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 16-JUN-2009, entry version 50. DE RecName: Full=DNA-directed RNA polymerase II subunit RPB2; DE EC=2.7.7.6; DE AltName: Full=DNA-directed RNA polymerase II subunit B; DE AltName: Full=RNA polymerase II subunit B2; DE AltName: Full=RNA polymerase II subunit 2; DE AltName: Full=DNA-directed RNA polymerase II 140 kDa polypeptide; GN Name=Polr2b; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription CC of DNA into RNA using the four ribonucleoside triphosphates as CC substrates. Second largest component of RNA polymerase II which CC synthesizes mRNA precursors and many functional non-coding RNAs. CC Proposed to contribute to the polymerase catalytic activity and CC forms the polymerase active center together with the largest CC subunit. Pol II is the central component of the basal RNA CC polymerase II transcription machinery. It is composed of mobile CC elements that move relative to each other. RPB2 is part of the CC core element with the central large cleft, the clamp element that CC moves to open and close the cleft and the jaws that are thought to CC grab the incoming DNA template (By similarity). CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). CC -!- SUBUNIT: Component of the RNA polymerase II (Pol II) complex CC consisting of 12 subunits (By similarity). CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). CC -!- MISCELLANEOUS: The binding of ribonucleoside triphosphate to the CC RNA polymerase II transcribing complex probably involves a two- CC step mechanism. The initial binding seems to occur at the entry CC (E) site and involves a magnesium ion coordinated by three CC conserved aspartate residues of the two largest RNA Pol II CC subunits (By similarity). CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BC038472; AAH38472.1; ALT_INIT; mRNA. DR IPI; IPI00320034; -. DR RefSeq; NP_722493.1; -. DR UniGene; Mm.273217; -. DR PhosphoSite; Q8CFI7; -. DR Ensembl; ENSMUSG00000029250; Mus musculus. DR GeneID; 231329; -. DR KEGG; mmu:231329; -. DR NMPDR; fig|10090.3.peg.11767; -. DR MGI; MGI:2388280; Polr2b. DR HOGENOM; Q8CFI7; -. DR HOVERGEN; Q8CFI7; -. DR OMA; Q8CFI7; FGPTYYQ. DR BRENDA; 2.7.7.6; 244. DR NextBio; 380519; -. DR Bgee; Q8CFI7; -. DR CleanEx; MM_POLR2B; -. DR GermOnline; ENSMUSG00000029250; Mus musculus. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW. DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0006350; P:transcription; IEA:UniProtKB-KW. DR InterPro; IPR015712; DNA-dir_RNA_pol_su2. DR InterPro; IPR007120; DNA-dir_RNA_pol_su2_6. DR InterPro; IPR007121; RNA_pol_bsu_CS. DR InterPro; IPR007644; RNA_pol_bsu_protrusion. DR InterPro; IPR007642; RNA_pol_Rpb2_2. 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 PANTHER; PTHR20856; RNA_pol_I_sub2; 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 2: Evidence at transcript level; KW DNA-directed RNA polymerase; Magnesium; Metal-binding; KW Nucleotidyltransferase; Nucleus; Transcription; Transferase; Zinc; KW Zinc-finger. FT CHAIN 1 1174 DNA-directed RNA polymerase II subunit FT RPB2. FT /FTId=PRO_0000048086. FT ZN_FING 1119 1140 C4-type. FT METAL 792 792 Magnesium; shared with RPB1 (By FT similarity). FT METAL 1119 1119 Zinc (By similarity). FT METAL 1122 1122 Zinc (By similarity). FT METAL 1137 1137 Zinc (By similarity). FT METAL 1140 1140 Zinc (By similarity). 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 //