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"name": {
"name": "N-terminal domain of transcription factor Specificity Protein (SP) 2",
"short": "SP2_N"
},
"description": [
{
"text": "<p>Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP2 contains the least conserved DNA-binding domain within the SP subfamily of proteins, and its DNA sequence specificity differs from the other SP proteins. It localizes primarily within subnuclear foci associated with the nuclear matrix, and can activate, or in some cases, repress expression from different promoters. The transcription factor SP2 serves as a paradigm for indirect genomic binding. It does not require its DNA-binding domain for genomic DNA binding and occupies target promoters independently of whether they contain a cognate DNA-binding motif. SP2 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP2. [[cite:PUB00150393], [cite:PUB00072868], [cite:PUB00150394], [cite:PUB00109107], [cite:PUB00109018], [cite:PUB00109019]]</p>",
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"PUB00109019": {
"PMID": 23134681,
"ISBN": null,
"volume": "27",
"issue": "2",
"year": 2013,
"title": "Shaking the family tree: identification of novel and biologically active alternatively spliced isoforms across the KLF family of transcription factors.",
"URL": null,
"raw_pages": "432-6",
"medline_journal": "FASEB J",
"ISO_journal": "FASEB J",
"authors": [
"Camacho-Vanegas O",
"Till J",
"Miranda-Lorenzo I",
"Ozturk B",
"Camacho SC",
"Martignetti JA."
],
"DOI_URL": null
},
"PUB00109107": {
"PMID": 1341900,
"ISBN": null,
"volume": "12",
"issue": "10",
"year": 1992,
"title": "Cloning of GT box-binding proteins: a novel Sp1 multigene family regulating T-cell receptor gene expression.",
"URL": null,
"raw_pages": "4251-61",
"medline_journal": "Mol Cell Biol",
"ISO_journal": "Mol Cell Biol",
"authors": [
"Kingsley C",
"Winoto A."
],
"DOI_URL": null
},
"PUB00150393": {
"PMID": 30337366,
"ISBN": null,
"volume": "293",
"issue": "50",
"year": 2018,
"title": "Transcription factor Sp2 potentiates binding of the TALE homeoproteins Pbx1:Prep1 and the histone-fold domain protein Nf-y to composite genomic sites.",
"URL": null,
"raw_pages": "19250-19262",
"medline_journal": "J Biol Chem",
"ISO_journal": "J Biol Chem",
"authors": [
"Volkel S",
"Stielow B",
"Finkernagel F",
"Berger D",
"Stiewe T",
"Nist A",
"Suske G."
],
"DOI_URL": null
},
"PUB00072868": {
"PMID": 20221402,
"ISBN": null,
"volume": "5",
"issue": "3",
"year": 2010,
"title": "Specificity protein 2 (Sp2) is essential for mouse development and autonomous proliferation of mouse embryonic fibroblasts.",
"URL": null,
"raw_pages": "e9587",
"medline_journal": "PLoS One",
"ISO_journal": "PLoS ONE",
"authors": [
"Baur F",
"Nau K",
"Sadic D",
"Allweiss L",
"Elsasser HP",
"Gillemans N",
"de Wit T",
"Kruger I",
"Vollmer M",
"Philipsen S",
"Suske G."
],
"DOI_URL": "http://dx.doi.org/10.1371/journal.pone.0009587"
},
"PUB00150394": {
"PMID": 25793500,
"ISBN": null,
"volume": "11",
"issue": "3",
"year": 2015,
"title": "Zinc finger independent genome-wide binding of Sp2 potentiates recruitment of histone-fold protein Nf-y distinguishing it from Sp1 and Sp3.",
"URL": null,
"raw_pages": "e1005102",
"medline_journal": "PLoS Genet",
"ISO_journal": "PLoS Genet",
"authors": [
"Volkel S",
"Stielow B",
"Finkernagel F",
"Stiewe T",
"Nist A",
"Suske G."
],
"DOI_URL": null
},
"PUB00109018": {
"PMID": 15820306,
"ISBN": null,
"volume": "85",
"issue": "5",
"year": 2005,
"title": "Mammalian SP/KLF transcription factors: bring in the family.",
"URL": null,
"raw_pages": "551-6",
"medline_journal": "Genomics",
"ISO_journal": "Genomics",
"authors": [
"Suske G",
"Bruford E",
"Philipsen S."
],
"DOI_URL": null
}
},
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"accession": "cl41773",
"name": "SP1-4_N"
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"taxa": 1900
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