TNPO1 Antibody

1. TNPO1-mediated nuclear import may constitute a novel input pathway of how cellular redox state signals to the clock, since redox stress increases binding of TNPO1 to PER1 and decreases its nuclear localization. TNPO1 is one of the novel players essential for normal circadian periods and potentially for redox regulation of the clock. PMID: 29377895
2. A molecular docking and dynamics study concluded that R521C and R521H mutations in FUS result in weak binding with Karyopherin-beta2 leading to amyotrophic lateral sclerosis. PMID: 27381509
3. Data suggest that micoRNA-128 targets the 3prime-untranslated region of nuclear import factor transportin 1 (TNPO1) mRNA. PMID: 28974576
4. the TNPO1-Rab8-ciliary targeting signals complex mediates selective entry into and retention of cargos within cilia. PMID: 27633000
5. Together, these results indicate that transportin-1 mediates YB-1 nuclear translocation. PMID: 27794479
6. findings suggest that a new player, i.e., O-GlcNAcylation, regulates hnRNP A1 translocation and interaction with Trn1, possibly affecting its function PMID: 27913144
7. Results show that Karyopherin-b2 binds to the N-terminal tail of histone H3 with high affinity even though H3 lacks a recognizable proline-tyrosine nuclear localization signal (PY-NLS). PMID: 27618664
8. FGF2 nuclear translocation is regulated by Karyopherin-beta2 and Ran GTPase in human glioblastoma cells PMID: 26056081
9. Kapbeta2 interacts with ULK2 through ULK2's putative PY-NLS motif, and facilitates transport from the cytoplasm to the nucleus, depending on its Ser1027 residue phosphorylation by PKA, thereby reducing autophagic activity. PMID: 26052940
10. Studies indicate potential roles of Tranportin-1 and Transportin-2 beyond protein nuclear import. PMID: 24780099
11. ADAR1 carries a unique nuclear localization signal (NLS) that overlaps one of its double-stranded RNA-binding domains (dsRBDs). This dsRBD-NLS is recognized by nuclear import receptor transportin 1 (also called karyopherin-beta2) in an RNA-sensitive manner. PMID: 24753571
12. Data suggest the C-terminal nuclear localization domain (QYP) is critical for RAM (RNMT-activating mini protein) to enter the cell nucleus where RAM activates RNMT resulting in mRNA cap methylation; TNPO1/TNPO2 mediate RAM nuclear entry. PMID: 24200467
13. C-terminal FUS mutations prevent TNPO 1 binding to the NLS, inhibiting nuclear import and promoting cytoplasmic aggregation. The presence of TNPO 1 in wild-type FUS aggregates in frontotemporal lobar degeneration-FUS distinguishes it from ALS. PMID: 22934812
14. Crystal structure of human Karyopherin beta2 bound to the PY-NLS of Saccharomyces cerevisiae Nab2 PMID: 23535894
15. The crystal structure of the FUS-NLS/Trn1 complex shows extensive contacts between the two proteins and a unique alpha-helical structure in the FUS-NLS. PMID: 23056579
16. Disulfide formation with transportin-1 is required for nuclear localization and the activation of FOXO4 induced by reactive oxygen species. PMID: 23333309
17. In case of L7, importin beta2 or importin beta3 are preferentially used by clusters with a high import efficiency. PMID: 23266416
18. These data imply a specific dysfunction in the interaction between Trn1 and FET proteins in the inclusion body formation in FTLD-FUS. PMID: 22842875
19. arginine methylation impairs TRN dependent nuclear import of FUS, by decreasing binding of TRN to a novel TRN-binding motif next to the proline-tyrosine nuclear localization signal of FUS. PMID: 22968170
20. Transportin binding might delay methylation of PABPN1 until after nuclear import. PMID: 21808065
21. Data demonstrate that Importin beta2 is necessary for localization of retinitis pigmentosa 2 (RP2) to the primary cilium, and identify two distinct binding sites of RP2, which interact independently with Importin beta2. PMID: 21285245
22. Nuclear import of fused in sarcoma (FUS) is dependent on Transportin, and interference with this transport pathway leads to cytoplasmic redistribution and recruitment of fused in sarcoma (FUS) into stress granules. PMID: 20606625
23. Results suggest that hnRNP H and F are nuclear shuttling proteins whose posttranslational modifications may alter interaction with transportin 1, nuclear localization, and hence function. PMID: 20308327
24. nuclear import of the HPV16 E6 oncoprotein in digitonin-permeabilized HeLa cells could be mediated by Kap beta2 PMID: 12551970
25. 1 major capsid protein of human papillomavirus type 11 interacts with Kap beta2 nuclear import receptor PMID: 12620808
26. HPV16 L2 interacts via its NLSs with a network of karyopherins and can enter the nucleus via several import pathways mediated by Kapalpha(2)beta(1) heterodimers, Kapbeta(2), and Kapbeta(3). PMID: 15507604
27. Results describe four crystal structures of human transoprtin 1 in a substrate-free form as well as in the complex with three nuclear localization signals. PMID: 17936704
28. the 3.0 A crystal structure of unliganded Kap beta2, which consists of a superhelix of 20 HEAT repeats PMID: 17997969
29. TRN1-binding to CCR2 promotes its nuclear translocation in a TRN1-dependent manner. PMID: 18846510
30. we identify transportin-1 as the import receptor for ADAR1. PMID: 19124606
31. Ran in complex with importin-beta has a higher affinity for GTP. This feature is responsible for the generation of Ran-GTP from Ran-GDP by importin-beta. PMID: 19549784
32. The interplay of the two negative regulators, transportin and importin beta, along with the positive regulator RanGTP, allows precise choreography of multiple cell cycle assembly events. PMID: 19641022

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HGNC: 6401

OMIM: 602901

KEGG: hsa:3842

STRING: 9606.ENSP00000336712

UniGene: Hs.482497