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Microprocessor complex subunit DGCR8 (DiGeorge syndrome critical region 8)

 DGCR8_HUMAN             Reviewed;         773 AA.
Q8WYQ5; B2R8G1; Q6DCB2; Q6MZE9; Q6Y2L0; Q96G39; Q96GP8; Q9H6L8;
Q9H6T7; Q9NRW2;
10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
30-AUG-2017, entry version 162.
RecName: Full=Microprocessor complex subunit DGCR8;
AltName: Full=DiGeorge syndrome critical region 8;
Name=DGCR8; Synonyms=C22orf12, DGCRK6; ORFNames=LP4941;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
PubMed=12705904; DOI=10.1016/S0006-291X(03)00554-0;
Shiohama A., Sasaki T., Noda S., Minoshima S., Shimizu N.;
"Molecular cloning and expression analysis of a novel gene DGCR8
located in the DiGeorge syndrome chromosomal region.";
Biochem. Biophys. Res. Commun. 304:184-190(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 204-773 (ISOFORM 1).
TISSUE=Hepatoma, and Testis;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
TISSUE=Brain, Muscle, and Testis;
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-247.
TISSUE=Heart;
Gong L., Millas S., Jen J., Yeh E.T.H.;
"Isolation and characterization of a novel human gene deleted in
DiGeorge syndrome.";
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 282-773.
TISSUE=Salivary gland;
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).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 427-773.
PubMed=15498874; DOI=10.1073/pnas.0404089101;
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H.,
Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
Gu J.;
"Large-scale cDNA transfection screening for genes related to cancer
development and progression.";
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
[9]
FUNCTION, AND INTERACTION WITH DROSHA.
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, AND IDENTIFICATION IN THE MICROPROCESSOR COMPLEX.
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, IDENTIFICATION IN THE MICROPROCESSOR COMPLEX, AND
RNA-BINDING.
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).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(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, INTERACTION WITH DROSHA, RNA-BINDING, SUBCELLULAR LOCATION,
AND MUTAGENESIS OF 568-ALA-ALA-569 AND 676-ALA-SER-677.
PubMed=16963499; DOI=10.1093/nar/gkl458;
Yeom K.-H., Lee Y., Han J., Suh M.R., Kim V.N.;
"Characterization of DGCR8/Pasha, the essential cofactor for Drosha in
primary miRNA processing.";
Nucleic Acids Res. 34:4622-4629(2006).
[16]
INTERACTION WITH ILF3; NCL AND DROSHA, SUBCELLULAR LOCATION, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17765891; DOI=10.1016/j.yexcr.2007.07.020;
Shiohama A., Sasaki T., Noda S., Minoshima S., Shimizu N.;
"Nucleolar localization of DGCR8 and identification of eleven DGCR8-
associated proteins.";
Exp. Cell Res. 313:4196-4207(2007).
[17]
FUNCTION, SUBUNIT, COFACTOR, AND MUTAGENESIS OF CYS-352 AND CYS-430.
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).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271; SER-275 AND
SER-377, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[20]
INTERACTION WITH DROSHA.
PubMed=19135890; DOI=10.1016/j.cell.2008.10.053;
Han J., Pedersen J.S., Kwon S.C., Belair C.D., Kim Y.-K., Yeom K.-H.,
Yang W.-Y., Haussler D., Blelloch R., Kim V.N.;
"Posttranscriptional crossregulation between Drosha and DGCR8.";
Cell 136:75-84(2009).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271 AND SER-275, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[23]
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).
[24]
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).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95; THR-371 AND SER-377,
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).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95; SER-275; SER-373 AND
SER-377, 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).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35 AND SER-92, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[28]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-707, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[29]
FUNCTION, INTERACTION WITH DROSHA, AND SUBUNIT.
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).
[30]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-500 AND LYS-707, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[31]
FUNCTION, AND RNA-BINDING.
PubMed=25799998; DOI=10.1038/nature14281;
Alarcon C.R., Lee H., Goodarzi H., Halberg N., Tavazoie S.F.;
"N6-methyladenosine marks primary microRNAs for processing.";
Nature 519:482-485(2015).
[32]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-424 AND LYS-500, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[33]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 493-720, RNA-BINDING, AND
MUTAGENESIS OF 561-LYS--LYS-565 AND 669-LYS--LYS-673.
PubMed=17704815; DOI=10.1038/nsmb1294;
Sohn S.Y., Bae W.J., Kim J.J., Yeom K.-H., Kim V.N., Cho Y.;
"Crystal structure of human DGCR8 core.";
Nat. Struct. Mol. Biol. 14:847-853(2007).
[34]
STRUCTURE BY NMR OF 502-586.
RIKEN structural genomics initiative (RSGI);
"Solution structure of DSRM domain in DGCR8 protein.";
Submitted (NOV-2005) to the PDB data bank.
[35]
X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 728-750 IN COMPLEX WITH
DROSHA, FUNCTION, INTERACTION WITH DROSHA, AND SUBUNIT.
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: Component of the microprocessor complex that acts as a
RNA- and heme-binding protein 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, DGCR8 function as a
molecular anchor necessary for the recognition of pri-miRNA at
dsRNA-ssRNA junction and directs DROSHA to cleave 11 bp away form
the junction to release hairpin-shaped pre-miRNAs that are
subsequently cut by the cytoplasmic DICER to generate mature
miRNAs (PubMed:26027739, PubMed:26748718). The heme-bound DGCR8
dimer binds pri-miRNAs as a cooperative trimer (of dimers) and is
active in triggering pri-miRNA cleavage, whereas the heme-free
DGCR8 monomer binds pri-miRNAs as a dimer and is much less active.
Both double-stranded and single-stranded regions of a pri-miRNA
are required for its binding (PubMed:15531877, PubMed:15574589,
PubMed:15589161, PubMed:16751099, PubMed:16906129,
PubMed:16963499, PubMed:17159994). Specifically recognizes and
binds N6-methyladenosine (m6A)-containing pri-miRNAs, a
modification required for pri-miRNAs processing (PubMed:25799998).
Involved in the silencing of embryonic stem cell self-renewal (By
similarity). {ECO:0000250|UniProtKB:Q9EQM6,
ECO:0000269|PubMed:15531877, ECO:0000269|PubMed:15574589,
ECO:0000269|PubMed:15589161, ECO:0000269|PubMed:16751099,
ECO:0000269|PubMed:16906129, ECO:0000269|PubMed:16963499,
ECO:0000269|PubMed:17159994, ECO:0000269|PubMed:25799998,
ECO:0000269|PubMed:26027739, ECO:0000269|PubMed:26748718}.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
Evidence={ECO:0000269|PubMed:17159994};
Note=Binds 1 heme group per homodimer.
{ECO:0000269|PubMed:17159994};
-!- SUBUNIT: Monomer; in absence of heme. Homodimer; the association
with heme promotes its dimerization (PubMed:17159994). 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:19135890, 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 ILF3, NCL and
DROSHA (PubMed:17765891). {ECO:0000269|PubMed:15531877,
ECO:0000269|PubMed:15574589, ECO:0000269|PubMed:15589161,
ECO:0000269|PubMed:16751099, ECO:0000269|PubMed:16963499,
ECO:0000269|PubMed:17159994, ECO:0000269|PubMed:17765891,
ECO:0000269|PubMed:19135890, ECO:0000269|PubMed:26748718}.
-!- INTERACTION:
Q9NRR4:DROSHA; NbExp=8; IntAct=EBI-528411, EBI-528367;
P50222:MEOX2; NbExp=3; IntAct=EBI-528411, EBI-748397;
Q96SB4:SRPK1; NbExp=3; IntAct=EBI-528411, EBI-539478;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16906129,
ECO:0000269|PubMed:16963499, ECO:0000269|PubMed:17159994,
ECO:0000269|PubMed:22118463}. Nucleus, nucleolus
{ECO:0000269|PubMed:17159994}. Note=Colocalizes with nucleolin and
DROSHA in the nucleolus. Mostly detected in the nucleolus as
electron-dense granular patches around the fibrillar center (FC)
and granular component (GC). Also detected in the nucleoplasm as
small foci adjacent to splicing speckles near the chromatin
structure. Localized with DROSHA in GW bodies (GWBs), also known
as P-bodies (PubMed:17159994).
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8WYQ5-1; Sequence=Displayed;
Name=2;
IsoId=Q8WYQ5-2; Sequence=VSP_003847, VSP_003848;
Name=3;
IsoId=Q8WYQ5-3; Sequence=VSP_012707;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
{ECO:0000269|PubMed:12705904}.
-!- DOMAIN: Both DRBM domains are required for efficient binding to
pri-miRNA. The region between residues 276 and 498 has an
autoinhibitory function on pri-miRNA processing activity.
-!- SEQUENCE CAUTION:
Sequence=AAO86726.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAB15165.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAB15238.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB050770; BAB83032.1; -; Genomic_DNA.
EMBL; CR456356; CAG30242.1; -; mRNA.
EMBL; AK025539; BAB15165.1; ALT_INIT; mRNA.
EMBL; AK025780; BAB15238.1; ALT_INIT; mRNA.
EMBL; AK313357; BAG36158.1; -; mRNA.
EMBL; AC006547; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC009323; AAH09323.2; -; mRNA.
EMBL; BC009984; AAH09984.1; -; mRNA.
EMBL; BC078147; AAH78147.1; -; mRNA.
EMBL; AF165527; AAF82263.1; -; mRNA.
EMBL; BX649187; CAE46205.2; -; mRNA.
EMBL; AY189282; AAO86726.1; ALT_INIT; mRNA.
CCDS; CCDS13773.1; -. [Q8WYQ5-1]
CCDS; CCDS54501.1; -. [Q8WYQ5-3]
RefSeq; NP_001177255.1; NM_001190326.1. [Q8WYQ5-3]
RefSeq; NP_073557.3; NM_022720.6. [Q8WYQ5-1]
UniGene; Hs.643452; -.
UniGene; Hs.713579; -.
PDB; 1X47; NMR; -; A=502-586.
PDB; 2YT4; X-ray; 2.60 A; A=493-720.
PDB; 3LE4; X-ray; 1.70 A; A=275-353.
PDB; 5B16; X-ray; 3.20 A; B/C=728-750.
PDBsum; 1X47; -.
PDBsum; 2YT4; -.
PDBsum; 3LE4; -.
PDBsum; 5B16; -.
ProteinModelPortal; Q8WYQ5; -.
SMR; Q8WYQ5; -.
BioGrid; 119986; 155.
DIP; DIP-29261N; -.
IntAct; Q8WYQ5; 25.
MINT; MINT-3048369; -.
STRING; 9606.ENSP00000263209; -.
iPTMnet; Q8WYQ5; -.
PhosphoSitePlus; Q8WYQ5; -.
BioMuta; DGCR8; -.
DMDM; 23813990; -.
EPD; Q8WYQ5; -.
MaxQB; Q8WYQ5; -.
PaxDb; Q8WYQ5; -.
PeptideAtlas; Q8WYQ5; -.
PRIDE; Q8WYQ5; -.
DNASU; 54487; -.
Ensembl; ENST00000351989; ENSP00000263209; ENSG00000128191. [Q8WYQ5-1]
Ensembl; ENST00000383024; ENSP00000372488; ENSG00000128191. [Q8WYQ5-3]
Ensembl; ENST00000407755; ENSP00000384726; ENSG00000128191. [Q8WYQ5-3]
GeneID; 54487; -.
KEGG; hsa:54487; -.
UCSC; uc002zri.4; human. [Q8WYQ5-1]
CTD; 54487; -.
DisGeNET; 54487; -.
GeneCards; DGCR8; -.
GeneCards; MIR1306; -.
GeneCards; MIR3618; -.
GeneReviews; DGCR8; -.
HGNC; HGNC:2847; DGCR8.
MIM; 609030; gene.
neXtProt; NX_Q8WYQ5; -.
OpenTargets; ENSG00000128191; -.
PharmGKB; PA27309; -.
eggNOG; KOG4334; Eukaryota.
eggNOG; ENOG410XS9I; LUCA.
GeneTree; ENSGT00390000015977; -.
HOVERGEN; HBG051344; -.
InParanoid; Q8WYQ5; -.
KO; K18419; -.
OMA; METYESP; -.
OrthoDB; EOG091G09GA; -.
PhylomeDB; Q8WYQ5; -.
TreeFam; TF324256; -.
Reactome; R-HSA-203927; MicroRNA (miRNA) biogenesis.
ChiTaRS; DGCR8; human.
EvolutionaryTrace; Q8WYQ5; -.
GeneWiki; DGCR8_(gene); -.
GenomeRNAi; 54487; -.
PRO; PR:Q8WYQ5; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000128191; -.
ExpressionAtlas; Q8WYQ5; baseline and differential.
Genevisible; Q8WYQ5; HS.
GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
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:MGI.
GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
GO; GO:0020037; F:heme binding; IDA:BHF-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0070878; F:primary miRNA binding; IDA:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
GO; GO:0010586; P:miRNA metabolic process; TAS:Reactome.
GO; GO:0031053; P:primary miRNA processing; IDA:BHF-UCL.
GO; GO:0072091; P:regulation of stem cell proliferation; IEA:Ensembl.
GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IEA:GOC.
CDD; cd00201; WW; 1.
InterPro; IPR014720; dsRBD_dom.
InterPro; IPR001202; WW_dom.
Pfam; PF00035; dsrm; 2.
SMART; SM00358; DSRM; 2.
SMART; SM00456; WW; 1.
SUPFAM; SSF51045; SSF51045; 1.
PROSITE; PS50137; DS_RBD; 1.
PROSITE; PS50020; WW_DOMAIN_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Heme; Iron;
Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; RNA-binding; Ubl conjugation.
CHAIN 1 773 Microprocessor complex subunit DGCR8.
/FTId=PRO_0000079878.
DOMAIN 301 334 WW. {ECO:0000255|PROSITE-
ProRule:PRU00224}.
DOMAIN 511 578 DRBM 1. {ECO:0000255|PROSITE-
ProRule:PRU00266}.
DOMAIN 620 685 DRBM 2. {ECO:0000255|PROSITE-
ProRule:PRU00266}.
REGION 1 342 Necessary for interaction with NCL.
{ECO:0000269|PubMed:17765891}.
REGION 1 275 Necessary for nuclear localization and
retention.
REGION 276 751 Necessary for heme-binding and pri-miRNA
processing.
REGION 701 773 Interaction with DROSHA.
{ECO:0000269|PubMed:26748718}.
METAL 352 352 Iron (heme axial ligand).
{ECO:0000305|PubMed:17159994}.
MOD_RES 35 35 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 92 92 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 95 95 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 271 271 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 275 275 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 279 279 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9EQM6}.
MOD_RES 371 371 Phosphothreonine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 373 373 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 377 377 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
CROSSLNK 424 424 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 500 500 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 707 707 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297}.
VAR_SEQ 303 304 LP -> VL (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_003847.
VAR_SEQ 305 773 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_003848.
VAR_SEQ 536 568 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_012707.
VARIANT 174 174 I -> V (in dbSNP:rs35987994).
/FTId=VAR_050952.
VARIANT 725 725 N -> D (in dbSNP:rs11546015).
/FTId=VAR_050953.
MUTAGEN 352 352 C->A,H: Inhibits heme-binding and
dimerization.
{ECO:0000269|PubMed:17159994}.
MUTAGEN 430 430 C->A: Does not inhibit heme-binding and
dimerization.
{ECO:0000269|PubMed:17159994}.
MUTAGEN 561 565 KKLAK->AALAA: Strongly reduces pri-miRNA
binding affinity.
{ECO:0000269|PubMed:17704815}.
MUTAGEN 568 569 AA->KK: Reduces pri-miRNA binding
affinity and pri-miRNA processing
activity. Does not inhibit interaction
with DROSHA. When associated with A-676
and S-677, strongly reduces binding
affinity and pri-miRNA processing
activity. {ECO:0000269|PubMed:16963499}.
MUTAGEN 669 673 KRVGK->AAVGA: Strongly reduces pri-miRNA
binding affinity.
{ECO:0000269|PubMed:17704815}.
MUTAGEN 676 677 AS->KK: Reduces pri-miRNA binding
affinity and pri-miRNA processing
activity. Slightly inhibits interaction
with DROSHA. When associated with A-568
and A-568, strongly reduces binding
affinity and pri-miRNA processing
activity. {ECO:0000269|PubMed:16963499}.
CONFLICT 241 247 DDFDNDV -> VCWQPLL (in Ref. 6; AAF82263).
{ECO:0000305}.
CONFLICT 274 274 P -> L (in Ref. 3; BAB15165).
{ECO:0000305}.
CONFLICT 343 343 H -> Y (in Ref. 3; BAB15165).
{ECO:0000305}.
CONFLICT 706 706 V -> A (in Ref. 3; BAB15165).
{ECO:0000305}.
STRAND 307 311 {ECO:0000244|PDB:3LE4}.
STRAND 315 321 {ECO:0000244|PDB:3LE4}.
TURN 322 325 {ECO:0000244|PDB:3LE4}.
STRAND 326 330 {ECO:0000244|PDB:3LE4}.
TURN 340 342 {ECO:0000244|PDB:3LE4}.
HELIX 347 349 {ECO:0000244|PDB:3LE4}.
STRAND 493 495 {ECO:0000244|PDB:2YT4}.
STRAND 502 505 {ECO:0000244|PDB:2YT4}.
HELIX 512 522 {ECO:0000244|PDB:2YT4}.
STRAND 529 534 {ECO:0000244|PDB:2YT4}.
STRAND 536 539 {ECO:0000244|PDB:1X47}.
STRAND 542 548 {ECO:0000244|PDB:2YT4}.
STRAND 551 560 {ECO:0000244|PDB:2YT4}.
HELIX 561 576 {ECO:0000244|PDB:2YT4}.
TURN 578 582 {ECO:0000244|PDB:2YT4}.
HELIX 594 600 {ECO:0000244|PDB:2YT4}.
HELIX 608 615 {ECO:0000244|PDB:2YT4}.
HELIX 620 629 {ECO:0000244|PDB:2YT4}.
STRAND 631 633 {ECO:0000244|PDB:2YT4}.
STRAND 637 640 {ECO:0000244|PDB:2YT4}.
STRAND 651 657 {ECO:0000244|PDB:2YT4}.
STRAND 660 668 {ECO:0000244|PDB:2YT4}.
HELIX 669 684 {ECO:0000244|PDB:2YT4}.
HELIX 691 698 {ECO:0000244|PDB:2YT4}.
HELIX 728 749 {ECO:0000244|PDB:5B16}.
SEQUENCE 773 AA; 86045 MW; 72D962BBE32890EC CRC64;
METDESPSPL PCGPAGEAVM ESRARPFQAL PREQSPPPPL QTSSGAEVMD VGSGGDGQSE
LPAEDPFNFY GASLLSKGSF SKGRLLIDPN CSGHSPRTAR HAPAVRKFSP DLKLLKDVKI
SVSFTESCRS KDRKVLYTGA ERDVRAECGL LLSPVSGDVH ACPFGGSVGD GVGIGGESAD
KKDEENELDQ EKRVEYAVLD ELEDFTDNLE LDEEGAGGFT AKAIVQRDRV DEEALNFPYE
DDFDNDVDAL LEEGLCAPKK RRTEEKYGGD SDHPSDGETS VQPMMTKIKT VLKSRGRPPT
EPLPDGWIMT FHNSGVPVYL HRESRVVTWS RPYFLGTGSI RKHDPPLSSI PCLHYKKMKD
NEEREQSSDL TPSGDVSPVK PLSRSAELEF PLDEPDSMGA DPGPPDEKDP LGAEAAPGAL
GQVKAKVEVC KDESVDLEEF RSYLEKRFDF EQVTVKKFRT WAERRQFNRE MKRKQAESER
PILPANQKLI TLSVQDAPTK KEFVINPNGK SEVCILHEYM QRVLKVRPVY NFFECENPSE
PFGASVTIDG VTYGSGTASS KKLAKNKAAR ATLEILIPDF VKQTSEEKPK DSEELEYFNH
ISIEDSRVYE LTSKAGLLSP YQILHECLKR NHGMGDTSIK FEVVPGKNQK SEYVMACGKH
TVRGWCKNKR VGKQLASQKI LQLLHPHVKN WGSLLRMYGR ESSKMVKQET SDKSVIELQQ
YAKKNKPNLH ILSKLQEEMK RLAEEREETR KKPKMSIVAS AQPGGEPLCT VDV


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