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KPNA2

The import of proteins into the nucleus is a process that involves at least 2 steps. The first is an energy-independent docking of the protein to the nuclear envelope and the second is an energy-dependent translocation through the nuclear pore complex. Imported proteins require a nuclear localization sequence (NLS) which generally consists of a short region of basic amino acids or 2 such regions spaced about 10 amino acids apart. Proteins involved in the first step of nuclear import have been identified in different systems. These include the Xenopus protein importin and its yeast homolog, SRP1 (a suppressor of certain temperature-sensitive mutations of RNA polymerase I in Saccharomyces cerevisiae), which bind to the NLS. KPNA2 protein interacts with the NLSs of DNA helicase Q1 and SV40 T antigen and may be involved in the nuclear transport of proteins. KPNA2 also may play a role in V(D)J recombination.
KPNA2
Protein class

Plasma proteins, Transporters

Predicted location

Intracellular

Single cell type specificity

Cell type enhanced (Early spermatids, Spermatocytes, Extravillous trophoblasts)

Immune cell specificity

Low immune cell specificity

Cell line specificity

Low cell line specificity

Interaction

Heterodimer; with KPNB1 (PubMed:17596301). Interacts with ANP32E (By similarity). Component of a complex containing CSE1L, RAN and KPNA2. Interacts directly with CSE1L. Interacts with PLAG1. Interacts with APEX1 (via N-terminus). Interacts with FRG1 (via N-terminus). Interacts with ARL4A, CTNNBL1 and NBN. Interacts with SNAI1 (via zinc fingers) and SNAI2 (via zinc fingers). Interacts with BAG6 (PubMed:29042515). Interacts with AIFM2; this interaction likely mediates the translocation of AIFM2 into the nucleus upon oxidative stress. (Microbial infection) Interacts with HIV-1 Vpr. (Microbial infection) Part of a tetrameric complex composed of CRM1, importin alpha/beta dimer and the Venezuelan equine encephalitis virus (VEEV) capsid; this complex blocks the receptor-mediated transport through the nuclear pore. (Microbial infection) Interacts with SARS-COV virus ORF6 protein; this interaction blocks the receptor-mediated transport through the nuclear pore. (Microbial infection) Interacts with Zika virus RNA-directed RNA polymerase NS5. (Microbial infection) Interacts with SARS-CoV-2 ORF6 protein; this interaction may inhibit IFN-beta production by blocking IRF3 nuclear translocation.

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