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RPAB2_DROME
ID   RPAB2_DROME             Reviewed;         131 AA.
AC   Q24320; Q9VNA7;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 169.
DE   RecName: Full=DNA-directed RNA polymerases I, II, and III subunit RPABC2;
DE            Short=RNA polymerases I, II, and III subunit ABC2;
DE   AltName: Full=RPB6 homolog;
GN   Name=RpII18; Synonyms=RpABC14; ORFNames=CG1163;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7651387; DOI=10.1128/mcb.15.9.4702;
RA   Shpakovski G.V., Acker J., Wintzerith M., Lacroix J.F., Thuriaux P.,
RA   Vigneron M.;
RT   "Four subunits that are shared by the three classes of RNA polymerase are
RT   functionally interchangeable between Homo sapiens and Saccharomyces
RT   cerevisiae.";
RL   Mol. Cell. Biol. 15:4702-4710(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Head;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC   -!- FUNCTION: DNA-dependent RNA polymerases catalyze the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       Common component of RNA polymerases I, II and III which synthesize
CC       ribosomal RNA precursors, mRNA precursors and many functional non-
CC       coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively.
CC       Pol II is the central component of the basal RNA polymerase II
CC       transcription machinery. Pols are composed of mobile elements that move
CC       relative to each other. In Pol II, RPB6 is part of the clamp element
CC       and together with parts of RPB1 and RPB2 forms a pocket to which the
CC       RPB4-RPB7 subcomplex binds (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the RNA polymerase I (Pol I), RNA polymerase II
CC       (Pol II) and RNA polymerase III (Pol III) complexes consisting of at
CC       least 13, 12 and 17 subunits, respectively. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the archaeal Rpo6/eukaryotic RPB6 RNA polymerase
CC       subunit family. {ECO:0000305}.
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DR   EMBL; Z47726; CAA87655.1; -; mRNA.
DR   EMBL; AE014297; AAF52039.1; -; Genomic_DNA.
DR   EMBL; BT001786; AAN71541.1; -; mRNA.
DR   PIR; S53013; S53013.
DR   RefSeq; NP_524910.1; NM_080171.4.
DR   AlphaFoldDB; Q24320; -.
DR   SMR; Q24320; -.
DR   BioGRID; 71310; 5.
DR   DIP; DIP-17541N; -.
DR   IntAct; Q24320; 2.
DR   STRING; 7227.FBpp0078433; -.
DR   PaxDb; Q24320; -.
DR   PRIDE; Q24320; -.
DR   DNASU; 48312; -.
DR   EnsemblMetazoa; FBtr0078787; FBpp0078433; FBgn0003275.
DR   GeneID; 48312; -.
DR   KEGG; dme:Dmel_CG1163; -.
DR   CTD; 48312; -.
DR   FlyBase; FBgn0003275; RpII18.
DR   VEuPathDB; VectorBase:FBgn0003275; -.
DR   eggNOG; KOG3405; Eukaryota.
DR   GeneTree; ENSGT00390000010415; -.
DR   HOGENOM; CLU_112527_2_0_1; -.
DR   InParanoid; Q24320; -.
DR   OMA; QEEDGYN; -.
DR   OrthoDB; 1488436at2759; -.
DR   PhylomeDB; Q24320; -.
DR   Reactome; R-DME-112382; Formation of RNA Pol II elongation complex.
DR   Reactome; R-DME-113418; Formation of the Early Elongation Complex.
DR   Reactome; R-DME-5578749; Transcriptional regulation by small RNAs.
DR   Reactome; R-DME-674695; RNA Polymerase II Pre-transcription Events.
DR   Reactome; R-DME-6781823; Formation of TC-NER Pre-Incision Complex.
DR   Reactome; R-DME-6782135; Dual incision in TC-NER.
DR   Reactome; R-DME-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-DME-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR   Reactome; R-DME-6803529; FGFR2 alternative splicing.
DR   Reactome; R-DME-6807505; RNA polymerase II transcribes snRNA genes.
DR   Reactome; R-DME-72086; mRNA Capping.
DR   Reactome; R-DME-72163; mRNA Splicing - Major Pathway.
DR   Reactome; R-DME-72165; mRNA Splicing - Minor Pathway.
DR   Reactome; R-DME-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR   Reactome; R-DME-73762; RNA Polymerase I Transcription Initiation.
DR   Reactome; R-DME-73772; RNA Polymerase I Promoter Escape.
DR   Reactome; R-DME-73776; RNA Polymerase II Promoter Escape.
DR   Reactome; R-DME-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR   Reactome; R-DME-75953; RNA Polymerase II Transcription Initiation.
DR   Reactome; R-DME-75955; RNA Polymerase II Transcription Elongation.
DR   Reactome; R-DME-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR   Reactome; R-DME-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
DR   Reactome; R-DME-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter.
DR   Reactome; R-DME-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR   Reactome; R-DME-9018519; Estrogen-dependent gene expression.
DR   BioGRID-ORCS; 48312; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 48312; -.
DR   PRO; PR:Q24320; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0003275; Expressed in testis and 13 other tissues.
DR   ExpressionAtlas; Q24320; baseline and differential.
DR   Genevisible; Q24320; DM.
DR   GO; GO:0005736; C:RNA polymerase I complex; ISS:FlyBase.
DR   GO; GO:0005665; C:RNA polymerase II, core complex; IDA:FlyBase.
DR   GO; GO:0005666; C:RNA polymerase III complex; ISS:FlyBase.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:InterPro.
DR   GO; GO:0006360; P:transcription by RNA polymerase I; ISS:FlyBase.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; ISS:FlyBase.
DR   GO; GO:0042797; P:tRNA transcription by RNA polymerase III; ISS:FlyBase.
DR   Gene3D; 3.90.940.10; -; 1.
DR   InterPro; IPR020708; DNA-dir_RNA_polK_14-18kDa_CS.
DR   InterPro; IPR006110; Pol_omega/Rpo6/RPB6.
DR   InterPro; IPR028363; RPB6.
DR   InterPro; IPR036161; RPB6/omega-like_sf.
DR   InterPro; IPR006111; Rpo6/Rpb6.
DR   Pfam; PF01192; RNA_pol_Rpb6; 1.
DR   PIRSF; PIRSF500154; RPB6; 1.
DR   PIRSF; PIRSF000778; RpoK/RPB6; 1.
DR   SMART; SM01409; RNA_pol_Rpb6; 1.
DR   SUPFAM; SSF63562; SSF63562; 1.
DR   PROSITE; PS01111; RNA_POL_K_14KD; 1.
PE   2: Evidence at transcript level;
KW   DNA-directed RNA polymerase; Nucleus; Reference proteome; Transcription.
FT   CHAIN           1..131
FT                   /note="DNA-directed RNA polymerases I, II, and III subunit
FT                   RPABC2"
FT                   /id="PRO_0000133803"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   131 AA;  14722 MW;  AAA7F7794EB3DF68 CRC64;
     MDDADYDNDD VGGDDFDDVD EDVDEDINQE EEADNIEIIA PGGAGGGGVP KSKRITTKYM
     TKYERARVLG TRALQIAMCA PIMVELDGET DPLQIAMKEL KQKKIPIIIR RYLPDHSYED
     WSIDELIMVD N
 
 
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