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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: Bromodomain adjacent to zinc finger domain protein 1A

UniprotKB/SwissProt ID: Q9NRL2 (Q9NRL2)

Gene Name: BAZ1A

Organism: Homo sapiens (Human)

Function: Regulatory subunit of the ATP-dependent ACF-1 and ACF-5 ISWI chromatin remodeling complexes, which form ordered nucleosome arrays on chromatin and slide edge- and center-positioned histone octamers away from their original location on the DNA template to facilitate access to DNA during DNA-templated processes such as DNA replication, transcription, and repair (PubMed:17099699, PubMed:28801535). Both complexes regulate the spacing of nucleosomes along the chromatin and have the ability to slide mononucleosomes to the center of a DNA template in an ATP-dependent manner (PubMed:14759371, PubMed:17099699, PubMed:28801535). The ACF-1 ISWI chromatin remodeling complex has a lower ATP hydrolysis rate than the ACF-5 ISWI chromatin remodeling complex (PubMed:28801535). Has a role in sensing the length of DNA which flank nucleosomes, which modulates the nucleosome spacing activity of the ACF-5 ISWI chromatin remodeling complex (PubMed:17099699). Involved in DNA replication and together with SMARCA5/SNF2H is required for replication of pericentric heterochromatin in S-phase (PubMed:12434153). May have a role in nuclear receptor-mediated transcription repression (PubMed:17519354)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Nucleus

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR037325 Acf1_Bromo
IPR047171 BAZ1A
IPR001487 Bromodomain
IPR036427 Bromodomain-like_sf
IPR018359 Bromodomain_CS
IPR018501 DDT_dom
IPR028942 WHIM1_dom
IPR028941 WHIM2_dom
IPR013136 WSTF_Acf1_Cbp146
IPR019786 Zinc_finger_PHD-type_CS
IPR011011 Znf_FYVE_PHD
IPR001965 Znf_PHD
IPR019787 Znf_PHD-finger
IPR013083 Znf_RING/FYVE/PHD

The S-nitrosylation sites of Q9NRL2

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 547 CSLKSLDLDS C TLSEILRLHI   
2 586 RGGFDATDDA C MELRLSNPSL   
3 764 KEFTRQEQIN C VTREPLTADE   
4 970 SSNAYDPSQM C AEKQLELRLR