RPAB2_MOUSE
ID RPAB2_MOUSE Reviewed; 127 AA.
AC P61219;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 136.
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=DNA-directed RNA polymerase II subunit F;
DE AltName: Full=RPB6 homolog;
GN Name=Polr2f;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pancreas;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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, POLR2F/RPB6 is part of the clamp
CC element and together with parts of RPB1 and RPB2 forms a pocket to
CC which the 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 {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the archaeal Rpo6/eukaryotic RPB6 RNA polymerase
CC subunit family. {ECO:0000305}.
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DR EMBL; AK007913; BAB25345.1; -; mRNA.
DR EMBL; BC024419; AAH24419.1; -; mRNA.
DR CCDS; CCDS27634.1; -.
DR RefSeq; NP_081507.1; NM_027231.2.
DR AlphaFoldDB; P61219; -.
DR SMR; P61219; -.
DR IntAct; P61219; 1.
DR STRING; 10090.ENSMUSP00000043566; -.
DR iPTMnet; P61219; -.
DR PhosphoSitePlus; P61219; -.
DR MaxQB; P61219; -.
DR PaxDb; P61219; -.
DR PeptideAtlas; P61219; -.
DR PRIDE; P61219; -.
DR ProteomicsDB; 260833; -.
DR Antibodypedia; 227; 131 antibodies from 26 providers.
DR DNASU; 69833; -.
DR Ensembl; ENSMUST00000230271; ENSMUSP00000155332; ENSMUSG00000033020.
DR GeneID; 69833; -.
DR KEGG; mmu:69833; -.
DR UCSC; uc007wst.1; mouse.
DR CTD; 5435; -.
DR MGI; MGI:1349393; Polr2f.
DR VEuPathDB; HostDB:ENSMUSG00000033020; -.
DR eggNOG; KOG3405; Eukaryota.
DR GeneTree; ENSGT00390000010415; -.
DR HOGENOM; CLU_112527_2_0_1; -.
DR InParanoid; P61219; -.
DR OMA; QEEDGYN; -.
DR OrthoDB; 1488436at2759; -.
DR PhylomeDB; P61219; -.
DR TreeFam; TF103041; -.
DR Reactome; R-MMU-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-MMU-113418; Formation of the Early Elongation Complex.
DR Reactome; R-MMU-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-MMU-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-MMU-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-MMU-6782135; Dual incision in TC-NER.
DR Reactome; R-MMU-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-MMU-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-MMU-6803529; FGFR2 alternative splicing.
DR Reactome; R-MMU-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-MMU-72086; mRNA Capping.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-MMU-72165; mRNA Splicing - Minor Pathway.
DR Reactome; R-MMU-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR Reactome; R-MMU-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-MMU-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-MMU-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-MMU-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-MMU-73863; RNA Polymerase I Transcription Termination.
DR Reactome; R-MMU-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-MMU-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-MMU-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR Reactome; R-MMU-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
DR Reactome; R-MMU-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter.
DR Reactome; R-MMU-76071; RNA Polymerase III Transcription Initiation From Type 3 Promoter.
DR Reactome; R-MMU-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR Reactome; R-MMU-9018519; Estrogen-dependent gene expression.
DR BioGRID-ORCS; 69833; 23 hits in 73 CRISPR screens.
DR ChiTaRS; Polr2f; mouse.
DR PRO; PR:P61219; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P61219; protein.
DR Bgee; ENSMUSG00000033020; Expressed in embryonic brain and 270 other tissues.
DR ExpressionAtlas; P61219; baseline and differential.
DR Genevisible; P61219; MM.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005736; C:RNA polymerase I complex; IBA:GO_Central.
DR GO; GO:0005665; C:RNA polymerase II, core complex; ISS:UniProtKB.
DR GO; GO:0005666; C:RNA polymerase III complex; IBA:GO_Central.
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:0006366; P:transcription by RNA polymerase II; ISS:UniProtKB.
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 Acetylation; DNA-directed RNA polymerase; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P61218"
FT CHAIN 2..127
FT /note="DNA-directed RNA polymerases I, II, and III subunit
FT RPABC2"
FT /id="PRO_0000133800"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P61218"
FT MOD_RES 2
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:O88828"
SQ SEQUENCE 127 AA; 14464 MW; 6366A0D7EB3F0921 CRC64;
MSDNEDNFDG DDFDDVEEDE GLDDLENAEE EGQENVEILP SGERPQANQK RITTPYMTKY
ERARVLGTRA LQIAMCAPVM VELEGETDPL LIAMKELKAR KIPIIIRRYL PDGSYEDWGV
DELIISD
