RPB2_HUMAN
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 03-AUG-2022, entry version 214.
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 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, IDENTIFICATION IN THE RNA POLYMERASE II CORE-COMPLEX, AND
RP 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 [7]
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 [8]
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 [9]
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 [10]
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 [11]
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 [12]
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).
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, ECO:0000269|PubMed:9852112}.
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. Interacts with MEN1.
CC {ECO:0000269|PubMed:14992727, ECO:0000269|PubMed:17998332,
CC ECO:0000269|PubMed:9852112}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9852112}.
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 ---------------------------------------------------------------------------
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_000938.2.
DR RefSeq; NP_001290197.1; NM_001303268.1.
DR RefSeq; NP_001290198.1; NM_001303269.1.
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 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 AlphaFoldDB; P30876; -.
DR SMR; P30876; -.
DR BioGRID; 111427; 259.
DR CORUM; P30876; -.
DR DIP; DIP-32910N; -.
DR IntAct; P30876; 86.
DR MINT; P30876; -.
DR STRING; 9606.ENSP00000370625; -.
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 EPD; P30876; -.
DR jPOST; P30876; -.
DR MassIVE; P30876; -.
DR MaxQB; P30876; -.
DR PaxDb; P30876; -.
DR PeptideAtlas; P30876; -.
DR PRIDE; P30876; -.
DR ProteomicsDB; 54745; -.
DR Antibodypedia; 12545; 188 antibodies from 27 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 CTD; 5431; -.
DR DisGeNET; 5431; -.
DR GeneCards; POLR2B; -.
DR HGNC; HGNC:9188; POLR2B.
DR HPA; ENSG00000047315; Low tissue specificity.
DR MIM; 180661; gene.
DR neXtProt; NX_P30876; -.
DR OpenTargets; ENSG00000047315; -.
DR PharmGKB; PA33508; -.
DR VEuPathDB; HostDB:ENSG00000047315; -.
DR eggNOG; KOG0214; Eukaryota.
DR GeneTree; ENSGT00950000183132; -.
DR InParanoid; P30876; -.
DR OMA; RDLHGTH; -.
DR OrthoDB; 42570at2759; -.
DR PhylomeDB; P30876; -.
DR TreeFam; TF103037; -.
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 SignaLink; P30876; -.
DR SIGNOR; P30876; -.
DR BioGRID-ORCS; 5431; 798 hits in 1081 CRISPR screens.
DR ChiTaRS; POLR2B; human.
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 215 other tissues.
DR ExpressionAtlas; P30876; baseline and differential.
DR Genevisible; P30876; HS.
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:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
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:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA: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 3D-structure; DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Methylation; Nucleotidyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; 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 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:0007744|PubMed:23186163"
FT MOD_RES 1052
FT /note="N6-methyllysine"
FT /evidence="ECO:0007744|PubMed:24129315"
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
