RPB1_MOUSE
ID RPB1_MOUSE Reviewed; 1970 AA.
AC P08775; Q5F298;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 3.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=DNA-directed RNA polymerase II subunit RPB1;
DE Short=RNA polymerase II subunit B1;
DE EC=2.7.7.6;
DE AltName: Full=DNA-directed RNA polymerase II subunit A;
DE AltName: Full=DNA-directed RNA polymerase III largest subunit;
GN Name=Polr2a; Synonyms=Rpii215, Rpo2-1;
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 [GENOMIC DNA].
RX PubMed=3038894; DOI=10.1016/s0021-9258(18)61020-8;
RA Ahearn J.M. Jr., Bartolomei M.S., West M.L., Cisek L.J., Corden J.L.;
RT "Cloning and sequence analysis of the mouse genomic locus encoding the
RT largest subunit of RNA polymerase II.";
RL J. Biol. Chem. 262:10695-10705(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1587-1970.
RX PubMed=2999785; DOI=10.1073/pnas.82.23.7934;
RA Corden J.L., Cadena D.L., Ahearn J.M. Jr., Dahmus M.E.;
RT "A unique structure at the carboxyl terminus of the largest subunit of
RT eukaryotic RNA polymerase II.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:7934-7938(1985).
RN [4]
RP SEQUENCE REVISION, AND PRESENCE OF AN ADDITIONAL EXON.
RX PubMed=1542581; DOI=10.1093/nar/20.4.910;
RA Wintzerith M., Acker J., Vicaire S., Vigneron M., Kedinger C.;
RT "Complete sequence of the human RNA polymerase II largest subunit.";
RL Nucleic Acids Res. 20:910-910(1992).
RN [5]
RP INTERACTION WITH SCAF8.
RX PubMed=8692929; DOI=10.1073/pnas.93.14.6975;
RA Yuryev A., Patturajan M., Litingtung Y., Joshi R.V., Gentile C., Gebara M.,
RA Corden J.L.;
RT "The C-terminal domain of the largest subunit of RNA polymerase II
RT interacts with a novel set of serine/arginine-rich proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:6975-6980(1996).
RN [6]
RP INTERACTION WITH MYO1C.
RX PubMed=11030652; DOI=10.1126/science.290.5490.337;
RA Pestic-Dragovich L., Stojiljkovic L., Philimonenko A.A., Nowak G., Ke Y.,
RA Settlage R.E., Shabanowitz J., Hunt D.F., Hozak P., de Lanerolle P.;
RT "A myosin I isoform in the nucleus.";
RL Science 290:337-341(2000).
RN [7]
RP UBIQUITINATION AT LYS-1859; LYS-1866; LYS-1873; LYS-1887; LYS-1908 AND
RP LYS-1922, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH WWP2, AND
RP MUTAGENESIS OF LYS-1859; LYS-1866; LYS-1873; LYS-1887; LYS-1908 AND
RP LYS-1922.
RX PubMed=17526739; DOI=10.1128/mcb.01667-06;
RA Li H., Zhang Z., Wang B., Zhang J., Zhao Y., Jin Y.;
RT "Wwp2-mediated ubiquitination of the RNA polymerase II large subunit in
RT mouse embryonic pluripotent stem cells.";
RL Mol. Cell. Biol. 27:5296-5305(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [9]
RP INTERACTION WITH SUPT6H.
RX PubMed=19141475; DOI=10.1101/gad.1720008;
RA Yoh S.M., Lucas J.S., Jones K.A.;
RT "The Iws1:Spt6:CTD complex controls cotranscriptional mRNA biosynthesis and
RT HYPB/Setd2-mediated histone H3K36 methylation.";
RL Genes Dev. 22:3422-3434(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1847; SER-1849; THR-1854;
RP SER-1857; TYR-1874; SER-1878; SER-1882; THR-1894; SER-1899; TYR-1909;
RP THR-1912; SER-1913; SER-1917; SER-1920; TYR-1923; THR-1926; SER-1927;
RP SER-1931 AND SER-1934, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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).
RN [12]
RP IDENTIFICATION IN A LARGE PER COMPLEX.
RX PubMed=22767893; DOI=10.1126/science.1221592;
RA Padmanabhan K., Robles M.S., Westerling T., Weitz C.J.;
RT "Feedback regulation of transcriptional termination by the mammalian
RT circadian clock PERIOD complex.";
RL Science 337:599-602(2012).
RN [13]
RP FUNCTION, ACETYLATION BY EP300, MUTAGENESIS OF LYS-1838; LYS-1859;
RP LYS-1866; LYS-1873; LYS-1887; LYS-1908; LYS-1922 AND LYS-1936, AND
RP SUBCELLULAR LOCATION.
RX PubMed=24207025; DOI=10.1016/j.molcel.2013.10.009;
RA Schroeder S., Herker E., Itzen F., He D., Thomas S., Gilchrist D.A.,
RA Kaehlcke K., Cho S., Pollard K.S., Capra J.A., Schnoelzer M., Cole P.A.,
RA Geyer M., Bruneau B.G., Adelman K., Ott M.;
RT "Acetylation of RNA polymerase II regulates growth-factor-induced gene
RT transcription in mammalian cells.";
RL Mol. Cell 52:314-324(2013).
RN [14]
RP METHYLATION AT LYS-1838; LYS-1859; LYS-1866; LYS-1873; LYS-1887; LYS-1908;
RP LYS-1922 AND LYS-1936, ACETYLATION, MUTAGENESIS OF LYS-1838; LYS-1859;
RP LYS-1866; LYS-1873; LYS-1887; LYS-1908; LYS-1922 AND LYS-1936, FUNCTION,
RP AND SUBCELLULAR LOCATION.
RX PubMed=26687004; DOI=10.7554/elife.11215;
RA Dias J.D., Rito T., Torlai Triglia E., Kukalev A., Ferrai C., Chotalia M.,
RA Brookes E., Kimura H., Pombo A.;
RT "Methylation of RNA polymerase II non-consensus Lysine residues marks early
RT transcription in mammalian cells.";
RL Elife 4:0-0(2015).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Largest and catalytic component of RNA polymerase II which synthesizes
CC mRNA precursors and many functional non-coding RNAs. Forms the
CC polymerase active center together with the second largest subunit. Pol
CC II is the central component of the basal RNA polymerase II
CC transcription machinery. It is composed of mobile elements that move
CC relative to each other. RPB1 is part of the core element with the
CC central large cleft, the clamp element that moves to open and close the
CC cleft and the jaws that are thought to grab the incoming DNA template.
CC At the start of transcription, a single-stranded DNA template strand of
CC the promoter is positioned within the central active site cleft of Pol
CC II. A bridging helix emanates from RPB1 and crosses the cleft near the
CC catalytic site and is thought to promote translocation of Pol II by
CC acting as a ratchet that moves the RNA-DNA hybrid through the active
CC site by switching from straight to bent conformations at each step of
CC nucleotide addition. During transcription elongation, Pol II moves on
CC the template as the transcript elongates (By similarity). Elongation is
CC influenced by the phosphorylation status of the C-terminal domain (CTD)
CC of Pol II largest subunit (RPB1), which serves as a platform for
CC assembly of factors that regulate transcription initiation, elongation,
CC termination and mRNA processing (By similarity). Regulation of gene
CC expression levels depends on the balance between methylation and
CC acetylation levels of tha CTD-lysines (PubMed:26687004). Initiation or
CC early elongation steps of transcription of growth-factors-induced
CC immediate early genes are regulated by the acetylation status of the
CC CTD (PubMed:24207025). Methylation and dimethylation have a repressive
CC effect on target genes expression (PubMed:26687004).
CC {ECO:0000250|UniProtKB:P24928, ECO:0000269|PubMed:24207025,
CC ECO:0000269|PubMed:26687004}.
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. Component of a complex which is at least composed of
CC HTATSF1/Tat-SF1, the P-TEFb complex components CDK9 and CCNT1, RNA
CC polymerase II, SUPT5H, and NCL/nucleolin. The large PER complex
CC involved in the repression of transcriptional termination is composed
CC of at least PER2, CDK9, DDX5, DHX9, NCBP1 and POLR2A (active).
CC Interacts (via the C-terminal domain (CTD)) with U2AF2; recruits PRPF19
CC and the Prp19 complex to the pre-mRNA and may couple transcription to
CC pre-mRNA splicing. Interacts (via the C-terminal domain (CTD)) with
CC SMN1/SMN2; recruits SMN1/SMN2 to RNA Pol II elongation complexes.
CC Interacts via the phosphorylated C-terminal domain with WDR82 and with
CC SETD1A and SETD1B only in the presence of WDR82. When phosphorylated at
CC 'Ser-5', interacts with MEN1; the unphosphorylated form, or
CC phosphorylated at 'Ser-2' does not interact. When phosphorylated at
CC 'Ser-2', interacts with SUPT6H (via SH2 domain). Interacts with RECQL5
CC and TCEA1; binding of RECQL5 prevents TCEA1 binding. The phosphorylated
CC C-terminal domain interacts with FNBP3 and SYNCRIP. Interacts with
CC ATF7IP. Interacts with DDX5. Interacts with WWP2. Interacts with SETX.
CC Interacts (phosphorylated) with PIH1D1. Interacts (via the C-terminal
CC domain (CTD)) with TDRD3. Interacts with PRMT5. Interacts with XRN2.
CC Interacts with SAFB/SAFB1. Interacts with CCNL1. Interacts with CCNL2,
CC MYO1C, PAF1 and SFRS19. Interacts (via C-terminus) with CMTR1, CTDSP1
CC and SCAF8. Interacts (via the C-terminal domain (CTD)) with CCNT2 (By
CC similarity). Interacts with FUS (By similarity). Interacts with MCM3AP
CC (By similarity). Interacts with kinase SRPK2; the interaction occurs
CC during the co-transcriptional formation of inappropriate R-loops (By
CC similarity). {ECO:0000250|UniProtKB:P24928,
CC ECO:0000269|PubMed:11030652, ECO:0000269|PubMed:17526739,
CC ECO:0000269|PubMed:19141475, ECO:0000269|PubMed:22767893,
CC ECO:0000269|PubMed:8692929}.
CC -!- INTERACTION:
CC P08775; Q6PDM2: Srsf1; NbExp=2; IntAct=EBI-2549849, EBI-2550360;
CC P08775; Q62093: Srsf2; NbExp=3; IntAct=EBI-2549849, EBI-2550402;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24207025,
CC ECO:0000269|PubMed:26687004}. Cytoplasm {ECO:0000250|UniProtKB:P24928}.
CC Chromosome {ECO:0000250|UniProtKB:P24928}. Note=Hypophosphorylated form
CC is mainly found in the cytoplasm, while the hyperphosphorylated and
CC active form is nuclear (By similarity). Co-localizes with kinase SRPK2
CC and helicase DDX23 at chromatin loci where unscheduled R-loops form (By
CC similarity). {ECO:0000250|UniProtKB:P24928}.
CC -!- DOMAIN: The C-terminal domain (CTD) serves as a platform for assembly
CC of factors that regulate transcription initiation, elongation,
CC termination and mRNA processing. {ECO:0000305}.
CC -!- PTM: The tandem heptapeptide repeats in the C-terminal domain (CTD) can
CC be highly phosphorylated. The phosphorylation activates Pol II.
CC Phosphorylation occurs mainly at residues 'Ser-2' and 'Ser-5' of the
CC heptapeptide repeat and is mediated, at least, by CDK7 and CDK9. CDK7
CC phosphorylation of POLR2A associated with DNA promotes transcription
CC initiation by triggering dissociation from DNA. Phosphorylation also
CC takes place at 'Ser-7' of the heptapeptide repeat, which is required
CC for efficient transcription of snRNA genes and processing of the
CC transcripts. The phosphorylation state is believed to result from the
CC balanced action of site-specific CTD kinases and phosphatases, and a
CC 'CTD code' that specifies the position of Pol II within the
CC transcription cycle has been proposed. Dephosphorylated by the protein
CC phosphatase CTDSP1. {ECO:0000250|UniProtKB:P24928}.
CC -!- PTM: Among tandem heptapeptide repeats of the C-terminal domain (CTD)
CC some do not match the Y-S-P-T-S-P-S consensus, the seventh serine
CC residue 'Ser-7' being replaced by a lysine. 'Lys-7' in these non-
CC consensus heptapeptide repeats can be alternatively acetylated,
CC methylated and dimethylated. EP300 is one of the enzyme able to
CC acetylate 'Lys-7'. Acetylation at 'Lys-7' of non-consensus heptapeptide
CC repeats is associated with 'Ser-2' phosphorylation and active
CC transcription. It may regulate initiation or early elongation steps of
CC transcription specially for inducible genes.
CC {ECO:0000269|PubMed:24207025, ECO:0000269|PubMed:26687004}.
CC -!- PTM: Ubiquitinated by WWP2 leading to proteasomal degradation
CC (PubMed:17526739). Following UV treatment, the elongating form of RNA
CC polymerase II (RNA pol IIo) is ubiquitinated on UV damage sites without
CC leading to degradation: ubiquitination is facilitated by KIAA1530/UVSSA
CC and promotes RNA pol IIo backtracking to allow access to the nucleotide
CC excision repair machinery (By similarity).
CC {ECO:0000250|UniProtKB:P24928, ECO:0000269|PubMed:17526739}.
CC -!- PTM: Methylated at Arg-1810 prior to transcription initiation when the
CC CTD is hypophosphorylated, phosphorylation at Ser-1805 and Ser-1808
CC preventing this methylation. Symmetrically or asymmetrically
CC dimethylated at Arg-1810 by PRMT5 and CARM1 respectively. Symmetric or
CC asymmetric dimethylation modulates interactions with CTD-binding
CC proteins like SMN1/SMN2 and TDRD3. SMN1/SMN2 interacts preferentially
CC with the symmetrically dimethylated form while TDRD3 interacts with the
CC asymmetric form. Through the recruitment of SMN1/SMN2, symmetric
CC dimethylation is required for resolving RNA-DNA hybrids created by RNA
CC polymerase II, that form R-loop in transcription terminal regions, an
CC important step in proper transcription termination. CTD dimethylation
CC may also facilitate the expression of select RNAs. Among tandem
CC heptapeptide repeats of the C-terminal domain (CTD) some do not match
CC the Y-S-P-T-S-P-S consensus, the seventh serine residue 'Ser-7' being
CC replaced by a lysine. 'Lys-7' in these non-consensus heptapeptide
CC repeats can be alternatively acetylated, methylated, dimethylated and
CC trimethylated. Methylation occurs in the earliest transcription stages
CC and precedes or is concomitant to 'Ser-5' and 'Ser-7' phosphorylation.
CC Dimethylation and trimehtylation at 'Lys-7' of non-consensus
CC heptapeptide repeats are exclusively associated with phosphorylated
CC CTD. {ECO:0000250|UniProtKB:P24928, ECO:0000269|PubMed:26687004}.
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 temporarily coordinated by three conserved
CC aspartate residues of the two largest RNA Pol II subunits. The
CC ribonucleoside triphosphate is transferred by a rotation to the
CC nucleotide addition (A) site for pairing with the template DNA. The
CC catalytic A site involves three conserved aspartate residues of the RNA
CC Pol II largest subunit which permanently coordinate a second magnesium
CC ion.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000305}.
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DR EMBL; M12130; AAA40071.1; -; Genomic_DNA.
DR EMBL; M14101; AAA40071.1; JOINED; Genomic_DNA.
DR EMBL; AL603707; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS70217.1; -.
DR PIR; A28490; A28490.
DR RefSeq; NP_001277997.1; NM_001291068.1.
DR AlphaFoldDB; P08775; -.
DR SMR; P08775; -.
DR BioGRID; 202996; 45.
DR DIP; DIP-46369N; -.
DR IntAct; P08775; 24.
DR MINT; P08775; -.
DR STRING; 10090.ENSMUSP00000050771; -.
DR iPTMnet; P08775; -.
DR PhosphoSitePlus; P08775; -.
DR EPD; P08775; -.
DR jPOST; P08775; -.
DR MaxQB; P08775; -.
DR PaxDb; P08775; -.
DR PRIDE; P08775; -.
DR ProteomicsDB; 262702; -.
DR Antibodypedia; 3208; 921 antibodies from 42 providers.
DR DNASU; 20020; -.
DR Ensembl; ENSMUST00000058470; ENSMUSP00000050771; ENSMUSG00000005198.
DR GeneID; 20020; -.
DR KEGG; mmu:20020; -.
DR UCSC; uc007jrk.2; mouse.
DR CTD; 5430; -.
DR MGI; MGI:98086; Polr2a.
DR VEuPathDB; HostDB:ENSMUSG00000005198; -.
DR eggNOG; KOG0260; Eukaryota.
DR GeneTree; ENSGT00930000151033; -.
DR InParanoid; P08775; -.
DR OMA; SLLHICM; -.
DR OrthoDB; 591636at2759; -.
DR PhylomeDB; P08775; -.
DR TreeFam; TF103036; -.
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; 20020; 17 hits in 75 CRISPR screens.
DR ChiTaRS; Polr2a; mouse.
DR PRO; PR:P08775; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P08775; protein.
DR Bgee; ENSMUSG00000005198; Expressed in retinal neural layer and 264 other tissues.
DR ExpressionAtlas; P08775; baseline and differential.
DR Genevisible; P08775; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000791; C:euchromatin; IDA:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0000974; C:Prp19 complex; ISO:MGI.
DR GO; GO:0005665; C:RNA polymerase II, core complex; ISS:UniProtKB.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; IDA:BHF-UCL.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0071453; P:cellular response to oxygen levels; IEA:Ensembl.
DR GO; GO:0006353; P:DNA-templated transcription, termination; ISS:UniProtKB.
DR GO; GO:0033120; P:positive regulation of RNA splicing; ISS:UniProtKB.
DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; ISS:UniProtKB.
DR DisProt; DP00181; -.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.274.100; -; 1.
DR Gene3D; 3.30.1360.140; -; 1.
DR Gene3D; 4.10.860.120; -; 2.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR000722; RNA_pol_asu.
DR InterPro; IPR000684; RNA_pol_II_repeat_euk.
DR InterPro; IPR006592; RNA_pol_N.
DR InterPro; IPR007080; RNA_pol_Rpb1_1.
DR InterPro; IPR007066; RNA_pol_Rpb1_3.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR007075; RNA_pol_Rpb1_6.
DR InterPro; IPR007073; RNA_pol_Rpb1_7.
DR InterPro; IPR038593; RNA_pol_Rpb1_7_sf.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; PTHR19376; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 1.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR Pfam; PF04992; RNA_pol_Rpb1_6; 1.
DR Pfam; PF04990; RNA_pol_Rpb1_7; 1.
DR Pfam; PF05001; RNA_pol_Rpb1_R; 27.
DR SMART; SM00663; RPOLA_N; 1.
DR PROSITE; PS00115; RNA_POL_II_REPEAT; 42.
PE 1: Evidence at protein level;
KW Acetylation; Chromosome; Cytoplasm; DNA-binding;
KW DNA-directed RNA polymerase; Magnesium; Metal-binding; Methylation;
KW Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transferase; Ubl conjugation; Zinc.
FT CHAIN 1..1970
FT /note="DNA-directed RNA polymerase II subunit RPB1"
FT /id="PRO_0000073941"
FT REPEAT 1593..1599
FT /note="1"
FT REPEAT 1600..1606
FT /note="2; approximate"
FT REPEAT 1608..1614
FT /note="3"
FT REPEAT 1615..1621
FT /note="4"
FT REPEAT 1622..1628
FT /note="5"
FT REPEAT 1629..1635
FT /note="6"
FT REPEAT 1636..1642
FT /note="7"
FT REPEAT 1643..1649
FT /note="8"
FT REPEAT 1650..1656
FT /note="9"
FT REPEAT 1657..1663
FT /note="10"
FT REPEAT 1664..1670
FT /note="11"
FT REPEAT 1671..1677
FT /note="12"
FT REPEAT 1678..1684
FT /note="13"
FT REPEAT 1685..1691
FT /note="14"
FT REPEAT 1692..1698
FT /note="15"
FT REPEAT 1699..1705
FT /note="16"
FT REPEAT 1706..1712
FT /note="17"
FT REPEAT 1713..1719
FT /note="18"
FT REPEAT 1720..1726
FT /note="19"
FT REPEAT 1727..1733
FT /note="20"
FT REPEAT 1734..1740
FT /note="21"
FT REPEAT 1741..1747
FT /note="22"
FT REPEAT 1748..1754
FT /note="23"
FT REPEAT 1755..1761
FT /note="24"
FT REPEAT 1762..1768
FT /note="25"
FT REPEAT 1769..1775
FT /note="26"
FT REPEAT 1776..1782
FT /note="27"
FT REPEAT 1783..1789
FT /note="28"
FT REPEAT 1790..1796
FT /note="29"
FT REPEAT 1797..1803
FT /note="30"
FT REPEAT 1804..1810
FT /note="31"
FT REPEAT 1811..1817
FT /note="32"
FT REPEAT 1818..1824
FT /note="33"
FT REPEAT 1825..1831
FT /note="34"
FT REPEAT 1832..1838
FT /note="35"
FT REPEAT 1839..1845
FT /note="36"
FT REPEAT 1846..1852
FT /note="37"
FT REPEAT 1853..1859
FT /note="38"
FT REPEAT 1860..1866
FT /note="39"
FT REPEAT 1867..1873
FT /note="40"
FT REPEAT 1874..1880
FT /note="41"
FT REPEAT 1881..1887
FT /note="42"
FT REPEAT 1888..1894
FT /note="43"
FT REPEAT 1895..1901
FT /note="44"
FT REPEAT 1902..1908
FT /note="45"
FT REPEAT 1909..1915
FT /note="46"
FT REPEAT 1916..1922
FT /note="47"
FT REPEAT 1923..1929
FT /note="48"
FT REPEAT 1930..1936
FT /note="49"
FT REPEAT 1940..1946
FT /note="50"
FT REPEAT 1947..1953
FT /note="51; approximate"
FT REPEAT 1954..1960
FT /note="52; approximate"
FT REGION 833..845
FT /note="Bridging helix"
FT REGION 1546..1970
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1593..1960
FT /note="C-terminal domain (CTD); 52 X 7 AA approximate
FT tandem repeats of Y-[ST]-P-[STQ]-[ST]-P-[SRNTEVKGN]"
FT COMPBIAS 1565..1584
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1607..1963
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 495
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 495
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="ligand shared with RPB2"
FT /evidence="ECO:0000250"
FT BINDING 497
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 497
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="ligand shared with RPB2"
FT /evidence="ECO:0000250"
FT BINDING 499
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1603
FT /note="Omega-N-methylated arginine; by CARM1; in vitro"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1810
FT /note="Asymmetric dimethylarginine; alternate; by CARM1"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1810
FT /note="Symmetric dimethylarginine; alternate; by PRMT5"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1838
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000305|PubMed:26687004"
FT MOD_RES 1838
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000305|PubMed:26687004"
FT MOD_RES 1840
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1843
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1845
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1847
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1849
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1850
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1854
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1857
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1859
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000305|PubMed:26687004"
FT MOD_RES 1859
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000305|PubMed:26687004"
FT MOD_RES 1860
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1861
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1863
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1864
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1866
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1866
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000305|PubMed:26687004"
FT MOD_RES 1866
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1866
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000305|PubMed:26687004"
FT MOD_RES 1867
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1868
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1870
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1873
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1873
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000305|PubMed:26687004"
FT MOD_RES 1873
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000305|PubMed:26687004"
FT MOD_RES 1874
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1875
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1877
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1878
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1881
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1882
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1885
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1887
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000305|PubMed:26687004"
FT MOD_RES 1887
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1887
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000305|PubMed:26687004"
FT MOD_RES 1894
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1896
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1899
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1906
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1908
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000305|PubMed:26687004"
FT MOD_RES 1909
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1912
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1913
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1915
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1916
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1917
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1919
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1920
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1922
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000305|PubMed:26687004"
FT MOD_RES 1922
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1922
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000305|PubMed:26687004"
FT MOD_RES 1923
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1926
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1927
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1929
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1930
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1931
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1933
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1934
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1936
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000305|PubMed:26687004"
FT MOD_RES 1936
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P24928"
FT MOD_RES 1936
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000305|PubMed:26687004"
FT MUTAGEN 1838
FT /note="K->R: Loss of acetylation and loss of regulation of
FT growth-factor-induced gene expression; when associated with
FT R-1859; R-1866; R-1873; R-1887; R-1908; R-1922 and R-1936."
FT /evidence="ECO:0000269|PubMed:24207025"
FT MUTAGEN 1838
FT /note="K->S: Loss of methylation and dimethylation but no
FT effect on phosphorylation; when associated with S-1859; S-
FT 1866; S-1873; S-1887; S-1908; S-1922 and S-1936."
FT /evidence="ECO:0000269|PubMed:26687004"
FT MUTAGEN 1859
FT /note="K->R: Loss of ubiquitination, no effect on
FT interaction with WWP2; when associated with R-1866; R-1873;
FT R-1887; R-1908 and R-1922. Loss of acetylation and loss of
FT regulation of growth-factor-induced gene expression; when
FT associated with R-1838; R-1866; R-1873; R-1887; R-1908; R-
FT 1922 and R-1936."
FT /evidence="ECO:0000269|PubMed:17526739,
FT ECO:0000269|PubMed:24207025"
FT MUTAGEN 1859
FT /note="K->S: Loss of methylation and dimethylation but no
FT effect on phosphorylation; when associated with S-1838; S-
FT 1866; S-1873; S-1887; S-1908; S-1922 and S-1936. Highly
FT decreases methylation and dimethylation; when associated
FT with S-1866; S-1873; S-1887; S-1908; S-1922 and S-1936.
FT Decreases methylation but no effect on dimethylation; when
FT associated with S-1866; S-1887; S-1908 and S-1936."
FT /evidence="ECO:0000269|PubMed:26687004"
FT MUTAGEN 1866
FT /note="K->R: Loss of ubiquitination, no effect on
FT interaction with WWP2; when associated with R-1859; R-1873;
FT R-1887; R-1908 and R-1922. Loss of acetylation and loss of
FT regulation of growth-factor-induced gene expression; when
FT associated with R-1859; R-1859; R-1873; R-1887; R-1908; R-
FT 1922 and R-1936."
FT /evidence="ECO:0000269|PubMed:17526739,
FT ECO:0000269|PubMed:24207025"
FT MUTAGEN 1866
FT /note="K->S: Loss of methylation and dimethylation but no
FT effect on phosphorylation; when associated with S-1838; S-
FT 1859; S-1873; S-1887; S-1908; S-1922 and S-1936. Highly
FT decreases methylation and dimethylation; when associated
FT with S-1859; S-1873; S-1887; S-1908; S-1922 and S-1936.
FT Decreases methylation but no effect on dimethylation; when
FT associated with S-1859; S-1887; S-1908 and S-1936."
FT /evidence="ECO:0000269|PubMed:26687004"
FT MUTAGEN 1873
FT /note="K->R: Loss of ubiquitination, no effect on
FT interaction with WWP2; when associated with R-1859; R-1866;
FT R-1887; R-1908 and R-1922. Loss of acetylation and loss of
FT regulation of growth-factor-induced gene expression; when
FT associated with R-1838; R-1859; R-1866; R-1887; R-1908; R-
FT 1922 and R-1936."
FT /evidence="ECO:0000269|PubMed:17526739,
FT ECO:0000269|PubMed:24207025"
FT MUTAGEN 1873
FT /note="K->S: Loss of methylation and dimethylation but no
FT effect on phosphorylation; when associated with S-1838; S-
FT 1859; S-1866; S-1887; S-1908; S-1922 and S-1936. Highly
FT decreases methylation and dimethylation; when associated
FT with S-1859; S-1866; S-1887; S-1908 and S-1936."
FT /evidence="ECO:0000269|PubMed:26687004"
FT MUTAGEN 1887
FT /note="K->R: Loss of ubiquitination, no effect on
FT interaction with WWP2; when associated with R-1859; R-1866;
FT R-1873; R-1908 and R-1922. Loss of acetylation and loss of
FT regulation of growth-factor-induced gene expression; when
FT associated with R-1838; R-1859; R-1866; R-1873; R-1908; R-
FT 1922 and R-1936."
FT /evidence="ECO:0000269|PubMed:17526739,
FT ECO:0000269|PubMed:24207025"
FT MUTAGEN 1887
FT /note="K->S: Loss of methylation and dimethylation but no
FT effect on phosphorylation; when associated with S-1838; S-
FT 1859; S-1866; S-1873; S-1908; S-1922 and S-1936. Highly
FT decreases methylation and dimethylation; when associated
FT with S-1859; S-1866; S-1873; S-1908; S-1922 and S-1936.
FT Decreases methylation but no effect on dimethylation; when
FT associated with S-1859; S-1866; S-1908 and S-1936."
FT /evidence="ECO:0000269|PubMed:26687004"
FT MUTAGEN 1908
FT /note="K->R: Loss of ubiquitination, no effect on
FT interaction with WWP2; when associated with R-1859; R-1866;
FT R-1873; R-1887 and R-1922. Loss of acetylation and loss of
FT regulation of growth-factor-induced gene expression; when
FT associated with R.1838; R-1859; R-1866; R-1873; R-1887; R-
FT 1922 and R-1936."
FT /evidence="ECO:0000269|PubMed:17526739,
FT ECO:0000269|PubMed:24207025"
FT MUTAGEN 1908
FT /note="K->S: Loss of methylation and dimethylation but no
FT effect on phosphorylation; when associated with S-1838; S-
FT 1859; S-1866; S-1873; S-1887; S-1922 and S-1936. Highly
FT decreases methylation and dimethylation; when associated
FT with S-1859; S-1866; S-1873; S-1887; S-1922 and S-1936.
FT Decreases methylation but no effect on dimethylation; when
FT associated with S-1859; S-1866; S-1887 and S-1936."
FT /evidence="ECO:0000269|PubMed:26687004"
FT MUTAGEN 1922
FT /note="K->R: Loss of ubiquitination, no effect on
FT interaction with WWP2; when associated with R-1859; R-1866;
FT R-1873; R-1887 and R-1908. Loss of acetylation and loss of
FT regulation of growth-factor-induced gene expression; when
FT associated with R-1838; R-1859; R-1866; R-1873; R-1887; R-
FT 1908 and R-1936."
FT /evidence="ECO:0000269|PubMed:17526739,
FT ECO:0000269|PubMed:24207025"
FT MUTAGEN 1922
FT /note="K->S: Loss of methylation and dimethylation but no
FT effect on phosphorylation; when associated with S-1838; S-
FT 1859; S-1866; S-1873; S-1887; S-1908 and S-1936. Highly
FT decreases methylation and dimethylation; when associated
FT with S-1859; S-1866; S-1873; S-1887; S-1908 and S-1936."
FT /evidence="ECO:0000269|PubMed:26687004"
FT MUTAGEN 1936
FT /note="K->R: Loss of acetylation and loss of regulation of
FT growth-factor-induced gene expression; when associated with
FT R-1838; R-1859; R-1866; R-1873; R-1887; R-1908 and R-1922."
FT /evidence="ECO:0000269|PubMed:24207025"
FT MUTAGEN 1936
FT /note="K->S: Loss of methylation and dimethylation but no
FT effect on phosphorylation; when associated with S-1838; S-
FT 1859; S-1866; S-1873; S-1887; S-1908 and S-1922. Highly
FT decreases methylation and dimethylation; when associated
FT with S-1859; S-1866; S-1873; S-1887; S-1908 and S-1922.
FT Decreases methylation but no effect on dimethylation; when
FT associated with S-1859; S-1866 and S-1887."
FT /evidence="ECO:0000269|PubMed:26687004"
FT CONFLICT 1498
FT /note="P -> R (in Ref. 1; AAA40071)"
FT /evidence="ECO:0000305"
FT CONFLICT 1499..1536
FT /note="Missing (in Ref. 1; AAA40071)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1970 AA; 217176 MW; 7D76F38FD92A657E CRC64;
MHGGGPPSGD SACPLRTIKR VQFGVLSPDE LKRMSVTEGG IKYPETTEGG RPKLGGLMDP
RQGVIERTGR CQTCAGNMTE CPGHFGHIEL AKPVFHVGFL VKTMKVLRCV CFFCSKLLVD
SNNPKIKDIL AKSKGQPKKR LTHVYDLCKG KNICEGGEEM DNKFGVEQPE GDEDLTKEKG
HGGCGRYQPR IRRSGLELYA EWKHVNEDSQ EKKILLSPER VHEIFKRISD EECFVLGMEP
RYARPEWMIV TVLPVPPLSV RPAVVMQGSA RNQDDLTHKL ADIVKINNQL RRNEQNGAAA
HVIAEDVKLL QFHVATMVDN ELPGLPRAMQ KSGRPLKSLK QRLKGKEGRV RGNLMGKRVD
FSARTVITPD PNLSIDQVGV PRSIAANMTF AEIVTPFNID RLQELVRRGN SQYPGAKYII
RDNGDRIDLR FHPKPSDLHL QTGYKVERHM CDGDIVIFNR QPTLHKMSMM GHRVRILPWS
TFRLNLSVTT PYNADFDGDE MNLHLPQSLE TRAEIQELAM VPRMIVTPQS NRPVMGIVQD
TLTAVRKFTK RDVFLERGEV MNLLMFLSTW DGKVPQPAIL KPRPLWTGKQ IFSLIIPGHI
NCIRTHSTHP DDEDSGPYKH ISPGDTKVVV ENGELIMGIL CKKSLGTSAG SLVHISYLEM
GHDITRLFYS NIQTVINNWL LIEGHTIGIG DSIADSKTYQ DIQNTIKKAK QDVIEVIEKA
HNNELEPTPG NTLRQTFENQ VNRILNDARD KTGSSAQKSL SEYNNFKSMV VSGAKGSKIN
ISQVIAVVGQ QNVEGKRIPF GFKHRTLPHF IKDDYGPESR GFVENSYLAG LTPTEFFFHA
MGGREGLIDT AVKTAETGYI QRRLIKSMES VMVKYDATVR NSINQVVQLR YGEDGLAGES
VEFQNLATLK PSNKAFEKKF RFDYTNERAL RRTLQEDLVK DVLSNAHIQN ELEREFERMR
EDREVLRVIF PTGDSKVVLP CNLLRMIWNA QKIFHINPRL PSDLHPIKVV EGVKELSKKL
VIVNGDDPLS RQAQENATLL FNIHLRSTLC SRRMAEEFRL SGEAFDWLLG EIESKFNQAI
AHPGEMVGAL AAQSLGEPAT QMTLNTFHYA GVSAKNVTLG VPRLKELINI SKKPKTPSLT
VFLLGQSARD AERAKDILCR LEHTTLRKVT ANTAIYYDPN PQSTVVAEDQ EWVNVYYEMP
DFDVARISPW LLRVELDRKH MTDRKLTMEQ IAEKINAGFG DDLNCIFNDD NAEKLVLRIR
IMNSDENKMQ EEEEVVDKMD DDVFLRCIES NMLTDMTLQG IEQISKVYMH LPQTDNKKKI
IITEDGEFKA LQEWILETDG VSLMRVLSEK DVDPVRTTSN DIVEIFTVLG IEAVRKALER
ELYHVISFDG SYVNYRHLAL LCDTMTCRGH LMAITRHGVN RQDTGPLMKC SFEETVDVLM
EAAAHGESDP MKGVSENIML GQLAPAGTGC FDLLLDAEKC KYGMEIPTNI PGLGAAGPTG
MFFGSAPSPM GGISPAMTPW NQGATPAYGA WSPSVGSGMT PGAAGFSPSA ASDASGFSPG
YSPAWSPTPG SPGSPGPSSP YIPSPGGAMS PSYSPTSPAY EPRSPGGYTP QSPSYSPTSP
SYSPTSPSYS PTSPNYSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP
TSPSYSPTSP SYSPTSPSYS PTSPSYSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS
YSPTSPNYSP TSPNYTPTSP SYSPTSPSYS PTSPNYTPTS PNYSPTSPSY SPTSPSYSPT
SPSYSPSSPR YTPQSPTYTP SSPSYSPSSP SYSPTSPKYT PTSPSYSPSS PEYTPASPKY
SPTSPKYSPT SPKYSPTSPT YSPTTPKYSP TSPTYSPTSP VYTPTSPKYS PTSPTYSPTS
PKYSPTSPTY SPTSPKGSTY SPTSPGYSPT SPTYSLTSPA ISPDDSDEEN
