269|PubMed:26748718}.
-!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
phosphomonoester. {ECO:0000269|PubMed:15565168,
ECO:0000269|PubMed:15574589, ECO:0000269|PubMed:26027739,
ECO:0000269|PubMed:26748718}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000305|PubMed:15574589};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000305|PubMed:15574589};
Note=Each RNase III domain binds at least one Mg(2+) or Mn(2+)
ion. {ECO:0000305};
-!- SUBUNIT: 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). {ECO:0000250|UniProtKB:Q5HZJ0,
ECO:0000269|PubMed:10976766, ECO:0000269|PubMed:15531877,
ECO:0000269|PubMed:15574589, ECO:0000269|PubMed:15589161,
ECO:0000269|PubMed:16751099, ECO:0000269|PubMed:18632581,
ECO:0000269|PubMed:26027739, ECO:0000269|PubMed:26748718}.
-!- INTERACTION:
Q8WYQ5:DGCR8; NbExp=8; IntAct=EBI-528367, EBI-528411;
P35637:FUS; NbExp=2; IntAct=EBI-528367, EBI-400434;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10948199,
ECO:0000269|PubMed:16906129, ECO:0000269|PubMed:22118463}.
Nucleus, nucleolus {ECO:0000269|PubMed:10948199}. 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.
{ECO:0000269|PubMed:10948199, ECO:0000269|PubMed:22118463}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q9NRR4-1; Sequence=Displayed;
Name=2;
IsoId=Q9NRR4-2; Sequence=VSP_005777;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q9NRR4-3; Sequence=VSP_012450, VSP_012451, VSP_012452,
VSP_012453;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q9NRR4-4; Sequence=VSP_012450, VSP_012451;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10948199}.
-!- 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.
{ECO:0000269|PubMed:15574589}.
-!- SIMILARITY: Belongs to the ribonuclease III family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD29637.1; Type=Frameshift; Positions=775; Evidence={ECO:0000305};
Sequence=BAA91511.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Protein Spotlight; Note=The dark side of RNA
- Issue 87 of October 2007;
URL="http://web.expasy.org/spotlight/back_issues/087";
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EMBL; AF189011; AAF80558.1; -; mRNA.
EMBL; BX647724; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AC008768; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC022417; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC106802; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AJ242976; CAB45133.1; -; mRNA.
EMBL; AK001121; BAA91511.1; ALT_INIT; mRNA.
EMBL; BC041162; AAH41162.1; -; mRNA.
EMBL; BC054003; AAH54003.1; -; mRNA.
EMBL; AF116910; AAD29637.1; ALT_FRAME; mRNA.
CCDS; CCDS47194.1; -. [Q9NRR4-4]
CCDS; CCDS47195.1; -. [Q9NRR4-1]
RefSeq; NP_001093882.1; NM_001100412.1. [Q9NRR4-4]
RefSeq; NP_037367.3; NM_013235.4. [Q9NRR4-1]
RefSeq; XP_005248348.1; XM_005248291.3. [Q9NRR4-1]
RefSeq; XP_005248351.1; XM_005248294.3. [Q9NRR4-2]
UniGene; Hs.97997; -.
PDB; 2KHX; NMR; -; A=1259-1337.
PDB; 2NA2; NMR; -; A=1259-1337.
PDB; 5B16; X-ray; 3.20 A; A=411-458, A=522-711, A=850-1365.
PDBsum; 2KHX; -.
PDBsum; 2NA2; -.
PDBsum; 5B16; -.
ProteinModelPortal; Q9NRR4; -.
SMR; Q9NRR4; -.
BioGrid; 118870; 41.
CORUM; Q9NRR4; -.
DIP; DIP-33300N; -.
IntAct; Q9NRR4; 27.
MINT; MINT-1184869; -.
STRING; 9606.ENSP00000339845; -.
iPTMnet; Q9NRR4; -.
PhosphoSitePlus; Q9NRR4; -.
BioMuta; DROSHA; -.
DMDM; 20139357; -.
EPD; Q9NRR4; -.
MaxQB; Q9NRR4; -.
PaxDb; Q9NRR4; -.
PeptideAtlas; Q9NRR4; -.
PRIDE; Q9NRR4; -.
Ensembl; ENST00000344624; ENSP00000339845; ENSG00000113360. [Q9NRR4-1]
Ensembl; ENST00000442743; ENSP00000409335; ENSG00000113360. [Q9NRR4-4]
Ensembl; ENST00000511367; ENSP00000425979; ENSG00000113360. [Q9NRR4-1]
Ensembl; ENST00000513349; ENSP00000424161; ENSG00000113360. [Q9NRR4-4]
GeneID; 29102; -.
KEGG; hsa:29102; -.
UCSC; uc003jhg.3; human. [Q9NRR4-1]
CTD; 29102; -.
DisGeNET; 29102; -.
EuPathDB; HostDB:ENSG00000113360.16; -.
GeneCards; DROSHA; -.
H-InvDB; HIX0004780; -.
HGNC; HGNC:17904; DROSHA.
HPA; HPA031150; -.
MIM; 608828; gene.
neXtProt; NX_Q9NRR4; -.
OpenTargets; ENSG00000113360; -.
PharmGKB; PA142671060; -.
eggNOG; KOG1817; Eukaryota.
eggNOG; COG0571; LUCA.
GeneTree; ENSGT00730000111052; -.
HOGENOM; HOG000122291; -.
HOVERGEN; HBG023130; -.
InParanoid; Q9NRR4; -.
KO; K03685; -.
OMA; LSRKVQH; -.
OrthoDB; EOG091G02A9; -.
PhylomeDB; Q9NRR4; -.
TreeFam; TF314734; -.
BRENDA; 3.1.26.3; 2681.
Reactome; R-HSA-203927; MicroRNA (miRNA) biogenesis.
ChiTaRS; DROSHA; human.
EvolutionaryTrace; Q9NRR4; -.
GeneWiki; RNASEN; -.
GenomeRNAi; 29102; -.
PRO; PR:Q9NRR4; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000113360; -.
CleanEx; HS_RNASEN; -.
ExpressionAtlas; Q9NRR4; baseline and differential.
Genevisible; Q9NRR4; HS.
GO; GO:0005925; C:focal adhesion; IDA:HPA.
GO; GO:0070877; C:microprocessor complex; IDA:BHF-UCL.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0017151; F:DEAD/H-box RNA helicase binding; IPI:BHF-UCL.
GO; GO:0003725; F:double-stranded RNA binding; IBA:GO_Central.
GO; GO:0001530; F:lipopolysaccharide binding; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0070878; F:primary miRNA binding; IPI:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
GO; GO:0070412; F:R-SMAD binding; IPI:BHF-UCL.
GO; GO:0004525; F:ribonuclease III activity; IDA:WormBase.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0046332; F:SMAD binding; IPI:BHF-UCL.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
GO; GO:0010586; P:miRNA metabolic process; TAS:Reactome.
GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
GO; GO:0031054; P:pre-miRNA processing; IBA:GO_Central.
GO; GO:0031053; P:primary miRNA processing; IDA:WormBase.
GO; GO:0030422; P:production of siRNA involved in RNA interference; IBA:GO_Central.
GO; GO:0050727; P:regulation of inflammatory response; IEA:Ensembl.
GO; GO:2000628; P:regulation of miRNA metabolic process; IEA:Ensembl.
GO; GO:0045589; P:regulation of regulatory T cell differentiation; IEA:Ensembl.
GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
GO; GO:0016075; P:rRNA catabolic process; IEA:InterPro.
CDD; cd00593; RIBOc; 2.
Gene3D; 1.10.1520.10; -; 2.
HAMAP; MF_00104; RNase_III; 1.
InterPro; IPR014720; dsRBD_dom.
InterPro; IPR011907; RNase_III.
InterPro; IPR000999; RNase_III_dom.
Pfam; PF00035; dsrm; 1.
Pfam; PF14622; Ribonucleas_3_3; 1.
Pfam; PF00636; Ribonuclease_3; 1.
SMART; SM00358; DSRM; 1.
SMART; SM00535; RIBOc; 2.
SUPFAM; SSF69065; SSF69065; 3.
PROSITE; PS50137; DS_RBD; 1.
PROSITE; PS00517; RNASE_3_1; 2.
PROSITE; PS50142; RNASE_3_2; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Endonuclease;
Hydrolase; Magnesium; Manganese; Metal-binding; Nuclease; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Ribosome biogenesis; RNA-binding; RNA-mediated gene silencing.
CHAIN 1 1374 Ribonuclease 3.
/FTId=PRO_0000180468.
DOMAIN 876 1056 RNase III 1.
DOMAIN 1107 1233 RNase III 2.
DOMAIN 1260 1334 DRBM.
REGION 390 1365 Necessary for interaction with DGCR8 and
pri-miRNA processing activity.
{ECO:0000269|PubMed:26027739,
ECO:0000269|PubMed:26748718}.
COMPBIAS 1 212 Pro-rich.
COMPBIAS 219 316 Arg-rich.
METAL 536 536 Zinc 1. {ECO:0000269|PubMed:26748718}.
METAL 538 538 Zinc 1. {ECO:0000269|PubMed:26748718}.
METAL 549 549 Zinc 1. {ECO:0000269|PubMed:26748718}.
METAL 561 561 Zinc 2. {ECO:0000269|PubMed:26748718}.
METAL 609 609 Zinc 2. {ECO:0000269|PubMed:26748718}.
METAL 676 676 Zinc 2. {ECO:0000269|PubMed:26748718}.
METAL 680 680 Zinc 2. {ECO:0000269|PubMed:26748718}.
METAL 969 969 Magnesium or manganese 1.
{ECO:0000250|UniProtKB:O67082}.
METAL 1026 1026 Zinc 1. {ECO:0000269|PubMed:26748718}.
METAL 1042 1042 Magnesium or manganese 1.
{ECO:0000250|UniProtKB:O67082}.
METAL 1045 1045 Magnesium or manganese 1.
{ECO:0000250|UniProtKB:O67082,
ECO:0000305|PubMed:15574589}.
METAL 1147 1147 Magnesium or manganese 2.
{ECO:0000250|UniProtKB:O67082}.
METAL 1219 1219 Magnesium or manganese 2.
{ECO:0000250|UniProtKB:O67082}.
METAL 1222 1222 Magnesium or manganese 2.
{ECO:0000250|UniProtKB:O67082,
ECO:0000305|PubMed:15574589}.
SITE 1215 1215 Important for activity. {ECO:0000250}.
MOD_RES 355 355 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 373 373 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 285 353 RERERERHRHRDNRRSPSLERSYKKEYKRSGRSYGLSVVPE
PAGCTPELPGEIIKNTDSWAPPLEIVNH -> S (in
isoform 2).
{ECO:0000303|PubMed:10976766}.
/FTId=VSP_005777.
VAR_SEQ 316 352 Missing (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_012450.
VAR_SEQ 353 353 H -> S (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_012451.
VAR_SEQ 1198 1229 EYAITNDKTKRPVALRTKTLADLLESFIAALY -> VWSIY
LLSNCDCCLLRPSLVFLQTMNEVCSLK (in isoform
3). {ECO:0000303|PubMed:15489334}.
/FTId=VSP_012452.
VAR_SEQ 1230 1374 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_012453.
VARIANT 67 67 P -> T (in dbSNP:rs35342496).
/FTId=VAR_051866.
VARIANT 321 321 S -> L (in dbSNP:rs55656741).
/FTId=VAR_061778.
MUTAGEN 536 536 C->A: Impairs protein folding and
stability; when associated with A-538.
{ECO:0000269|PubMed:26748718}.
MUTAGEN 538 538 C->A: Impairs protein folding and
stability; when associated with A-536.
{ECO:0000269|PubMed:26748718}.
MUTAGEN 561 561 C->A: Impairs protein folding and
stability. {ECO:0000269|PubMed:26748718}.
MUTAGEN 622 623 RF->AA: Abolishes RNase activity.
{ECO:0000269|PubMed:26748718}.
MUTAGEN 676 676 C->A: Impairs protein folding and
stability. {ECO:0000269|PubMed:26748718}.
MUTAGEN 835 836 RR->AA: Abolishes RNase activity.
{ECO:0000269|PubMed:26748718}.
MUTAGEN 914 914 R->M: Impairs RNase activity.
{ECO:0000269|PubMed:26748718}.
MUTAGEN 923 923 R->A: Abolishes RNase activity; when
associated with A-927.
{ECO:0000269|PubMed:26748718}.
MUTAGEN 927 927 Y->A: Abolishes RNase activity; when
associated with A-923.
{ECO:0000269|PubMed:26748718}.
MUTAGEN 938 940 RKK->QQQ: Abolishes RNase activity.
{ECO:0000269|PubMed:26748718}.
MUTAGEN 993 993 E->A,Q: No effect on pri-miRNA processing
activity. {ECO:0000269|PubMed:15574589}.
MUTAGEN 1045 1045 E->Q: Impairs pri-miRNA processing
activity. Abolishes cleavage of the 3'
strand. Abolishes enzyme activity; when
associated with Q-1222.
{ECO:0000269|PubMed:15574589,
ECO:0000269|PubMed:26027739}.
MUTAGEN 1077 1077 V->E: Loss of one DGCR8 interaction site;
no effect on the second DGCR8 interaction
site. {ECO:0000269|PubMed:26748718}.
MUTAGEN 1171 1171 E->A,Q: No effect on pri-miRNA processing
activity. {ECO:0000269|PubMed:15574589}.
MUTAGEN 1194 1194 L->R: Abolishes interaction with DGCR8.
{ECO:0000269|PubMed:26748718}.
MUTAGEN 1222 1222 E->Q: Impairs pri-miRNA processing
activity. Abolishes cleavage of the 5'
strand. Abolishes enzyme activity; when
associated with Q-1045.
{ECO:0000269|PubMed:15574589,
ECO:0000269|PubMed:26027739}.
MUTAGEN 1243 1243 V->D: Abolishes interaction with DGCR8.
{ECO:0000269|PubMed:26748718}.
CONFLICT 166 174 YQYPPGYSH -> RERERTSLE (in Ref. 4;
CAB45133). {ECO:0000305}.
CONFLICT 612 612 L -> P (in Ref. 4; CAB45133).
{ECO:0000305}.
CONFLICT 1020 1020 R -> P (in Ref. 1; AAF80558).
{ECO:0000305}.
CONFLICT 1230 1230 I -> T (in Ref. 1; AAF80558).
{ECO:0000305}.
CONFLICT 1272 1272 L -> R (in Ref. 2; BX647724).
{ECO:0000305}.
STRAND 413 415 {ECO:0000244|PDB:5B16}.
STRAND 420 423 {ECO:0000244|PDB:5B16}.
HELIX 441 451 {ECO:0000244|PDB:5B16}.
TURN 455 457 {ECO:0000244|PDB:5B16}.
HELIX 506 510 {ECO:0000244|PDB:5B16}.
STRAND 531 535 {ECO:0000244|PDB:5B16}.
TURN 547 550 {ECO:0000244|PDB:5B16}.
STRAND 563 565 {ECO:0000244|PDB:5B16}.
TURN 568 570 {ECO:0000244|PDB:5B16}.
STRAND 572 580 {ECO:0000244|PDB:5B16}.
STRAND 582 584 {ECO:0000244|PDB:5B16}.
STRAND 591 593 {ECO:0000244|PDB:5B16}.
STRAND 595 610 {ECO:0000244|PDB:5B16}.
STRAND 618 632 {ECO:0000244|PDB:5B16}.
HELIX 642 652 {ECO:0000244|PDB:5B16}.
TURN 653 656 {ECO:0000244|PDB:5B16}.
STRAND 678 686 {ECO:0000244|PDB:5B16}.
STRAND 694 696 {ECO:0000244|PDB:5B16}.
HELIX 699 708 {ECO:0000244|PDB:5B16}.
STRAND 737 743 {ECO:0000244|PDB:5B16}.
STRAND 751 754 {ECO:0000244|PDB:5B16}.
HELIX 856 860 {ECO:0000244|PDB:5B16}.
HELIX 863 875 {ECO:0000244|PDB:5B16}.
HELIX 876 878 {ECO:0000244|PDB:5B16}.
HELIX 880 883 {ECO:0000244|PDB:5B16}.
HELIX 890 897 {ECO:0000244|PDB:5B16}.
HELIX 910 919 {ECO:0000244|PDB:5B16}.
HELIX 966 986 {ECO:0000244|PDB:5B16}.
HELIX 993 1004 {ECO:0000244|PDB:5B16}.
HELIX 1006 1013 {ECO:0000244|PDB:5B16}.
HELIX 1014 1016 {ECO:0000244|PDB:5B16}.
HELIX 1018 1021 {ECO:0000244|PDB:5B16}.
HELIX 1033 1054 {ECO:0000244|PDB:5B16}.
HELIX 1057 1068 {ECO:0000244|PDB:5B16}.
HELIX 1072 1079 {ECO:0000244|PDB:5B16}.
HELIX 1085 1088 {ECO:0000244|PDB:5B16}.
HELIX 1095 1098 {ECO:0000244|PDB:5B16}.
HELIX 1104 1114 {ECO:0000244|PDB:5B16}.
HELIX 1121 1127 {ECO:0000244|PDB:5B16}.
HELIX 1144 1164 {ECO:0000244|PDB:5B16}.
HELIX 1171 1181 {ECO:0000244|PDB:5B16}.
HELIX 1184 1194 {ECO:0000244|PDB:5B16}.
STRAND 1203 1205 {ECO:0000244|PDB:5B16}.
HELIX 1214 1231 {ECO:0000244|PDB:5B16}.
HELIX 1234 1244 {ECO:0000244|PDB:5B16}.
HELIX 1246 1248 {ECO:0000244|PDB:5B16}.
HELIX 1249 1254 {ECO:0000244|PDB:5B16}.
HELIX 1261 1269 {ECO:0000244|PDB:5B16}.
STRAND 1275 1277 {ECO:0000244|PDB:2KHX}.
STRAND 1283 1291 {ECO:0000244|PDB:5B16}.
STRAND 1292 1294 {ECO:0000244|PDB:2KHX}.
STRAND 1297 1304 {ECO:0000244|PDB:5B16}.
STRAND 1307 1316 {ECO:0000244|PDB:5B16}.
HELIX 1317 1330 {ECO:0000244|PDB:5B16}.
SEQUENCE 1374 AA; 159316 MW; ED6FDEA09F3B8092 CRC64;
MMQGNTCHRM SFHPGRGCPR GRGGHGARPS APSFRPQNLR LLHPQQPPVQ YQYEPPSAPS
TTFSNSPAPN FLPPRPDFVP FPPPMPPSAQ GPLPPCPIRP PFPNHQMRHP FPVPPCFPPM
PPPMPCPNNP PVPGAPPGQG TFPFMMPPPS MPHPPPPPVM PQQVNYQYPP GYSHHNFPPP
SFNSFQNNPS SFLPSANNSS SPHFRHLPPY PLPKAPSERR SPERLKHYDD HRHRDHSHGR
GERHRSLDRR ERGRSPDRRR QDSRYRSDYD RGRTPSRHRS YERSRERERE RHRHRDNRRS
PSLERSYKKE YKRSGRSYGL SVVPEPAGCT PELPGEIIKN TDSWAPPLEI VNHRSPSREK
KRARWEEEKD RWSDNQSSGK DKNYTSIKEK EPEETMPDKN EEEEEELLKP VWIRCTHSEN
YYSSDPMDQV GDSTVVGTSR LRDLYDKFEE ELGSRQEKAK AARPPWEPPK TKLDEDLESS
SESECESDED STCSSSSDSE VFDVIAEIKR KKAHPDRLHD ELWYNDPGQM NDGPLCKCSA
KARRTGIRHS IYPGEEAIKP CRPMTNNAGR LFHYRITVSP PTNFLTDRPT VIEYDDHEYI
FEGFSMFAHA PLTNIPLCKV IRFNIDYTIH FIEEMMPENF CVKGLELFSL FLFRDILELY
DWNLKGPLFE DSPPCCPRFH FMPRFVRFLP DGGKEVLSMH QILLYLLRCS KALVPEEEIA
NMLQWEELEW QKYAEECKGM IVTNPGTKPS SVRIDQLDRE QFNPDVITFP IIVHFGIRPA
QLSYAGDPQY QKLWKSYVKL RHLLANSPKV KQTDKQKLAQ REEALQKIRQ KNTMRREVTV
ELSSQGFWKT GIRSDVCQHA MMLPVLTHHI RYHQCLMHLD KLIGYTFQDR CLLQLAMTHP
SHHLNFGMNP DHARNSLSNC GIRQPKYGDR KVHHMHMRKK GINTLINIMS RLGQDDPTPS
RINHNERLEF LGDAVVEFLT SVHLYYLFPS LEEGGLATYR TAIVQNQHLA MLAKKLELDR
FMLYAHGPDL CRESDLRHAM ANCFEALIGA VYLEGSLEEA KQLFGRLLFN DPDLREVWLN
YPLHPLQLQE PNTDRQLIET SPVLQKLTEF EEAIGVIFTH VRLLARAFTL RTVGFNHLTL
GHNQRMEFLG DSIMQLVATE YLFIHFPDHH EGHLTLLRSS LVNNRTQAKV AEELGMQEYA
ITNDKTKRPV ALRTKTLADL LESFIAALYI DKDLEYVHTF MNVCFFPRLK EFILNQDWND
PKSQLQQCCL TLRTEGKEPD IPLYKTLQTV GPSHARTYTV AVYFKGERIG CGKGPSIQQA
EMGAAMDALE KYNFPQMAHQ KRFIERKYRQ ELKEMRWERE HQEREPDETE DIKK


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