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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: E3 ubiquitin-protein ligase UHRF2

UniprotKB/SwissProt ID: Q96PU4 (Q96PU4)

Gene Name: UHRF2

Organism: Homo sapiens (Human)

Function: E3 ubiquitin ligase that plays important roles in DNA methylation, histone modifications, cell cycle and DNA repair (PubMed:15178429, PubMed:23404503, PubMed:27743347, PubMed:29506131). Acts as a specific reader for 5-hydroxymethylcytosine (5hmC) and thereby recruits various substrates to these sites to ubiquitinate them (PubMed:24813944, PubMed:27129234). This activity also allows the maintenance of 5mC levels at specific genomic loci and regulates neuron-related gene expression (By similarity). Participates in cell cycle regulation by ubiquitinating cyclins CCND1 and CCNE1 and thereby inducing G1 arrest (PubMed:15178429, PubMed:15361834, PubMed:21952639). Also ubiquitinates PCNP leading to its degradation by the proteasome (PubMed:12176013, PubMed:14741369). Plays an active role in DNA damage repair by ubiquitinating p21/CDKN1A leading to its proteasomal degradation (PubMed:29923055). Also promotes DNA repair by acting as an interstrand cross-links (ICLs) sensor. Mechanistically, cooperates with UHRF1 to ensure recruitment of FANCD2 to ICLs, leading to FANCD2 monoubiquitination and subsequent activation (PubMed:30335751). Contributes to UV-induced DNA damage response by physically interacting with ATR in response to irradiation, thereby promoting ATR activation (PubMed:33848395)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Nucleus. Chromosome

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR047467 PHD_UHRF2
IPR015947 PUA-like_sf
IPR047466 RING-HC_UHRF2
IPR036987 SRA-YDG_sf
IPR003105 SRA_YDG
IPR021991 TTD_dom
IPR047407 Tudor_UHRF2_rpt1
IPR000626 Ubiquitin-like_dom
IPR029071 Ubiquitin-like_domsf
IPR047468 Ubl_UHRF2
IPR045134 UHRF1/2-like
IPR011011 Znf_FYVE_PHD
IPR001965 Znf_PHD
IPR019787 Znf_PHD-finger
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
IPR017907 Znf_RING_CS

The S-nitrosylation sites of Q96PU4

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 14 QVRTIDGSKT C TIEDVSRKAT