Synthesized acetyl-peptide derived from the Internal region of human CRM1 around the acetylation site of K568.

Acetyl-CRM1 (K568) Polyclonal Antibody detects endogenous levels of CRM1 protein only when acetylation at K568.The name of modified sites may be influenced by many factors, such as species (the modified site was not originally found in human samples) and the change of protein sequence (the previous protein sequence is incomplete, and the protein sequence may be prolonged with the development of protein sequencing technology). When naming, we will use the "numbers" in historical reference to keep the sites consistent with the reports. The antibody binds to the following modification sequence (lowercase letters are modification sites):VNkLF

XPO1

Exportin-1

XPO1 ;
CRM1 ;
Exportin-1 ;
Exp1 ;
Chromosome region maintenance 1 protein homolog

This cell-cycle-regulated gene encodes a protein that mediates leucine-rich nuclear export signal (NES)-dependent protein transport. The protein specifically inhibits the nuclear export of Rev and U snRNAs. It is involved in the control of several cellular processes by controlling the localization of cyclin B, MPAK, and MAPKAP kinase 2. This protein also regulates NFAT and AP-1. [provided by RefSeq, Jan 2015],

Function:Mediates the nuclear export of cellular proteins (cargos) bearing a leucine-rich nuclear export signal (NES) and of RNAs. In the nucleus, in association with RANBP3, binds cooperatively to the NES on its target protein and to the GTPase RAN in its active GTP-bound form (Ran-GTP). Docking of this complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of an nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the cargo from the export receptor. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Involved in U3 snoRNA transport from Cajal bodies to nucleoli. Binds to late precursor U3 snoRNA bearing a TMG cap. Several viruses, among them HIV-1, HTLV-1 and influenza A use it to export their unspliced or incompletely spliced RNAs out of the nucleus. Interacts with, and mediates the nuclear export of HIV-1 Rev and HTLV-1 Rex proteins. Involved in HTLV-1 Rex multimerization.,miscellaneous:Cellular target of leptomycin B (LMB), a XPO1/CRM1 nuclear export inhibitor.,PTM:Phosphorylated upon DNA damage, probably by ATM or ATR.,similarity:Belongs to the exportin family.,similarity:Contains 1 importin N-terminal domain.,similarity:Contains 10 HEAT repeats.,subcellular location:Located in the nucleoplasm, Cajal bodies and nucleoli. Shuttles between the nucleus/nucleolus and the cytoplasm.,subunit:Found in a U snRNA export complex with RNUXA/PHAX, NCBP1, NCBP2, RAN, XPO1 and m7G-capped RNA (By similarity). Component of a nuclear export receptor complex composed of KPNB1, RAN, SNUPN and XPO1. Found in a trimeric export complex with SNUPN, RAN and XPO1. Found in a nuclear export complex with RANBP3 and RAN. Found in a 60S ribosomal subunit export complex with NMD3, RAN, XPO1. Interacts with DDX3X, NMD3, NUPL2, NUP88, NUP214 and RANBP3. Also found in complex with several viral proteins involved in RNAs' nuclear export like HIV-1 Rev and HTLV-1 Rex. Interacts presumably with influenza A nucleoprotein. Interacts with Epstein-Barr virus BMLF1.,tissue specificity:Expressed in heart, brain, placenta, lung, liver, skeletal muscle, pancreas, spleen, thymus, prostate, testis, ovary, small intestine, colon and peripheral blood leukocytes. Not expressed in the kidney.,

Cytoplasm. Nucleus, nucleoplasm. Nucleus, Cajal body. Nucleus, nucleolus. Located in the nucleoplasm, Cajal bodies and nucleoli. Shuttles between the nucleus/nucleolus and the cytoplasm.

>>Ribosome biogenesis in eukaryotes ;
>>Nucleocytoplasmic transport ;
>>Viral life cycle - HIV-1 ;
>>Influenza A ;
>>Human T-cell leukemia virus 1 infection