NP_511124.1
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NCBI GenBank Nucleotide #
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UniProt Primary Accession #
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UniProt Secondary Accession #
UniProt Related Accession #
NCBI Official Full Name
RNA polymerase II 215kD subunit
NCBI Official Synonym Full Names
RNA polymerase II 215kD subunit
NCBI Official Synonym Symbols
5; 8WG16; CG1554; CTD; DmelCG1554; dRpb1; dRPB1; H5; II; l(1)10Ca; l(1)DC912; l(1)DF912; l(1)G0040; l(1)L5; L5; POL; pol II; Pol II; Pol II CTD; Pol II Ser5P; Pol II0[ser2]; Pol II0[ser5]; Pol IIa; Pol IIo; Pol IIo[ser2]; Pol IIo[Ser2]; Pol IIo[ser5]; Pol [Similar Products]
NCBI Protein Information
CG1554 gene product from transcript CG1554-RA; CG1554-PA; Pol II CTD; Pol II large subunit; RNA Pol II; RNA polymerase II; RNA polymerase II 215kD subunit; RNA polymerase II large subunit; RNA polymerase IIo; RNA polymeraseII-215 kd subunit; RNA-polymerase II; RpII215-PA; Ultrabithorax-like; polymerase II CTD
UniProt Protein Name
DNA-directed RNA polymerase II subunit RPB1
UniProt Synonym Protein Names
DNA-directed RNA polymerase III largest subunit
UniProt Synonym Gene Names
UniProt Entry Name
RPB1_DROME
UniProt Comments for RpII215
Function: 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.
Catalytic activity: Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
Subunit structure: Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits
By similarity.
Subcellular location: Nucleus
By similarity.
Post-translational modification: The tandem 7 residues repeats in the C-terminal domain (CTD) can be highly phosphorylated. The phosphorylation activates Pol II. Phosphorylation occurs mainly at residues 'Ser-2' and 'Ser-5' of the heptapepdtide repeat. The phosphorylation state is believed to result from the balanced action of site-specific CTD kinases and phosphatase, and a 'CTD code' that specifies the position of Pol II within the transcription cycle has been proposed.
Miscellaneous: The binding of ribonucleoside triphosphate to the RNA polymerase II transcribing complex probably involves a two-step mechanism. The initial binding seems to occur at the entry (E) site and involves a magnesium ion temporarily coordinated by three conserved aspartate residues of the two largest RNA Pol II subunits. The ribonucleoside triphosphate is transferred by a rotation to the nucleotide addition (A) site for pairing with the template DNA. The catalytic A site involves three conserved aspartate residues of the RNA Pol II largest subunit which permanently coordinate a second magnesium ion.
Sequence similarities: Belongs to the RNA polymerase beta' chain family.
Research Articles on RpII215
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Products associated with anti-RpII215 antibody
Pathways associated with anti-RpII215 antibody
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