##gff-version 3 P08775 UniProtKB Chain 1 1970 . . . ID=PRO_0000073941;Note=DNA-directed RNA polymerase II subunit RPB1 P08775 UniProtKB Repeat 1593 1599 . . . Note=1 P08775 UniProtKB Repeat 1600 1606 . . . Note=2%3B approximate P08775 UniProtKB Repeat 1608 1614 . . . Note=3 P08775 UniProtKB Repeat 1615 1621 . . . Note=4 P08775 UniProtKB Repeat 1622 1628 . . . Note=5 P08775 UniProtKB Repeat 1629 1635 . . . Note=6 P08775 UniProtKB Repeat 1636 1642 . . . Note=7 P08775 UniProtKB Repeat 1643 1649 . . . Note=8 P08775 UniProtKB Repeat 1650 1656 . . . Note=9 P08775 UniProtKB Repeat 1657 1663 . . . Note=10 P08775 UniProtKB Repeat 1664 1670 . . . Note=11 P08775 UniProtKB Repeat 1671 1677 . . . Note=12 P08775 UniProtKB Repeat 1678 1684 . . . Note=13 P08775 UniProtKB Repeat 1685 1691 . . . Note=14 P08775 UniProtKB Repeat 1692 1698 . . . Note=15 P08775 UniProtKB Repeat 1699 1705 . . . Note=16 P08775 UniProtKB Repeat 1706 1712 . . . Note=17 P08775 UniProtKB Repeat 1713 1719 . . . Note=18 P08775 UniProtKB Repeat 1720 1726 . . . Note=19 P08775 UniProtKB Repeat 1727 1733 . . . Note=20 P08775 UniProtKB Repeat 1734 1740 . . . Note=21 P08775 UniProtKB Repeat 1741 1747 . . . Note=22 P08775 UniProtKB Repeat 1748 1754 . . . Note=23 P08775 UniProtKB Repeat 1755 1761 . . . Note=24 P08775 UniProtKB Repeat 1762 1768 . . . Note=25 P08775 UniProtKB Repeat 1769 1775 . . . Note=26 P08775 UniProtKB Repeat 1776 1782 . . . Note=27 P08775 UniProtKB Repeat 1783 1789 . . . Note=28 P08775 UniProtKB Repeat 1790 1796 . . . Note=29 P08775 UniProtKB Repeat 1797 1803 . . . Note=30 P08775 UniProtKB Repeat 1804 1810 . . . Note=31 P08775 UniProtKB Repeat 1811 1817 . . . Note=32 P08775 UniProtKB Repeat 1818 1824 . . . Note=33 P08775 UniProtKB Repeat 1825 1831 . . . Note=34 P08775 UniProtKB Repeat 1832 1838 . . . Note=35 P08775 UniProtKB Repeat 1839 1845 . . . Note=36 P08775 UniProtKB Repeat 1846 1852 . . . Note=37 P08775 UniProtKB Repeat 1853 1859 . . . Note=38 P08775 UniProtKB Repeat 1860 1866 . . . Note=39 P08775 UniProtKB Repeat 1867 1873 . . . Note=40 P08775 UniProtKB Repeat 1874 1880 . . . Note=41 P08775 UniProtKB Repeat 1881 1887 . . . Note=42 P08775 UniProtKB Repeat 1888 1894 . . . Note=43 P08775 UniProtKB Repeat 1895 1901 . . . Note=44 P08775 UniProtKB Repeat 1902 1908 . . . Note=45 P08775 UniProtKB Repeat 1909 1915 . . . Note=46 P08775 UniProtKB Repeat 1916 1922 . . . Note=47 P08775 UniProtKB Repeat 1923 1929 . . . Note=48 P08775 UniProtKB Repeat 1930 1936 . . . Note=49 P08775 UniProtKB Repeat 1940 1946 . . . Note=50 P08775 UniProtKB Repeat 1947 1953 . . . Note=51%3B approximate P08775 UniProtKB Repeat 1954 1960 . . . Note=52%3B approximate P08775 UniProtKB Region 832 873 . . . Note=Bridging helix;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G3MZY8 P08775 UniProtKB Region 1083 1124 . . . Note=Trigger loop;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G3MZY8 P08775 UniProtKB Region 1546 1970 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P08775 UniProtKB Region 1593 1960 . . . Note=C-terminal domain (CTD)%3B 52 X 7 AA approximate tandem repeats of Y-[ST]-P-[STQ]-[ST]-P-[SRNTEVKGN] P08775 UniProtKB Compositional bias 1565 1584 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P08775 UniProtKB Compositional bias 1607 1963 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P08775 UniProtKB Binding site 67 67 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G3MZY8 P08775 UniProtKB Binding site 71 71 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Binding site 74 74 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Binding site 81 81 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Binding site 84 84 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Binding site 111 111 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Binding site 114 114 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Binding site 154 154 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Binding site 184 184 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Binding site 346 346 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G3MZY8 P08775 UniProtKB Binding site 358 358 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G3MZY8 P08775 UniProtKB Binding site 460 460 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G3MZY8 P08775 UniProtKB Binding site 493 493 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Binding site 495 495 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Binding site 495 495 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Binding site 497 497 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G3MZY8 P08775 UniProtKB Binding site 497 497 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04050 P08775 UniProtKB Binding site 499 499 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Binding site 499 499 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G3MZY8 P08775 UniProtKB Binding site 1416 1416 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G3MZY8 P08775 UniProtKB Binding site 1421 1421 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G3MZY8 P08775 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Modified residue 27 27 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Modified residue 217 217 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Modified residue 1603 1603 . . . Note=Omega-N-methylated arginine%3B by CARM1%3B in vitro;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Modified residue 1810 1810 . . . Note=Asymmetric dimethylarginine%3B alternate%3B by CARM1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Modified residue 1810 1810 . . . Note=Symmetric dimethylarginine%3B alternate%3B by PRMT5;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Modified residue 1838 1838 . . . Note=N6%2CN6-dimethyllysine%3B alternate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26687004;Dbxref=PMID:26687004 P08775 UniProtKB Modified residue 1838 1838 . . . Note=N6-methyllysine%3B alternate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26687004;Dbxref=PMID:26687004 P08775 UniProtKB Modified residue 1840 1840 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Modified residue 1843 1843 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Modified residue 1845 1845 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Modified residue 1847 1847 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P08775 UniProtKB Modified residue 1849 1849 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P08775 UniProtKB Modified residue 1850 1850 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Modified residue 1854 1854 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P08775 UniProtKB Modified residue 1857 1857 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P08775 UniProtKB Modified residue 1859 1859 . . . Note=N6%2CN6-dimethyllysine%3B alternate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26687004;Dbxref=PMID:26687004 P08775 UniProtKB Modified residue 1859 1859 . . . Note=N6-methyllysine%3B alternate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26687004;Dbxref=PMID:26687004 P08775 UniProtKB Modified residue 1860 1860 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Modified residue 1861 1861 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Modified residue 1863 1863 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Modified residue 1864 1864 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Modified residue 1866 1866 . . . Note=N6%2CN6%2CN6-trimethyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Modified residue 1866 1866 . . . Note=N6%2CN6-dimethyllysine%3B alternate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26687004;Dbxref=PMID:26687004 P08775 UniProtKB Modified residue 1866 1866 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Modified residue 1866 1866 . . . Note=N6-methyllysine%3B alternate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26687004;Dbxref=PMID:26687004 P08775 UniProtKB Modified residue 1867 1867 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Modified residue 1868 1868 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Modified residue 1870 1870 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Modified residue 1873 1873 . . . Note=N6%2CN6%2CN6-trimethyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Modified residue 1873 1873 . . . Note=N6%2CN6-dimethyllysine%3B alternate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26687004;Dbxref=PMID:26687004 P08775 UniProtKB Modified residue 1873 1873 . . . Note=N6-methyllysine%3B alternate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26687004;Dbxref=PMID:26687004 P08775 UniProtKB Modified residue 1874 1874 . . . Note=Phosphotyrosine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P08775 UniProtKB Modified residue 1875 1875 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Modified residue 1877 1877 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Modified residue 1878 1878 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P08775 UniProtKB Modified residue 1881 1881 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Modified residue 1882 1882 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P08775 UniProtKB Modified residue 1885 1885 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Modified residue 1887 1887 . . . Note=N6%2CN6-dimethyllysine%3B alternate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26687004;Dbxref=PMID:26687004 P08775 UniProtKB Modified residue 1887 1887 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Modified residue 1887 1887 . . . Note=N6-methyllysine%3B alternate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26687004;Dbxref=PMID:26687004 P08775 UniProtKB Modified residue 1894 1894 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P08775 UniProtKB Modified residue 1896 1896 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Modified residue 1899 1899 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P08775 UniProtKB Modified residue 1906 1906 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Modified residue 1908 1908 . . . Note=N6%2CN6-dimethyllysine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26687004;Dbxref=PMID:26687004 P08775 UniProtKB Modified residue 1909 1909 . . . Note=Phosphotyrosine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P08775 UniProtKB Modified residue 1912 1912 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P08775 UniProtKB Modified residue 1913 1913 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P08775 UniProtKB Modified residue 1915 1915 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Modified residue 1916 1916 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Modified residue 1917 1917 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P08775 UniProtKB Modified residue 1919 1919 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Modified residue 1920 1920 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P08775 UniProtKB Modified residue 1922 1922 . . . Note=N6%2CN6-dimethyllysine%3B alternate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26687004;Dbxref=PMID:26687004 P08775 UniProtKB Modified residue 1922 1922 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Modified residue 1922 1922 . . . Note=N6-methyllysine%3B alternate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26687004;Dbxref=PMID:26687004 P08775 UniProtKB Modified residue 1923 1923 . . . Note=Phosphotyrosine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P08775 UniProtKB Modified residue 1926 1926 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P08775 UniProtKB Modified residue 1927 1927 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P08775 UniProtKB Modified residue 1929 1929 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Modified residue 1930 1930 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Modified residue 1931 1931 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P08775 UniProtKB Modified residue 1933 1933 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Modified residue 1934 1934 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P08775 UniProtKB Modified residue 1936 1936 . . . Note=N6%2CN6-dimethyllysine%3B alternate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26687004;Dbxref=PMID:26687004 P08775 UniProtKB Modified residue 1936 1936 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Modified residue 1936 1936 . . . Note=N6-methyllysine%3B alternate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26687004;Dbxref=PMID:26687004 P08775 UniProtKB Cross-link 1268 1268 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)%3B by NEDD4;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P24928 P08775 UniProtKB Mutagenesis 1268 1268 . . . Note=Mice appear phenotypically normal. Simultaneous knockout of Xpa leads to growth retardation%2C skeletal abnormalities%2C cataracts%2C progressive motor neuron degeneration and death at 5-6 months. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32142649;Dbxref=PMID:32142649 P08775 UniProtKB Mutagenesis 1838 1838 . . . Note=Loss of acetylation and loss of regulation of growth-factor-induced gene expression%3B when associated with R-1859%3B R-1866%3B R-1873%3B R-1887%3B R-1908%3B R-1922 and R-1936. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24207025;Dbxref=PMID:24207025 P08775 UniProtKB Mutagenesis 1838 1838 . . . Note=Loss of methylation and dimethylation but no effect on phosphorylation%3B when associated with S-1859%3B S-1866%3B S-1873%3B S-1887%3B S-1908%3B S-1922 and S-1936. K->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26687004;Dbxref=PMID:26687004 P08775 UniProtKB Mutagenesis 1859 1859 . . . Note=Loss of ubiquitination%2C no effect on interaction with WWP2%3B when associated with R-1866%3B R-1873%3B R-1887%3B R-1908 and R-1922. Loss of acetylation and loss of regulation of growth-factor-induced gene expression%3B when associated with R-1838%3B R-1866%3B R-1873%3B R-1887%3B R-1908%3B R-1922 and R-1936. K->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17526739,ECO:0000269|PubMed:24207025;Dbxref=PMID:17526739,PMID:24207025 P08775 UniProtKB Mutagenesis 1859 1859 . . . Note=Loss of methylation and dimethylation but no effect on phosphorylation%3B when associated with S-1838%3B S-1866%3B S-1873%3B S-1887%3B S-1908%3B S-1922 and S-1936. Highly decreases methylation and dimethylation%3B when associated with S-1866%3B S-1873%3B S-1887%3B S-1908%3B S-1922 and S-1936. Decreases methylation but no effect on dimethylation%3B when associated with S-1866%3B S-1887%3B S-1908 and S-1936. K->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26687004;Dbxref=PMID:26687004 P08775 UniProtKB Mutagenesis 1866 1866 . . . Note=Loss of ubiquitination%2C no effect on interaction with WWP2%3B when associated with R-1859%3B R-1873%3B R-1887%3B R-1908 and R-1922. Loss of acetylation and loss of regulation of growth-factor-induced gene expression%3B when associated with R-1859%3B R-1859%3B R-1873%3B R-1887%3B R-1908%3B R-1922 and R-1936. K->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17526739,ECO:0000269|PubMed:24207025;Dbxref=PMID:17526739,PMID:24207025 P08775 UniProtKB Mutagenesis 1866 1866 . . . Note=Loss of methylation and dimethylation but no effect on phosphorylation%3B when associated with S-1838%3B S-1859%3B S-1873%3B S-1887%3B S-1908%3B S-1922 and S-1936. Highly decreases methylation and dimethylation%3B when associated with S-1859%3B S-1873%3B S-1887%3B S-1908%3B S-1922 and S-1936. Decreases methylation but no effect on dimethylation%3B when associated with S-1859%3B S-1887%3B S-1908 and S-1936. K->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26687004;Dbxref=PMID:26687004 P08775 UniProtKB Mutagenesis 1873 1873 . . . Note=Loss of ubiquitination%2C no effect on interaction with WWP2%3B when associated with R-1859%3B R-1866%3B R-1887%3B R-1908 and R-1922. Loss of acetylation and loss of regulation of growth-factor-induced gene expression%3B when associated with R-1838%3B R-1859%3B R-1866%3B R-1887%3B R-1908%3B R-1922 and R-1936. K->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17526739,ECO:0000269|PubMed:24207025;Dbxref=PMID:17526739,PMID:24207025 P08775 UniProtKB Mutagenesis 1873 1873 . . . Note=Loss of methylation and dimethylation but no effect on phosphorylation%3B when associated with S-1838%3B S-1859%3B S-1866%3B S-1887%3B S-1908%3B S-1922 and S-1936. Highly decreases methylation and dimethylation%3B when associated with S-1859%3B S-1866%3B S-1887%3B S-1908 and S-1936. K->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26687004;Dbxref=PMID:26687004 P08775 UniProtKB Mutagenesis 1887 1887 . . . Note=Loss of ubiquitination%2C no effect on interaction with WWP2%3B when associated with R-1859%3B R-1866%3B R-1873%3B R-1908 and R-1922. Loss of acetylation and loss of regulation of growth-factor-induced gene expression%3B when associated with R-1838%3B R-1859%3B R-1866%3B R-1873%3B R-1908%3B R-1922 and R-1936. K->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17526739,ECO:0000269|PubMed:24207025;Dbxref=PMID:17526739,PMID:24207025 P08775 UniProtKB Mutagenesis 1887 1887 . . . Note=Loss of methylation and dimethylation but no effect on phosphorylation%3B when associated with S-1838%3B S-1859%3B S-1866%3B S-1873%3B S-1908%3B S-1922 and S-1936. Highly decreases methylation and dimethylation%3B when associated with S-1859%3B S-1866%3B S-1873%3B S-1908%3B S-1922 and S-1936. Decreases methylation but no effect on dimethylation%3B when associated with S-1859%3B S-1866%3B S-1908 and S-1936. K->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26687004;Dbxref=PMID:26687004 P08775 UniProtKB Mutagenesis 1908 1908 . . . Note=Loss of ubiquitination%2C no effect on interaction with WWP2%3B when associated with R-1859%3B R-1866%3B R-1873%3B R-1887 and R-1922. Loss of acetylation and loss of regulation of growth-factor-induced gene expression%3B when associated with R.1838%3B R-1859%3B R-1866%3B R-1873%3B R-1887%3B R-1922 and R-1936. K->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17526739,ECO:0000269|PubMed:24207025;Dbxref=PMID:17526739,PMID:24207025 P08775 UniProtKB Mutagenesis 1908 1908 . . . Note=Loss of methylation and dimethylation but no effect on phosphorylation%3B when associated with S-1838%3B S-1859%3B S-1866%3B S-1873%3B S-1887%3B S-1922 and S-1936. Highly decreases methylation and dimethylation%3B when associated with S-1859%3B S-1866%3B S-1873%3B S-1887%3B S-1922 and S-1936. Decreases methylation but no effect on dimethylation%3B when associated with S-1859%3B S-1866%3B S-1887 and S-1936. K->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26687004;Dbxref=PMID:26687004 P08775 UniProtKB Mutagenesis 1922 1922 . . . Note=Loss of ubiquitination%2C no effect on interaction with WWP2%3B when associated with R-1859%3B R-1866%3B R-1873%3B R-1887 and R-1908. Loss of acetylation and loss of regulation of growth-factor-induced gene expression%3B when associated with R-1838%3B R-1859%3B R-1866%3B R-1873%3B R-1887%3B R-1908 and R-1936. K->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17526739,ECO:0000269|PubMed:24207025;Dbxref=PMID:17526739,PMID:24207025 P08775 UniProtKB Mutagenesis 1922 1922 . . . Note=Loss of methylation and dimethylation but no effect on phosphorylation%3B when associated with S-1838%3B S-1859%3B S-1866%3B S-1873%3B S-1887%3B S-1908 and S-1936. Highly decreases methylation and dimethylation%3B when associated with S-1859%3B S-1866%3B S-1873%3B S-1887%3B S-1908 and S-1936. K->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26687004;Dbxref=PMID:26687004 P08775 UniProtKB Mutagenesis 1936 1936 . . . Note=Loss of acetylation and loss of regulation of growth-factor-induced gene expression%3B when associated with R-1838%3B R-1859%3B R-1866%3B R-1873%3B R-1887%3B R-1908 and R-1922. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24207025;Dbxref=PMID:24207025 P08775 UniProtKB Mutagenesis 1936 1936 . . . Note=Loss of methylation and dimethylation but no effect on phosphorylation%3B when associated with S-1838%3B S-1859%3B S-1866%3B S-1873%3B S-1887%3B S-1908 and S-1922. Highly decreases methylation and dimethylation%3B when associated with S-1859%3B S-1866%3B S-1873%3B S-1887%3B S-1908 and S-1922. Decreases methylation but no effect on dimethylation%3B when associated with S-1859%3B S-1866 and S-1887. K->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26687004;Dbxref=PMID:26687004 P08775 UniProtKB Sequence conflict 1498 1498 . . . Note=P->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 P08775 UniProtKB Sequence conflict 1499 1536 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305