Transcription factor Sp3

Function

Transcriptional factor that can act as an activator or repressor depending on isoform and/or post-translational modifications. Binds to GT and GC boxes promoter elements. Competes with SP1 for the GC-box promoters. Weak activator of transcription but can activate a number of genes involved in different processes such as cell-cycle regulation, hormone-induction and house-keeping.

Classification

Family (Pfam)

PF00096 zf-C2H2

InterPro

Znf_C2H2_sf, Znf_C2H2_type

Functional cluster

RNA-Polymerase II Transcription Factors

Gene Ontology · 20

• GO:0000785 chromatin
• GO:0005654 nucleoplasm
• GO:0005634 nucleus
• GO:0016605 PML body
• GO:0032993 protein-DNA complex
• GO:0017053 transcription repressor complex
• GO:0003682 chromatin binding
• GO:0000981 DNA-binding transcription factor activity, RNA polymerase II-specific
• GO:0001227 DNA-binding transcription repressor activity, RNA polymerase II-specific
• GO:0000978 RNA polymerase II cis-regulatory region sequence-specific DNA binding
• GO:0000977 RNA polymerase II transcription regulatory region sequence-specific DNA binding
• GO:0061629 RNA polymerase II-specific DNA-binding transcription factor binding
• GO:1990837 sequence-specific double-stranded DNA binding
• GO:0008270 zinc ion binding
• GO:0006351 DNA-templated transcription
• GO:0045892 negative regulation of DNA-templated transcription
• GO:0045893 positive regulation of DNA-templated transcription
• GO:0045944 positive regulation of transcription by RNA polymerase II
• GO:0006355 regulation of DNA-templated transcription
• GO:0006357 regulation of transcription by RNA polymerase II

Neighborhood · nearest proteins

Related proteins · sequence + function similarity

• Transcription factor Sp3 1.00
• Transcription factor Sp3 0.99
• Transcription factor Sp4 0.94
• Transcription factor Sp4 0.94
• Transcription factor Sp1 0.92
• Transcription factor Sp1 0.92
• Transcription factor Sp1 0.91
• Transcription factor Sp2 0.86
• Nuclear transcription factor Y subunit alpha 0.86
• Nuclear transcription factor Y subunit alpha 0.86
• Transcription factor Sp2 0.85
• Nuclear transcription factor Y subunit alpha 0.85

Co-cited proteins · studied together in the literature

• Transcription factor Sp4 2 shared papers
• Transcription factor Sp3 1 shared papers
• Transcription factor Sp2 2 shared papers
• DNA-dependent ATPase/E3 ubiquitin-protein ligase HLTF 1 shared papers
• Transcription factor Sp1 3 shared papers
• Histone deacetylase 1 2 shared papers
• Histone deacetylase 2 1 shared papers
• Homeobox protein Meis2 1 shared papers
• Krueppel-like factor 4 2 shared papers
• Pre-B-cell leukemia transcription factor 1 1 shared papers
• Histone acetyltransferase p300 1 shared papers
• Transcription factor Sp9 1 shared papers

Literature · 33 cited papers

• The evolution of the 9aaTAD domain in Sp2 proteins: inactivation with valines and intron reservoirs. Cell. Mol. Life Sci. · 2020
• Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation. Nat. Struct. Mol. Biol. · 2017
• SUMO-2 orchestrates chromatin modifiers in response to DNA damage. Cell Rep. · 2015
• System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability. Mol. Cell. Proteomics · 2015
• Uncovering global SUMOylation signaling networks in a site-specific manner. Nat. Struct. Mol. Biol. · 2014
• Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli. Proc. Natl. Acad. Sci. U.S.A. · 2014
• An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J. Proteomics · 2014
• Toward a comprehensive characterization of a human cancer cell phosphoproteome. J. Proteome Res. · 2013
• Cooperative transcriptional activation by Klf4, Meis2, and Pbx1. Mol. Cell. Biol. · 2011
• System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. Sci. Signal. · 2011
• Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci. Signal. · 2010
• Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci. Signal. · 2009
• … and 21 more in the literature graph