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Q8WYQ5

- DGCR8_HUMAN

UniProt

Q8WYQ5 - DGCR8_HUMAN

Protein

Microprocessor complex subunit DGCR8

Gene

DGCR8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 1 (01 Mar 2002)
      Previous versions | rss
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    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
    3. protein binding Source: IntAct

    GO - Biological processi

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

    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

    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.
    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.
    Mutagenesisi669 – 6735KRVGK → AAVGA: Strongly reduces pri-miRNA binding affinity.
    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.

    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

    ArrayExpressiQ8WYQ5.
    BgeeiQ8WYQ5.
    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.
    HOVERGENiHBG051344.
    InParanoidiQ8WYQ5.
    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

    METDESPSPL PCGPAGEAVM ESRARPFQAL PREQSPPPPL QTSSGAEVMD    50
    VGSGGDGQSE LPAEDPFNFY GASLLSKGSF SKGRLLIDPN CSGHSPRTAR 100
    HAPAVRKFSP DLKLLKDVKI SVSFTESCRS KDRKVLYTGA ERDVRAECGL 150
    LLSPVSGDVH ACPFGGSVGD GVGIGGESAD KKDEENELDQ EKRVEYAVLD 200
    ELEDFTDNLE LDEEGAGGFT AKAIVQRDRV DEEALNFPYE DDFDNDVDAL 250
    LEEGLCAPKK RRTEEKYGGD SDHPSDGETS VQPMMTKIKT VLKSRGRPPT 300
    EPLPDGWIMT FHNSGVPVYL HRESRVVTWS RPYFLGTGSI RKHDPPLSSI 350
    PCLHYKKMKD NEEREQSSDL TPSGDVSPVK PLSRSAELEF PLDEPDSMGA 400
    DPGPPDEKDP LGAEAAPGAL GQVKAKVEVC KDESVDLEEF RSYLEKRFDF 450
    EQVTVKKFRT WAERRQFNRE MKRKQAESER PILPANQKLI TLSVQDAPTK 500
    KEFVINPNGK SEVCILHEYM QRVLKVRPVY NFFECENPSE PFGASVTIDG 550
    VTYGSGTASS KKLAKNKAAR ATLEILIPDF VKQTSEEKPK DSEELEYFNH 600
    ISIEDSRVYE LTSKAGLLSP YQILHECLKR NHGMGDTSIK FEVVPGKNQK 650
    SEYVMACGKH TVRGWCKNKR VGKQLASQKI LQLLHPHVKN WGSLLRMYGR 700
    ESSKMVKQET SDKSVIELQQ YAKKNKPNLH ILSKLQEEMK RLAEEREETR 750
    KKPKMSIVAS AQPGGEPLCT VDV 773
    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.
    HOVERGENi HBG051344.
    InParanoidi Q8WYQ5.
    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

    ArrayExpressi Q8WYQ5.
    Bgeei Q8WYQ5.
    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

    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 1, 2014
    This is version 133 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