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A8DYY5

- RPAP2_DROME

UniProt

A8DYY5 - RPAP2_DROME

Protein

Putative RNA polymerase II subunit B1 CTD phosphatase RPAP2 homolog

Gene

CG34183

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 40 (01 Oct 2014)
      Sequence version 1 (13 Nov 2007)
      Previous versions | rss
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    Functioni

    Putative RNA polymerase II subunit B1 C-terminal domain (CTD) phosphatase involved in RNA polymerase II transcription regulation.By similarity

    Catalytic activityi

    [a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri46 – 12984RTR1-typeAdd
    BLAST

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. phosphoprotein phosphatase activity Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Putative RNA polymerase II subunit B1 CTD phosphatase RPAP2 homolog (EC:3.1.3.16)
    Alternative name(s):
    RNA polymerase II-associated protein 2
    Gene namesi
    ORF Names:CG34183
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2L

    Organism-specific databases

    FlyBaseiFBgn0085212. CG34183.

    Subcellular locationi

    Nucleus By similarity

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 143143Putative RNA polymerase II subunit B1 CTD phosphatase RPAP2 homologPRO_0000416290Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi7227.FBpp0111291.

    Structurei

    3D structure databases

    ProteinModelPortaliA8DYY5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the RPAP2 family.Curated
    Contains 1 RTR1-type zinc finger.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri46 – 12984RTR1-typeAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    GeneTreeiENSGT00390000017965.
    InParanoidiA8DYY5.
    OMAiSEYIKSQ.
    OrthoDBiEOG7XWPQD.
    PhylomeDBiA8DYY5.

    Family and domain databases

    InterProiIPR007308. DUF408.
    [Graphical view]
    PfamiPF04181. RPAP2_Rtr1. 1 hit.
    [Graphical view]
    PROSITEiPS51479. ZF_RTR1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    A8DYY5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTTEKGEQLR QQLIAAVVKK RAAIARAHEI VVRLLEPGIP EPEFLSLLCE    50
    IGPPNYSDIV DEREINKLCG YPLCSTVLEN VPKQKYSISA SKNKVYDITE 100
    RKKFCSGYCF KASEYIKSQV PTSPLWLRDR ETRPSFQLLP RNT 143
    Length:143
    Mass (Da):16,330
    Last modified:November 13, 2007 - v1
    Checksum:iB96163550CC3AC7E
    GO

    Sequence cautioni

    The sequence ABL75686.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti24 – 241Missing in ABL75663. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014134 Genomic DNA. Translation: ABV53661.1.
    BT029562 mRNA. Translation: ABL75622.1.
    BT029604 mRNA. Translation: ABL75663.1.
    BT029627 mRNA. Translation: ABL75686.1. Different initiation.
    RefSeqiNP_001097134.1. NM_001103664.2.
    UniGeneiDm.25279.

    Genome annotation databases

    EnsemblMetazoaiFBtr0112376; FBpp0111291; FBgn0085212.
    GeneIDi5740752.
    KEGGidme:Dmel_CG34183.
    UCSCiCG34183-RA. d. melanogaster.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014134 Genomic DNA. Translation: ABV53661.1 .
    BT029562 mRNA. Translation: ABL75622.1 .
    BT029604 mRNA. Translation: ABL75663.1 .
    BT029627 mRNA. Translation: ABL75686.1 . Different initiation.
    RefSeqi NP_001097134.1. NM_001103664.2.
    UniGenei Dm.25279.

    3D structure databases

    ProteinModelPortali A8DYY5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 7227.FBpp0111291.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0112376 ; FBpp0111291 ; FBgn0085212 .
    GeneIDi 5740752.
    KEGGi dme:Dmel_CG34183.
    UCSCi CG34183-RA. d. melanogaster.

    Organism-specific databases

    FlyBasei FBgn0085212. CG34183.

    Phylogenomic databases

    GeneTreei ENSGT00390000017965.
    InParanoidi A8DYY5.
    OMAi SEYIKSQ.
    OrthoDBi EOG7XWPQD.
    PhylomeDBi A8DYY5.

    Miscellaneous databases

    GenomeRNAii 5740752.
    NextBioi 20891790.

    Family and domain databases

    InterProi IPR007308. DUF408.
    [Graphical view ]
    Pfami PF04181. RPAP2_Rtr1. 1 hit.
    [Graphical view ]
    PROSITEi PS51479. ZF_RTR1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    2. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    3. Stapleton M., Carlson J., Frise E., Kapadia B., Park S., Wan K., Yu C., Celniker S.
      Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.

    Entry informationi

    Entry nameiRPAP2_DROME
    AccessioniPrimary (citable) accession number: A8DYY5
    Secondary accession number(s): A1A6P2, A1A6T3, A1A6V6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 21, 2012
    Last sequence update: November 13, 2007
    Last modified: October 1, 2014
    This is version 40 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3