RPB2_MOUSE
ID RPB2_MOUSE Reviewed; 1174 AA.
AC Q8CFI7;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=DNA-directed RNA polymerase II subunit RPB2;
DE EC=2.7.7.6;
DE AltName: Full=DNA-directed RNA polymerase II 140 kDa polypeptide;
DE AltName: Full=DNA-directed RNA polymerase II subunit B;
DE AltName: Full=RNA polymerase II subunit 2;
DE AltName: Full=RNA polymerase II subunit B2;
GN Name=Polr2b;
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=FVB/N; TISSUE=Mammary tumor;
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).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Second largest component of RNA polymerase II which synthesizes mRNA
CC precursors and many functional non-coding RNAs. Proposed to contribute
CC to the polymerase catalytic activity and forms the polymerase active
CC center together with the largest subunit. Pol II is the central
CC component of the basal RNA polymerase II transcription machinery. It is
CC composed of mobile elements that move relative to each other. RPB2 is
CC part of the core element with the central large cleft, the clamp
CC element that moves to open and close the cleft and the jaws that are
CC thought to grab the incoming DNA template (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.6;
CC -!- SUBUNIT: Component of the RNA polymerase II (Pol II) complex consisting
CC of 12 subunits. Interacts with WDR82 (By similarity). Interacts with
CC MEN1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- MISCELLANEOUS: The binding of ribonucleoside triphosphate to the RNA
CC polymerase II transcribing complex probably involves a two-step
CC mechanism. The initial binding seems to occur at the entry (E) site and
CC involves a magnesium ion coordinated by three conserved aspartate
CC residues of the two largest RNA Pol II subunits (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH38472.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC038472; AAH38472.1; ALT_INIT; mRNA.
DR CCDS; CCDS51528.1; -.
DR RefSeq; NP_722493.2; NM_153798.2.
DR AlphaFoldDB; Q8CFI7; -.
DR SMR; Q8CFI7; -.
DR BioGRID; 231111; 25.
DR DIP; DIP-57023N; -.
DR IntAct; Q8CFI7; 14.
DR MINT; Q8CFI7; -.
DR STRING; 10090.ENSMUSP00000031167; -.
DR iPTMnet; Q8CFI7; -.
DR PhosphoSitePlus; Q8CFI7; -.
DR EPD; Q8CFI7; -.
DR MaxQB; Q8CFI7; -.
DR PaxDb; Q8CFI7; -.
DR PeptideAtlas; Q8CFI7; -.
DR PRIDE; Q8CFI7; -.
DR ProteomicsDB; 300435; -.
DR Antibodypedia; 12545; 188 antibodies from 27 providers.
DR DNASU; 231329; -.
DR Ensembl; ENSMUST00000031167; ENSMUSP00000031167; ENSMUSG00000029250.
DR GeneID; 231329; -.
DR KEGG; mmu:231329; -.
DR UCSC; uc008xwe.2; mouse.
DR CTD; 5431; -.
DR MGI; MGI:2388280; Polr2b.
DR VEuPathDB; HostDB:ENSMUSG00000029250; -.
DR eggNOG; KOG0214; Eukaryota.
DR GeneTree; ENSGT00950000183132; -.
DR HOGENOM; CLU_000524_5_2_1; -.
DR InParanoid; Q8CFI7; -.
DR OMA; RDLHGTH; -.
DR OrthoDB; 42570at2759; -.
DR PhylomeDB; Q8CFI7; -.
DR TreeFam; TF103037; -.
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-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-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-MMU-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
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-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR Reactome; R-MMU-9018519; Estrogen-dependent gene expression.
DR BioGRID-ORCS; 231329; 25 hits in 74 CRISPR screens.
DR ChiTaRS; Polr2b; mouse.
DR PRO; PR:Q8CFI7; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8CFI7; protein.
DR Bgee; ENSMUSG00000029250; Expressed in saccule of membranous labyrinth and 263 other tissues.
DR Genevisible; Q8CFI7; MM.
DR GO; GO:0000781; C:chromosome, telomeric region; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005665; C:RNA polymerase II, core complex; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR GO; GO:0006366; P:transcription by RNA polymerase II; ISS:UniProtKB.
DR CDD; cd00653; RNA_pol_B_RPB2; 1.
DR Gene3D; 2.40.270.10; -; 1.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 1.
DR InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR InterPro; IPR007121; RNA_pol_bsu_CS.
DR InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR InterPro; IPR007642; RNA_pol_Rpb2_2.
DR InterPro; IPR037034; RNA_pol_Rpb2_2_sf.
DR InterPro; IPR007645; RNA_pol_Rpb2_3.
DR InterPro; IPR007646; RNA_pol_Rpb2_4.
DR InterPro; IPR007647; RNA_pol_Rpb2_5.
DR InterPro; IPR007641; RNA_pol_Rpb2_7.
DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR PANTHER; PTHR20856; PTHR20856; 1.
DR Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR Pfam; PF04561; RNA_pol_Rpb2_2; 1.
DR Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR Pfam; PF04566; RNA_pol_Rpb2_4; 1.
DR Pfam; PF04567; RNA_pol_Rpb2_5; 1.
DR Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR PROSITE; PS01166; RNA_POL_BETA; 1.
PE 1: Evidence at protein level;
KW DNA-directed RNA polymerase; Magnesium; Metal-binding; Methylation;
KW Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1174
FT /note="DNA-directed RNA polymerase II subunit RPB2"
FT /id="PRO_0000048086"
FT ZN_FING 1119..1140
FT /note="C4-type"
FT BINDING 792
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="ligand shared with RPB1"
FT /evidence="ECO:0000250"
FT BINDING 1119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 937
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30876"
FT MOD_RES 1052
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P30876"
SQ SEQUENCE 1174 AA; 133911 MW; F941FA6EC03E2160 CRC64;
MYDADEDMQY DEDDDEITPD LWQEACWIVI SSYFDEKGLV RQQLDSFDEF IQMSVQRIVE
DAPPIDLQAE AQHASGEVEE PPRYLLKFEQ IYLSKPTHWE RDGAPSPMMP NEARLRNLTY
SAPLYVDITK TVIKEGEEQL QTQHQKTFIG KIPIMLRSTY CLLNGLTDRD LCELNECPLD
PGGYFIINGS EKVLIAQEKM ATNTVYVFAK KDSKYAYTGE CRSCLENSSR PTSTIWVSML
ARGGQGAKKS AIGQRIVATL PYIKQEVPII IVFRALGFVS DRDILEHIIY DFEDPEMMEM
VKPSLDEAFV IQEQNVALNF IGSRGAKPGV TKEKRIKYAK EVLQKEMLPH VGVSDFCETK
KAYFLGYMVH RLLLAALGRR ELDDRDHYGN KRLDLAGPLL AFLFRGMFKN LLKEVRIYAQ
KFIDRGKDFN LELAIKTRII SDGLKYSLAT GNWGDQKKAH QARAGVSQVL NRLTFASTLS
HLRRLNSPIG RDGKLAKPRQ LHNTLWGMVC PAETPEGHAV GLVKNLALMA YISVGSQPSP
ILEFLEEWSM ENLEEISPAA IADATKIFVN GCWVGIHKDP EQLMNTLRKL RRQMDIIVSE
VSMIRDIRER EIRIYTDAGR ICRPLLIVEK QKLLLKKRHI DQLKEREYNN YSWQDLVASG
VVEYIDTLEE ETVMLAMTPD DLQEKEVAYC STYTHCEIHP SMILGVCASI IPFPDHNQSP
RNTYQSAMGK QAMGVYITNF HVRMDTLAHV LYYPQKPLVT TRSMEYLRFR ELPAGINSIV
AIASYTGYNQ EDSVIMNRSA VDRGFFRSVF YRSYKEQESK KGFDQEEVFE KPTRETCQGM
RHAIYEKLDD DGLIAPGVRV SGDDVIIGKT VTLPENEDEL ESTNRRYTKR DCSTFLRTSE
TGIVDQVMVT LNQEGYKFCK IRVRSVRIPQ IGDKFASRHG QKGTCGIQYR QEDMPFTCEG
ITPDIIINPH AIPSRMTIGH LIECLQGKVS ANKGEIGDAT PFNDAVNVQK ISNLLSDYGY
HLRGNEVLYN GFTGRKITSQ IFIGPTYYQR LKHMVDDKIH SRARGPIQIL NRQPMEGRSR
DGGLRFGEME RDCQIAHGAA QFLRERLFEA SDPYQVHVCN LCGIMAIANT RTHTYECRGC
RNKTQISLVR MPYACKLLFQ ELMSMSIAPR MMSV
