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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: General transcription and DNA repair factor IIH helicase/translocase subunit XPB

UniprotKB/SwissProt ID: P19447 (P19447)

Gene Name: ERCC3

Organism: Homo sapiens (Human)

Function: ATP-dependent 3'-5' DNA helicase/translocase (PubMed:17466626, PubMed:27193682, PubMed:33902107, PubMed:8465201, PubMed:8663148). Binds dsDNA rather than ssDNA, unzipping it in a translocase rather than classical helicase activity (PubMed:27193682, PubMed:33902107). Component of the general transcription and DNA repair factor IIH (TFIIH) core complex (PubMed:10024882, PubMed:17466626, PubMed:8157004, PubMed:8465201). When complexed to CDK-activating kinase (CAK), involved in RNA transcription by RNA polymerase II. The ATPase activity of XPB/ERCC3, but not its helicase activity, is required for DNA opening; it may wrap around the damaged DNA wedging it open, causing localized melting that allows XPD/ERCC2 helicase to anchor (PubMed:10024882, PubMed:17466626). In transcription, TFIIH has an essential role in transcription initiation (PubMed:30894545, PubMed:8157004). When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape (PubMed:8157004). The ATP-dependent helicase activity of XPB/ERCC3 is required for promoter opening and promoter escape (PubMed:10024882). In transcription pre-initiation complexes induces and propagates a DNA twist to open DNA (PubMed:27193682, PubMed:33902107). Also involved in transcription-coupled nucleotide excision repair (NER) of damaged DNA (PubMed:17466626, PubMed:2111438, PubMed:8157004). In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. The structure of the TFIIH transcription complex differs from the NER-TFIIH complex; large movements by XPD/ERCC2 and XPB/ERCC3 are stabilized by XPA (PubMed:31253769, PubMed:33902107). XPA retains XPB/ERCC3 at the 5' end of a DNA bubble (mimicking DNA damage) (PubMed:31253769)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Nucleus

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR050615 ATP-dep_DNA_Helicase
IPR032438 ERCC3_RAD25_C
IPR006935 Helicase/UvrB_N
IPR014001 Helicase_ATP-bd
IPR001650 Helicase_C-like
IPR027417 P-loop_NTPase
IPR001161 XPB/Ssl2
IPR032830 XPB/Ssl2_N

The S-nitrosylation sites of P19447

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 159 PDGIMQFIKL C TVSYGKVKLV   
2 355 GKSLVGVTAA C TVRKRCLVLG