Curated Information
Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Curated Information Page
PubMed Id: 16880534 
This page summarizes selected information from the article referenced above and curated into PhosphoSitePlus®, a comprehensive online resource for the study of protein post-translational modifications (NAR, 2012,40:D261-70). To learn more about the scope of PhosphoSitePlus®, click here.
Chiang MY, et al. (2006) Identification of a conserved negative regulatory sequence that influences the leukemogenic activity of NOTCH1. Mol Cell Biol 26, 6261-71 16880534
Only sites from this record are displayed on this page. Click on the protein name to open the protein page, and on the RSD number to open the site page. For the complete dataset, click the download button, on the right.
Download Sites

S2521-p - Notch 1 (human)
Orthologous residues
Notch 1 (human): S2521‑p, Notch 1 (mouse): S2497‑p
Characterization
 Methods used to characterize site in vivo 2D analysis, [32P] bio-synthetic labeling, mutation of modification site
 Relevant cell lines - cell types - tissues:  293T (epithelial), bone marrow, U2OS (bone cell) [GR (human)]
 Cellular systems studied:  cell lines, primary cells
 Species studied:  human, mouse
Downstream Regulation
 Effect of modification (function):  protein degradation, receptor inactivation, altered
 Comments:  Alanine mutation of 4 serines (S2522/S2523/S2524/S2525) causes increased protein stability.
Associated Diseases
Diseases: Alterations: Comments:
acute lymphocytic leukemia deletion of site mutation of four serines (2521-2524) to alanine increases leukemogenetic activity of Notch 1; region deleted in ALL

S2522-p - Notch 1 (human)
Orthologous residues
Notch 1 (human): S2522‑p, Notch 1 (mouse): S2498‑p
Characterization
 Methods used to characterize site in vivo 2D analysis, [32P] bio-synthetic labeling, mutation of modification site
 Relevant cell lines - cell types - tissues:  293T (epithelial), bone marrow, U2OS (bone cell) [GR (human)]
 Cellular systems studied:  cell lines, primary cells
 Species studied:  human, mouse
Downstream Regulation
 Effect of modification (function):  protein degradation, receptor inactivation, altered
 Comments:  Alanine mutation of 4 serines (S2522/S2523/S2524/S2525) causes increased protein stability.
Associated Diseases
Diseases: Alterations: Comments:
acute lymphocytic leukemia deletion of site mutation of four serines (2521-2524) to alanine increases leukemogenetic activity of Notch 1; region deleted in ALL

S2523-p - Notch 1 (human)
Orthologous residues
Notch 1 (human): S2523‑p, Notch 1 (mouse): S2499‑p
Characterization
 Methods used to characterize site in vivo 2D analysis, [32P] bio-synthetic labeling, mutation of modification site
 Relevant cell lines - cell types - tissues:  293T (epithelial), bone marrow, U2OS (bone cell) [GR (human)]
 Cellular systems studied:  cell lines, primary cells
 Species studied:  human, mouse
Downstream Regulation
 Effect of modification (function):  protein degradation, receptor inactivation, altered
 Comments:  Alanine mutation of 4 serines (S2522/S2523/S2524/S2525) causes increased protein stability.
Associated Diseases
Diseases: Alterations: Comments:
acute lymphocytic leukemia deletion of site mutation of four serines (2521-2524) to alanine increases leukemogenetic activity of Notch 1; region deleted in ALL

S2524-p - Notch 1 (human)
Orthologous residues
Notch 1 (human): S2524‑p, Notch 1 (mouse): S2500‑p
Characterization
 Methods used to characterize site in vivo 2D analysis, [32P] bio-synthetic labeling, mutation of modification site
 Relevant cell lines - cell types - tissues:  293T (epithelial), bone marrow, U2OS (bone cell) [GR (human)]
 Cellular systems studied:  cell lines, primary cells
 Species studied:  human, mouse
Downstream Regulation
 Effect of modification (function):  protein degradation, receptor inactivation, altered
 Comments:  Alanine mutation of 4 serines (S2522/S2523/S2524/S2525) causes increased protein stability.
Associated Diseases
Diseases: Alterations: Comments:
acute lymphocytic leukemia deletion of site mutation of four serines (2521-2524) to alanine increases leukemogenetic activity of Notch 1; region deleted in ALL


Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.