Thr739
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Home > Phosphorylation Site Page: > Thr739  -  SP1 (human)

Site Information
sEGSGtAtPSALITT   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 448227

In vivo Characterization
Methods used to characterize site in vivo:
[32P] bio-synthetic labeling ( 7 , 11 ) , electrophoretic mobility shift ( 11 , 12 ) , immunoprecipitation ( 2 , 7 , 10 ) , mass spectrometry ( 2 ) , mutation of modification site ( 2 , 7 , 8 , 9 , 11 , 13 ) , phospho-antibody ( 2 , 4 , 10 , 12 , 13 ) , western blotting ( 2 , 4 , 7 , 10 , 13 )
Disease tissue studied:
brain cancer ( 2 ) , glioma ( 2 )
Relevant cell line - cell type - tissue:
A431 (epithelial) ( 7 ) , B104-1-1 (fibroblast) ( 10 ) , C6 (glial) ( 2 ) , Dede (fibroblast) ( 13 ) , HaCaT (keratinocyte) ( 12 ) , HeLa (cervical) ( 2 , 8 ) , lung ( 2 ) , MCF-7E ( 9 ) , SL2 ( 13 ) , VSMC [TRAIL (mouse), homozygous knockout] ( 4 ) , WKY ('muscle, smooth') ( 11 )

Upstream Regulation
Regulatory protein:
HSP90A (human) ( 7 )
Putative in vivo kinases:
CDK1 (human) ( 2 ) , ERK1 (rat) ( 11 , 12 ) , ERK2 (human) ( 11 , 13 ) , JNK1 (human) ( 7 , 8 )
Kinases, in vitro:
CDK1 (human) ( 2 ) , ERK1 (human) ( 6 ) , ERK2 (human) ( 6 , 13 ) , JNK1 (human) ( 7 , 8 )
Putative upstream phosphatases:
PPP2CA (human) ( 2 )
Phosphatases, in vitro:
PPP2CA (human) ( 2 ) , PPP2CB (human) ( 12 )
Treatments:
estradiol ( 13 ) , FGF2 ( 11 ) , geldanamycin ( 7 ) , nocodazole ( 2 , 8 ) , PD98059 ( 11 , 12 ) , perifosine ( 12 ) , serum ( 13 ) , SP600125 ( 8 )

Downstream Regulation
Effects of modification on SP1:
molecular association, regulation ( 2 ) , protein degradation ( 5 ) , protein stabilization ( 7 , 8 )
Effects of modification on biological processes:
cell cycle regulation ( 2 , 8 ) , transcription, altered ( 4 , 13 ) , transcription, induced ( 8 , 12 ) , transcription, inhibited ( 2 , 11 )
Induce interaction with:
ACTB (human) ( 2 ) , MYO3A (human) ( 2 )
Inhibit interaction with:
DNA ( 2 )

Disease / Diagnostics Relevance
Relevant diseases:
lung cancer ( 2 )

References 

1

Yang HC, et al. (2014) Pin1-mediated Sp1 phosphorylation by CDK1 increases Sp1 stability and decreases its DNA-binding activity during mitosis. Nucleic Acids Res 42, 13573-87
25398907   Curated Info

2

Chuang JY, et al. (2012) Sp1 phosphorylation by cyclin-dependent kinase 1/cyclin B1 represses its DNA-binding activity during mitosis in cancer cells. Oncogene 31, 4946-59
22266860   Curated Info

3

Wang YT, Yang WB, Chang WC, Hung JJ (2011) Interplay of posttranslational modifications in Sp1 mediates Sp1 stability during cell cycle progression. J Mol Biol 414, 1-14
21983342   Curated Info

4

Chan J, et al. (2010) TRAIL promotes VSMC proliferation and neointima formation in a FGF-2-, Sp1 phosphorylation-, and NFkappaB-dependent manner. Circ Res 106, 1061-71
20150555   Curated Info

5

Wei S, et al. (2009) Thiazolidinediones mimic glucose starvation in facilitating Sp1 degradation through the up-regulation of beta-transducin repeat-containing protein. Mol Pharmacol 76, 47-57
19372209   Curated Info

6

Kim HS, Lim IK (2009) Phosphorylated extracellular signal-regulated protein kinases 1 and 2 phosphorylate Sp1 on serine 59 and regulate cellular senescence via transcription of p21Sdi1/Cip1/Waf1. J Biol Chem 284, 15475-86
19318349   Curated Info

7

Wang SA, et al. (2009) Heat shock protein 90 is important for Sp1 stability during mitosis. J Mol Biol 387, 1106-19
19245816   Curated Info

8

Chuang JY, et al. (2008) Phosphorylation by c-Jun NH2-terminal Kinase 1 Regulates the Stability of Transcription Factor Sp1 during Mitosis. Mol Biol Cell 19, 1139-1151
18199680   Curated Info

9

Spengler ML, Guo LW, Brattain MG (2008) Phosphorylation mediates Sp1 coupled activities of proteolytic processing, desumoylation and degradation. Cell Cycle 7, 623-30
18239466   Curated Info

10

Hsu MC, Chang HC, Hung WC (2006) HER-2/neu represses the metastasis suppressor RECK via ERK and Sp transcription factors to promote cell invasion. J Biol Chem 281, 4718-25
16377629   Curated Info

11

Bonello MR, Khachigian LM (2004) Fibroblast growth factor-2 represses platelet-derived growth factor receptor-alpha (PDGFR-alpha) transcription via ERK1/2-dependent Sp1 phosphorylation and an atypical cis-acting element in the proximal PDGFR-alpha promoter. J Biol Chem 279, 2377-82
14593115   Curated Info

12

De Siervi A, et al. (2004) Transcriptional activation of p21(waf1/cip1) by alkylphospholipids: role of the mitogen-activated protein kinase pathway in the transactivation of the human p21(waf1/cip1) promoter by Sp1. Cancer Res 64, 743-50
14744793   Curated Info

13

Milanini-Mongiat J, Pouysségur J, Pagès G (2002) Identification of two Sp1 phosphorylation sites for p42/p44 mitogen-activated protein kinases: their implication in vascular endothelial growth factor gene transcription. J Biol Chem 277, 20631-9
11904305   Curated Info