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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: Nuclear autoantigenic sperm protein

UniprotKB/SwissProt ID: Q99MD9 (Q99MD9)

Gene Name: Nasp

Organism: Mus musculus (Mouse)

Function: Component of the histone chaperone network (By similarity). Binds and stabilizes histone H3-H4 not bound to chromatin to maintain a soluble reservoir and modulate degradation by chaperone-mediated autophagy (By similarity). Required for DNA replication, normal cell cycle progression and cell proliferation. Forms a cytoplasmic complex with HSP90 and linker H1 histones and stimulates HSP90 ATPase activity. NASP and H1 histone are subsequently released from the complex and translocate to the nucleus where the histone is released for binding to DNA

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm. Nucleus

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR051730 NASP-like
IPR019544 Tetratricopeptide_SHNi-TPR_dom
IPR011990 TPR-like_helical_dom_sf
IPR019734 TPR_rpt

The S-nitrosylation sites of Q99MD9

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 694 KPTDGASSSN C VTDISHLVRK