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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: SAP domain-containing ribonucleoprotein

UniprotKB/SwissProt ID: Q9D1J3 (Q9D1J3)

Gene Name: Sarnp

Organism: Mus musculus (Mouse)

Function: Binds both single-stranded and double-stranded DNA with higher affinity for the single-stranded form. Specifically binds to scaffold/matrix attachment region DNA. Also binds single-stranded RNA. Enhances RNA unwinding activity of DDX39A. May participate in important transcriptional or translational control of cell growth, metabolism and carcinogenesis. Component of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and specifically associates with spliced mRNA and not with unspliced pre-mRNA. The TREX complex is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NXF1 pathway. Associates with DDX39B, which facilitates RNA binding of DDX39B and likely plays a role in mRNA export

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Nucleus. Nucleus speckle

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR003034 SAP_dom
IPR036361 SAP_dom_sf
IPR052240 SAP_domain_ribonucleoprotein