Sp1
entrez
20683
canonical
uniprot
O89090
canonical
ensembl
ENSMUSG00000001280
resolver
ensp
ENSMUSP00000001326
resolver
enst
ENSMUST00000001326
resolver
genesymbol
Sp1
resolver
uniprot
G3X8Q0
resolver
uniprot
O89087
resolver
uniprot
Q62251
resolver
uniprot
Q64167
resolver
uniprot_entry
G3X8Q0_MOUSE
resolver
uniprot_entry
SP1_MOUSE
resolver
uniprot_sec
O89087
resolver
uniprot_sec
Q62251
resolver
uniprot_sec
Q64167
resolver
amino_acid_sequence
MSDQDHSMDEVTAVVKIEKDVGGNNGGSGNGGGAAFSQTRSSSTGSSSSSGGGGGQESQPSPLALLAATCSRIESPNENSNNSQGPSQSGGTGELDLTATQLSQGANGWQIISSSSGATPTSKEQSGNSTNGSNGSESSKNRTVSGGQYVVAATPNLQNQQVLTGLPGVMPNIQYQVIPQFQTVDGQQLQFAATGAQVQQDGSGQIQIIPGANQQIIPNRGSGGNIIAAMPNLLQQAVPLQGLANNVLSGQTQYVTNVPVALNGNITLLPVNSVSAATLTPSSQAGTISSSGSQESSSQPVTSGTAISSASLVSSQASSSSFFTNANSYSTTTTTSNMGIMNFTSSGSSGTSSQGQTPQRVGGLQGSDSLNIQQNQTSGGSLQGSQQKEGEQSQQTQQQQILIQPQLVQGGQALQALQAAPLSGQTFTTQAISQETLQNLQLQAVQNSGPIIIRTPTVGPNGQVSWQTLQLQNLQVQNPQAQTITLAPMQGVSLGQTSSSNTTLTPIASAASIPAGTVTVNAAQLSSMPGLQTINLSALGTSGIQVHQLPGLPLAIANTPGDHGTQLGLHGSGGDGIHDETAGGEGENSSDLQPQAGRRTRREACTCPYCKDSEGRASGDPGKKKQHICHIQGCGKVYGKTSHLRAHLRWHTGERPFMCNWSYCGKRFTRSDELQRHKRTHTGEKKFACPECPKRFMRSDHLSKHIKTHQNKKGGPGVALSVGTLPLDSGAGSEGTATPSALITTNMVAMEAICPEGIARLANSGINVMQVTELQSINISGNGF
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 a role in the recruitment of SMARCA4/BRG1 on the c-FOS promoter Plays an essential role in the regulation of FE65 gene expression (By similarity). Positively regulates the transcription of the core clock component BMAL1 (PubMed:24030830). Plays a role in protecting cells against oxidative stress following brain injury by regulating the expression of RNF112 (PubMed:27918959). {ECO:0000250|UniProtKB:P08047, ECO:0000250|UniProtKB:Q01714, ECO:0000269|PubMed:24030830, ECO:0000269|PubMed:27918959}.
uniprot
proteins
mass_dalton
80732
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-61 enhances proteolytic cleavage. Phosphorylation on Ser-7 enhances ubiquitination and protein degradation. Hyperphosphorylation on Ser-103 in response to DNA damage has no effect on transcriptional activity. MAPK1/MAPK3-mediated phosphorylation on Thr-455 and Thr-738 enhances VEGF transcription but, represses FGF2-triggered PDGFR-alpha transcription. Also implicated in the repression of RECK by ERBB2. Hyperphosphorylated on Thr-280 and Thr-738 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-642 by PKCzeta is critical for TSA-activated LHR gene expression through release of its repressor, p107. Phosphorylation on Thr-669, Ser-671 and Thr-682 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-61 and Thr-682 can both be dephosphorylated by PP2A during cell-cycle interphase. Dephosphorylation on Ser-61 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 (By similarity). {ECO:0000250}.; PTM: Acetylated. Acetylation/deacetylation events affect transcriptional activity. Deacetylation leads to an increase in the expression of the 12(s)-lipooxygenase gene through recruitment of p300 to the promoter. Deacetylated by HDAC6 which leads to increased expression of ENG and positive regulation of angiogenesis. {ECO:0000250|UniProtKB:P08047}.; PTM: Ubiquitinated. Ubiquitination occurs on the C-terminal proteolytically-cleaved peptide and is triggered by phosphorylation (By similarity). {ECO:0000250}.; PTM: Sumoylated with SUMO1. Sumoylation modulates proteolytic cleavage of the N-terminal repressor domain. Sumoylation levels are attenuated during tumorigenesis. Phosphorylation mediates SP1 desumoylation (By similarity). {ECO:0000250}.; PTM: Proteolytic cleavage in the N-terminal repressor domain is prevented by sumoylation. The C-terminal cleaved product is susceptible to degradation (By similarity). {ECO:0000250}.; 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. Inhibited by peroxisomome proliferator receptor gamma (PPARgamma) (By similarity). {ECO:0000250}.
uniprot
proteins
protein_family
Sp1 C2H2-type zinc-finger protein family
uniprot
proteins
pubmed
10215616
uniprot
proteins
pubmed
1633330
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
24030830
uniprot
proteins
pubmed
27918959
uniprot
proteins
pubmed
7568082
uniprot
proteins
pubmed
7799962
uniprot
proteins
pubmed
9454706
uniprot
proteins
pubmed
9628590
uniprot
proteins
sequence_length
784
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27918959}. Cytoplasm {ECO:0000250}. Note=Nuclear location is governed by glycosylated/phosphorylated states. Insulin promotes nuclear location, while glucagon favors cytoplasmic location (By similarity). {ECO:0000250}.
uniprot
proteins