Q01714 · SP1_RAT
- ProteinTranscription factor Sp1
- GeneSp1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids786 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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). Binds also 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. Positively regulates the transcription of the core clock component BMAL1 (By similarity).
Plays a role in the recruitment of SMARCA4/BRG1 on the c-FOS promoter (PubMed:19081374).
Plays a role in protecting cells against oxidative stress following brain injury by regulating the expression of RNF112 (By similarity).
Plays a role in the recruitment of SMARCA4/BRG1 on the c-FOS promoter (PubMed:19081374).
Plays a role in protecting cells against oxidative stress following brain injury by regulating the expression of RNF112 (By similarity).
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 64-65 | Cleavage | ||||
Sequence: LL |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTranscription factor Sp1
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionQ01714
- Secondary accessions
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, cross-link, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylserine | ||||
Sequence: S | ||||||
Modified residue | 2 | Phosphoserine | ||||
Sequence: S | ||||||
Chain | PRO_0000047139 | 2-786 | Transcription factor Sp1 | |||
Sequence: SDQDHSMDEVTAVKIEKGVGGNNGGSGNGGGAAFSQTRSSSTGSSSSSGGGGGQESQPSPLALLAATCSRIESPNENSNNSQGPSQSGGTGELDLTATQLSQGANGWQIISSSSGATPTSKEQSGNSTNGSNGSESSKNRTVSGGQYVVAATPNLQNQQVLTGLPGVMPNIQYQVIPQFQTVDGQQLQFAATGAQVQQDGSGQIQIIPGANQQIITNRGSGGNIIAAMPNLLQQAVPLQGLANNVLSGQTQYVTNVPVALNGNITLLPVNSVSAATLTPSSQAGTISSSGSQESGSQPVTSGTAISSASLVSSQASSSSFFTNANSYSTTTTTSNMGIMNFTSSGSSGTSSQGQTSQRVGGLQGSDSLNIQQNQTSGGSLQGSQQKEGEQSQQTQQQQILIQPQLVQGGQALQALQAAPLSGQTFTTQAISQETLQNLQLQAVQNSGPIIIRTPTVGPNGQVSWQTLQLQNLQVQNPQAQTITLAPMQGVSLGQTSSSNTTLTPIASAASIPAGTVTVNAAQLSSMPGLQTINLSALGTSGIQVHQLPGLPLAIANTPGDHGAQLGLHGPGGDGIHDETAGGEEGENSPDPQPQAGRRTRREACTCPYCKDSEGRGSGDPGKKKQHICHIQGCGKVYGKTSHLRAHLRWHTGERPFMCNWSYCGKRFTRSDELQRHKRTHTGEKKFACPECPKRFMRSDHLSKHIKTHQNKKGGPGVALSVGTLPLDSGAGSEGSGTATPSALITTNMVAMEAICPEGIARLANSGINVMQVTELQSINISGNGF | ||||||
Modified residue | 7 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 15 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate | ||||
Sequence: K | ||||||
Cross-link | 15 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | ||||||
Modified residue | 60 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 102 | Phosphoserine; by ATM | ||||
Sequence: S | ||||||
Modified residue | 279 | Phosphothreonine; by MAPK8 | ||||
Sequence: T | ||||||
Modified residue | 454 | Phosphothreonine; by MAPK1 and MAPK3 | ||||
Sequence: T | ||||||
Glycosylation | 492 | O-linked (GlcNAc) serine | ||||
Sequence: S | ||||||
Modified residue | 613 | Phosphoserine; alternate | ||||
Sequence: S | ||||||
Glycosylation | 613 | O-linked (GlcNAc) serine; alternate | ||||
Sequence: S | ||||||
Modified residue | 641 | Phosphothreonine; alternate | ||||
Sequence: T | ||||||
Glycosylation | 641 | O-linked (GlcNAc) threonine; alternate | ||||
Sequence: T | ||||||
Modified residue | 642 | Phosphoserine; by PKC/PRKCZ; alternate | ||||
Sequence: S | ||||||
Glycosylation | 642 | O-linked (GlcNAc) serine; alternate | ||||
Sequence: S | ||||||
Modified residue | 652 | Phosphothreonine; by PKC/PRKCZ | ||||
Sequence: T | ||||||
Modified residue | 669 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 671 | Phosphoserine; by PKC/PRKCZ | ||||
Sequence: S | ||||||
Modified residue | 682 | Phosphothreonine; by PKC/PRKCZ | ||||
Sequence: T | ||||||
Modified residue | 699 | Phosphoserine; alternate | ||||
Sequence: S | ||||||
Glycosylation | 699 | O-linked (GlcNAc) serine; alternate | ||||
Sequence: S | ||||||
Modified residue | 703 | Phosphoserine; alternate | ||||
Sequence: S | ||||||
Glycosylation | 703 | O-linked (GlcNAc) serine; alternate | ||||
Sequence: S | ||||||
Modified residue | 704 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 740 | Phosphothreonine; by MAPK1, MAPK3 and MAPK8 | ||||
Sequence: T |
Post-translational modification
Phosphorylated on multiple serine and threonine residues. Phosphorylation is coupled to ubiquitination, sumoylation and proteolytic processing. Phosphorylation on Ser-60 enhances proteolytic cleavage. Phosphorylation on Ser-7 enhances ubiquitination and protein degradation. Hyperphosphorylation on Ser-102 in response to DNA damage has no effect on transcriptional activity. MAPK1/MAPK3-mediated phosphorylation on Thr-454 and Thr-740 enhances VEGF transcription but, represses FGF2-triggered PDGFR-alpha transcription. Also implicated in the repression of RECK by ERBB2. Hyperphosphorylated on Thr-279 and Thr-740 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-60 and Thr-682 can both be dephosphorylated by PP2A during cell-cycle interphase. Dephosphorylation on Ser-60 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).
Acetylated. Acetylation/deacetylation events affect transcriptional activity. Deacetylation leads to an increase in the expression the 12(s)-lipooxygenase gene though recruitment of p300 to the promoter (By similarity).
Ubiquitinated. Ubiquitination occurs on the C-terminal proteolytically-cleaved peptide and is triggered by phosphorylation (By similarity).
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).
Proteolytic cleavage in the N-terminal repressor domain is prevented by sumoylation. The C-terminal cleaved product is susceptible to degradation (By similarity).
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).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in all tissues tested, including lung, kidney, spleen and thymus.
Gene expression databases
Interaction
Subunit
Interacts with ATF7IP, ATF7IP2, BAHD1, POGZ, HCFC1, AATF and PHC2. Interacts with SV40 VP2/3 proteins. Interacts with SV40 major capsid protein VP1; this interaction leads to a cooperativity between the 2 proteins in DNA binding. Interacts with HLTF; the interaction may be required for basal transcriptional activity of HLTF. Interacts (deacetylated form) with EP300; the interaction enhances gene expression. Interacts with HDAC1 and JUN. Interacts with ELF1; the interaction is inhibited by glycosylation of SP1. Interaction with NFYA; the interaction is inhibited by glycosylation of SP1 (By similarity).
Interacts with SMARCA4/BRG1 (PubMed:19081374).
Interacts with ATF7IP and TBP. Interacts with MEIS2 and PBX1. Interacts with EGR1. Interacts with RNF112 in an oxidative stress-regulated manner (By similarity).
Interacts with ZBTB7A; ZBTB7A prevents the binding to GC-rich motifs in promoters and represses the transcriptional activity of SP1 (By similarity).
Interacts with DDX3X; this interaction potentiates SP1-induced CDKN1A/WAF1/CIP1 transcription (By similarity).
Interacts with MSX1; the interaction may inhibit MSX1 autoinactivation (By similarity).
Interacts with MSX3 (By similarity).
Interacts with SMARCA4/BRG1 (PubMed:19081374).
Interacts with ATF7IP and TBP. Interacts with MEIS2 and PBX1. Interacts with EGR1. Interacts with RNF112 in an oxidative stress-regulated manner (By similarity).
Interacts with ZBTB7A; ZBTB7A prevents the binding to GC-rich motifs in promoters and represses the transcriptional activity of SP1 (By similarity).
Interacts with DDX3X; this interaction potentiates SP1-induced CDKN1A/WAF1/CIP1 transcription (By similarity).
Interacts with MSX1; the interaction may inhibit MSX1 autoinactivation (By similarity).
Interacts with MSX3 (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q01714 | Nfya P18576 | 2 | EBI-862787, EBI-862695 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, motif, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-94 | Disordered | ||||
Sequence: MSDQDHSMDEVTAVKIEKGVGGNNGGSGNGGGAAFSQTRSSSTGSSSSSGGGGGQESQPSPLALLAATCSRIESPNENSNNSQGPSQSGGTGEL | ||||||
Region | 2-83 | Repressor domain | ||||
Sequence: SDQDHSMDEVTAVKIEKGVGGNNGGSGNGGGAAFSQTRSSSTGSSSSSGGGGGQESQPSPLALLAATCSRIESPNENSNNSQ | ||||||
Compositional bias | 29-64 | Polar residues | ||||
Sequence: NGGGAAFSQTRSSSTGSSSSSGGGGGQESQPSPLAL | ||||||
Compositional bias | 71-94 | Polar residues | ||||
Sequence: RIESPNENSNNSQGPSQSGGTGEL | ||||||
Region | 110-143 | Disordered | ||||
Sequence: IISSSSGATPTSKEQSGNSTNGSNGSESSKNRTV | ||||||
Region | 147-252 | Transactivation domain A (Gln-rich) | ||||
Sequence: QYVVAATPNLQNQQVLTGLPGVMPNIQYQVIPQFQTVDGQQLQFAATGAQVQQDGSGQIQIIPGANQQIITNRGSGGNIIAAMPNLLQQAVPLQGLANNVLSGQTQ | ||||||
Region | 262-496 | Transactivation domain B (Gln-rich) | ||||
Sequence: NGNITLLPVNSVSAATLTPSSQAGTISSSGSQESGSQPVTSGTAISSASLVSSQASSSSFFTNANSYSTTTTTSNMGIMNFTSSGSSGTSSQGQTSQRVGGLQGSDSLNIQQNQTSGGSLQGSQQKEGEQSQQTQQQQILIQPQLVQGGQALQALQAAPLSGQTFTTQAISQETLQNLQLQAVQNSGPIIIRTPTVGPNGQVSWQTLQLQNLQVQNPQAQTITLAPMQGVSLGQT | ||||||
Region | 281-303 | Disordered | ||||
Sequence: SSQAGTISSSGSQESGSQPVTSG | ||||||
Region | 332-397 | Disordered | ||||
Sequence: TTTSNMGIMNFTSSGSSGTSSQGQTSQRVGGLQGSDSLNIQQNQTSGGSLQGSQQKEGEQSQQTQQ | ||||||
Motif | 463-471 | 9aaTAD | ||||
Sequence: VSWQTLQLQ | ||||||
Region | 497-611 | Transactivation domain C (highly charged) | ||||
Sequence: SSSNTTLTPIASAASIPAGTVTVNAAQLSSMPGLQTINLSALGTSGIQVHQLPGLPLAIANTPGDHGAQLGLHGPGGDGIHDETAGGEEGENSPDPQPQAGRRTRREACTCPYCK | ||||||
Region | 562-600 | Disordered | ||||
Sequence: HGAQLGLHGPGGDGIHDETAGGEEGENSPDPQPQAGRRT | ||||||
Region | 620-786 | VZV IE62-binding | ||||
Sequence: DPGKKKQHICHIQGCGKVYGKTSHLRAHLRWHTGERPFMCNWSYCGKRFTRSDELQRHKRTHTGEKKFACPECPKRFMRSDHLSKHIKTHQNKKGGPGVALSVGTLPLDSGAGSEGSGTATPSALITTNMVAMEAICPEGIARLANSGINVMQVTELQSINISGNGF | ||||||
Zinc finger | 627-656 | C2H2-type 1 | ||||
Sequence: HICHIQGCGKVYGKTSHLRAHLRWHTGERP | ||||||
Zinc finger | 657-686 | C2H2-type 2 | ||||
Sequence: FMCNWSYCGKRFTRSDELQRHKRTHTGEKK | ||||||
Zinc finger | 687-714 | C2H2-type 3 | ||||
Sequence: FACPECPKRFMRSDHLSKHIKTHQNKKG | ||||||
Region | 709-786 | Domain D | ||||
Sequence: HQNKKGGPGVALSVGTLPLDSGAGSEGSGTATPSALITTNMVAMEAICPEGIARLANSGINVMQVTELQSINISGNGF |
Domain
The 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.
Sequence similarities
Belongs to the Sp1 C2H2-type zinc-finger protein family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length786
- Mass (Da)80,772
- Last updated2005-06-21 v2
- Checksum3DE2AD93F95E7C0B
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 29-64 | Polar residues | ||||
Sequence: NGGGAAFSQTRSSSTGSSSSSGGGGGQESQPSPLAL | ||||||
Compositional bias | 71-94 | Polar residues | ||||
Sequence: RIESPNENSNNSQGPSQSGGTGEL | ||||||
Sequence conflict | 78 | in Ref. 1; BAA02235 | ||||
Sequence: N → NEN |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D12768 EMBL· GenBank· DDBJ | BAA02235.1 EMBL· GenBank· DDBJ | mRNA | ||
AB077988 EMBL· GenBank· DDBJ | BAC05486.1 EMBL· GenBank· DDBJ | Genomic DNA |