ID RPB2_HUMAN Reviewed; 1174 AA. AC P30876; A8K1A8; Q8IZ61; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 02-SEP-2026, entry version 233. DE RecName: Full=DNA-directed RNA polymerase II subunit RPB2; DE EC=2.7.7.6 {ECO:0000269|PubMed:27193682, ECO:0000269|PubMed:30190596, ECO:0000269|PubMed:9852112}; DE AltName: Full=3'-5' exoribonuclease; DE EC=3.1.13.- {ECO:0000269|PubMed:8381534}; 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; DE AltName: Full=RNA-directed RNA polymerase II subunit RPB2; DE EC=2.7.7.48 {ECO:0000269|PubMed:23395899}; GN Name=POLR2B {ECO:0000312|HGNC:HGNC:9188}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1518060; DOI=10.1016/0022-2836(92)91071-v; RA Acker J., Wintzerith M., Vigneron M., Kedinger C.; RT "Primary structure of the second largest subunit of human RNA polymerase II RT (or B)."; RL J. Mol. Biol. 226:1295-1299(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skin; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 699-1174. RC TISSUE=Brain; RX PubMed=9110174; DOI=10.1101/gr.7.4.353; RA Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., RA Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.; RT "Large-scale concatenation cDNA sequencing."; RL Genome Res. 7:353-358(1997). RN [6] RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION. RX PubMed=8381534; DOI=10.1073/pnas.90.3.843; RA Wang D., Hawley D.K.; RT "Identification of a 3'-->5' exonuclease activity associated with human RNA RT polymerase II."; RL Proc. Natl. Acad. Sci. U.S.A. 90:843-847(1993). RN [7] RP FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION IN THE RNA POLYMERASE II RP CORE-COMPLEX, AND SUBCELLULAR LOCATION. RX PubMed=9852112; DOI=10.1074/jbc.273.51.34444; RA Kershnar E., Wu S.-Y., Chiang C.-M.; RT "Immunoaffinity purification and functional characterization of human RT transcription factor IIH and RNA polymerase II from clonal cell lines that RT conditionally express epitope-tagged subunits of the multiprotein RT complexes."; RL J. Biol. Chem. 273:34444-34453(1998). RN [8] RP INTERACTION WITH MEN1. RX PubMed=14992727; DOI=10.1016/s1097-2765(04)00081-4; RA Hughes C.M., Rozenblatt-Rosen O., Milne T.A., Copeland T.D., Levine S.S., RA Lee J.C., Hayes D.N., Shanmugam K.S., Bhattacharjee A., Biondi C.A., RA Kay G.F., Hayward N.K., Hess J.L., Meyerson M.; RT "Menin associates with a trithorax family histone methyltransferase complex RT and with the hoxc8 locus."; RL Mol. Cell 13:587-597(2004). RN [9] RP INTERACTION WITH WDR82. RX PubMed=17998332; DOI=10.1128/mcb.01356-07; RA Lee J.H., Skalnik D.G.; RT "Wdr82 is a C-terminal domain-binding protein that recruits the Setd1A RT Histone H3-Lys4 methyltransferase complex to transcription start sites of RT transcribed human genes."; RL Mol. Cell. Biol. 28:609-618(2008). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [11] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=23395899; DOI=10.1038/emboj.2013.18; RA Wagner S.D., Yakovchuk P., Gilman B., Ponicsan S.L., Drullinger L.F., RA Kugel J.F., Goodrich J.A.; RT "RNA polymerase II acts as an RNA-dependent RNA polymerase to extend and RT destabilize a non-coding RNA."; RL EMBO J. 32:781-790(2013). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-937, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [14] RP METHYLATION [LARGE SCALE ANALYSIS] AT LYS-1052, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [15] RP STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS) IN COMPLEX WITH ZN(2+); RP MG(2+) AND PROMOTER DNA, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND RP SUBUNIT. RX PubMed=27193682; DOI=10.1038/nature17970; RA He Y., Yan C., Fang J., Inouye C., Tjian R., Ivanov I., Nogales E.; RT "Near-atomic resolution visualization of human transcription promoter RT opening."; RL Nature 533:359-365(2016). RN [16] RP STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS), FUNCTION, CATALYTIC RP ACTIVITY, AND SUBUNIT. RX PubMed=30190596; DOI=10.1038/s41594-018-0118-5; RA Jishage M., Yu X., Shi Y., Ganesan S.J., Chen W.Y., Sali A., Chait B.T., RA Asturias F.J., Roeder R.G.; RT "Architecture of Pol II(G) and molecular mechanism of transcription RT regulation by Gdown1."; RL Nat. Struct. Mol. Biol. 25:859-867(2018). CC -!- FUNCTION: Catalytic core component of RNA polymerase II (Pol II), a CC DNA-dependent RNA polymerase which synthesizes mRNA precursors and many CC functional non-coding RNAs using the four ribonucleoside triphosphates CC as substrates (By similarity) (PubMed:27193682, PubMed:30190596, CC PubMed:9852112). Pol II-mediated transcription cycle proceeds through CC transcription initiation, transcription elongation and transcription CC termination stages. During transcription initiation, Pol II pre- CC initiation complex (PIC) is recruited to DNA promoters, with focused- CC type promoters containing either the initiator (Inr) element, or the CC TATA-box found in cell-type specific genes and dispersed-type promoters CC that often contain hypomethylated CpG islands usually found in CC housekeeping genes. Once the polymerase has escaped from the promoter CC it enters the elongation phase during which RNA is actively CC polymerized, based on complementarity with the template DNA strand. CC Transcription termination involves the release of the RNA transcript CC and polymerase from the DNA (PubMed:27193682, PubMed:30190596, CC PubMed:9852112). Forms Pol II active center together with the largest CC subunit POLR2A/RPB1. Appends one nucleotide at a time to the 3' end of CC the nascent RNA, with POLR2A/RPB1 most likely contributing a Mg(2+)- CC coordinating DxDGD motif and POLR2B/RPB2 participating in the CC coordination of a second Mg(2+) ion and providing lysine residues CC believed to facilitate Watson-Crick base pairing between the incoming CC nucleotide and template base. Typically, Mg(2+) ions direct a 5' CC nucleoside triphosphate to form a phosphodiester bond with the 3' CC hydroxyl of the preceding nucleotide of the nascent RNA, with the CC elimination of pyrophosphate. The reversible pyrophosphorolysis can CC occur at high pyrophosphate concentrations (By similarity) CC (PubMed:30190596, PubMed:9852112). Can proofread the nascent RNA CC transcript by means of a 3' -> 5' exonuclease activity. If a CC ribonucleotide is mis-incorporated, backtracks along the template DNA CC and cleaves the phosphodiester bond releasing the mis-incorporated 5'- CC ribonucleotide (By similarity) (PubMed:8381534). CC {ECO:0000250|UniProtKB:A5PJW8, ECO:0000269|PubMed:27193682, CC ECO:0000269|PubMed:30190596, ECO:0000269|PubMed:8381534, CC ECO:0000269|PubMed:9852112}. CC -!- FUNCTION: RNA-dependent RNA polymerase that catalyzes the extension of CC a non-coding RNA (ncRNA) at the 3'-end using the four ribonucleoside CC triphosphates as substrates. An internal ncRNA sequence near the 3'-end CC serves as a template in a single-round Pol II-mediated RNA CC polymerization reaction. May decrease the stability of ncRNAs that CC repress Pol II-mediated gene transcription. CC {ECO:0000269|PubMed:23395899}. CC -!- CATALYTIC ACTIVITY: CC Reaction=RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + CC diphosphate; 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; Evidence={ECO:0000269|PubMed:27193682, CC ECO:0000269|PubMed:30190596, ECO:0000269|PubMed:9852112}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21249; CC Evidence={ECO:0000269|PubMed:27193682, ECO:0000269|PubMed:30190596, CC ECO:0000269|PubMed:9852112}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21250; CC Evidence={ECO:0000305|PubMed:8381534}; CC -!- CATALYTIC ACTIVITY: CC Reaction=RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + CC diphosphate; Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA- CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; CC EC=2.7.7.48; Evidence={ECO:0000269|PubMed:23395899}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21249; CC Evidence={ECO:0000269|PubMed:23395899}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 3'-end ribonucleotidyl-ribonucleotide-RNA + H2O = a 3'-end CC ribonucleotide-RNA + a ribonucleoside 5'-phosphate + H(+); CC Xref=Rhea:RHEA:77763, Rhea:RHEA-COMP:17428, Rhea:RHEA-COMP:18982, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58043, CC ChEBI:CHEBI:74896, ChEBI:CHEBI:197502; CC Evidence={ECO:0000269|PubMed:8381534}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77764; CC Evidence={ECO:0000269|PubMed:8381534}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:27193682}; CC Note=Two Mg(2+) ions are coordinated by both the catalytic residues and CC the nucleic acid substrate to enhance substrate recognition and CC catalytic efficiency. {ECO:0000269|PubMed:27193682}; CC -!- ACTIVITY REGULATION: Pol II enzymatic activities are inhibited by CC alpha-amanitin. 3'->5' exonuclease activity is stimulated by TFIIS, CC whereas pyrophosphorolysis is enhanced by TFIIF. CC {ECO:0000269|PubMed:8381534}. CC -!- SUBUNIT: Component of the RNA polymerase II (Pol II) core complex CC consisting of 12 subunits: a ten-subunit catalytic core composed of CC POLR2A/RPB1, POLR2B/RPB2, POLR2C/RPB3, POLR2I/RPB9, POLR2J/RPB11, CC POLR2E/RPABC1, POLR2F/RPABC2, POLR2H/RPABC3, POLR2K/RPABC4 and CC POLR2L/RPABC5 and a mobile stalk composed of two subunits POLR2D/RPB4 CC and POLR2G/RPB7, protruding from the core and functioning primarily in CC transcription initiation. Part of Pol II(G) complex, in which Pol II CC core associates with an additional subunit POLR2M; unlike conventional CC Pol II, Pol II(G) functions as a transcriptional repressor. Part of CC TBP-based Pol II pre-initiation complex (PIC), in which Pol II core CC assembles with general transcription factors and other specific CC initiation factors including GTF2E1, GTF2E2, GTF2F1, GTF2F2, TCEA1, CC ERCC2, ERCC3, GTF2H2, GTF2H3, GTF2H4, GTF2H5, GTF2A1, GTF2A2, GTF2B and CC TBP; this large multi-subunit PIC complex mediates DNA unwinding and CC targets Pol II core to the transcription start site where the first CC phosphodiester bond forms (PubMed:27193682, PubMed:30190596, CC PubMed:9852112). Interacts with WDR82 (PubMed:14992727, CC PubMed:17998332). Interacts with MEN1 (PubMed:14992727). CC {ECO:0000269|PubMed:14992727, ECO:0000269|PubMed:17998332, CC ECO:0000269|PubMed:27193682, ECO:0000269|PubMed:30190596, CC ECO:0000269|PubMed:9852112}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9852112}. CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X63563; CAA45124.1; -; mRNA. DR EMBL; AK289823; BAF82512.1; -; mRNA. DR EMBL; CH471057; EAX05519.1; -; Genomic_DNA. DR EMBL; BC023503; AAH23503.2; -; mRNA. DR EMBL; AF055028; AAC09367.1; -; mRNA. DR CCDS; CCDS3511.1; -. DR PIR; S28976; S28976. DR RefSeq; NP_000929.1; NM_000938.3. DR RefSeq; NP_001290197.1; NM_001303268.2. DR RefSeq; NP_001290198.1; NM_001303269.2. DR PDB; 5IY6; EM; 7.20 A; B=1-1174. DR PDB; 5IY7; EM; 8.60 A; B=1-1174. DR PDB; 5IY8; EM; 7.90 A; B=1-1174. DR PDB; 5IY9; EM; 6.30 A; B=1-1174. DR PDB; 5IYA; EM; 5.40 A; B=1-1174. DR PDB; 5IYB; EM; 3.90 A; B=1-1174. DR PDB; 5IYC; EM; 3.90 A; B=1-1174. DR PDB; 5IYD; EM; 3.90 A; B=1-1174. DR PDB; 6DRD; EM; 3.90 A; B=1-1174. DR PDB; 6O9L; EM; 7.20 A; B=1-1174. DR PDB; 6XRE; EM; 4.60 A; B=1-1174. DR PDB; 7LBM; EM; 4.80 A; B=1-1174. DR PDB; 8XRJ; EM; 3.60 A; B=1-1174. DR PDB; 8XRM; EM; 3.13 A; B=1-1174. DR PDB; 8XSO; EM; 2.70 A; B=1-1174. DR PDB; 8XVS; EM; 4.10 A; B=1-1174. DR PDB; 9EHZ; EM; 2.60 A; B=1-1174. DR PDB; 9EI1; EM; 3.20 A; B=1-1174. DR PDB; 9EI3; EM; 3.20 A; B=1-1174. DR PDB; 9EI4; EM; 3.70 A; B=1-1174. DR AlphaFoldDB; P30876; -. DR EMDB; EMD-22294; -. DR EMDB; EMD-23255; -. DR EMDB; EMD-38604; -. DR EMDB; EMD-38607; -. DR EMDB; EMD-38624; -. DR EMDB; EMD-38717; -. DR EMDB; EMD-48071; -. DR EMDB; EMD-48073; -. DR EMDB; EMD-48075; -. DR EMDB; EMD-48076; -. DR EMDB; EMD-7997; -. DR EMDB; EMD-8132; -. DR EMDB; EMD-8133; -. DR EMDB; EMD-8134; -. DR EMDB; EMD-8135; -. DR EMDB; EMD-8136; -. DR EMDB; EMD-8137; -. DR EMDB; EMD-8138; -. DR SMR; P30876; -. DR BioGRID; 111427; 403. DR ComplexPortal; CPX-2387; DNA-directed RNA polymerase II complex, Pol II(G) variant. DR ComplexPortal; CPX-7481; DNA-directed RNA polymerase II complex. DR CORUM; P30876; -. DR DIP; DIP-32910N; -. DR FunCoup; P30876; 3422. DR IntAct; P30876; 197. DR MINT; P30876; -. DR NDEx; IQUERY-CP-POLR2B; 4 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000370625; -. DR BindingDB; P30876; -. DR ChEMBL; CHEMBL6066157; -. DR GlyCosmos; P30876; 1 site, 1 glycan. DR GlyGen; P30876; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P30876; -. DR PhosphoSitePlus; P30876; -. DR SwissPalm; P30876; -. DR BioMuta; POLR2B; -. DR DMDM; 401012; -. DR jPOST; P30876; -. DR MassIVE; P30876; -. DR PaxDb; 9606-ENSP00000370625; -. DR PeptideAtlas; P30876; -. DR ProteomicsDB; 54745; -. DR Pumba; P30876; -. DR Antibodypedia; 12545; 187 antibodies from 29 providers. DR DNASU; 5431; -. DR Ensembl; ENST00000314595.6; ENSP00000312735.5; ENSG00000047315.17. DR Ensembl; ENST00000381227.5; ENSP00000370625.1; ENSG00000047315.17. DR GeneID; 5431; -. DR KEGG; hsa:5431; -. DR MANE-Select; ENST00000314595.6; ENSP00000312735.5; NM_000938.3; NP_000929.1. DR UCSC; uc003hcl.1; human. DR AGR; HGNC:9188; -. DR ClinPGx; PA33508; -. DR CTD; 5431; -. DR DisGeNET; 5431; -. DR GeneCards; POLR2B; -. DR HGNC; HGNC:9188; POLR2B. DR HPA; ENSG00000047315; Low tissue specificity. DR MIM; 180661; gene. DR OpenTargets; ENSG00000047315; -. DR VEuPathDB; HostDB:ENSG00000047315; -. DR eggNOG; KOG0214; Eukaryota. DR GeneTree; ENSGT00950000183132; -. DR InParanoid; P30876; -. DR OMA; CYDRNDS; -. DR OrthoDB; 10248617at2759; -. DR PAN-GO; P30876; 3 GO annotations based on evolutionary models. DR PhylomeDB; P30876; -. DR PathwayCommons; P30876; -. DR Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex. DR Reactome; R-HSA-113418; Formation of the Early Elongation Complex. DR Reactome; R-HSA-167152; Formation of HIV elongation complex in the absence of HIV Tat. DR Reactome; R-HSA-167158; Formation of the HIV-1 Early Elongation Complex. DR Reactome; R-HSA-167160; RNA Pol II CTD phosphorylation and interaction with CE during HIV infection. DR Reactome; R-HSA-167161; HIV Transcription Initiation. DR Reactome; R-HSA-167162; RNA Polymerase II HIV Promoter Escape. DR Reactome; R-HSA-167172; Transcription of the HIV genome. DR Reactome; R-HSA-167200; Formation of HIV-1 elongation complex containing HIV-1 Tat. DR Reactome; R-HSA-167238; Pausing and recovery of Tat-mediated HIV elongation. DR Reactome; R-HSA-167242; Abortive elongation of HIV-1 transcript in the absence of Tat. DR Reactome; R-HSA-167243; Tat-mediated HIV elongation arrest and recovery. DR Reactome; R-HSA-167246; Tat-mediated elongation of the HIV-1 transcript. DR Reactome; R-HSA-167287; HIV elongation arrest and recovery. DR Reactome; R-HSA-167290; Pausing and recovery of HIV elongation. DR Reactome; R-HSA-168325; Viral Messenger RNA Synthesis. DR Reactome; R-HSA-203927; MicroRNA (miRNA) biogenesis. DR Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs. DR Reactome; R-HSA-5601884; PIWI-interacting RNA (piRNA) biogenesis. DR Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis. DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events. DR Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex. DR Reactome; R-HSA-6781827; Transcription-Coupled Nucleotide Excision Repair (TC-NER). DR Reactome; R-HSA-6782135; Dual incision in TC-NER. DR Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER. DR Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes. DR Reactome; R-HSA-6803529; FGFR2 alternative splicing. DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes. DR Reactome; R-HSA-72086; mRNA Capping. DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway. DR Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway. DR Reactome; R-HSA-72203; Processing of Capped Intron-Containing Pre-mRNA. DR Reactome; R-HSA-73776; RNA Polymerase II Promoter Escape. DR Reactome; R-HSA-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening. DR Reactome; R-HSA-75953; RNA Polymerase II Transcription Initiation. DR Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation. DR Reactome; R-HSA-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance. DR Reactome; R-HSA-77075; RNA Pol II CTD phosphorylation and interaction with CE. DR Reactome; R-HSA-8851708; Signaling by FGFR2 IIIa TM. DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression. DR Reactome; R-HSA-9670095; Inhibition of DNA recombination at telomere. DR Reactome; R-HSA-9770562; mRNA Polyadenylation. DR Reactome; R-HSA-9918481; Dengue Virus-Host Interactions. DR SignaLink; P30876; -. DR SIGNOR; P30876; -. DR Agora; ENSG00000047315; -. DR BioGRID-ORCS; 5431; 829 hits in 1159 CRISPR screens. DR CD-CODE; DEE660B4; Stress granule. DR ChiTaRS; POLR2B; human. DR EvolutionaryTrace; P30876; -. DR GeneWiki; POLR2B; -. DR GenomeRNAi; 5431; -. DR Pharos; P30876; Tbio. DR PRO; PR:P30876; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; P30876; protein. DR Bgee; ENSG00000047315; Expressed in epithelium of nasopharynx and 217 other cell types or tissues. DR ExpressionAtlas; P30876; baseline and differential. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005665; C:RNA polymerase II, core complex; IDA:UniProtKB. DR GO; GO:0034062; F:5'-3' RNA polymerase activity; EXP:UniProtKB. DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl. DR GO; GO:0003677; F:DNA binding; TAS:ProtInc. DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IDA:UniProtKB. DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0003968; F:RNA-directed RNA polymerase activity; IDA:UniProtKB. DR GO; GO:0006354; P:DNA-templated transcription elongation; IBA:GO_Central. DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0006368; P:transcription elongation by RNA polymerase II; IDA:ComplexPortal. DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IDA:ComplexPortal. DR CDD; cd00653; RNA_pol_B_RPB2; 1. DR FunFam; 2.40.270.10:FF:000026; -; 1. DR FunFam; 2.40.50.150:FF:000002; DNA-directed RNA polymerase subunit beta; 1. DR FunFam; 3.90.1070.20:FF:000001; DNA-directed RNA polymerase subunit beta; 1. DR FunFam; 3.90.1100.10:FF:000003; DNA-directed RNA polymerase subunit beta; 1. DR FunFam; 3.90.1100.10:FF:000043; DNA-directed RNA polymerase subunit beta; 1. DR FunFam; 3.90.1110.10:FF:000002; DNA-directed RNA polymerase subunit beta; 1. DR FunFam; 3.90.1800.10:FF:000002; DNA-directed RNA polymerase subunit beta; 1. DR Gene3D; 2.40.50.150; -; 1. DR Gene3D; 3.90.1070.20; -; 1. DR Gene3D; 3.90.1100.10; -; 1. DR Gene3D; 2.40.270.10; DNA-directed RNA polymerase, subunit 2, domain 6; 1. DR Gene3D; 3.90.1800.10; RNA polymerase alpha subunit dimerisation domain; 1. DR Gene3D; 3.90.1110.10; RNA polymerase Rpb2, domain 2; 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 NCBIfam; NF007175; PRK09606.1; 1. DR PANTHER; PTHR20856; DNA-DIRECTED RNA POLYMERASE I SUBUNIT 2; 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 SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1. DR PROSITE; PS01166; RNA_POL_BETA; 1. DR PDBsum; 5IY6; -. DR PDBsum; 5IY7; -. DR PDBsum; 5IY8; -. DR PDBsum; 5IY9; -. DR PDBsum; 5IYA; -. DR PDBsum; 5IYB; -. DR PDBsum; 5IYC; -. DR PDBsum; 5IYD; -. DR PDBsum; 6DRD; -. DR PDBsum; 6O9L; -. DR PDBsum; 6XRE; -. DR PDBsum; 7LBM; -. DR PDBsum; 8XRJ; -. DR PDBsum; 8XRM; -. DR PDBsum; 8XSO; -. DR PDBsum; 8XVS; -. DR PDBsum; 9EHZ; -. DR PDBsum; 9EI1; -. DR PDBsum; 9EI3; -. DR PDBsum; 9EI4; -. PE 1: Evidence at protein level; KW 3D-structure; DNA-directed RNA polymerase; Hydrolase; Magnesium; KW Metal-binding; Methylation; Nucleotidyltransferase; Nucleus; KW Phosphoprotein; Proteomics identification; Reference proteome; KW RNA-directed RNA polymerase; Transcription; Transferase; Zinc; Zinc-finger. FT CHAIN 1..1174 FT /note="DNA-directed RNA polymerase II subunit RPB2" FT /id="PRO_0000048085" FT ZN_FING 1119..1140 FT /note="C4-type" FT /evidence="ECO:0000269|PubMed:27193682, FT ECO:0007744|PDB:5IY6" FT BINDING 409 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /ligand_label="promoter" FT /evidence="ECO:0000269|PubMed:27193682, FT ECO:0007744|PDB:5IYD" FT BINDING 456 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /ligand_label="template strand" FT /evidence="ECO:0000250|UniProtKB:A5PJW8" FT BINDING 731 FT /ligand="RNA" FT /ligand_id="ChEBI:CHEBI:33697" FT /evidence="ECO:0000250|UniProtKB:A5PJW8" FT BINDING 792 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="ligand shared with POLR2A/RPB1" FT /evidence="ECO:0000269|PubMed:27193682, FT ECO:0007744|PDB:5IYD" FT BINDING 841 FT /ligand="RNA" FT /ligand_id="ChEBI:CHEBI:33697" FT /evidence="ECO:0000250|UniProtKB:A5PJW8" FT BINDING 890 FT /ligand="RNA" FT /ligand_id="ChEBI:CHEBI:33697" FT /evidence="ECO:0000250|UniProtKB:A5PJW8" FT BINDING 942 FT /ligand="RNA" FT /ligand_id="ChEBI:CHEBI:33697" FT /evidence="ECO:0000250|UniProtKB:A5PJW8" FT BINDING 1078 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /ligand_label="template strand" FT /evidence="ECO:0000250|UniProtKB:A5PJW8" FT BINDING 1085 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /ligand_label="template strand" FT /evidence="ECO:0000250|UniProtKB:A5PJW8" FT BINDING 1119 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:27193682, FT ECO:0007744|PDB:5IY6" FT BINDING 1122 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:27193682, FT ECO:0007744|PDB:5IY6" FT BINDING 1137 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:27193682, FT ECO:0007744|PDB:5IY6" FT BINDING 1140 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:27193682, FT ECO:0007744|PDB:5IY6" FT MOD_RES 937 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1052 FT /note="N6-methyllysine" FT /evidence="ECO:0007744|PubMed:24129315" FT HELIX 22..36 FT /evidence="ECO:0007829|PDB:9EHZ" FT HELIX 41..49 FT /evidence="ECO:0007829|PDB:9EHZ" FT HELIX 50..54 FT /evidence="ECO:0007829|PDB:9EHZ" FT HELIX 55..61 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 65..67 FT /evidence="ECO:0007829|PDB:9EHZ" FT TURN 72..74 FT /evidence="ECO:0007829|PDB:8XRM" FT STRAND 83..93 FT /evidence="ECO:0007829|PDB:9EHZ" FT HELIX 94..96 FT /evidence="ECO:0007829|PDB:8XRM" FT STRAND 97..100 FT /evidence="ECO:0007829|PDB:9EHZ" FT TURN 101..103 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 104..107 FT /evidence="ECO:0007829|PDB:9EHZ" FT HELIX 110..116 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 121..133 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 135..137 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 141..153 FT /evidence="ECO:0007829|PDB:9EHZ" FT TURN 162..165 FT /evidence="ECO:0007829|PDB:9EHZ" FT HELIX 168..173 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 185..187 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 190..193 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 196..200 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 202..204 FT /evidence="ECO:0007829|PDB:8XSO" FT STRAND 205..208 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 211..225 FT /evidence="ECO:0007829|PDB:9EHZ" FT TURN 226..228 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 229..240 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 246..248 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 251..253 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 256..259 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 263..265 FT /evidence="ECO:0007829|PDB:9EHZ" FT HELIX 269..274 FT /evidence="ECO:0007829|PDB:9EHZ" FT TURN 275..277 FT /evidence="ECO:0007829|PDB:9EHZ" FT HELIX 281..288 FT /evidence="ECO:0007829|PDB:9EHZ" FT HELIX 295..307 FT /evidence="ECO:0007829|PDB:9EHZ" FT TURN 308..310 FT /evidence="ECO:0007829|PDB:8XSO" FT HELIX 314..323 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 325..327 FT /evidence="ECO:0007829|PDB:9EHZ" FT HELIX 332..341 FT /evidence="ECO:0007829|PDB:9EHZ" FT HELIX 342..346 FT /evidence="ECO:0007829|PDB:9EHZ" FT TURN 349..351 FT /evidence="ECO:0007829|PDB:9EHZ" FT HELIX 355..357 FT /evidence="ECO:0007829|PDB:9EHZ" FT HELIX 358..377 FT /evidence="ECO:0007829|PDB:9EHZ" FT HELIX 381..383 FT /evidence="ECO:0007829|PDB:9EHZ" FT HELIX 388..390 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 391..394 FT /evidence="ECO:0007829|PDB:9EHZ" FT HELIX 396..423 FT /evidence="ECO:0007829|PDB:9EHZ" FT TURN 432..434 FT /evidence="ECO:0007829|PDB:9EHZ" FT HELIX 437..450 FT /evidence="ECO:0007829|PDB:9EHZ" FT TURN 457..461 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 467..469 FT /evidence="ECO:0007829|PDB:9EHZ" FT HELIX 475..482 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 483..486 FT /evidence="ECO:0007829|PDB:9EHZ" FT TURN 497..499 FT /evidence="ECO:0007829|PDB:9EHZ" FT HELIX 503..505 FT /evidence="ECO:0007829|PDB:9EHZ" FT TURN 506..508 FT /evidence="ECO:0007829|PDB:9EHZ" FT TURN 518..522 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 523..526 FT /evidence="ECO:0007829|PDB:9EHZ" FT HELIX 539..547 FT /evidence="ECO:0007829|PDB:9EHZ" FT TURN 553..555 FT /evidence="ECO:0007829|PDB:9EHZ" FT HELIX 558..560 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 561..569 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 572..578 FT /evidence="ECO:0007829|PDB:9EHZ" FT HELIX 580..593 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 595..597 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 602..606 FT /evidence="ECO:0007829|PDB:9EHZ" FT TURN 607..610 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 611..615 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 621..629 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 632..634 FT /evidence="ECO:0007829|PDB:9EHZ" FT HELIX 637..644 FT /evidence="ECO:0007829|PDB:9EHZ" FT TURN 647..650 FT /evidence="ECO:0007829|PDB:9EHZ" FT HELIX 653..658 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 661..666 FT /evidence="ECO:0007829|PDB:9EHZ" FT HELIX 667..670 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 675..677 FT /evidence="ECO:0007829|PDB:9EHZ" FT HELIX 679..682 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 683..687 FT /evidence="ECO:0007829|PDB:8XRM" FT HELIX 700..703 FT /evidence="ECO:0007829|PDB:9EHZ" FT HELIX 707..710 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 711..713 FT /evidence="ECO:0007829|PDB:9EI1" FT HELIX 714..716 FT /evidence="ECO:0007829|PDB:9EHZ" FT HELIX 719..729 FT /evidence="ECO:0007829|PDB:9EHZ" FT TURN 738..742 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 746..753 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 758..760 FT /evidence="ECO:0007829|PDB:9EHZ" FT TURN 762..771 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 776..783 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 785..787 FT /evidence="ECO:0007829|PDB:9EHZ" FT TURN 788..792 FT /evidence="ECO:0007829|PDB:8XRM" FT STRAND 794..797 FT /evidence="ECO:0007829|PDB:9EHZ" FT HELIX 798..802 FT /evidence="ECO:0007829|PDB:9EHZ" FT TURN 803..806 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 808..817 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 822..824 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 827..829 FT /evidence="ECO:0007829|PDB:9EHZ" FT TURN 834..836 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 837..839 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 852..854 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 865..867 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 869..872 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 889..891 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 902..911 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 913..915 FT /evidence="ECO:0007829|PDB:9EI1" FT STRAND 917..927 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 934..937 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 942..949 FT /evidence="ECO:0007829|PDB:9EHZ" FT TURN 951..953 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 964..967 FT /evidence="ECO:0007829|PDB:9EHZ" FT HELIX 969..971 FT /evidence="ECO:0007829|PDB:9EHZ" FT TURN 972..975 FT /evidence="ECO:0007829|PDB:9EHZ" FT HELIX 978..993 FT /evidence="ECO:0007829|PDB:9EHZ" FT HELIX 1008..1016 FT /evidence="ECO:0007829|PDB:9EHZ" FT TURN 1017..1019 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 1024..1026 FT /evidence="ECO:0007829|PDB:9EHZ" FT TURN 1031..1033 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 1041..1052 FT /evidence="ECO:0007829|PDB:9EHZ" FT TURN 1056..1058 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 1060..1064 FT /evidence="ECO:0007829|PDB:9EHZ" FT TURN 1069..1071 FT /evidence="ECO:0007829|PDB:9EHZ" FT TURN 1078..1081 FT /evidence="ECO:0007829|PDB:9EHZ" FT HELIX 1082..1084 FT /evidence="ECO:0007829|PDB:9EHZ" FT HELIX 1088..1097 FT /evidence="ECO:0007829|PDB:9EHZ" FT HELIX 1100..1104 FT /evidence="ECO:0007829|PDB:9EHZ" FT HELIX 1105..1110 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 1113..1125 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 1127..1129 FT /evidence="ECO:0007829|PDB:9EHZ" FT TURN 1130..1133 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 1134..1137 FT /evidence="ECO:0007829|PDB:9EHZ" FT TURN 1138..1141 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 1142..1144 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 1146..1152 FT /evidence="ECO:0007829|PDB:9EHZ" FT HELIX 1153..1164 FT /evidence="ECO:0007829|PDB:9EHZ" FT STRAND 1170..1172 FT /evidence="ECO:0007829|PDB:9EHZ" SQ SEQUENCE 1174 AA; 133897 MW; 32BEDF7F95E4DE10 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 RHAIYDKLDD 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 //