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Q8WYQ5

- DGCR8_HUMAN

UniProt

Q8WYQ5 - DGCR8_HUMAN

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Protein

Microprocessor complex subunit DGCR8

Gene

DGCR8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.7 Publications

Cofactori

Binds 1 heme group per homodimer.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi352 – 3521Iron (heme axial ligand)Curated

GO - Molecular functioni

  1. double-stranded RNA binding Source: UniProtKB
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. gene expression Source: Reactome
  2. primary miRNA processing Source: MGI
Complete GO annotation...

Keywords - Ligandi

Heme, Iron, Metal-binding, RNA-binding

Enzyme and pathway databases

ReactomeiREACT_12417. MicroRNA (miRNA) biogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Microprocessor complex subunit DGCR8
Alternative name(s):
DiGeorge syndrome critical region 8
Gene namesi
Name:DGCR8
Synonyms:C22orf12, DGCRK6
ORF Names:LP4941
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:2847. DGCR8.

Subcellular locationi

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.

GO - Cellular componenti

  1. cytoplasm Source: LIFEdb
  2. microtubule cytoskeleton Source: HPA
  3. nucleoplasm Source: Reactome
  4. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi352 – 3521C → A or H: Inhibits heme-binding and dimerization. 1 Publication
Mutagenesisi430 – 4301C → A: Does not inhibit heme-binding and dimerization. 1 Publication
Mutagenesisi561 – 5655KKLAK → AALAA: Strongly reduces pri-miRNA binding affinity. 1 Publication
Mutagenesisi568 – 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. 1 Publication
Mutagenesisi669 – 6735KRVGK → AAVGA: Strongly reduces pri-miRNA binding affinity. 1 Publication
Mutagenesisi676 – 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. 1 Publication

Organism-specific databases

PharmGKBiPA27309.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 773773Microprocessor complex subunit DGCR8PRO_0000079878Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei95 – 951Phosphoserine2 Publications
Modified residuei271 – 2711Phosphoserine2 Publications
Modified residuei275 – 2751Phosphoserine2 Publications
Modified residuei371 – 3711Phosphothreonine1 Publication
Modified residuei377 – 3771Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8WYQ5.
PaxDbiQ8WYQ5.
PRIDEiQ8WYQ5.

PTM databases

PhosphoSiteiQ8WYQ5.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiQ8WYQ5.
ExpressionAtlasiQ8WYQ5. baseline and differential.
GenevestigatoriQ8WYQ5.

Organism-specific databases

HPAiHPA019965.

Interactioni

Subunit structurei

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.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DROSHAQ9NRR47EBI-528411,EBI-528367
SRPK1Q96SB43EBI-528411,EBI-539478

Protein-protein interaction databases

BioGridi119986. 30 interactions.
DIPiDIP-29261N.
IntActiQ8WYQ5. 4 interactions.
MINTiMINT-3048369.

Structurei

Secondary structure

1
773
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi307 – 3115
Beta strandi315 – 3217
Turni322 – 3254
Beta strandi326 – 3305
Turni340 – 3423
Helixi347 – 3493
Beta strandi493 – 4953
Beta strandi502 – 5054
Helixi512 – 52211
Beta strandi529 – 5346
Beta strandi536 – 5394
Beta strandi542 – 5487
Beta strandi551 – 56010
Helixi561 – 57616
Turni578 – 5825
Helixi594 – 6007
Helixi608 – 6158
Helixi620 – 62910
Beta strandi631 – 6333
Beta strandi637 – 6404
Beta strandi651 – 6577
Beta strandi660 – 6689
Helixi669 – 68416
Helixi691 – 6988

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X47NMR-A502-586[»]
2YT4X-ray2.60A493-720[»]
3LE4X-ray1.70A275-353[»]
ProteinModelPortaliQ8WYQ5.
SMRiQ8WYQ5. Positions 298-352, 492-701.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8WYQ5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini301 – 33434WWPROSITE-ProRule annotationAdd
BLAST
Domaini511 – 57868DRBM 1PROSITE-ProRule annotationAdd
BLAST
Domaini620 – 68566DRBM 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 342342Necessary for interaction with NCLAdd
BLAST
Regioni1 – 275275Necessary for nuclear localization and retentionAdd
BLAST
Regioni276 – 751476Necessary for heme-binding and pri-miRNA processingAdd
BLAST
Regioni484 – 773290Necessary for interaction with DROSHAAdd
BLAST

Domaini

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 similaritiesi

Contains 2 DRBM (double-stranded RNA-binding) domains.PROSITE-ProRule annotation
Contains 1 WW domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG300512.
GeneTreeiENSGT00390000015977.
HOVERGENiHBG051344.
InParanoidiQ8WYQ5.
KOiK18419.
OMAiIPVYLHR.
OrthoDBiEOG75J0MG.
PhylomeDBiQ8WYQ5.
TreeFamiTF324256.

Family and domain databases

Gene3Di3.30.160.20. 1 hit.
InterProiIPR014720. dsRNA-bd_dom.
IPR001202. WW_dom.
[Graphical view]
PfamiPF00035. dsrm. 2 hits.
[Graphical view]
SMARTiSM00358. DSRM. 2 hits.
SM00456. WW. 1 hit.
[Graphical view]
SUPFAMiSSF51045. SSF51045. 1 hit.
PROSITEiPS50137. DS_RBD. 1 hit.
PS50020. WW_DOMAIN_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8WYQ5-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
METDESPSPL PCGPAGEAVM ESRARPFQAL PREQSPPPPL QTSSGAEVMD
60 70 80 90 100
VGSGGDGQSE LPAEDPFNFY GASLLSKGSF SKGRLLIDPN CSGHSPRTAR
110 120 130 140 150
HAPAVRKFSP DLKLLKDVKI SVSFTESCRS KDRKVLYTGA ERDVRAECGL
160 170 180 190 200
LLSPVSGDVH ACPFGGSVGD GVGIGGESAD KKDEENELDQ EKRVEYAVLD
210 220 230 240 250
ELEDFTDNLE LDEEGAGGFT AKAIVQRDRV DEEALNFPYE DDFDNDVDAL
260 270 280 290 300
LEEGLCAPKK RRTEEKYGGD SDHPSDGETS VQPMMTKIKT VLKSRGRPPT
310 320 330 340 350
EPLPDGWIMT FHNSGVPVYL HRESRVVTWS RPYFLGTGSI RKHDPPLSSI
360 370 380 390 400
PCLHYKKMKD NEEREQSSDL TPSGDVSPVK PLSRSAELEF PLDEPDSMGA
410 420 430 440 450
DPGPPDEKDP LGAEAAPGAL GQVKAKVEVC KDESVDLEEF RSYLEKRFDF
460 470 480 490 500
EQVTVKKFRT WAERRQFNRE MKRKQAESER PILPANQKLI TLSVQDAPTK
510 520 530 540 550
KEFVINPNGK SEVCILHEYM QRVLKVRPVY NFFECENPSE PFGASVTIDG
560 570 580 590 600
VTYGSGTASS KKLAKNKAAR ATLEILIPDF VKQTSEEKPK DSEELEYFNH
610 620 630 640 650
ISIEDSRVYE LTSKAGLLSP YQILHECLKR NHGMGDTSIK FEVVPGKNQK
660 670 680 690 700
SEYVMACGKH TVRGWCKNKR VGKQLASQKI LQLLHPHVKN WGSLLRMYGR
710 720 730 740 750
ESSKMVKQET SDKSVIELQQ YAKKNKPNLH ILSKLQEEMK RLAEEREETR
760 770
KKPKMSIVAS AQPGGEPLCT VDV
Length:773
Mass (Da):86,045
Last modified:March 1, 2002 - v1
Checksum:i72D962BBE32890EC
GO
Isoform 2 (identifier: Q8WYQ5-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     303-304: LP → VL
     305-773: Missing.

Show »
Length:304
Mass (Da):32,831
Checksum:iFA7800BFE8FD462A
GO
Isoform 3 (identifier: Q8WYQ5-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     536-568: Missing.

Note: No experimental confirmation available.

Show »
Length:740
Mass (Da):82,750
Checksum:i5EEDDD1111DE7DC6
GO

Sequence cautioni

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.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti241 – 2477DDFDNDV → VCWQPLL in AAF82263. 1 PublicationCurated
Sequence conflicti274 – 2741P → L(PubMed:14702039)Curated
Sequence conflicti343 – 3431H → Y in BAB15165. (PubMed:14702039)Curated
Sequence conflicti706 – 7061V → A in BAB15165. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti174 – 1741I → V.
Corresponds to variant rs35987994 [ dbSNP | Ensembl ].
VAR_050952
Natural varianti725 – 7251N → D.
Corresponds to variant rs11546015 [ dbSNP | Ensembl ].
VAR_050953

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei303 – 3042LP → VL in isoform 2. 2 PublicationsVSP_003847
Alternative sequencei305 – 773469Missing in isoform 2. 2 PublicationsVSP_003848Add
BLAST
Alternative sequencei536 – 56833Missing in isoform 3. 1 PublicationVSP_012707Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS13773.1. [Q8WYQ5-1]
CCDS54501.1. [Q8WYQ5-3]
RefSeqiNP_001177255.1. NM_001190326.1. [Q8WYQ5-3]
NP_073557.3. NM_022720.6. [Q8WYQ5-1]
UniGeneiHs.643452.
Hs.713579.

Genome annotation databases

EnsembliENST00000351989; ENSP00000263209; ENSG00000128191. [Q8WYQ5-1]
ENST00000383024; ENSP00000372488; ENSG00000128191. [Q8WYQ5-3]
ENST00000407755; ENSP00000384726; ENSG00000128191. [Q8WYQ5-3]
GeneIDi54487.
KEGGihsa:54487.
UCSCiuc002zri.3. human. [Q8WYQ5-1]
uc010grz.3. human. [Q8WYQ5-3]

Polymorphism databases

DMDMi23813990.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS13773.1. [Q8WYQ5-1 ]
CCDS54501.1. [Q8WYQ5-3 ]
RefSeqi NP_001177255.1. NM_001190326.1. [Q8WYQ5-3 ]
NP_073557.3. NM_022720.6. [Q8WYQ5-1 ]
UniGenei Hs.643452.
Hs.713579.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali Q8WYQ5.
SMRi Q8WYQ5. Positions 298-352, 492-701.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119986. 30 interactions.
DIPi DIP-29261N.
IntActi Q8WYQ5. 4 interactions.
MINTi MINT-3048369.

PTM databases

PhosphoSitei Q8WYQ5.

Polymorphism databases

DMDMi 23813990.

Proteomic databases

MaxQBi Q8WYQ5.
PaxDbi Q8WYQ5.
PRIDEi Q8WYQ5.

Protocols and materials databases

DNASUi 54487.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000351989 ; ENSP00000263209 ; ENSG00000128191 . [Q8WYQ5-1 ]
ENST00000383024 ; ENSP00000372488 ; ENSG00000128191 . [Q8WYQ5-3 ]
ENST00000407755 ; ENSP00000384726 ; ENSG00000128191 . [Q8WYQ5-3 ]
GeneIDi 54487.
KEGGi hsa:54487.
UCSCi uc002zri.3. human. [Q8WYQ5-1 ]
uc010grz.3. human. [Q8WYQ5-3 ]

Organism-specific databases

CTDi 54487.
GeneCardsi GC22P020070.
GeneReviewsi DGCR8.
HGNCi HGNC:2847. DGCR8.
HPAi HPA019965.
MIMi 609030. gene.
neXtProti NX_Q8WYQ5.
PharmGKBi PA27309.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG300512.
GeneTreei ENSGT00390000015977.
HOVERGENi HBG051344.
InParanoidi Q8WYQ5.
KOi K18419.
OMAi IPVYLHR.
OrthoDBi EOG75J0MG.
PhylomeDBi Q8WYQ5.
TreeFami TF324256.

Enzyme and pathway databases

Reactomei REACT_12417. MicroRNA (miRNA) biogenesis.

Miscellaneous databases

ChiTaRSi DGCR8. human.
EvolutionaryTracei Q8WYQ5.
GeneWikii DGCR8_(gene).
GenomeRNAii 54487.
NextBioi 56807.
PROi Q8WYQ5.
SOURCEi Search...

Gene expression databases

Bgeei Q8WYQ5.
ExpressionAtlasi Q8WYQ5. baseline and differential.
Genevestigatori Q8WYQ5.

Family and domain databases

Gene3Di 3.30.160.20. 1 hit.
InterProi IPR014720. dsRNA-bd_dom.
IPR001202. WW_dom.
[Graphical view ]
Pfami PF00035. dsrm. 2 hits.
[Graphical view ]
SMARTi SM00358. DSRM. 2 hits.
SM00456. WW. 1 hit.
[Graphical view ]
SUPFAMi SSF51045. SSF51045. 1 hit.
PROSITEi PS50137. DS_RBD. 1 hit.
PS50020. WW_DOMAIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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] [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.
    , 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. 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] [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. 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. 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. 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. 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. 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. 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.

Entry informationi

Entry nameiDGCR8_HUMAN
AccessioniPrimary (citable) accession number: Q8WYQ5
Secondary accession number(s): B2R8G1
, Q6DCB2, Q6MZE9, Q6Y2L0, Q96G39, Q96GP8, Q9H6L8, Q9H6T7, Q9NRW2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: March 1, 2002
Last modified: October 29, 2014
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3