UniProtKB - P08047 (SP1_HUMAN)
Protein
Transcription factor Sp1
Gene
SP1
Organism
Homo sapiens (Human)
Status
Functioni
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. 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 ARNTL/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:21798247, PubMed:21046154). 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).By similarity17 Publications
Miscellaneous
In the hepatoma cell line Hep-G2, SP1 precursor mRNA may undergo homotype trans-splicing leading to the duplication of exons 2 and 3.
Regions
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Zinc fingeri | 626 – 650 | C2H2-type 1PROSITE-ProRule annotationAdd BLAST | 25 | |
| Zinc fingeri | 656 – 680 | C2H2-type 2PROSITE-ProRule annotationAdd BLAST | 25 | |
| Zinc fingeri | 686 – 708 | C2H2-type 3PROSITE-ProRule annotationAdd BLAST | 23 |
GO - Molecular functioni
- bHLH transcription factor binding Source: BHF-UCL
- cis-regulatory region sequence-specific DNA binding Source: ARUK-UCL
- DNA binding Source: UniProtKB
- DNA-binding transcription activator activity, RNA polymerase II-specific Source: ARUK-UCL
- DNA-binding transcription factor activity Source: UniProtKB
- DNA-binding transcription factor activity, RNA polymerase II-specific Source: NTNU_SB
- double-stranded DNA binding Source: BHF-UCL
- histone acetyltransferase binding Source: Ensembl
- histone deacetylase binding Source: BHF-UCL
- HMG box domain binding Source: UniProtKB
- metal ion binding Source: UniProtKB-KW
- protein C-terminus binding Source: UniProtKB
- protein homodimerization activity Source: UniProtKB
- repressing transcription factor binding Source: CAFA
- RNA polymerase II cis-regulatory region sequence-specific DNA binding Source: ARUK-UCL
- RNA polymerase II regulatory region sequence-specific DNA binding Source: UniProtKB
- RNA polymerase II repressing transcription factor binding Source: BHF-UCL
- sequence-specific DNA binding Source: HGNC-UCL
- transcription factor binding Source: UniProtKB
- transcription regulatory region DNA binding Source: BHF-UCL
GO - Biological processi
- cellular response to insulin stimulus Source: Ensembl
- positive regulation by host of viral transcription Source: UniProtKB
- positive regulation of amyloid-beta formation Source: ARUK-UCL
- positive regulation of angiogenesis Source: BHF-UCL
- positive regulation of blood vessel endothelial cell migration Source: BHF-UCL
- positive regulation of gene expression Source: BHF-UCL
- positive regulation of hydrogen sulfide biosynthetic process Source: BHF-UCL
- positive regulation of transcription, DNA-templated Source: UniProtKB
- positive regulation of transcription by RNA polymerase II Source: UniProtKB
- positive regulation of vascular endothelial cell proliferation Source: BHF-UCL
- regulation of cholesterol biosynthetic process Source: Reactome
- regulation of transcription, DNA-templated Source: UniProtKB
- regulation of transcription by RNA polymerase II Source: GO_Central
- response to hydroperoxide Source: UniProtKB
- rhythmic process Source: UniProtKB-KW
- snRNA transcription by RNA polymerase II Source: Reactome
- viral process Source: UniProtKB-KW
Keywordsi
| Molecular function | Activator, DNA-binding, Repressor |
| Biological process | Biological rhythms, Host-virus interaction, Transcription, Transcription regulation |
| Ligand | Metal-binding, Zinc |
Enzyme and pathway databases
| Reactomei | R-HSA-1989781 PPARA activates gene expression R-HSA-2173796 SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription R-HSA-2426168 Activation of gene expression by SREBF (SREBP) R-HSA-2559585 Oncogene Induced Senescence R-HSA-6807505 RNA polymerase II transcribes snRNA genes R-HSA-9018519 Estrogen-dependent gene expression |
| SignaLinki | P08047 |
| SIGNORi | P08047 |
Names & Taxonomyi
| Protein namesi | Recommended name: Transcription factor Sp1 |
| Gene namesi | Name:SP1 Synonyms:TSFP1 |
| Organismi | Homo sapiens (Human) |
| Taxonomic identifieri | 9606 [NCBI] |
| Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
| Proteomesi |
|
Organism-specific databases
| EuPathDBi | HostDB:ENSG00000185591.9 |
| HGNCi | HGNC:11205 SP1 |
| MIMi | 189906 gene |
| neXtProti | NX_P08047 |
Subcellular locationi
Nucleus
- nuclear chromatin Source: BHF-UCL
- nuclear euchromatin Source: ARUK-UCL
- nucleoplasm Source: ParkinsonsUK-UCL
- nucleus Source: GO_Central
Other locations
- cytoplasm Source: UniProtKB-SubCell
- protein-DNA complex Source: ARUK-UCL
- transcriptional repressor complex Source: CAFA
Keywords - Cellular componenti
Cytoplasm, NucleusPathology & Biotechi
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Mutagenesisi | 7 | S → A: Increase in protein stability. No change in sumoylation. 1 Publication | 1 | |
| Mutagenesisi | 15 | V → R: Enhanced transcriptional activity. | 1 | |
| Mutagenesisi | 16 | K → R: Loss of sumoylation. No cleavage and reduced transcriptional activity. 1 Publication | 1 | |
| Mutagenesisi | 18 | E → A: Loss of sumoylation. Increased cleavage and enhanced transcriptional activity. 1 Publication | 1 | |
| Mutagenesisi | 19 | K → R: No effect on sumoylation nor on proteolytic cleavage. 1 Publication | 1 | |
| Mutagenesisi | 36 | S → A: No effect on phosphorylation on DNA damage. 1 Publication | 1 | |
| Mutagenesisi | 56 | S → A: No effect on phosphorylation on DNA damage. 1 Publication | 1 | |
| Mutagenesisi | 59 | S → A: Loss of phosphorylation. No effect on activated MAPK8-mediated phosphorylation. Similar loss of phosphorylation as by dephosphorylation by PP2AC. Reduced proteolytic processing. 3 Publications | 1 | |
| Mutagenesisi | 59 | S → E: Some association with chromatin, increased phosphorylation levels and decreased glycosylation. 3 Publications | 1 | |
| Mutagenesisi | 73 | S → A: Little effect on activated MAPK8-mediated phosphorylation. 1 Publication | 1 | |
| Mutagenesisi | 81 | S → A: No effect on phosphorylation on DNA damage. 1 Publication | 1 | |
| Mutagenesisi | 85 | S → A: No effect on phosphorylation on DNA damage. 1 Publication | 1 | |
| Mutagenesisi | 98 | T → A: No effect on phosphorylation on DNA damage. 1 Publication | 1 | |
| Mutagenesisi | 101 | S → A: Significant reduction of phosphorylation on DNA damage. 2 Publications | 1 | |
| Mutagenesisi | 101 | S → D: Increase in phosphorylation on DNA damage. 2 Publications | 1 | |
| Mutagenesisi | 117 | T → A: No effect on activated MAPK8-mediated phosphorylation. 1 Publication | 1 | |
| Mutagenesisi | 220 | S → A: No effect on dephosphorylation by PP2A. 1 Publication | 1 | |
| Mutagenesisi | 250 | T → A: No effect on phosphorylation on DNA damage. 1 Publication | 1 | |
| Mutagenesisi | 278 | 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. 1 Publication | 1 | |
| Mutagenesisi | 278 | T → D: Increased protein stability during mitosis; when associated with D-739. 1 Publication | 1 | |
| Mutagenesisi | 281 | S → A: No effect on phosphorylation on DNA damage. 1 Publication | 1 | |
| Mutagenesisi | 291 | S → A: No effect on phosphorylation on DNA damage. 1 Publication | 1 | |
| Mutagenesisi | 296 | S → A: No effect on phosphorylation on DNA damage. 1 Publication | 1 | |
| Mutagenesisi | 313 | S → A: No effect on phosphorylation on DNA damage. 1 Publication | 1 | |
| Mutagenesisi | 351 | S → A: No effect on phosphorylation on DNA damage. 1 Publication | 1 | |
| Mutagenesisi | 355 | T → A: No effect on dephosphorylation by PP2A. 2 Publications | 1 | |
| Mutagenesisi | 394 | T → A: No effect on phosphorylation on DNA damage. 1 Publication | 1 | |
| Mutagenesisi | 427 | T → A: No effect on phosphorylation on DNA damage. 1 Publication | 1 | |
| Mutagenesisi | 431 | S → A: No effect on phosphorylation on DNA damage. 1 Publication | 1 | |
| Mutagenesisi | 453 | 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. 3 Publications | 1 | |
| Mutagenesisi | 491 | S → A: Loss of O-glycosylation. Increase in transcriptional activity. 2 Publications | 1 | |
| Mutagenesisi | 612 | S → A: Diminished glycosylation. Inhibits transcriptional activity; when associated with A-640; A-641; A-698 and A-702. 1 Publication | 1 | |
| Mutagenesisi | 640 | T → A: Diminished glycosylation. Inhibits transcriptional activity; when associated with A-612; A-641; A-698 and A-702. 1 Publication | 1 | |
| Mutagenesisi | 641 | S → A: Abolishes PRKCzeta-mediated phosphorylation. Diminished glycosylation. Inhibits transcriptional activity; when associated with A-612; A-640; A-641 and A-702. 2 Publications | 1 | |
| Mutagenesisi | 651 | T → A: No effect on dephosphorylation by PP2A. 1 Publication | 1 | |
| Mutagenesisi | 668 | T → A: Abolishes PRKCzeta-mediated but not PKCdelta-mediated phosphorylation. No effect on DNA binding; when associated with A-670 and A-681. 1 Publication | 1 | |
| Mutagenesisi | 670 | S → A: Abolishes PRKCzeta-mediated but not PKCdelta-mediated phosphorylation. No effect on DNA binding; when associated with A-668 and A-681. 1 Publication | 1 | |
| Mutagenesisi | 681 | 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. 2 Publications | 1 | |
| Mutagenesisi | 698 | S → A: Diminished glycosylation. Inhibits transcriptional activity; when associated with A-612; A-640; A-641 and A-702. 1 Publication | 1 | |
| Mutagenesisi | 702 | S → A: Diminished glycosylation. Inhibits transcriptional activity; when associated with A-612; A-640; A-641 and A-698. 1 Publication | 1 | |
| Mutagenesisi | 703 | K → A: Abolishes acetylation. Increases recruitment of p300 to the promoter and enhances gene transcription. 1 Publication | 1 | |
| Mutagenesisi | 728 | S → A: Exhibits attenuated endoproteolytic cleavage; when associated with A-732. 1 Publication | 1 | |
| Mutagenesisi | 732 | S → A: Exhibits attenuated endoproteolytic cleavage; when associated with A-728. 1 Publication | 1 | |
| Mutagenesisi | 739 | 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. 4 Publications | 1 | |
| Mutagenesisi | 739 | T → D: Increased protein stability during mitosis; when associated with D-278. 4 Publications | 1 |
Organism-specific databases
| DisGeNETi | 6667 |
| OpenTargetsi | ENSG00000185591 |
| PharmGKBi | PA36042 |
Miscellaneous databases
| Pharosi | P08047 Tbio |
Chemistry databases
| ChEMBLi | CHEMBL6103 |
Polymorphism and mutation databases
| BioMutai | SP1 |
| DMDMi | 13638437 |
PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Initiator methioninei | RemovedCombined sources | |||
| ChainiPRO_0000047137 | 2 – 785 | Transcription factor Sp1Add BLAST | 784 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Modified residuei | 2 | N-acetylserineCombined sources | 1 | |
| Modified residuei | 2 | PhosphoserineCombined sources | 1 | |
| Modified residuei | 7 | PhosphoserineCombined sources1 Publication | 1 | |
| Cross-linki | 16 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate | ||
| Cross-linki | 16 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources | ||
| Modified residuei | 59 | PhosphoserineCombined sources3 Publications | 1 | |
| Modified residuei | 101 | Phosphoserine; by ATM2 Publications | 1 | |
| Modified residuei | 278 | Phosphothreonine; by MAPK81 Publication | 1 | |
| Modified residuei | 453 | Phosphothreonine; by MAPK1 and MAPK33 Publications | 1 | |
| Glycosylationi | 491 | O-linked (GlcNAc) serine2 Publications | 1 | |
| Modified residuei | 612 | Phosphoserine; alternate1 Publication | 1 | |
| Glycosylationi | 612 | O-linked (GlcNAc) serine; alternate1 Publication | 1 | |
| Modified residuei | 640 | Phosphothreonine; alternate1 Publication | 1 | |
| Glycosylationi | 640 | O-linked (GlcNAc) threonine; alternate1 Publication | 1 | |
| Modified residuei | 641 | Phosphoserine; by PKC/PRKCZ; alternate2 Publications | 1 | |
| Glycosylationi | 641 | O-linked (GlcNAc) serine; alternate1 Publication | 1 | |
| Modified residuei | 651 | Phosphothreonine; by PKC/PRKCZCombined sources | 1 | |
| Modified residuei | 668 | Phosphothreonine1 Publication | 1 | |
| Modified residuei | 670 | Phosphoserine; by PKC/PRKCZ1 Publication | 1 | |
| Modified residuei | 681 | Phosphothreonine; by PKC/PRKCZ2 Publications | 1 | |
| Modified residuei | 698 | Phosphoserine; alternate1 Publication | 1 | |
| Glycosylationi | 698 | O-linked (GlcNAc) serine; alternate1 Publication | 1 | |
| Modified residuei | 702 | Phosphoserine; alternate1 Publication1 Publication | 1 | |
| Glycosylationi | 702 | O-linked (GlcNAc) serine; alternate1 Publication | 1 | |
| Modified residuei | 703 | N6-acetyllysine1 Publication | 1 | |
| Modified residuei | 739 | Phosphothreonine; by MAPK1, MAPK3 and MAPK83 Publications | 1 |
Post-translational modificationi
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.11 Publications
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.1 Publication
Ubiquitinated. Ubiquitination occurs on the C-terminal proteolytically-cleaved peptide and is triggered by phosphorylation.1 Publication
Sumoylated with SUMO1. Sumoylation modulates proteolytic cleavage of the N-terminal repressor domain. Sumoylation levels are attenuated during tumorigenesis. Phosphorylation mediates SP1 desumoylation.
Proteolytic cleavage in the N-terminal repressor domain is prevented by sumoylation. The C-terminal cleaved product is susceptible to degradation.
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).
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Sitei | 63 – 64 | CleavageCurated | 2 |
Keywords - PTMi
Acetylation, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
| EPDi | P08047 |
| jPOSTi | P08047 |
| MassIVEi | P08047 |
| MaxQBi | P08047 |
| PaxDbi | P08047 |
| PeptideAtlasi | P08047 |
| PRIDEi | P08047 |
| ProteomicsDBi | 33987 52061 [P08047-1] |
PTM databases
| GlyConnecti | 605 |
| iPTMneti | P08047 |
| PhosphoSitePlusi | P08047 |
| UniCarbKBi | P08047 |
Expressioni
Tissue specificityi
Up-regulated in adenocarcinomas of the stomach (at protein level). Isoform 3 is ubiquitously expressed at low levels.1 Publication
Inductioni
By insulin.1 Publication
Gene expression databases
| Bgeei | ENSG00000185591 Expressed in nipple and 207 other tissues |
| ExpressionAtlasi | P08047 baseline and differential |
| Genevisiblei | P08047 HS |
Organism-specific databases
| HPAi | ENSG00000185591 Low tissue specificity |
Interactioni
Subunit structurei
Interacts with ATF7IP, ATF7IP2, BAHD1, POGZ, HCFC1, AATF and PHC2.
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.
Interacts with ATF7IP and TBP.
Interacts with MEIS2 isoform 4 and PBX1 isoform PBX1a.
Interacts with EGR1 (PubMed:10391891, PubMed:10976766, PubMed:12021324, PubMed:12847090, PubMed:12855699, PubMed:15691849, PubMed:16478997, PubMed:19106100, PubMed:19285002, PubMed:19302979, PubMed:19666599, PubMed:20121949, PubMed:21746878, PubMed:7592727, PubMed:9466902).
Interacts with SMARCA4/BRG1.
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 (PubMed:12004059).
Interacts with DDX3X; this interaction potentiates SP1-induced CDKN1A/WAF1/CIP1 transcription (PubMed:16818630).
By similarity13 Publications(Microbial infection) Interacts with varicella-zoster virus IE62 protein.
1 Publication(Microbial infection) 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.
2 Publications(Microbial infection) Interacts with HIV-1 Vpr; the interaction is inhibited by SP1 O-glycosylation.
1 PublicationBinary interactionsi
Hide detailsP08047
GO - Molecular functioni
- bHLH transcription factor binding Source: BHF-UCL
- histone acetyltransferase binding Source: Ensembl
- histone deacetylase binding Source: BHF-UCL
- HMG box domain binding Source: UniProtKB
- protein C-terminus binding Source: UniProtKB
- protein homodimerization activity Source: UniProtKB
- repressing transcription factor binding Source: CAFA
- RNA polymerase II repressing transcription factor binding Source: BHF-UCL
- transcription factor binding Source: UniProtKB
Protein-protein interaction databases
| BioGRIDi | 112550, 245 interactors |
| CORUMi | P08047 |
| DIPi | DIP-36N |
| ELMi | P08047 |
| IntActi | P08047, 73 interactors |
| MINTi | P08047 |
| STRINGi | 9606.ENSP00000329357 |
Miscellaneous databases
| RNActi | P08047 protein |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
| SMRi | P08047 |
| ModBasei | Search... |
| PDBe-KBi | Search... |
Miscellaneous databases
| EvolutionaryTracei | P08047 |
Family & Domainsi
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Regioni | 2 – 82 | Repressor domainAdd BLAST | 81 | |
| Regioni | 146 – 251 | Transactivation domain A (Gln-rich)Add BLAST | 106 | |
| Regioni | 261 – 495 | Transactivation domain B (Gln-rich)Add BLAST | 235 | |
| Regioni | 496 – 610 | Transactivation domain C (highly charged)Add BLAST | 115 | |
| Regioni | 619 – 785 | VZV IE62-bindingAdd BLAST | 167 | |
| Regioni | 708 – 785 | Domain DAdd BLAST | 78 |
Motif
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Motifi | 462 – 470 | 9aaTAD1 Publication | 9 |
Compositional bias
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Compositional biasi | 36 – 143 | Ser/Thr-richAdd BLAST | 108 | |
| Compositional biasi | 271 – 379 | Ser/Thr-richAdd BLAST | 109 |
Domaini
The 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.1 Publication
Sequence similaritiesi
Belongs to the Sp1 C2H2-type zinc-finger protein family.Curated
Zinc finger
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Zinc fingeri | 626 – 650 | C2H2-type 1PROSITE-ProRule annotationAdd BLAST | 25 | |
| Zinc fingeri | 656 – 680 | C2H2-type 2PROSITE-ProRule annotationAdd BLAST | 25 | |
| Zinc fingeri | 686 – 708 | C2H2-type 3PROSITE-ProRule annotationAdd BLAST | 23 |
Keywords - Domaini
Repeat, Zinc-fingerPhylogenomic databases
| eggNOGi | KOG1721 Eukaryota COG5048 LUCA |
| GeneTreei | ENSGT00940000157804 |
| HOGENOMi | CLU_019688_2_0_1 |
| InParanoidi | P08047 |
| KOi | K04684 |
| OMAi | EACTCPM |
| OrthoDBi | 1085860at2759 |
| PhylomeDBi | P08047 |
| TreeFami | TF350150 |
Family and domain databases
| DisProti | DP00378 |
| IDEALi | IID00266 |
| InterProi | View protein in InterPro IPR036236 Znf_C2H2_sf IPR013087 Znf_C2H2_type |
| Pfami | View protein in Pfam PF00096 zf-C2H2, 3 hits |
| SMARTi | View protein in SMART SM00355 ZnF_C2H2, 3 hits |
| SUPFAMi | SSF57667 SSF57667, 1 hit |
| PROSITEi | View protein in PROSITE PS00028 ZINC_FINGER_C2H2_1, 3 hits PS50157 ZINC_FINGER_C2H2_2, 3 hits |
Sequences (3+)i
Sequence statusi: Complete.
Sequence processingi: The displayed sequence is further processed into a mature form.
This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basketThis entry has 3 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All
Isoform 1 (identifier: P08047-1) [UniParc]FASTAAdd to basket
Also known as: Sp1a
This isoform has been chosen as the canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
10 20 30 40 50
MSDQDHSMDE MTAVVKIEKG VGGNNGGNGN GGGAFSQARS SSTGSSSSTG
60 70 80 90 100
GGGQESQPSP LALLAATCSR IESPNENSNN SQGPSQSGGT GELDLTATQL
110 120 130 140 150
SQGANGWQII SSSSGATPTS KEQSGSSTNG SNGSESSKNR TVSGGQYVVA
160 170 180 190 200
AAPNLQNQQV LTGLPGVMPN IQYQVIPQFQ TVDGQQLQFA ATGAQVQQDG
210 220 230 240 250
SGQIQIIPGA NQQIITNRGS GGNIIAAMPN LLQQAVPLQG LANNVLSGQT
260 270 280 290 300
QYVTNVPVAL NGNITLLPVN SVSAATLTPS SQAVTISSSG SQESGSQPVT
310 320 330 340 350
SGTTISSASL VSSQASSSSF FTNANSYSTT TTTSNMGIMN FTTSGSSGTN
360 370 380 390 400
SQGQTPQRVS GLQGSDALNI QQNQTSGGSL QAGQQKEGEQ NQQTQQQQIL
410 420 430 440 450
IQPQLVQGGQ ALQALQAAPL SGQTFTTQAI SQETLQNLQL QAVPNSGPII
460 470 480 490 500
IRTPTVGPNG QVSWQTLQLQ NLQVQNPQAQ TITLAPMQGV SLGQTSSSNT
510 520 530 540 550
TLTPIASAAS IPAGTVTVNA AQLSSMPGLQ TINLSALGTS GIQVHPIQGL
560 570 580 590 600
PLAIANAPGD HGAQLGLHGA GGDGIHDDTA GGEEGENSPD AQPQAGRRTR
610 620 630 640 650
REACTCPYCK DSEGRGSGDP GKKKQHICHI QGCGKVYGKT SHLRAHLRWH
660 670 680 690 700
TGERPFMCTW SYCGKRFTRS DELQRHKRTH TGEKKFACPE CPKRFMRSDH
710 720 730 740 750
LSKHIKTHQN KKGGPGVALS VGTLPLDSGA GSEGSGTATP SALITTNMVA
760 770 780
MEAICPEGIA RLANSGINVM QVADLQSINI SGNGF
Computationally mapped potential isoform sequencesi
There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket| H3BVI2 | H3BVI2_HUMAN | Transcription factor Sp1 | SP1 | 230 | Annotation score: | ||
| H3BUU5 | H3BUU5_HUMAN | Transcription factor Sp1 | SP1 | 162 | Annotation score: |
Sequence cautioni
The sequence AAH43224 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Sequence conflicti | 366 | D → G AA sequence (PubMed:3319186).Curated | 1 | |
| Sequence conflicti | 670 | S → F AA sequence (PubMed:3319186).Curated | 1 |
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Natural variantiVAR_019971 | 737 | T → A. Corresponds to variant dbSNP:rs3741665Ensembl. | 1 |
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Alternative sequenceiVSP_053934 | 1 – 7 | Missing in isoform 2. Curated | 7 | |
| Alternative sequenceiVSP_053935 | 54 – 101 | Missing in isoform 3. 1 PublicationAdd BLAST | 48 |
Sequence databases
| Select the link destinations: EMBLi GenBanki DDBJi Links Updated | FN908228 mRNA Translation: CBM42955.1 AC068889 Genomic DNA No translation available. AC073611 Genomic DNA No translation available. CH471054 Genomic DNA Translation: EAW96699.1 BC043224 mRNA Translation: AAH43224.1 Different initiation. BC062539 mRNA Translation: AAH62539.1 AF252284 mRNA Translation: AAF67726.1 AB039286 Genomic DNA Translation: BAB13476.1 J03133 mRNA Translation: AAA61154.1 AF255682 mRNA Translation: AAF78781.1 AJ272134 mRNA Translation: CAB75345.1 |
| CCDSi | CCDS44898.1 [P08047-2] CCDS8857.1 [P08047-1] |
| PIRi | A29635 |
| RefSeqi | NP_001238754.1, NM_001251825.1 [P08047-3] NP_003100.1, NM_003109.1 [P08047-2] NP_612482.2, NM_138473.2 [P08047-1] XP_011536998.1, XM_011538696.2 |
Genome annotation databases
| Ensembli | ENST00000327443; ENSP00000329357; ENSG00000185591 [P08047-1] ENST00000426431; ENSP00000404263; ENSG00000185591 [P08047-2] |
| GeneIDi | 6667 |
| KEGGi | hsa:6667 |
| UCSCi | uc001scw.4 human [P08047-1] |
Keywords - Coding sequence diversityi
Alternative splicing, PolymorphismSimilar proteinsi
Cross-referencesi
Sequence databases
| Select the link destinations: EMBLi GenBanki DDBJi Links Updated | FN908228 mRNA Translation: CBM42955.1 AC068889 Genomic DNA No translation available. AC073611 Genomic DNA No translation available. CH471054 Genomic DNA Translation: EAW96699.1 BC043224 mRNA Translation: AAH43224.1 Different initiation. BC062539 mRNA Translation: AAH62539.1 AF252284 mRNA Translation: AAF67726.1 AB039286 Genomic DNA Translation: BAB13476.1 J03133 mRNA Translation: AAA61154.1 AF255682 mRNA Translation: AAF78781.1 AJ272134 mRNA Translation: CAB75345.1 |
| CCDSi | CCDS44898.1 [P08047-2] CCDS8857.1 [P08047-1] |
| PIRi | A29635 |
| RefSeqi | NP_001238754.1, NM_001251825.1 [P08047-3] NP_003100.1, NM_003109.1 [P08047-2] NP_612482.2, NM_138473.2 [P08047-1] XP_011536998.1, XM_011538696.2 |
3D structure databases
| Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1SP1 | NMR | - | A | 684-712 | [»] | |
| 1SP2 | NMR | - | A | 654-684 | [»] | |
| 1VA1 | NMR | - | A | 619-654 | [»] | |
| 1VA2 | NMR | - | A | 654-684 | [»] | |
| 1VA3 | NMR | - | A | 684-712 | [»] | |
| SMRi | P08047 | |||||
| ModBasei | Search... | |||||
| PDBe-KBi | Search... | |||||
Protein-protein interaction databases
| BioGRIDi | 112550, 245 interactors |
| CORUMi | P08047 |
| DIPi | DIP-36N |
| ELMi | P08047 |
| IntActi | P08047, 73 interactors |
| MINTi | P08047 |
| STRINGi | 9606.ENSP00000329357 |
Chemistry databases
| ChEMBLi | CHEMBL6103 |
PTM databases
| GlyConnecti | 605 |
| iPTMneti | P08047 |
| PhosphoSitePlusi | P08047 |
| UniCarbKBi | P08047 |
Polymorphism and mutation databases
| BioMutai | SP1 |
| DMDMi | 13638437 |
Proteomic databases
| EPDi | P08047 |
| jPOSTi | P08047 |
| MassIVEi | P08047 |
| MaxQBi | P08047 |
| PaxDbi | P08047 |
| PeptideAtlasi | P08047 |
| PRIDEi | P08047 |
| ProteomicsDBi | 33987 52061 [P08047-1] |
Protocols and materials databases
| Antibodypediai | 892 1014 antibodies |
Genome annotation databases
| Ensembli | ENST00000327443; ENSP00000329357; ENSG00000185591 [P08047-1] ENST00000426431; ENSP00000404263; ENSG00000185591 [P08047-2] |
| GeneIDi | 6667 |
| KEGGi | hsa:6667 |
| UCSCi | uc001scw.4 human [P08047-1] |
Organism-specific databases
| CTDi | 6667 |
| DisGeNETi | 6667 |
| EuPathDBi | HostDB:ENSG00000185591.9 |
| GeneCardsi | SP1 |
| HGNCi | HGNC:11205 SP1 |
| HPAi | ENSG00000185591 Low tissue specificity |
| MIMi | 189906 gene |
| neXtProti | NX_P08047 |
| OpenTargetsi | ENSG00000185591 |
| PharmGKBi | PA36042 |
| GenAtlasi | Search... |
Phylogenomic databases
| eggNOGi | KOG1721 Eukaryota COG5048 LUCA |
| GeneTreei | ENSGT00940000157804 |
| HOGENOMi | CLU_019688_2_0_1 |
| InParanoidi | P08047 |
| KOi | K04684 |
| OMAi | EACTCPM |
| OrthoDBi | 1085860at2759 |
| PhylomeDBi | P08047 |
| TreeFami | TF350150 |
Enzyme and pathway databases
| Reactomei | R-HSA-1989781 PPARA activates gene expression R-HSA-2173796 SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription R-HSA-2426168 Activation of gene expression by SREBF (SREBP) R-HSA-2559585 Oncogene Induced Senescence R-HSA-6807505 RNA polymerase II transcribes snRNA genes R-HSA-9018519 Estrogen-dependent gene expression |
| SignaLinki | P08047 |
| SIGNORi | P08047 |
Miscellaneous databases
| BioGRID-ORCSi | 6667 112 hits in 811 CRISPR screens |
| ChiTaRSi | SP1 human |
| EvolutionaryTracei | P08047 |
| GeneWikii | Sp1_transcription_factor |
| GenomeRNAii | 6667 |
| Pharosi | P08047 Tbio |
| PROi | PR:P08047 |
| RNActi | P08047 protein |
| SOURCEi | Search... |
Gene expression databases
| Bgeei | ENSG00000185591 Expressed in nipple and 207 other tissues |
| ExpressionAtlasi | P08047 baseline and differential |
| Genevisiblei | P08047 HS |
Family and domain databases
| DisProti | DP00378 |
| IDEALi | IID00266 |
| InterProi | View protein in InterPro IPR036236 Znf_C2H2_sf IPR013087 Znf_C2H2_type |
| Pfami | View protein in Pfam PF00096 zf-C2H2, 3 hits |
| SMARTi | View protein in SMART SM00355 ZnF_C2H2, 3 hits |
| SUPFAMi | SSF57667 SSF57667, 1 hit |
| PROSITEi | View protein in PROSITE PS00028 ZINC_FINGER_C2H2_1, 3 hits PS50157 ZINC_FINGER_C2H2_2, 3 hits |
| ProtoNeti | Search... |
| MobiDBi | Search... |
Entry informationi
| Entry namei | SP1_HUMAN | |
| Accessioni | P08047Primary (citable) accession number: P08047 Secondary accession number(s): E4Z9M7 Q9NYE7 | |
| Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 1, 1988 |
| Last sequence update: | April 27, 2001 | |
| Last modified: | June 17, 2020 | |
| This is version 242 of the entry and version 3 of the sequence. See complete history. | ||
| Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - Human chromosome 12
Human chromosome 12: entries, gene names and cross-references to MIM
