dbPTM

RPB1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RPB1_MOUSE
UniProt AC	P08775
Protein Name	DNA-directed RNA polymerase II subunit RPB1
Gene Name	Polr2a
Organism	Mus musculus (Mouse).
Sequence Length	1970
Subcellular Localization	Nucleus . Cytoplasm . Hypophosphorylated form is mainly found in the cytoplasm, while the hyperphosphorylated and active form is nuclear.
Protein Description	DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Forms the polymerase active center together with the second largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB1 is part of the core element with the central large cleft, the clamp element that moves to open and close the cleft and the jaws that are thought to grab the incoming DNA template. At the start of transcription, a single-stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol II. A bridging helix emanates from RPB1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol II by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition. During transcription elongation, Pol II moves on the template as the transcript elongates (By similarity). Elongation is influenced by the phosphorylation status of the C-terminal domain (CTD) of Pol II largest subunit (RPB1), which serves as a platform for assembly of factors that regulate transcription initiation, elongation, termination and mRNA processing (By similarity). Regulation of gene expression levels depends on the balance between methylation and acetylation levels of tha CTD-lysines. [PubMed: 26687004 Initiation or early elongation steps of transcription of growth-factors-induced immediate early genes are regulated by the acetylation status of the CTD]
Protein Sequence	MHGGGPPSGDSACPLRTIKRVQFGVLSPDELKRMSVTEGGIKYPETTEGGRPKLGGLMDPRQGVIERTGRCQTCAGNMTECPGHFGHIELAKPVFHVGFLVKTMKVLRCVCFFCSKLLVDSNNPKIKDILAKSKGQPKKRLTHVYDLCKGKNICEGGEEMDNKFGVEQPEGDEDLTKEKGHGGCGRYQPRIRRSGLELYAEWKHVNEDSQEKKILLSPERVHEIFKRISDEECFVLGMEPRYARPEWMIVTVLPVPPLSVRPAVVMQGSARNQDDLTHKLADIVKINNQLRRNEQNGAAAHVIAEDVKLLQFHVATMVDNELPGLPRAMQKSGRPLKSLKQRLKGKEGRVRGNLMGKRVDFSARTVITPDPNLSIDQVGVPRSIAANMTFAEIVTPFNIDRLQELVRRGNSQYPGAKYIIRDNGDRIDLRFHPKPSDLHLQTGYKVERHMCDGDIVIFNRQPTLHKMSMMGHRVRILPWSTFRLNLSVTTPYNADFDGDEMNLHLPQSLETRAEIQELAMVPRMIVTPQSNRPVMGIVQDTLTAVRKFTKRDVFLERGEVMNLLMFLSTWDGKVPQPAILKPRPLWTGKQIFSLIIPGHINCIRTHSTHPDDEDSGPYKHISPGDTKVVVENGELIMGILCKKSLGTSAGSLVHISYLEMGHDITRLFYSNIQTVINNWLLIEGHTIGIGDSIADSKTYQDIQNTIKKAKQDVIEVIEKAHNNELEPTPGNTLRQTFENQVNRILNDARDKTGSSAQKSLSEYNNFKSMVVSGAKGSKINISQVIAVVGQQNVEGKRIPFGFKHRTLPHFIKDDYGPESRGFVENSYLAGLTPTEFFFHAMGGREGLIDTAVKTAETGYIQRRLIKSMESVMVKYDATVRNSINQVVQLRYGEDGLAGESVEFQNLATLKPSNKAFEKKFRFDYTNERALRRTLQEDLVKDVLSNAHIQNELEREFERMREDREVLRVIFPTGDSKVVLPCNLLRMIWNAQKIFHINPRLPSDLHPIKVVEGVKELSKKLVIVNGDDPLSRQAQENATLLFNIHLRSTLCSRRMAEEFRLSGEAFDWLLGEIESKFNQAIAHPGEMVGALAAQSLGEPATQMTLNTFHYAGVSAKNVTLGVPRLKELINISKKPKTPSLTVFLLGQSARDAERAKDILCRLEHTTLRKVTANTAIYYDPNPQSTVVAEDQEWVNVYYEMPDFDVARISPWLLRVELDRKHMTDRKLTMEQIAEKINAGFGDDLNCIFNDDNAEKLVLRIRIMNSDENKMQEEEEVVDKMDDDVFLRCIESNMLTDMTLQGIEQISKVYMHLPQTDNKKKIIITEDGEFKALQEWILETDGVSLMRVLSEKDVDPVRTTSNDIVEIFTVLGIEAVRKALERELYHVISFDGSYVNYRHLALLCDTMTCRGHLMAITRHGVNRQDTGPLMKCSFEETVDVLMEAAAHGESDPMKGVSENIMLGQLAPAGTGCFDLLLDAEKCKYGMEIPTNIPGLGAAGPTGMFFGSAPSPMGGISPAMTPWNQGATPAYGAWSPSVGSGMTPGAAGFSPSAASDASGFSPGYSPAWSPTPGSPGSPGPSSPYIPSPGGAMSPSYSPTSPAYEPRSPGGYTPQSPSYSPTSPSYSPTSPSYSPTSPNYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPNYSPTSPNYTPTSPSYSPTSPSYSPTSPNYTPTSPNYSPTSPSYSPTSPSYSPTSPSYSPSSPRYTPQSPTYTPSSPSYSPSSPSYSPTSPKYTPTSPSYSPSSPEYTPASPKYSPTSPKYSPTSPKYSPTSPTYSPTTPKYSPTSPTYSPTSPVYTPTSPKYSPTSPTYSPTSPKYSPTSPTYSPTSPKGSTYSPTSPGYSPTSPTYSLTSPAISPDDSDEEN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MHGGGPPS -------CCCCCCCC	31.36	-
27	Phosphorylation	RVQFGVLSPDELKRM EEEEEECCHHHHHHC	28.09	26745281
121	Phosphorylation	CSKLLVDSNNPKIKD HHHHHHCCCCHHHHH	30.90	25266776
127	Acetylation	DSNNPKIKDILAKSK CCCCHHHHHHHHHCC	44.86	15603141
139	Acetylation	KSKGQPKKRLTHVYD HCCCCCCCCCCHHHH	60.36	68707
145	Phosphorylation	KKRLTHVYDLCKGKN CCCCCHHHHHHCCCC	8.80	-
177	Ubiquitination	EGDEDLTKEKGHGGC CCCCCCHHHCCCCCC	65.80	-
217	Phosphorylation	QEKKILLSPERVHEI HHCEECCCHHHHHHH	22.67	28066266
226	Acetylation	ERVHEIFKRISDEEC HHHHHHHHHCCHHHC	55.26	19849963
285	Acetylation	HKLADIVKINNQLRR HHHHHHHHHHHHHHH	39.80	7609797
411	Phosphorylation	ELVRRGNSQYPGAKY HHHHCCCCCCCCCEE	33.64	23737553
413	Phosphorylation	VRRGNSQYPGAKYII HHCCCCCCCCCEEEE	11.94	23737553
468	Phosphorylation	QPTLHKMSMMGHRVR CCCCHHHHHCCCCEE	15.49	25195567
699	Phosphorylation	SIADSKTYQDIQNTI HHHCCCHHHHHHHHH	14.13	25338131
705	Phosphorylation	TYQDIQNTIKKAKQD HHHHHHHHHHHHHHH	20.14	25338131
710	Acetylation	QNTIKKAKQDVIEVI HHHHHHHHHHHHHHH	56.78	88943
758	Ubiquitination	KTGSSAQKSLSEYNN HCCCHHHHHHHHHHC	53.75	22790023
796	Ubiquitination	GQQNVEGKRIPFGFK ECCCCCCCCCCCCCC	33.38	-
878	Phosphorylation	VMVKYDATVRNSINQ HHHHCCHHHHHHHHH	19.66	-
914	Ubiquitination	ATLKPSNKAFEKKFR CCCCCCCHHHHHHHC	59.81	-
918	Ubiquitination	PSNKAFEKKFRFDYT CCCHHHHHHHCCCCC	51.24	-
919	Ubiquitination	SNKAFEKKFRFDYTN CCHHHHHHHCCCCCC	34.28	-
1014	Ubiquitination	IKVVEGVKELSKKLV CEEHHHHHHHHCCEE	64.89	22790023
1017	Phosphorylation	VEGVKELSKKLVIVN HHHHHHHHCCEEEEC	28.92	30482847
1136	Phosphorylation	NISKKPKTPSLTVFL CCCCCCCCCCEEEEE	27.00	26745281
1138	Phosphorylation	SKKPKTPSLTVFLLG CCCCCCCCEEEEECC	41.73	26745281
1264	Phosphorylation	LRIRIMNSDENKMQE EEEEECCCCCCHHHH	28.99	22817900
1268	Ubiquitination	IMNSDENKMQEEEEV ECCCCCCHHHHHHHH	39.65	22790023
1348	Phosphorylation	VSLMRVLSEKDVDPV CCCCHHHHCCCCCCC	39.48	29176673
1350	Ubiquitination	LMRVLSEKDVDPVRT CCHHHHCCCCCCCCC	60.73	27667366
1424	Phosphorylation	HGVNRQDTGPLMKCS CCCCCCCCCCCCCCC	32.15	-
1603	Methylation	TSPAYEPRSPGGYTP CCCCCCCCCCCCCCC	43.47	-
1616	Phosphorylation	TPQSPSYSPTSPSYS CCCCCCCCCCCCCCC	26.49	21639898
1618	O-linked_Glycosylation	QSPSYSPTSPSYSPT CCCCCCCCCCCCCCC	47.53	50085001
1618	Phosphorylation	QSPSYSPTSPSYSPT CCCCCCCCCCCCCCC	47.53	-
1619	Phosphorylation	SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC	18.42	20231280
1626	Phosphorylation	SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC	18.42	1899239
1647	Phosphorylation	SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC	18.42	1899239
1654	Phosphorylation	SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC	18.42	1899239
1661	Phosphorylation	SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC	18.42	1899239
1668	Phosphorylation	SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC	18.42	1899239
1675	Phosphorylation	SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC	18.42	1899239
1682	Phosphorylation	SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC	18.42	1899239
1689	Phosphorylation	SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC	18.42	1899239
1696	Phosphorylation	SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC	18.42	1899239
1703	Phosphorylation	SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC	18.42	1899239
1710	Phosphorylation	SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC	18.42	1899239
1717	Phosphorylation	SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC	18.42	1899239
1724	Phosphorylation	SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC	18.42	1899239
1731	Phosphorylation	SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC	18.42	1899239
1738	Phosphorylation	SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC	18.42	1899239
1766	Phosphorylation	SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC	18.42	1899239
1794	Phosphorylation	SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC	18.42	1899239
1804	Phosphorylation	YSPTSPSYSPSSPRY CCCCCCCCCCCCCCC	28.16	22817900
1810	Asymmetric dimethylarginine	SYSPSSPRYTPQSPT CCCCCCCCCCCCCCC	50.32	-
1810	Methylation	SYSPSSPRYTPQSPT CCCCCCCCCCCCCCC	50.32	42658001
1811	Phosphorylation	YSPSSPRYTPQSPTY CCCCCCCCCCCCCCC	26.59	26643407
1812	Phosphorylation	SPSSPRYTPQSPTYT CCCCCCCCCCCCCCC	19.01	26643407
1815	Phosphorylation	SPRYTPQSPTYTPSS CCCCCCCCCCCCCCC	22.03	26643407
1817	Phosphorylation	RYTPQSPTYTPSSPS CCCCCCCCCCCCCCC	45.32	26643407
1818	Phosphorylation	YTPQSPTYTPSSPSY CCCCCCCCCCCCCCC	21.75	26643407
1819	Phosphorylation	TPQSPTYTPSSPSYS CCCCCCCCCCCCCCC	21.12	26643407
1821	Phosphorylation	QSPTYTPSSPSYSPS CCCCCCCCCCCCCCC	47.26	26643407
1822	Phosphorylation	SPTYTPSSPSYSPSS CCCCCCCCCCCCCCC	21.04	26643407
1824	Phosphorylation	TYTPSSPSYSPSSPS CCCCCCCCCCCCCCC	39.94	26643407
1825	Phosphorylation	YTPSSPSYSPSSPSY CCCCCCCCCCCCCCC	28.16	26643407
1826	Phosphorylation	TPSSPSYSPSSPSYS CCCCCCCCCCCCCCC	23.73	26745281
1828	Phosphorylation	SSPSYSPSSPSYSPT CCCCCCCCCCCCCCC	49.27	26745281
1829	Phosphorylation	SPSYSPSSPSYSPTS CCCCCCCCCCCCCCC	22.65	26745281
1831	Phosphorylation	SYSPSSPSYSPTSPK CCCCCCCCCCCCCCC	39.94	26643407
1832	Phosphorylation	YSPSSPSYSPTSPKY CCCCCCCCCCCCCCC	23.27	26745281
1833	Phosphorylation	SPSSPSYSPTSPKYT CCCCCCCCCCCCCCC	26.49	26745281
1835	Phosphorylation	SSPSYSPTSPKYTPT CCCCCCCCCCCCCCC	52.28	21082442
1836	Phosphorylation	SPSYSPTSPKYTPTS CCCCCCCCCCCCCCC	23.84	27818261
1838	Methylation	SYSPTSPKYTPTSPS CCCCCCCCCCCCCCC	62.62	26687004
1839	Phosphorylation	YSPTSPKYTPTSPSY CCCCCCCCCCCCCCC	22.72	27087446
1840	Phosphorylation	SPTSPKYTPTSPSYS CCCCCCCCCCCCCCC	26.64	23375375
1842	Phosphorylation	TSPKYTPTSPSYSPS CCCCCCCCCCCCCCC	45.53	22942356
1843	Phosphorylation	SPKYTPTSPSYSPSS CCCCCCCCCCCCCCC	17.04	27087446
1845	Phosphorylation	KYTPTSPSYSPSSPE CCCCCCCCCCCCCCC	37.70	27087446
1846	Phosphorylation	YTPTSPSYSPSSPEY CCCCCCCCCCCCCCC	28.16	23375375
1847	Phosphorylation	TPTSPSYSPSSPEYT CCCCCCCCCCCCCCC	23.73	23375375
1849	Phosphorylation	TSPSYSPSSPEYTPA CCCCCCCCCCCCCCC	53.21	27087446
1850	Phosphorylation	SPSYSPSSPEYTPAS CCCCCCCCCCCCCCC	25.74	27087446
1853	Phosphorylation	YSPSSPEYTPASPKY CCCCCCCCCCCCCCC	22.77	21082442
1854	Phosphorylation	SPSSPEYTPASPKYS CCCCCCCCCCCCCCC	15.66	22942356
1857	Phosphorylation	SPEYTPASPKYSPTS CCCCCCCCCCCCCCC	24.11	25521595
1859	Methylation	EYTPASPKYSPTSPK CCCCCCCCCCCCCCC	56.73	26687004
1859	Ubiquitination	EYTPASPKYSPTSPK CCCCCCCCCCCCCCC	56.73	17526739
1860	Phosphorylation	YTPASPKYSPTSPKY CCCCCCCCCCCCCCC	24.22	21082442
1861	Phosphorylation	TPASPKYSPTSPKYS CCCCCCCCCCCCCCC	28.03	23684622
1863	Phosphorylation	ASPKYSPTSPKYSPT CCCCCCCCCCCCCCC	52.28	23375375
1864	Phosphorylation	SPKYSPTSPKYSPTS CCCCCCCCCCCCCCC	23.84	25521595
1866	Acetylation	KYSPTSPKYSPTSPK CCCCCCCCCCCCCCC	59.12	-
1866	Methylation	KYSPTSPKYSPTSPK CCCCCCCCCCCCCCC	59.12	26687004
1866	Ubiquitination	KYSPTSPKYSPTSPK CCCCCCCCCCCCCCC	59.12	17526739
1867	Phosphorylation	YSPTSPKYSPTSPKY CCCCCCCCCCCCCCC	24.22	23684622
1868	Phosphorylation	SPTSPKYSPTSPKYS CCCCCCCCCCCCCCC	28.03	23375375
1870	Phosphorylation	TSPKYSPTSPKYSPT CCCCCCCCCCCCCCC	52.28	23684622
1871	Phosphorylation	SPKYSPTSPKYSPTS CCCCCCCCCCCCCCC	23.84	25521595
1873	Methylation	KYSPTSPKYSPTSPT CCCCCCCCCCCCCCC	59.12	26687004
1873	Ubiquitination	KYSPTSPKYSPTSPT CCCCCCCCCCCCCCC	59.12	17526739
1874	Phosphorylation	YSPTSPKYSPTSPTY CCCCCCCCCCCCCCC	24.22	23527152
1875	Phosphorylation	SPTSPKYSPTSPTYS CCCCCCCCCCCCCCC	28.03	23375375
1877	Phosphorylation	TSPKYSPTSPTYSPT CCCCCCCCCCCCCCC	41.20	23684622
1878	Phosphorylation	SPKYSPTSPTYSPTT CCCCCCCCCCCCCCC	20.73	26824392
1880	Phosphorylation	KYSPTSPTYSPTTPK CCCCCCCCCCCCCCC	36.08	23684622
1881	Phosphorylation	YSPTSPTYSPTTPKY CCCCCCCCCCCCCCC	18.94	21082442
1882	Phosphorylation	SPTSPTYSPTTPKYS CCCCCCCCCCCCCCC	20.46	23684622
1884	Phosphorylation	TSPTYSPTTPKYSPT CCCCCCCCCCCCCCC	50.19	23684622
1885	Phosphorylation	SPTYSPTTPKYSPTS CCCCCCCCCCCCCCC	22.59	25521595
1887	Acetylation	TYSPTTPKYSPTSPT CCCCCCCCCCCCCCC	57.16	-
1887	Methylation	TYSPTTPKYSPTSPT CCCCCCCCCCCCCCC	57.16	26687004
1887	Ubiquitination	TYSPTTPKYSPTSPT CCCCCCCCCCCCCCC	57.16	17526739
1888	Phosphorylation	YSPTTPKYSPTSPTY CCCCCCCCCCCCCCC	22.53	27087446
1889	Phosphorylation	SPTTPKYSPTSPTYS CCCCCCCCCCCCCCC	28.03	22942356
1891	Phosphorylation	TTPKYSPTSPTYSPT CCCCCCCCCCCCCCC	41.20	22942356
1892	Phosphorylation	TPKYSPTSPTYSPTS CCCCCCCCCCCCCCC	20.73	25521595
1894	Phosphorylation	KYSPTSPTYSPTSPV CCCCCCCCCCCCCCC	36.08	27087446
1895	Phosphorylation	YSPTSPTYSPTSPVY CCCCCCCCCCCCCCC	18.94	23375375
1896	Phosphorylation	SPTSPTYSPTSPVYT CCCCCCCCCCCCCCC	24.95	23375375
1898	Phosphorylation	TSPTYSPTSPVYTPT CCCCCCCCCCCCCCC	39.46	23375375
1899	Phosphorylation	SPTYSPTSPVYTPTS CCCCCCCCCCCCCCC	18.76	22942356
1902	Phosphorylation	YSPTSPVYTPTSPKY CCCCCCCCCCCCCCC	15.47	27087446
1903	Phosphorylation	SPTSPVYTPTSPKYS CCCCCCCCCCCCCCC	21.96	23684622
1905	Phosphorylation	TSPVYTPTSPKYSPT CCCCCCCCCCCCCCC	50.27	23684622
1906	Phosphorylation	SPVYTPTSPKYSPTS CCCCCCCCCCCCCCC	22.16	25521595
1908	Methylation	VYTPTSPKYSPTSPT CCCCCCCCCCCCCCC	59.12	26687004
1908	Ubiquitination	VYTPTSPKYSPTSPT CCCCCCCCCCCCCCC	59.12	17526739
1909	Phosphorylation	YTPTSPKYSPTSPTY CCCCCCCCCCCCCCC	24.22	25521595
1910	Phosphorylation	TPTSPKYSPTSPTYS CCCCCCCCCCCCCCC	28.03	25521595
1912	Phosphorylation	TSPKYSPTSPTYSPT CCCCCCCCCCCCCCC	41.20	25521595
1913	Phosphorylation	SPKYSPTSPTYSPTS CCCCCCCCCCCCCCC	20.73	27087446
1915	Phosphorylation	KYSPTSPTYSPTSPK CCCCCCCCCCCCCCC	36.08	25521595
1916	Phosphorylation	YSPTSPTYSPTSPKY CCCCCCCCCCCCCCC	18.94	25521595
1917	Phosphorylation	SPTSPTYSPTSPKYS CCCCCCCCCCCCCCC	24.95	25521595
1919	Phosphorylation	TSPTYSPTSPKYSPT CCCCCCCCCCCCCCC	52.28	25521595
1920	Phosphorylation	SPTYSPTSPKYSPTS CCCCCCCCCCCCCCC	23.84	27087446
1922	Acetylation	TYSPTSPKYSPTSPT CCCCCCCCCCCCCCC	59.12	-
1922	Methylation	TYSPTSPKYSPTSPT CCCCCCCCCCCCCCC	59.12	26687004
1922	Ubiquitination	TYSPTSPKYSPTSPT CCCCCCCCCCCCCCC	59.12	17526739
1923	Phosphorylation	YSPTSPKYSPTSPTY CCCCCCCCCCCCCCC	24.22	27087446
1924	Phosphorylation	SPTSPKYSPTSPTYS CCCCCCCCCCCCCCC	28.03	27742792
1926	Phosphorylation	TSPKYSPTSPTYSPT CCCCCCCCCCCCCCC	41.20	27087446
1927	Phosphorylation	SPKYSPTSPTYSPTS CCCCCCCCCCCCCCC	20.73	27087446
1929	Phosphorylation	KYSPTSPTYSPTSPK CCCCCCCCCCCCCCC	36.08	27087446
1930	Phosphorylation	YSPTSPTYSPTSPKG CCCCCCCCCCCCCCC	18.94	27087446
1931	Phosphorylation	SPTSPTYSPTSPKGS CCCCCCCCCCCCCCC	24.95	27087446
1933	Phosphorylation	TSPTYSPTSPKGSTY CCCCCCCCCCCCCCC	52.28	27742792
1934	Phosphorylation	SPTYSPTSPKGSTYS CCCCCCCCCCCCCCC	28.18	27087446
1936	Acetylation	TYSPTSPKGSTYSPT CCCCCCCCCCCCCCC	66.32	-
1936	Methylation	TYSPTSPKGSTYSPT CCCCCCCCCCCCCCC	66.32	26687004
1940	Phosphorylation	TSPKGSTYSPTSPGY CCCCCCCCCCCCCCC	17.85	28833060
1941	Phosphorylation	SPKGSTYSPTSPGYS CCCCCCCCCCCCCCC	23.07	28833060
1943	Phosphorylation	KGSTYSPTSPGYSPT CCCCCCCCCCCCCCC	41.43	28833060
1944	Phosphorylation	GSTYSPTSPGYSPTS CCCCCCCCCCCCCCC	21.51	28833060
1947	Phosphorylation	YSPTSPGYSPTSPTY CCCCCCCCCCCCCCC	18.17	28833060
1948	Phosphorylation	SPTSPGYSPTSPTYS CCCCCCCCCCCCCCC	27.84	28833060
1950	Phosphorylation	TSPGYSPTSPTYSLT CCCCCCCCCCCCCCC	41.20	28833060
1951	Phosphorylation	SPGYSPTSPTYSLTS CCCCCCCCCCCCCCC	20.73	28833060
1953	Phosphorylation	GYSPTSPTYSLTSPA CCCCCCCCCCCCCCC	26.05	28833060
1954	Phosphorylation	YSPTSPTYSLTSPAI CCCCCCCCCCCCCCC	12.69	28833060
1955	Phosphorylation	SPTSPTYSLTSPAIS CCCCCCCCCCCCCCC	27.87	28833060
1957	Phosphorylation	TSPTYSLTSPAISPD CCCCCCCCCCCCCCC	27.07	28833060
1958	Phosphorylation	SPTYSLTSPAISPDD CCCCCCCCCCCCCCC	20.02	28833060
1962	Phosphorylation	SLTSPAISPDDSDEE CCCCCCCCCCCCCCC	25.12	28833060
1966	Phosphorylation	PAISPDDSDEEN--- CCCCCCCCCCCC---	55.06	27087446

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
1616	S	Phosphorylation	Kinase	BRD4	O60885	PSP
1616	S	Phosphorylation	Kinase	CDK1	P11440	PSP
1619	S	Phosphorylation	Kinase	CDK1	P11440	PSP
1619	S	Phosphorylation	Kinase	CDK7	P50613	PSP
1619	S	Phosphorylation	Kinase	CDK7	Q03147	PSP
1934	S	Phosphorylation	Kinase	MTOR	Q9JLN9	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	Wwp2	Q9DBH0	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
2	S	Phosphorylation	-
Phosphorylation occurs mainly at residues 'Ser-2' and 'Ser-5' of the heptapeptide repeat and is mediated, at least, by CDK7 and CDK9.
2	S	Phosphorylation	26687004
Acetylation at 'Lys-7' of non-consensus heptapeptide repeats is associated with 'Ser-2' phosphorylation and active transcription.
2	S	Acetylation	26687004
Acetylation at 'Lys-7' of non-consensus heptapeptide repeats is associated with 'Ser-2' phosphorylation and active transcription.
5	S	Methylation	26687004
Methylation occurs in the earliest transcription stages and precedes or is concomitant to 'Ser-5' and 'Ser-7' phosphorylation.
5	S	Phosphorylation	26687004
Methylation occurs in the earliest transcription stages and precedes or is concomitant to 'Ser-5' and 'Ser-7' phosphorylation.
5	S	Phosphorylation	-
Phosphorylation occurs mainly at residues 'Ser-2' and 'Ser-5' of the heptapeptide repeat and is mediated, at least, by CDK7 and CDK9.
7	K	Methylation	26687004
Dimethylation and trimehtylation at 'Lys-7' of non-consensus heptapeptide repeats are exclusively associated with phosphorylated CTD.
7	S	Methylation	26687004
Methylation occurs in the earliest transcription stages and precedes or is concomitant to 'Ser-5' and 'Ser-7' phosphorylation.
7	K	Phosphorylation	26687004
Dimethylation and trimehtylation at 'Lys-7' of non-consensus heptapeptide repeats are exclusively associated with phosphorylated CTD.
7	K	Phosphorylation	26687004
Acetylation at 'Lys-7' of non-consensus heptapeptide repeats is associated with 'Ser-2' phosphorylation and active transcription.
7	K	Methylation	26687004
'Lys-7' in these non-consensus heptapeptide repeats can be alternatively acetylated, methylated, dimethylated and trimethylated.
7	K	Methylation	26687004
'Lys-7' in these non-consensus heptapeptide repeats can be alternatively acetylated, methylated and dimethylated.
7	K	Acetylation	26687004
EP300 is one of the enzyme able to acetylate 'Lys-7'.
7	K	Acetylation	26687004
Acetylation at 'Lys-7' of non-consensus heptapeptide repeats is associated with 'Ser-2' phosphorylation and active transcription.
7	K	Acetylation	26687004
'Lys-7' in these non-consensus heptapeptide repeats can be alternatively acetylated, methylated, dimethylated and trimethylated.
7	K	Acetylation	26687004
'Lys-7' in these non-consensus heptapeptide repeats can be alternatively acetylated, methylated and dimethylated.
7	S	Phosphorylation	26687004
Methylation occurs in the earliest transcription stages and precedes or is concomitant to 'Ser-5' and 'Ser-7' phosphorylation.
7	S	Phosphorylation	-
Phosphorylation also takes place at 'Ser-7' of the heptapeptide repeat, which is required for efficient transcription of snRNA genes and processing of the transcripts.
1805	S	Methylation	26687004
Methylated at Arg-1810 prior to transcription initiation when the CTD is hypophosphorylated, phosphorylation at Ser-1805 and Ser-1808 preventing this methylation.
1805	S	Phosphorylation	26687004
Methylated at Arg-1810 prior to transcription initiation when the CTD is hypophosphorylated, phosphorylation at Ser-1805 and Ser-1808 preventing this methylation.
1808	S	Phosphorylation	26687004
Methylated at Arg-1810 prior to transcription initiation when the CTD is hypophosphorylated, phosphorylation at Ser-1805 and Ser-1808 preventing this methylation.
1808	S	Methylation	26687004
Methylated at Arg-1810 prior to transcription initiation when the CTD is hypophosphorylated, phosphorylation at Ser-1805 and Ser-1808 preventing this methylation.
1810	R	Methylation	26687004
Methylated at Arg-1810 prior to transcription initiation when the CTD is hypophosphorylated, phosphorylation at Ser-1805 and Ser-1808 preventing this methylation.
1810	R	Phosphorylation	26687004
Methylated at Arg-1810 prior to transcription initiation when the CTD is hypophosphorylated, phosphorylation at Ser-1805 and Ser-1808 preventing this methylation.
1810	R	Methylation	26687004
Symmetrically or asymmetrically dimethylated at Arg-1810 by PRMT5 and CARM1 respectively.

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of RPB1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NONO_HUMAN	NONO	physical	12358429
PPIG_HUMAN	PPIG	physical	9153302
SMCA4_MOUSE	Smarca4	physical	15999204
NF1_MOUSE	Nf1	physical	15999204
HNRPU_MOUSE	Hnrnpu	physical	21235343
SCAFB_HUMAN	SCAF11	physical	9224939
C10_HUMAN	C12orf57	physical	9224939
WWP2_MOUSE	Wwp2	physical	17526739

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of RPB1_MOUSE

Related Literatures of Post-Translational Modification

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