Tag | Content |
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CPLM ID | CPLM-002708 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | DNA-directed RNA polymerase II subunit RPB1 |
Protein Synonyms/Alias | RNA polymerase II subunit B1; DNA-directed RNA polymerase II subunit A; DNA-directed RNA polymerase III largest subunit |
Gene Name | Polr2a |
Gene Synonyms/Alias | Rpii215; Rpo2-1 |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
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758 | KTGSSAQKSLSEYNN | ubiquitination | [1] | 1014 | IKVVEGVKELSKKLV | ubiquitination | [1] | 1268 | IMNSDENKMQEEEEV | ubiquitination | [1] |
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Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
Functional 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. 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). |
Sequence Annotation | REPEAT 1593 1599 1. REPEAT 1600 1606 2; approximate. REPEAT 1608 1614 3. REPEAT 1615 1621 4. REPEAT 1622 1628 5. REPEAT 1629 1635 6. REPEAT 1636 1642 7. REPEAT 1643 1649 8. REPEAT 1650 1656 9. REPEAT 1657 1663 10. REPEAT 1664 1670 11. REPEAT 1671 1677 12. REPEAT 1678 1684 13. REPEAT 1685 1691 14. REPEAT 1692 1698 15. REPEAT 1699 1705 16. REPEAT 1706 1712 17. REPEAT 1713 1719 18. REPEAT 1720 1726 19. REPEAT 1727 1733 20. REPEAT 1734 1740 21. REPEAT 1741 1747 22. REPEAT 1748 1754 23. REPEAT 1755 1761 24. REPEAT 1762 1768 25. REPEAT 1769 1775 26. REPEAT 1776 1782 27. REPEAT 1783 1789 28. REPEAT 1790 1796 29. REPEAT 1797 1803 30. REPEAT 1804 1810 31. REPEAT 1811 1817 32. REPEAT 1818 1824 33. REPEAT 1825 1831 34. REPEAT 1832 1838 35. REPEAT 1839 1845 36. REPEAT 1846 1852 37. REPEAT 1853 1859 38. REPEAT 1860 1866 39. REPEAT 1867 1873 40. REPEAT 1874 1880 41. REPEAT 1881 1887 42. REPEAT 1888 1894 43. REPEAT 1895 1901 44. REPEAT 1902 1908 45. REPEAT 1909 1915 46. REPEAT 1916 1922 47. REPEAT 1923 1929 48. REPEAT 1930 1936 49. REPEAT 1940 1946 50. REPEAT 1947 1953 51; approximate. REPEAT 1954 1960 52; approximate. REGION 833 845 Bridging helix. REGION 1593 1960 52 X 7 AA approximate tandem repeats of METAL 71 71 Zinc 1 (By similarity). METAL 74 74 Zinc 1 (By similarity). METAL 81 81 Zinc 1 (By similarity). METAL 84 84 Zinc 1 (By similarity). METAL 111 111 Zinc 2 (By similarity). METAL 114 114 Zinc 2 (By similarity). METAL 154 154 Zinc 2 (By similarity). METAL 184 184 Zinc 2 (By similarity). METAL 495 495 Magnesium 1; catalytic (By similarity). METAL 495 495 Magnesium 2; shared with RPB2 (By METAL 497 497 Magnesium 1; catalytic (By similarity). METAL 497 497 Magnesium 2; shared with RPB2 (By METAL 499 499 Magnesium 1; catalytic (By similarity). MOD_RES 1 1 N-acetylmethionine (By similarity). MOD_RES 1810 1810 Omega-N-methylated arginine; by CARM1 (By MOD_RES 1843 1843 Phosphoserine (By similarity). MOD_RES 1849 1849 Phosphoserine (By similarity). MOD_RES 1854 1854 Phosphothreonine (By similarity). MOD_RES 1874 1874 Phosphotyrosine (By similarity). MOD_RES 1878 1878 Phosphoserine. MOD_RES 1882 1882 Phosphoserine (By similarity). MOD_RES 1896 1896 Phosphoserine (By similarity). MOD_RES 1899 1899 Phosphoserine (By similarity). MOD_RES 1909 1909 Phosphotyrosine (By similarity). MOD_RES 1913 1913 Phosphoserine (By similarity). MOD_RES 1917 1917 Phosphoserine (By similarity). MOD_RES 1920 1920 Phosphoserine (By similarity). MOD_RES 1923 1923 Phosphotyrosine. MOD_RES 1927 1927 Phosphoserine. MOD_RES 1931 1931 Phosphoserine (By similarity). MOD_RES 1933 1933 Phosphothreonine. MOD_RES 1934 1934 Phosphoserine (By similarity). |
Keyword | Acetylation; Complete proteome; DNA-binding; DNA-directed RNA polymerase; Magnesium; Metal-binding; Methylation; Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription; Transferase; Ubl conjugation; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1970 AA |
Protein Sequence | MHGGGPPSGD SACPLRTIKR VQFGVLSPDE LKRMSVTEGG IKYPETTEGG RPKLGGLMDP 60 RQGVIERTGR CQTCAGNMTE CPGHFGHIEL AKPVFHVGFL VKTMKVLRCV CFFCSKLLVD 120 SNNPKIKDIL AKSKGQPKKR LTHVYDLCKG KNICEGGEEM DNKFGVEQPE GDEDLTKEKG 180 HGGCGRYQPR IRRSGLELYA EWKHVNEDSQ EKKILLSPER VHEIFKRISD EECFVLGMEP 240 RYARPEWMIV TVLPVPPLSV RPAVVMQGSA RNQDDLTHKL ADIVKINNQL RRNEQNGAAA 300 HVIAEDVKLL QFHVATMVDN ELPGLPRAMQ KSGRPLKSLK QRLKGKEGRV RGNLMGKRVD 360 FSARTVITPD PNLSIDQVGV PRSIAANMTF AEIVTPFNID RLQELVRRGN SQYPGAKYII 420 RDNGDRIDLR FHPKPSDLHL QTGYKVERHM CDGDIVIFNR QPTLHKMSMM GHRVRILPWS 480 TFRLNLSVTT PYNADFDGDE MNLHLPQSLE TRAEIQELAM VPRMIVTPQS NRPVMGIVQD 540 TLTAVRKFTK RDVFLERGEV MNLLMFLSTW DGKVPQPAIL KPRPLWTGKQ IFSLIIPGHI 600 NCIRTHSTHP DDEDSGPYKH ISPGDTKVVV ENGELIMGIL CKKSLGTSAG SLVHISYLEM 660 GHDITRLFYS NIQTVINNWL LIEGHTIGIG DSIADSKTYQ DIQNTIKKAK QDVIEVIEKA 720 HNNELEPTPG NTLRQTFENQ VNRILNDARD KTGSSAQKSL SEYNNFKSMV VSGAKGSKIN 780 ISQVIAVVGQ QNVEGKRIPF GFKHRTLPHF IKDDYGPESR GFVENSYLAG LTPTEFFFHA 840 MGGREGLIDT AVKTAETGYI QRRLIKSMES VMVKYDATVR NSINQVVQLR YGEDGLAGES 900 VEFQNLATLK PSNKAFEKKF RFDYTNERAL RRTLQEDLVK DVLSNAHIQN ELEREFERMR 960 EDREVLRVIF PTGDSKVVLP CNLLRMIWNA QKIFHINPRL PSDLHPIKVV EGVKELSKKL 1020 VIVNGDDPLS RQAQENATLL FNIHLRSTLC SRRMAEEFRL SGEAFDWLLG EIESKFNQAI 1080 AHPGEMVGAL AAQSLGEPAT QMTLNTFHYA GVSAKNVTLG VPRLKELINI SKKPKTPSLT 1140 VFLLGQSARD AERAKDILCR LEHTTLRKVT ANTAIYYDPN PQSTVVAEDQ EWVNVYYEMP 1200 DFDVARISPW LLRVELDRKH MTDRKLTMEQ IAEKINAGFG DDLNCIFNDD NAEKLVLRIR 1260 IMNSDENKMQ EEEEVVDKMD DDVFLRCIES NMLTDMTLQG IEQISKVYMH LPQTDNKKKI 1320 IITEDGEFKA LQEWILETDG VSLMRVLSEK DVDPVRTTSN DIVEIFTVLG IEAVRKALER 1380 ELYHVISFDG SYVNYRHLAL LCDTMTCRGH LMAITRHGVN RQDTGPLMKC SFEETVDVLM 1440 EAAAHGESDP MKGVSENIML GQLAPAGTGC FDLLLDAEKC KYGMEIPTNI PGLGAAGPTG 1500 MFFGSAPSPM GGISPAMTPW NQGATPAYGA WSPSVGSGMT PGAAGFSPSA ASDASGFSPG 1560 YSPAWSPTPG SPGSPGPSSP YIPSPGGAMS PSYSPTSPAY EPRSPGGYTP QSPSYSPTSP 1620 SYSPTSPSYS PTSPNYSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP 1680 TSPSYSPTSP SYSPTSPSYS PTSPSYSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS 1740 YSPTSPNYSP TSPNYTPTSP SYSPTSPSYS PTSPNYTPTS PNYSPTSPSY SPTSPSYSPT 1800 SPSYSPSSPR YTPQSPTYTP SSPSYSPSSP SYSPTSPKYT PTSPSYSPSS PEYTPASPKY 1860 SPTSPKYSPT SPKYSPTSPT YSPTTPKYSP TSPTYSPTSP VYTPTSPKYS PTSPTYSPTS 1920 PKYSPTSPTY SPTSPKGSTY SPTSPGYSPT SPTYSLTSPA ISPDDSDEEN 1970 |
Gene Ontology | GO:0005665; C:DNA-directed RNA polymerase II, core complex; ISS:UniProtKB. GO:0003677; F:DNA binding; IDA:MGI. GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-KW. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0004672; F:protein kinase activity; IEA:Compara. GO:0006366; P:transcription from RNA polymerase II promoter; ISS:UniProtKB. |
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