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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: Small ribosomal subunit protein uS3

UniprotKB/SwissProt ID: P23396 (P23396)

Gene Name: RPS3

Organism: Homo sapiens (Human)

Function: Component of the small ribosomal subunit (PubMed:23636399, PubMed:8706699). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399, PubMed:8706699). Has endonuclease activity and plays a role in repair of damaged DNA (PubMed:7775413). Cleaves phosphodiester bonds of DNAs containing altered bases with broad specificity and cleaves supercoiled DNA more efficiently than relaxed DNA (PubMed:15707971). Displays high binding affinity for 7,8-dihydro-8-oxoguanine (8-oxoG), a common DNA lesion caused by reactive oxygen species (ROS) (PubMed:14706345). Has also been shown to bind with similar affinity to intact and damaged DNA (PubMed:18610840). Stimulates the N-glycosylase activity of the base excision protein OGG1 (PubMed:15518571). Enhances the uracil excision activity of UNG1 (PubMed:18973764). Also stimulates the cleavage of the phosphodiester backbone by APEX1 (PubMed:18973764). When located in the mitochondrion, reduces cellular ROS levels and mitochondrial DNA damage (PubMed:23911537). Has also been shown to negatively regulate DNA repair in cells exposed to hydrogen peroxide (PubMed:17049931). Plays a role in regulating transcription as part of the NF-kappa-B p65-p50 complex where it binds to the RELA/p65 subunit, enhances binding of the complex to DNA and promotes transcription of target genes (PubMed:18045535). Represses its own translation by binding to its cognate mRNA (PubMed:20217897). Binds to and protects TP53/p53 from MDM2-mediated ubiquitination (PubMed:19656744). Involved in spindle formation and chromosome movement during mitosis by regulating microtubule polymerization (PubMed:23131551). Involved in induction of apoptosis through its role in activation of CASP8 (PubMed:14988002). Induces neuronal apoptosis by interacting with the E2F1 transcription factor and acting synergistically with it to up-regulate pro-apoptotic proteins BCL2L11/BIM and HRK/Dp5 (PubMed:20605787). Interacts with TRADD following exposure to UV radiation and induces apoptosis by caspase-dependent JNK activation (PubMed:22510408)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm. Nucleus. Nucleus, nucleolus. Mitochondrion inner membrane. Cytoplasm, cytoskeleton, spindle

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR015946 KH_dom-like_a/b
IPR004044 KH_dom_type_2
IPR009019 KH_sf_prok-type
IPR036419 Ribosomal_S3_C_sf
IPR001351 Ribosomal_uS3_C
IPR018280 Ribosomal_uS3_CS
IPR005703 Ribosomal_uS3_euk/arc

The S-nitrosylation sites of P23396

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 119 LLGGLAVRRA C YGVLRFIMES  CCCCCCCCCC C CCCCCHHHHH  2.63%
2 134 RFIMESGAKG C EVVVSGKLRG  CCCCCCCCCC C CCCCCHHHHH  3.37% 2212679
3 97 YAEKVATRGL C AIAQAESLRY  CCCCCCCCCC C CCCCCHHHHH  2.61% 22178444
25040305
20140087