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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 damage-binding protein 1

UniprotKB/SwissProt ID: Q3U1J4 (Q3U1J4)

Gene Name: Ddb1

Organism: Mus musculus (Mouse)

Function: Protein, which is both involved in DNA repair and protein ubiquitination, as part of the UV-DDB complex and DCX (DDB1-CUL4-X-box) complexes, respectively (PubMed:12107171, PubMed:26431207, PubMed:28790135). Core component of the UV-DDB complex (UV-damaged DNA-binding protein complex), a complex that recognizes UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair (PubMed:12107171). The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches (By similarity). Also functions as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). The functional specificity of the DCX E3 ubiquitin-protein ligase complex is determined by the variable substrate recognition component recruited by DDB1 (By similarity). DCX(DDB2) (also known as DDB1-CUL4-ROC1, CUL4-DDB-ROC1 and CUL4-DDB-RBX1) may ubiquitinate histone H2A, histone H3 and histone H4 at sites of UV-induced DNA damage (By similarity). The ubiquitination of histones may facilitate their removal from the nucleosome and promote subsequent DNA repair (By similarity). DCX(DDB2) also ubiquitinates XPC, which may enhance DNA-binding by XPC and promote NER (By similarity). DCX(DTL) plays a role in PCNA-dependent polyubiquitination of CDT1 and MDM2-dependent ubiquitination of TP53 in response to radiation-induced DNA damage and during DNA replication (By similarity). DCX(ERCC8) (the CSA complex) plays a role in transcription-coupled repair (TCR) (By similarity). The DDB1-CUL4A-DTL E3 ligase complex regulates the circadian clock function by mediating the ubiquitination and degradation of CRY1 (PubMed:26431207). DDB1-mediated CRY1 degradation promotes FOXO1 protein stability and FOXO1-mediated gluconeogenesis in the liver (PubMed:28790135). By acting on TET dioxygenses, essential for oocyte maintenance at the primordial follicle stage, hence essential for female fertility (PubMed:24357321). Maternal factor required for proper zygotic genome activation and genome reprogramming (PubMed:24357321)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm. Nucleus

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR018846 Beta-prop_RSE1/DDB1/CPSF1_1st
IPR004871 Cleavage/polyA-sp_fac_asu_C
IPR011047 Quinoprotein_ADH-like_sf
IPR050358 RSE1/DDB1/CFT1/CPSF1
IPR015943 WD40/YVTN_repeat-like_dom_sf

The S-nitrosylation sites of Q3U1J4

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 128 TGIIGIIDPE C RMIGLRLYDG  CCCEEEEECC C CCEECCEEEC  4.33% 20925432
2 378 ERQGQGQLVT C SGAFKEGSLR  CCCEEEEECC C CCEECCEEEC  2.48% 21278135
3 725 VPLYESPRKI C YQEVSQCFGV  CCCEEEEECC C CCEECCEEEC  3%