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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: DNA-directed RNA polymerase II subunit RPB2

UniprotKB/SwissProt ID: P30876 (P30876)

Gene Name: POLR2B

Organism: Homo sapiens (Human)

Function: Catalytic core component of RNA polymerase II (Pol II), a DNA-dependent RNA polymerase which synthesizes mRNA precursors and many functional non-coding RNAs using the four ribonucleoside triphosphates as substrates (By similarity) (PubMed:27193682, PubMed:30190596, PubMed:9852112). Pol II-mediated transcription cycle proceeds through transcription initiation, transcription elongation and transcription termination stages. During transcription initiation, Pol II pre-initiation complex (PIC) is recruited to DNA promoters, with focused-type promoters containing either the initiator (Inr) element, or the TATA-box found in cell-type specific genes and dispersed-type promoters that often contain hypomethylated CpG islands usually found in housekeeping genes. Once the polymerase has escaped from the promoter it enters the elongation phase during which RNA is actively polymerized, based on complementarity with the template DNA strand. Transcription termination involves the release of the RNA transcript and polymerase from the DNA (PubMed:27193682, PubMed:30190596, PubMed:9852112). Forms Pol II active center together with the largest subunit POLR2A/RPB1. Appends one nucleotide at a time to the 3' end of the nascent RNA, with POLR2A/RPB1 most likely contributing a Mg(2+)-coordinating DxDGD motif and POLR2B/RPB2 participating in the coordination of a second Mg(2+) ion and providing lysine residues believed to facilitate Watson-Crick base pairing between the incoming nucleotide and template base. Typically, Mg(2+) ions direct a 5' nucleoside triphosphate to form a phosphodiester bond with the 3' hydroxyl of the preceding nucleotide of the nascent RNA, with the elimination of pyrophosphate. The reversible pyrophosphorolysis can occur at high pyrophosphate concentrations (By similarity) (PubMed:30190596, PubMed:9852112). Can proofread the nascent RNA transcript by means of a 3' -> 5' exonuclease activity. If a ribonucleotide is mis-incorporated, backtracks along the template DNA and cleaves the phosphodiester bond releasing the mis-incorporated 5'-ribonucleotide (By similarity) (PubMed:8381534) RNA-dependent RNA polymerase that catalyzes the extension of a non-coding RNA (ncRNA) at the 3'-end using the four ribonucleoside triphosphates as substrates. An internal ncRNA sequence near the 3'-end serves as a template in a single-round Pol II-mediated RNA polymerization reaction. May decrease the stability of ncRNAs that repress Pol II-mediated gene transcription

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Nucleus

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR015712 DNA-dir_RNA_pol_su2
IPR007120 DNA-dir_RNAP_su2_dom
IPR037033 DNA-dir_RNAP_su2_hyb_sf
IPR007121 RNA_pol_bsu_CS
IPR007644 RNA_pol_bsu_protrusion
IPR007642 RNA_pol_Rpb2_2
IPR037034 RNA_pol_Rpb2_2_sf
IPR007645 RNA_pol_Rpb2_3
IPR007646 RNA_pol_Rpb2_4
IPR007647 RNA_pol_Rpb2_5
IPR007641 RNA_pol_Rpb2_7
IPR014724 RNA_pol_RPB2_OB-fold

The S-nitrosylation sites of P30876

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 1093 GLRFGEMERD C QIAHGAAQFL   
2 1122 DPYQVHVCNL C GIMAIANTRT   
3 161 KIPIMLRSTY C LLNGLTDRDL   
4 221 KDSKYAYTGE C RSCLENSSRP   
5 357 MLPHVGVSDF C ETKKAYFLGY   
6 945 FASRHGQKGT C GIQYRQEDMP   
7 958 QYRQEDMPFT C EGITPDIIIN