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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 I subunit RPA2

UniprotKB/SwissProt ID: Q9H9Y6 (Q9H9Y6)

Gene Name: POLR1B

Organism: Homo sapiens (Human)

Function: Catalytic core component of RNA polymerase I (Pol I), a DNA-dependent RNA polymerase which synthesizes ribosomal RNA precursors using the four ribonucleoside triphosphates as substrates. Transcribes 47S pre-rRNAs from multicopy rRNA gene clusters, giving rise to 5.8S, 18S and 28S ribosomal RNAs (PubMed:11250903, PubMed:11283244, PubMed:16858408, PubMed:34671025, PubMed:34887565, PubMed:36271492). Pol I-mediated transcription cycle proceeds through transcription initiation, transcription elongation and transcription termination stages. During transcription initiation, Pol I pre-initiation complex (PIC) is recruited by the selectivity factor 1 (SL1/TIF-IB) complex bound to the core promoter that precedes an rDNA repeat unit. The PIC assembly bends the promoter favoring the formation of the transcription bubble and promoter escape. 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. Highly processive, assembles in structures referred to as 'Miller trees' where many elongating Pol I complexes queue and transcribe the same rDNA coding regions. At terminator sequences downstream of the rDNA gene, PTRF interacts with Pol I and halts Pol I transcription leading to the release of the RNA transcript and polymerase from the DNA (PubMed:11250903, PubMed:11283244, PubMed:16858408, PubMed:34671025, PubMed:34887565, PubMed:36271492). Forms Pol I active center together with the largest subunit POLR1A/RPA1. Appends one nucleotide at a time to the 3' end of the nascent RNA, with POLR1A/RPA1 contributing a Mg(2+)-coordinating DxDGD motif, and POLR1B/RPA2 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 the 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. Has proofreading activity: Pauses and backtracks to allow the cleavage of a missincorporated nucleotide via POLR1H/RPA12. High Pol I processivity is associated with decreased transcription fidelity (By similarity) (PubMed:11250903, PubMed:11283244, PubMed:16809778, PubMed:16858408, PubMed:34671025, PubMed:34887565, PubMed:36271492)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Nucleus, nucleolus. Chromosome

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
IPR007641 RNA_pol_Rpb2_7
IPR014724 RNA_pol_RPB2_OB-fold
IPR009674 Rpa2_dom_4

The S-nitrosylation sites of Q9H9Y6

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 103 CKEANVYPAE C RGRRSTYRGK   
2 1061 SFLLHDRLFN C SDRSVAHVCV   
3 307 QKQVLNYLGE C FRVKLNVPDW   
4 347 KSNTEKFYML C LMTRKLFALA   
5 454 GLGLLQDSGL C VVADKLNFIR   
6 689 HNQSPRNMYQ C QMGKQTMGFP   
7 847 FVMYYKSKEN C VVDNIKVCSN