Q8WYQ5 (DGCR8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Microprocessor complex subunit DGCR8

Alternative name(s):
DiGeorge syndrome critical region 8

Gene names

Name:	DGCR8
Synonyms:	C22orf12, DGCRK6
ORF Names:	LP4941

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	773 AA.
Sequence status	Complete.
Protein existence	Evidence 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.13 Ref.14 Ref.16
Cofactor	Binds 1 heme group per homodimer. Ref.16
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.14 Ref.15 Ref.16 Ref.19
Subcellular location	Nucleus. Nucleus › nucleolus. 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.13 Ref.14 Ref.15
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.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	Heme Iron Metal-binding RNA-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	primary miRNA processing Inferred from direct assay Ref.11Ref.10. Source: MGI
Cellular component	cytoplasm Inferred from direct assay. Source: HPA microtubule cytoskeleton Inferred from direct assay. Source: HPA nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Traceable author statement. Source: Reactome
Molecular function	double-stranded RNA binding Inferred from direct assay Ref.22. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction Ref.10. Source: IntAct ribonuclease III activity Traceable author statement. Source: Reactome
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DROSHA	Q9NRR4	4	EBI-528411,EBI-528367

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 773

773

Microprocessor complex subunit DGCR8

PRO_0000079878

Regions

Domain

301 – 334

34

WW

Domain

511 – 578

68

DRBM 1

Domain

620 – 685

66

DRBM 2

Region

1 – 342

342

Necessary for interaction with NCL

Region

1 – 275

275

Necessary for nuclear localization and retention

Region

276 – 751

476

Necessary for heme-binding and pri-miRNA processing

Region

484 – 773

290

Necessary for interaction with DROSHA

Sites

Metal binding

352

1

Iron (heme axial ligand) Probable

Amino acid modifications

Modified residue

92

1

Phosphoserine Ref.18

Modified residue

95

1

Phosphoserine Ref.17 Ref.18

Modified residue

109

1

Phosphoserine Ref.18

Modified residue

271

1

Phosphoserine Ref.18 Ref.20

Modified residue

275

1

Phosphoserine Ref.18 Ref.20

Modified residue

377

1

Phosphoserine Ref.18

Natural variations

Alternative sequence

303 – 304

2

LP → VL in isoform 2.

VSP_003847

Alternative sequence

305 – 773

469

Missing in isoform 2.

VSP_003848

Alternative sequence

536 – 568

33

Missing in isoform 3.

VSP_012707

Natural variant

174

1

I → V.
Corresponds to variant rs35987994 [ dbSNP | Ensembl ].

VAR_050952

Natural variant

725

1

N → D.
Corresponds to variant rs11546015 [ dbSNP | Ensembl ].

VAR_050953

Experimental info

Mutagenesis

352

1

C → A or H: Inhibits heme-binding and dimerization. Ref.14 Ref.16

Mutagenesis

430

1

C → A: Does not inhibit heme-binding and dimerization. Ref.14 Ref.16

Mutagenesis

561 – 565

5

KKLAK → AALAA: Strongly reduces pri-miRNA binding affinity. Ref.14 Ref.22

Mutagenesis

568 – 569

2

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. Ref.14

Mutagenesis

669 – 673

5

KRVGK → AAVGA: Strongly reduces pri-miRNA binding affinity. Ref.14 Ref.22

Mutagenesis

676 – 677

2

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. Ref.14

Sequence conflict

241 – 247

7

DDFDNDV → VCWQPLL in AAF82263. Ref.6

Sequence conflict

274

1

P → L Ref.3

Sequence conflict

343

1

H → Y in BAB15165. Ref.3

Sequence conflict

706

1

V → A in BAB15165. Ref.3

Secondary structure

1

.

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773

Helix Strand Turn

Details...

Beta strand

493 – 495

3

Beta strand

502 – 505

4

Helix

512 – 522

11

Beta strand

529 – 534

6

Beta strand

542 – 548

7

Beta strand

551 – 560

10

Helix

561 – 576

16

Turn

578 – 582

5

Helix

594 – 600

7

Helix

608 – 615

8

Helix

620 – 629

10

Beta strand

631 – 633

3

Beta strand

637 – 640

4

Beta strand

651 – 657

7

Beta strand

660 – 668

9

Helix

669 – 684

16

Helix

691 – 698

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 72D962BBE32890EC	FASTA	773	86,045
	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
	Isoform 2 [UniParc]. Checksum: FA7800BFE8FD462A	FASTA	304	32,831
	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 EPVL
	Isoform 3 [UniParc]. Checksum: 5EEDDD1111DE7DC6	FASTA	740	82,750
	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 NFFECARATL 550 560 570 580 590 600 EILIPDFVKQ TSEEKPKDSE ELEYFNHISI EDSRVYELTS KAGLLSPYQI LHECLKRNHG 610 620 630 640 650 660 MGDTSIKFEV VPGKNQKSEY VMACGKHTVR GWCKNKRVGK QLASQKILQL LHPHVKNWGS 670 680 690 700 710 720 LLRMYGRESS KMVKQETSDK SVIELQQYAK KNKPNLHILS KLQEEMKRLA EEREETRKKP 730 740 KMSIVASAQP GGEPLCTVDV

References

	« Hide 'large scale' referencesShow '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: 12705904] [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: 15461802] [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. , 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: 14702039] [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. , 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: 10591208] [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: 15489334] [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: 17974005] [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. , 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: 15498874] [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: 15589161] [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: 15574589] [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: 15531877] [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: 16751099] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE MICROPROCESSOR COMPLEX, RNA-BINDING.
[13]	"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: 16906129] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[14]	"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: 16963499] [Abstract] Cited for: FUNCTION, INTERACTION WITH DROSHA, RNA-BINDING, SUBCELLULAR LOCATION, MUTAGENESIS OF 568-ALA-ALA-569 AND 676-ALA-SER-677.
[15]	"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: 17765891] [Abstract] Cited for: INTERACTION WITH ILF3; NCL AND DROSHA, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[16]	"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: 17159994] [Abstract] Cited for: FUNCTION, SUBUNIT, HEME-BINDING, MUTAGENESIS OF CYS-352 AND CYS-430.
[17]	"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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92; SER-95; SER-109; SER-271; SER-275 AND SER-377, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"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: 19135890] [Abstract] Cited for: INTERACTION WITH DROSHA.
[20]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271 AND SER-275, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[21]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]	"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: 17704815] [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.
[23]	"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.

IPI

IPI00165970.
IPI00216207.
IPI00549380.

RefSeq

NP_001177255.1. NM_001190326.1.
NP_073557.3. NM_022720.6.

UniGene

Hs.643452.
Hs.713579.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1X47	NMR	-	A	502-586	[»]
2YT4	X-ray	2.60	A	493-720	[»]
3LE4	X-ray	1.70	A	275-353	[»]

ProteinModelPortal

Q8WYQ5.

SMR

Q8WYQ5. Positions 298-352, 492-701.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29261N.

IntAct

Q8WYQ5. 4 interactions.

STRING

Q8WYQ5.

PTM databases

PhosphoSite

Q8WYQ5.

Polymorphism databases

DMDM

23813990.

Proteomic databases

PRIDE

Q8WYQ5.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000351989; ENSP00000263209; ENSG00000128191.

GeneID

54487.

KEGG

hsa:54487.

UCSC

uc002zri.1. human.
uc010grz.1. human.

Organism-specific databases

CTD

54487.

GeneCards

GC22P020070.

H-InvDB

HIX0016249.

HGNC

HGNC:2847. DGCR8.

HPA

HPA019965.

MIM

609030. gene.

neXtProt

NX_Q8WYQ5.

PharmGKB

PA27309.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG12856.

GeneTree

ENSGT00390000015977.

HOVERGEN

HBG051344.

InParanoid

Q8WYQ5.

OMA

KKRRMEE.

OrthoDB

EOG49P9XT.

PhylomeDB

Q8WYQ5.

Enzyme and pathway databases

Reactome

REACT_12472. Regulatory RNA pathways.

Gene expression databases

ArrayExpress

Q8WYQ5.

Bgee

Q8WYQ5.

Genevestigator

Q8WYQ5.

GermOnline

ENSG00000128191. Homo sapiens.

Family and domain databases

InterPro

IPR001159. Ds-RNA-bd.
IPR014720. dsRNA-bd-like.
IPR001202. WW_Rsp5_WWP.
[Graphical view]

Gene3D

G3DSA:3.30.160.20. dsRNA-bd-like. 1 hit.
G3DSA:2.20.70.10. G3DSA:2.20.70.10. 1 hit.

Pfam

PF00035. dsrm. 2 hits.
[Graphical view]

SMART

SM00358. DSRM. 2 hits.
SM00456. WW. 1 hit.
[Graphical view]

PROSITE

PS50137. DS_RBD. 1 hit.
PS01159. WW_DOMAIN_1. False negative.
PS50020. WW_DOMAIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

56807.

SOURCE

Search...

Entry information

Entry name

DGCR8_HUMAN

Accession

Primary (citable) accession number: Q8WYQ5
Secondary accession number(s): B2R8G1 , 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:	January 25, 2012
This is version 105 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.