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Phosphorylation Site Page:
Thr74 - Bcl-2 (human)

Site Information
ARTSPLQtPAAPGAA   SwissProt Entrez-Gene
Predicted information:  Scansite
Orthologous residues: Bcl‑2 (rat): (P74), Bcl‑2 (mouse): (P74)
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 448632

In vivo Characterization
Methods used to characterize site in vivo: electrophoretic mobility shift (2), mutation of modification site (1, 2, 3, 4), phospho-antibody (3), western blotting (3, 4)
Relevant cell line - cell type - tissue: COS (fibroblast) (4), epithelial-'kidney, tubule' (2), HeLa (cervical) (3), HUVEC (endothelial) (3), WEHI-7 (T lymphocyte) (1)

Controlled by
Regulatory protein: JNK3 (mouse) (4), RAC1 (human) (4)
Putative upstream kinases: ERK2 (human) (3)
Kinases, in vitro: ERK1 (human) (3), JNK3 (mouse) (4)

Downstream Regulation
Effects of modification on Bcl-2: protein stabilization (3), ubiquitination (3)
Effects of modification on biological processes: apoptosis, altered (2), apoptosis, induced (3), apoptosis, inhibited (1)



Huang ST, Cidlowski JA (2002) Phosphorylation status modulates Bcl-2 function during glucocorticoid-induced apoptosis in T lymphocytes. FASEB J 16, 825-32
12039864   Curated Info


Thomas A, Giesler T, White E (2000) p53 mediates bcl-2 phosphorylation and apoptosis via activation of the Cdc42/JNK1 pathway. Oncogene 19, 5259-69
11077443   Curated Info


Breitschopf K, et al. (2000) Posttranslational modification of Bcl-2 facilitates its proteasome-dependent degradation: molecular characterization of the involved signaling pathway. Mol Cell Biol 20, 1886-96
10669763   Curated Info


Maundrell K, et al. (1997) Bcl-2 undergoes phosphorylation by c-Jun N-terminal kinase/stress-activated protein kinases in the presence of the constitutively active GTP-binding protein Rac1. J Biol Chem 272, 25238-42
9312139   Curated Info

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