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Q8WYQ5 (DGCR8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Microprocessor complex subunit DGCR8
Alternative name(s):
DiGeorge syndrome critical region 8
Gene names
Name:DGCR8
Synonyms:C22orf12, DGCRK6
ORF Names:LP4941
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length773 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. 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. Involved in the silencing of embryonic stem cells self-renewal. Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.17

Cofactor

Binds 1 heme group per homodimer. Ref.17

Subunit structure

Monomer; in absence of heme. Homodimer; the association with heme promotes its dimerization. Component of the microprocessor complex, or pri-miRNA processing protein complex, which is composed of DGCR8 (heme-free or heme-bound forms) and DROSHA. The microprocessor complex may contain multiple subunit of DGCR8 and DROSHA. Interacts with ILF3, NCL and DROSHA. Ref.9 Ref.10 Ref.11 Ref.12 Ref.15 Ref.16 Ref.17 Ref.20

Subcellular location

Nucleus. Nucleusnucleolus. 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. Ref.14 Ref.15 Ref.16

Tissue specificity

Ubiquitously expressed. Ref.1

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 similarities

Contains 2 DRBM (double-stranded RNA-binding) domains.

Contains 1 WW domain.

Sequence caution

The sequence AAO86726.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAB15165.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAB15238.1 differs from that shown. Reason: Erroneous initiation.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DROSHAQ9NRR45EBI-528411,EBI-528367
SRPK1Q96SB43EBI-528411,EBI-539478

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8WYQ5-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8WYQ5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     303-304: LP → VL
     305-773: Missing.
Isoform 3 (identifier: Q8WYQ5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     536-568: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 773773Microprocessor complex subunit DGCR8
PRO_0000079878

Regions

Domain301 – 33434WW
Domain511 – 57868DRBM 1
Domain620 – 68566DRBM 2
Region1 – 342342Necessary for interaction with NCL
Region1 – 275275Necessary for nuclear localization and retention
Region276 – 751476Necessary for heme-binding and pri-miRNA processing
Region484 – 773290Necessary for interaction with DROSHA

Sites

Metal binding3521Iron (heme axial ligand) Probable

Amino acid modifications

Modified residue951Phosphoserine Ref.18 Ref.24
Modified residue2711Phosphoserine Ref.19 Ref.21
Modified residue2751Phosphoserine Ref.19 Ref.21
Modified residue3711Phosphothreonine Ref.24
Modified residue3771Phosphoserine Ref.19 Ref.24

Natural variations

Alternative sequence303 – 3042LP → VL in isoform 2.
VSP_003847
Alternative sequence305 – 773469Missing in isoform 2.
VSP_003848
Alternative sequence536 – 56833Missing in isoform 3.
VSP_012707
Natural variant1741I → V.
Corresponds to variant rs35987994 [ dbSNP | Ensembl ].
VAR_050952
Natural variant7251N → D.
Corresponds to variant rs11546015 [ dbSNP | Ensembl ].
VAR_050953

Experimental info

Mutagenesis3521C → A or H: Inhibits heme-binding and dimerization. Ref.15 Ref.17
Mutagenesis4301C → A: Does not inhibit heme-binding and dimerization. Ref.15 Ref.17
Mutagenesis561 – 5655KKLAK → AALAA: Strongly reduces pri-miRNA binding affinity. Ref.15 Ref.25
Mutagenesis568 – 5692AA → 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. Ref.15
Mutagenesis669 – 6735KRVGK → AAVGA: Strongly reduces pri-miRNA binding affinity. Ref.15 Ref.25
Mutagenesis676 – 6772AS → 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. Ref.15
Sequence conflict241 – 2477DDFDNDV → VCWQPLL in AAF82263. Ref.6
Sequence conflict2741P → L Ref.3
Sequence conflict3431H → Y in BAB15165. Ref.3
Sequence conflict7061V → A in BAB15165. Ref.3

Secondary structure

............................................. 773
Helix Strand Turn

Details...

Sequences

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

Last modified March 1, 2002. Version 1.
Checksum: 72D962BBE32890EC

FASTA77386,045
        10         20         30         40         50         60 
METDESPSPL PCGPAGEAVM ESRARPFQAL PREQSPPPPL QTSSGAEVMD VGSGGDGQSE 

        70         80         90        100        110        120 
LPAEDPFNFY GASLLSKGSF SKGRLLIDPN CSGHSPRTAR HAPAVRKFSP DLKLLKDVKI 

       130        140        150        160        170        180 
SVSFTESCRS KDRKVLYTGA ERDVRAECGL LLSPVSGDVH ACPFGGSVGD GVGIGGESAD 

       190        200        210        220        230        240 
KKDEENELDQ EKRVEYAVLD ELEDFTDNLE LDEEGAGGFT AKAIVQRDRV DEEALNFPYE 

       250        260        270        280        290        300 
DDFDNDVDAL LEEGLCAPKK RRTEEKYGGD SDHPSDGETS VQPMMTKIKT VLKSRGRPPT 

       310        320        330        340        350        360 
EPLPDGWIMT FHNSGVPVYL HRESRVVTWS RPYFLGTGSI RKHDPPLSSI PCLHYKKMKD 

       370        380        390        400        410        420 
NEEREQSSDL TPSGDVSPVK PLSRSAELEF PLDEPDSMGA DPGPPDEKDP LGAEAAPGAL 

       430        440        450        460        470        480 
GQVKAKVEVC KDESVDLEEF RSYLEKRFDF EQVTVKKFRT WAERRQFNRE MKRKQAESER 

       490        500        510        520        530        540 
PILPANQKLI TLSVQDAPTK KEFVINPNGK SEVCILHEYM QRVLKVRPVY NFFECENPSE 

       550        560        570        580        590        600 
PFGASVTIDG VTYGSGTASS KKLAKNKAAR ATLEILIPDF VKQTSEEKPK DSEELEYFNH 

       610        620        630        640        650        660 
ISIEDSRVYE LTSKAGLLSP YQILHECLKR NHGMGDTSIK FEVVPGKNQK SEYVMACGKH 

       670        680        690        700        710        720 
TVRGWCKNKR VGKQLASQKI LQLLHPHVKN WGSLLRMYGR ESSKMVKQET SDKSVIELQQ 

       730        740        750        760        770 
YAKKNKPNLH ILSKLQEEMK RLAEEREETR KKPKMSIVAS AQPGGEPLCT VDV 

« Hide

Isoform 2 [UniParc].

Checksum: FA7800BFE8FD462A
Show »

FASTA30432,831
Isoform 3 [UniParc].

Checksum: 5EEDDD1111DE7DC6
Show »

FASTA74082,750

References

« Hide 'large scale' references
[1]"Molecular cloning and expression analysis of a novel gene DGCR8 located in the DiGeorge syndrome chromosomal region."
Shiohama A., Sasaki T., Noda S., Minoshima S., Shimizu N.
Biochem. Biophys. Res. Commun. 304:184-190(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), TISSUE SPECIFICITY.
[2]"A genome annotation-driven approach to cloning the human ORFeome."
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.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 204-773 (ISOFORM 1).
Tissue: Hepatoma and Testis.
[4]"The DNA sequence of human chromosome 22."
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. expand/collapse author list , 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.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORMS 1; 2 AND 3).
Tissue: Brain, Muscle and Testis.
[6]"Isolation and characterization of a novel human gene deleted in DiGeorge syndrome."
Gong L., Millas S., Jen J., Yeh E.T.H.
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-247.
Tissue: Heart.
[7]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 282-773.
Tissue: Salivary gland.
[8]"Large-scale cDNA transfection screening for genes related to cancer development and progression."
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. expand/collapse author list , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 427-773.
[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 DROSHA.
[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.
[11]"The microprocessor complex mediates the genesis of microRNAs."
Gregory R.I., Yan K.-P., Amuthan G., Chendrimada T., Doratotaj B., Cooch N., Shiekhattar R.
Nature 432:235-240(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE MICROPROCESSOR COMPLEX.
[12]"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, RNA-BINDING.
[13]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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]"Characterization of DGCR8/Pasha, the essential cofactor for Drosha in primary miRNA processing."
Yeom K.-H., Lee Y., Han J., Suh M.R., Kim V.N.
Nucleic Acids Res. 34:4622-4629(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH DROSHA, RNA-BINDING, SUBCELLULAR LOCATION, MUTAGENESIS OF 568-ALA-ALA-569 AND 676-ALA-SER-677.
[16]"Nucleolar localization of DGCR8 and identification of eleven DGCR8-associated proteins."
Shiohama A., Sasaki T., Noda S., Minoshima S., Shimizu N.
Exp. Cell Res. 313:4196-4207(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ILF3; NCL AND DROSHA, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[17]"Heme is involved in microRNA processing."
Faller M., Matsunaga M., Yin S., Loo J.A., Guo F.
Nat. Struct. Mol. Biol. 14:23-29(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, HEME-BINDING, MUTAGENESIS OF CYS-352 AND CYS-430.
[18]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271; SER-275 AND SER-377, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"Posttranscriptional crossregulation between Drosha and DGCR8."
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.
Cell 136:75-84(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DROSHA.
[21]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271 AND SER-275, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[22]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[23]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"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-95; THR-371 AND SER-377, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"Crystal structure of human DGCR8 core."
Sohn S.Y., Bae W.J., Kim J.J., Yeom K.-H., Kim V.N., Cho Y.
Nat. Struct. Mol. Biol. 14:847-853(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 493-720, RNA-BINDING, MUTAGENESIS OF 561-LYS--LYS-565 AND 669-LYS--LYS-673.
[26]"Solution structure of DSRM domain in DGCR8 protein."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 502-586.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB050770 Genomic DNA. Translation: BAB83032.1.
CR456356 mRNA. Translation: CAG30242.1.
AK025539 mRNA. Translation: BAB15165.1. Different initiation.
AK025780 mRNA. Translation: BAB15238.1. Different initiation.
AK313357 mRNA. Translation: BAG36158.1.
AC006547 Genomic DNA. No translation available.
BC009323 mRNA. Translation: AAH09323.2.
BC009984 mRNA. Translation: AAH09984.1.
BC078147 mRNA. Translation: AAH78147.1.
AF165527 mRNA. Translation: AAF82263.1.
BX649187 mRNA. Translation: CAE46205.2.
AY189282 mRNA. Translation: AAO86726.1. Different initiation.
CCDSCCDS13773.1. [Q8WYQ5-1]
CCDS54501.1. [Q8WYQ5-3]
RefSeqNP_001177255.1. NM_001190326.1. [Q8WYQ5-3]
NP_073557.3. NM_022720.6. [Q8WYQ5-1]
UniGeneHs.643452.
Hs.713579.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1X47NMR-A502-586[»]
2YT4X-ray2.60A493-720[»]
3LE4X-ray1.70A275-353[»]
ProteinModelPortalQ8WYQ5.
SMRQ8WYQ5. Positions 298-352, 492-701.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119986. 24 interactions.
DIPDIP-29261N.
IntActQ8WYQ5. 3 interactions.
MINTMINT-3048369.

PTM databases

PhosphoSiteQ8WYQ5.

Polymorphism databases

DMDM23813990.

Proteomic databases

MaxQBQ8WYQ5.
PaxDbQ8WYQ5.
PRIDEQ8WYQ5.

Protocols and materials databases

DNASU54487.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000351989; ENSP00000263209; ENSG00000128191. [Q8WYQ5-1]
ENST00000383024; ENSP00000372488; ENSG00000128191. [Q8WYQ5-3]
ENST00000407755; ENSP00000384726; ENSG00000128191. [Q8WYQ5-3]
GeneID54487.
KEGGhsa:54487.
UCSCuc002zri.3. human. [Q8WYQ5-1]
uc010grz.3. human. [Q8WYQ5-3]

Organism-specific databases

CTD54487.
GeneCardsGC22P020070.
GeneReviewsDGCR8.
HGNCHGNC:2847. DGCR8.
HPAHPA019965.
MIM609030. gene.
neXtProtNX_Q8WYQ5.
PharmGKBPA27309.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG300512.
HOVERGENHBG051344.
InParanoidQ8WYQ5.
OMAIPVYLHR.
OrthoDBEOG75J0MG.
PhylomeDBQ8WYQ5.
TreeFamTF324256.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ8WYQ5.
BgeeQ8WYQ5.
GenevestigatorQ8WYQ5.

Family and domain databases

Gene3D3.30.160.20. 1 hit.
InterProIPR014720. dsRNA-bd_dom.
IPR001202. WW_dom.
[Graphical view]
PfamPF00035. dsrm. 2 hits.
[Graphical view]
SMARTSM00358. DSRM. 2 hits.
SM00456. WW. 1 hit.
[Graphical view]
SUPFAMSSF51045. SSF51045. 1 hit.
PROSITEPS50137. DS_RBD. 1 hit.
PS50020. WW_DOMAIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDGCR8. human.
EvolutionaryTraceQ8WYQ5.
GeneWikiDGCR8_(gene).
GenomeRNAi54487.
NextBio56807.
PROQ8WYQ5.
SOURCESearch...

Entry information

Entry nameDGCR8_HUMAN
AccessionPrimary (citable) accession number: Q8WYQ5
Secondary accession number(s): B2R8G1 expand/collapse secondary AC list , Q6DCB2, Q6MZE9, Q6Y2L0, Q96G39, Q96GP8, Q9H6L8, Q9H6T7, Q9NRW2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: March 1, 2002
Last modified: July 9, 2014
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM