Phospho-ERBB2IP (Y1104) Antibody

1. Our data uncovered an important role of Erbin in regulating hepatocellular carcinoma (HCC) tumorigenesis through inactivating ERalpha-mediated tumor-suppressive signaling, suggesting a new strategy for tamoxifen therapy in HCC by targeting Erbin/ERalpha signaling axis. PMID: 28192186
2. STAT3 activation promotes ERBIN expression and negatively regulates TGF-beta activity by the formation of a STAT3-ERBIN-SMAD2/3 complex. PMID: 28126831
3. Erbin loss accelerates cell cycle though down-regulating p21 and p27 expression. Erbin is a novel negative modulator of Akt1-Skp2-p27 signaling pathway. PMID: 26025650
4. Erbin promotes tumourigenesis and tumour growth in colorectal cancer by stabilizing epidermal growth factor receptor PMID: 25521828
5. Erbin is an ErbB2 regulator for breast tumor formation and progression PMID: 25288731
6. analysis of the C-terminal ligand specificity of the erbin PDZ domain PMID: 24813123
7. Data reveal that Erbin is a negative regulator of AKT activation and suggest that Erbin may play a role in breast cancer progression. PMID: 23711387
8. DSG1 and Erbin cooperate to repress MAPK signaling and promote keratinocyte differentiation. PMID: 23524970
9. These results unravel a critical role of c-Myb in promoting Erbin transcription in G2/M phase and also predict an unappreciated function of Erbin in cell cycle progression. PMID: 22880131
10. Data conclude that LAP2 is widely overexpressed in diverse digestive tract cancers and LAP2beta regulates motility of cancer cells and suggest that LAP2beta may have utility for diagnostics and therapeutics in digestive tract cancers. PMID: 22745766
11. ERBIN binds to SARA using a domain (amino acids 1208-1265) that also interacts with SMAD2 and SMAD3, which we have called the SSID (SARA- and SMAD-interacting domain) PMID: 21878490
12. PDZ domain binds with high affinity and specificity to the carboxyl termini of delta-catenin and ARVCF PMID: 11821434
13. interacts in vivo with p0071 and may be involved in the organization of adherens junctions and the desmosomes of epithelia PMID: 12047349
14. Erbin is a novel suppressor of Ras signaling by disrupting the Ras-Raf interaction; a negative regulator of the Ras-Raf-Erk signaling pathway PMID: 12379659
15. selective binding and sequestration of this residue in its unphosphorylated state by the Erbin PDZ provides a novel mechanism for regulation of the ErbB2-mediated signaling and oncogenicity PMID: 12444095
16. In this review, erbin is shown to inhibit epidermal growth factor signaling by preventing the activation of the Raf-1 kinase by Ras. PMID: 12966186
17. Erbin is a regulator of Nod2-dependent NF-kappaB signaling with a role in inflammatory responses PMID: 16203728
18. Erbin has a regulatory role in the Ras-Raf-MEK pathway and may inhibit ERK activation by disrupting the Sur-8-Ras/Raf interaction PMID: 16301319
19. Structural analyses reveal that the differences between Erbin PDZ domain and the first PDZ domain of ZO-1 in specificity can be accounted for by two key differences in primary sequence. PMID: 16737969
20. ErbB2, APC, beta-catenin, c-Rel and HTLV-1 Tax were identified as ligands of the PDZ domain of Erbin. PMID: 17100642
21. Results define Erbin as a novel negative modulator of Smad2/Smad3 functions and expand the physiological role of Erbin to the regulation of TGFbeta signaling. PMID: 17591701
22. Both palmitoylation and leucine-rich repeats are required for the plasma membrane localization of ERBIN. PMID: 18498353
23. erbin acts as a negative regulator of beta-catenin/T-cell-factor-dependent gene expression. An erbin mutant with a deletion of the N-terminal leucine-rich repeat allows the PDZ domain of erbin to increase beta-catenin/T-cell-factor-dependent transcription PMID: 18667832
24. Arginine 279, glutamic acid 246 in Smad3 and glutamic acid 1321 in Erbin are important for these proteins binding. PMID: 19013433
25. This review discusses all-intracellular and membrane-associated localization of Densin-180 and its signaling, including a phosphorylation-rich area. PMID: 19187442

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HGNC: 15842

OMIM: 606944

KEGG: hsa:55914

STRING: 9606.ENSP00000370330

UniGene: Hs.591774