SP1
entrez
6667
canonical
uniprot
P08047
canonical
ensembl
ENSG00000185591
resolver
ensp
ENSP00000329357
resolver
ensp
ENSP00000404263
resolver
genesymbol
SP1
resolver
genesymbol_syn
TSFP1
resolver
hgnc
HGNC:11205
resolver
uniprot
E4Z9M7
resolver
uniprot
G5E9M8
resolver
uniprot
Q86TN8
resolver
uniprot
Q9H3Q5
resolver
uniprot
Q9NR51
resolver
uniprot
Q9NY21
resolver
uniprot
Q9NYE7
resolver
uniprot_entry
SP1_HUMAN
resolver
uniprot_sec
E4Z9M7
resolver
uniprot_sec
G5E9M8
resolver
uniprot_sec
Q86TN8
resolver
uniprot_sec
Q9H3Q5
resolver
uniprot_sec
Q9NR51
resolver
uniprot_sec
Q9NY21
resolver
uniprot_sec
Q9NYE7
resolver
amino_acid_sequence
MSDQDHSMDEMTAVVKIEKGVGGNNGGNGNGGGAFSQARSSSTGSSSSTGGGGQESQPSPLALLAATCSRIESPNENSNNSQGPSQSGGTGELDLTATQLSQGANGWQIISSSSGATPTSKEQSGSSTNGSNGSESSKNRTVSGGQYVVAAAPNLQNQQVLTGLPGVMPNIQYQVIPQFQTVDGQQLQFAATGAQVQQDGSGQIQIIPGANQQIITNRGSGGNIIAAMPNLLQQAVPLQGLANNVLSGQTQYVTNVPVALNGNITLLPVNSVSAATLTPSSQAVTISSSGSQESGSQPVTSGTTISSASLVSSQASSSSFFTNANSYSTTTTTSNMGIMNFTTSGSSGTNSQGQTPQRVSGLQGSDALNIQQNQTSGGSLQAGQQKEGEQNQQTQQQQILIQPQLVQGGQALQALQAAPLSGQTFTTQAISQETLQNLQLQAVPNSGPIIIRTPTVGPNGQVSWQTLQLQNLQVQNPQAQTITLAPMQGVSLGQTSSSNTTLTPIASAASIPAGTVTVNAAQLSSMPGLQTINLSALGTSGIQVHPIQGLPLAIANAPGDHGAQLGLHGAGGDGIHDDTAGGEEGENSPDAQPQAGRRTRREACTCPYCKDSEGRGSGDPGKKKQHICHIQGCGKVYGKTSHLRAHLRWHTGERPFMCTWSYCGKRFTRSDELQRHKRTHTGEKKFACPECPKRFMRSDHLSKHIKTHQNKKGGPGVALSVGTLPLDSGAGSEGSGTATPSALITTNMVAMEAICPEGIARLANSGINVMQVADLQSINISGNGF
uniprot
proteins
function
FUNCTION: Transcription factor that can activate or repress transcription in response to physiological and pathological stimuli. Binds with high affinity to GC-rich motifs and regulates the expression of a large number of genes involved in a variety of processes such as cell growth, apoptosis, differentiation and immune responses. Highly regulated by post-translational modifications (phosphorylations, sumoylation, proteolytic cleavage, glycosylation and acetylation). Also binds the PDGFR-alpha G-box promoter. May have a role in modulating the cellular response to DNA damage. Implicated in chromatin remodeling. Plays an essential role in the regulation of FE65 gene expression. In complex with ATF7IP, maintains telomerase activity in cancer cells by inducing TERT and TERC gene expression. Isoform 3 is a stronger activator of transcription than isoform 1. Positively regulates the transcription of the core clock component BMAL1 (PubMed:10391891, PubMed:11371615, PubMed:11904305, PubMed:14593115, PubMed:16377629, PubMed:16478997, PubMed:16943418, PubMed:17049555, PubMed:18171990, PubMed:18199680, PubMed:18239466, PubMed:18513490, PubMed:18619531, PubMed:19193796, PubMed:20091743, PubMed:21046154, PubMed:21798247). Plays a role in the recruitment of SMARCA4/BRG1 on the c-FOS promoter. Plays a role in protecting cells against oxidative stress following brain injury by regulating the expression of RNF112 (By similarity). {ECO:0000250|UniProtKB:O89090, ECO:0000250|UniProtKB:Q01714, ECO:0000269|PubMed:10391891, ECO:0000269|PubMed:11371615, ECO:0000269|PubMed:11904305, ECO:0000269|PubMed:14593115, ECO:0000269|PubMed:16377629, ECO:0000269|PubMed:16478997, ECO:0000269|PubMed:16943418, ECO:0000269|PubMed:17049555, ECO:0000269|PubMed:18171990, ECO:0000269|PubMed:18199680, ECO:0000269|PubMed:18239466, ECO:0000269|PubMed:18513490, ECO:0000269|PubMed:18619531, ECO:0000269|PubMed:19193796, ECO:0000269|PubMed:20091743, ECO:0000269|PubMed:21046154, ECO:0000269|PubMed:21798247}.
uniprot
proteins
mass_dalton
80693
uniprot
proteins
mutagenesis
MUTAGEN 7; /note="S->A: Increase in protein stability. No change in sumoylation."; /evidence="ECO:0000269|PubMed:18239466"; MUTAGEN 15; /note="V->R: Enhanced transcriptional activity."; MUTAGEN 16; /note="K->R: Loss of sumoylation. No cleavage and reduced transcriptional activity."; /evidence="ECO:0000269|PubMed:16407261"; MUTAGEN 18; /note="E->A: Loss of sumoylation. Increased cleavage and enhanced transcriptional activity."; /evidence="ECO:0000269|PubMed:16407261"; MUTAGEN 19; /note="K->R: No effect on sumoylation nor on proteolytic cleavage."; /evidence="ECO:0000269|PubMed:16407261"; MUTAGEN 36; /note="S->A: No effect on phosphorylation on DNA damage."; /evidence="ECO:0000269|PubMed:18619531"; MUTAGEN 56; /note="S->A: No effect on phosphorylation on DNA damage."; /evidence="ECO:0000269|PubMed:18619531"; MUTAGEN 59; /note="S->A: Loss of phosphorylation. No effect on activated MAPK8-mediated phosphorylation. Similar loss of phosphorylation as by dephosphorylation by PP2AC. Reduced proteolytic processing."; /evidence="ECO:0000269|PubMed:17049555, ECO:0000269|PubMed:18199680, ECO:0000269|PubMed:18239466"; MUTAGEN 59; /note="S->E: Some association with chromatin, increased phosphorylation levels and decreased glycosylation."; /evidence="ECO:0000269|PubMed:17049555, ECO:0000269|PubMed:18199680, ECO:0000269|PubMed:18239466"; MUTAGEN 73; /note="S->A: Little effect on activated MAPK8-mediated phosphorylation."; /evidence="ECO:0000269|PubMed:18199680"; MUTAGEN 81; /note="S->A: No effect on phosphorylation on DNA damage."; /evidence="ECO:0000269|PubMed:18619531"; MUTAGEN 85; /note="S->A: No effect on phosphorylation on DNA damage."; /evidence="ECO:0000269|PubMed:18619531"; MUTAGEN 98; /note="T->A: No effect on phosphorylation on DNA damage."; /evidence="ECO:0000269|PubMed:18619531"; MUTAGEN 101; /note="S->A: Significant reduction of phosphorylation on DNA damage."; /evidence="ECO:0000269|PubMed:18171990, ECO:0000269|PubMed:18619531"; MUTAGEN 101; /note="S->D: Increase in phosphorylation on DNA damage."; /evidence="ECO:0000269|PubMed:18171990, ECO:0000269|PubMed:18619531"; MUTAGEN 117; /note="T->A: No effect on activated MAPK8-mediated phosphorylation."; /evidence="ECO:0000269|PubMed:18199680"; MUTAGEN 220; /note="S->A: No effect on dephosphorylation by PP2A."; /evidence="ECO:0000269|PubMed:17049555"; MUTAGEN 250; /note="T->A: No effect on phosphorylation on DNA damage."; /evidence="ECO:0000269|PubMed:18619531"; MUTAGEN 278; /note="T->A: Almost complete abolition of activated MAPK8-mediated phosphorylation and 40% reduction in protein levels during mitosis. Protein levels reduced by 70% during mitosis; when associated with A-739."; /evidence="ECO:0000269|PubMed:18199680"; MUTAGEN 278; /note="T->D: Increased protein stability during mitosis; when associated with D-739."; /evidence="ECO:0000269|PubMed:18199680"; MUTAGEN 281; /note="S->A: No effect on phosphorylation on DNA damage."; /evidence="ECO:0000269|PubMed:18619531"; MUTAGEN 291; /note="S->A: No effect on phosphorylation on DNA damage."; /evidence="ECO:0000269|PubMed:18619531"; MUTAGEN 296; /note="S->A: No effect on phosphorylation on DNA damage."; /evidence="ECO:0000269|PubMed:18619531"; MUTAGEN 313; /note="S->A: No effect on phosphorylation on DNA damage."; /evidence="ECO:0000269|PubMed:18619531"; MUTAGEN 351; /note="S->A: No effect on phosphorylation on DNA damage."; /evidence="ECO:0000269|PubMed:18619531"; MUTAGEN 355; /note="T->A: No effect on dephosphorylation by PP2A."; /evidence="ECO:0000269|PubMed:11904305, ECO:0000269|PubMed:17049555"; MUTAGEN 394; /note="T->A: No effect on phosphorylation on DNA damage."; /evidence="ECO:0000269|PubMed:18619531"; MUTAGEN 427; /note="T->A: No effect on phosphorylation on DNA damage."; /evidence="ECO:0000269|PubMed:18619531"; MUTAGEN 431; /note="S->A: No effect on phosphorylation on DNA damage."; /evidence="ECO:0000269|PubMed:18619531"; MUTAGEN 453; /note="T->A: Abolishes MAPK-mediated phosphorylation, 50% reduction in MAPK1/MAPK3-mediated activity on VEGF promoter and no effect on dephosphorylation by PP2A. Greatly reduced MAPK1-mediated activity on VEGF promoter; when associated with A-739."; /evidence="ECO:0000269|PubMed:11904305, ECO:0000269|PubMed:14593115, ECO:0000269|PubMed:17049555"; MUTAGEN 491; /note="S->A: Loss of O-glycosylation. Increase in transcriptional activity."; /evidence="ECO:0000269|PubMed:11371615, ECO:0000269|PubMed:9343410"; MUTAGEN 612; /note="S->A: Diminished glycosylation. Inhibits transcriptional activity; when associated with A-640; A-641; A-698 and A-702."; /evidence="ECO:0000269|PubMed:18513490"; MUTAGEN 640; /note="T->A: Diminished glycosylation. Inhibits transcriptional activity; when associated with A-612; A-641; A-698 and A-702."; /evidence="ECO:0000269|PubMed:18513490"; MUTAGEN 641; /note="S->A: Abolishes PRKCzeta-mediated phosphorylation. Diminished glycosylation. Inhibits transcriptional activity; when associated with A-612; A-640; A-641 and A-702."; /evidence="ECO:0000269|PubMed:16943418, ECO:0000269|PubMed:18513490"; MUTAGEN 651; /note="T->A: No effect on dephosphorylation by PP2A."; /evidence="ECO:0000269|PubMed:17049555"; MUTAGEN 668; /note="T->A: Abolishes PRKCzeta-mediated but not PKCdelta-mediated phosphorylation. No effect on DNA binding; when associated with A-670 and A-681."; /evidence="ECO:0000269|PubMed:18258854"; MUTAGEN 670; /note="S->A: Abolishes PRKCzeta-mediated but not PKCdelta-mediated phosphorylation. No effect on DNA binding; when associated with A-668 and A-681."; /evidence="ECO:0000269|PubMed:18258854"; MUTAGEN 681; /note="T->A: Abolishes PRKCzeta-mediated but not PKCdelta-mediated phosphorylation. Some effect on dephosphorylation by PP2A. No effect on DNA binding; when associated with A-668 and A-681."; /evidence="ECO:0000269|PubMed:17049555, ECO:0000269|PubMed:18258854"; MUTAGEN 698; /note="S->A: Diminished glycosylation. Inhibits transcriptional activity; when associated with A-612; A-640; A-641 and A-702."; /evidence="ECO:0000269|PubMed:18513490"; MUTAGEN 702; /note="S->A: Diminished glycosylation. Inhibits transcriptional activity; when associated with A-612; A-640; A-641 and A-698."; /evidence="ECO:0000269|PubMed:18513490"; MUTAGEN 703; /note="K->A: Abolishes acetylation. Increases recruitment of p300 to the promoter and enhances gene transcription."; /evidence="ECO:0000269|PubMed:16478997"; MUTAGEN 728; /note="S->A: Exhibits attenuated endoproteolytic cleavage; when associated with A-732."; /evidence="ECO:0000269|PubMed:18239466"; MUTAGEN 732; /note="S->A: Exhibits attenuated endoproteolytic cleavage; when associated with A-728."; /evidence="ECO:0000269|PubMed:18239466"; MUTAGEN 739; /note="T->A: Abolishes MAPK-mediated phosphorylation. 50% reduction in MAPK1/MAPK3-mediated activity on VEGF promoter, 40% reduction in protein levels during mitosis and no effect on dephosphorylation by PP2A. Greatly reduced MAPK1-mediated activity on VEGF promoter; when associated with A-453. Protein levels during mitosis reduced by 70%; when associated with A-278."; /evidence="ECO:0000269|PubMed:11904305, ECO:0000269|PubMed:14593115, ECO:0000269|PubMed:17049555, ECO:0000269|PubMed:18199680"; MUTAGEN 739; /note="T->D: Increased protein stability during mitosis; when associated with D-278."; /evidence="ECO:0000269|PubMed:11904305, ECO:0000269|PubMed:14593115, ECO:0000269|PubMed:17049555, ECO:0000269|PubMed:18199680
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on multiple serine and threonine residues. Phosphorylation is coupled to ubiquitination, sumoylation and proteolytic processing. Phosphorylation on Ser-59 enhances proteolytic cleavage. Phosphorylation on Ser-7 enhances ubiquitination and protein degradation. Hyperphosphorylation on Ser-101 in response to DNA damage has no effect on transcriptional activity. MAPK1/MAPK3-mediated phosphorylation on Thr-453 and Thr-739 enhances VEGF transcription but, represses FGF2-triggered PDGFR-alpha transcription. Also implicated in the repression of RECK by ERBB2. Hyperphosphorylated on Thr-278 and Thr-739 during mitosis by MAPK8 shielding SP1 from degradation by the ubiquitin-dependent pathway. Phosphorylated in the zinc-finger domain by calmodulin-activated PKCzeta. Phosphorylation on Ser-641 by PKCzeta is critical for TSA-activated LHR gene expression through release of its repressor, p107. Phosphorylation on Thr-668, Ser-670 and Thr-681 is stimulated by angiotensin II via the AT1 receptor inducing increased binding to the PDGF-D promoter. This phosphorylation is increased in injured artey wall. Ser-59 and Thr-681 can both be dephosphorylated by PP2A during cell-cycle interphase. Dephosphorylation on Ser-59 leads to increased chromatin association during interphase and increases the transcriptional activity. On insulin stimulation, sequentially glycosylated and phosphorylated on several C-terminal serine and threonine residues. {ECO:0000269|PubMed:11904305, ECO:0000269|PubMed:14593115, ECO:0000269|PubMed:16332679, ECO:0000269|PubMed:16377629, ECO:0000269|PubMed:16943418, ECO:0000269|PubMed:17049555, ECO:0000269|PubMed:18171990, ECO:0000269|PubMed:18199680, ECO:0000269|PubMed:18239466, ECO:0000269|PubMed:18258854, ECO:0000269|PubMed:18619531}.; PTM: Acetylated (PubMed:16478997, PubMed:38534334). Acetylation/deacetylation events affect transcriptional activity (PubMed:16478997, PubMed:38534334). Deacetylation leads to an increase in the expression of the 12(s)-lipooxygenase gene through recruitment of p300 to the promoter (PubMed:16478997). Deacetylated by HDAC6 which leads to increased expression of ENG and positive regulation of angiogenesis (PubMed:38534334). {ECO:0000269|PubMed:16478997, ECO:0000269|PubMed:38534334}.; PTM: Ubiquitinated. Ubiquitination occurs on the C-terminal proteolytically-cleaved peptide and is triggered by phosphorylation. {ECO:0000269|PubMed:18239466}.; PTM: Sumoylated with SUMO1. Sumoylation modulates proteolytic cleavage of the N-terminal repressor domain. Sumoylation levels are attenuated during tumorigenesis. Phosphorylation mediates SP1 desumoylation.; PTM: Proteolytic cleavage in the N-terminal repressor domain is prevented by sumoylation. The C-terminal cleaved product is susceptible to degradation.; PTM: O-glycosylated; Contains 8 N-acetylglucosamine side chains. Levels are controlled by insulin and the SP1 phosphorylation states. Insulin-mediated O-glycosylation locates SP1 to the nucleus, where it is sequentially deglycosylated and phosphorylated. O-glycosylation affects transcriptional activity through disrupting the interaction with a number of transcription factors including ELF1 and NFYA. Also inhibits interaction with the HIV1 promoter. Inhibited by peroxisomome proliferator receptor gamma (PPARgamma).
uniprot
proteins
protein_family
Sp1 C2H2-type zinc-finger protein family
uniprot
proteins
pubmed
10391891
uniprot
proteins
pubmed
10973950
uniprot
proteins
pubmed
10976766
uniprot
proteins
pubmed
11371615
uniprot
proteins
pubmed
11904305
uniprot
proteins
pubmed
12004059
uniprot
proteins
pubmed
12021324
uniprot
proteins
pubmed
12847090
uniprot
proteins
pubmed
12855699
uniprot
proteins
pubmed
14593115
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15691849
uniprot
proteins
pubmed
16332679
uniprot
proteins
pubmed
16377629
uniprot
proteins
pubmed
16407261
uniprot
proteins
pubmed
16478997
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
16818630
uniprot
proteins
pubmed
16943418
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17049555
uniprot
proteins
pubmed
18171990
uniprot
proteins
pubmed
18199680
uniprot
proteins
pubmed
18239466
uniprot
proteins
pubmed
18258854
uniprot
proteins
pubmed
18513490
uniprot
proteins
pubmed
18619531
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19106100
uniprot
proteins
pubmed
19193796
uniprot
proteins
pubmed
19285002
uniprot
proteins
pubmed
19302979
uniprot
proteins
pubmed
19666599
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20091743
uniprot
proteins
pubmed
20121949
uniprot
proteins
pubmed
20953893
uniprot
proteins
pubmed
21046154
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21746878
uniprot
proteins
pubmed
21798247
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
31375868
uniprot
proteins
pubmed
3139301
uniprot
proteins
pubmed
3142690
uniprot
proteins
pubmed
3319186
uniprot
proteins
pubmed
38534334
uniprot
proteins
pubmed
7592727
uniprot
proteins
pubmed
8626793
uniprot
proteins
pubmed
9065444
uniprot
proteins
pubmed
9343410
uniprot
proteins
pubmed
9466902
uniprot
proteins
sequence_length
785
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nuclear location is governed by glycosylated/phosphorylated states. Insulin promotes nuclear location, while glucagon favors cytoplasmic location.
uniprot
proteins