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P08047

- SP1_HUMAN

UniProt

P08047 - SP1_HUMAN

Protein

Transcription factor Sp1

Gene

SP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 184 (01 Oct 2014)
      Sequence version 3 (27 Apr 2001)
      Previous versions | rss
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    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 a role in the recruitment of SMARCA4/BRG1 on the c-FOS promoter. 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/BMAL1.16 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei63 – 642CleavageCurated

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri626 – 65025C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri656 – 68025C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri686 – 70823C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. bHLH transcription factor binding Source: BHF-UCL
    2. core promoter sequence-specific DNA binding Source: UniProtKB
    3. DNA binding Source: UniProtKB
    4. double-stranded DNA binding Source: BHF-UCL
    5. enhancer binding Source: Ensembl
    6. histone deacetylase binding Source: BHF-UCL
    7. HMG box domain binding Source: UniProtKB
    8. metal ion binding Source: UniProtKB-KW
    9. protein binding Source: UniProtKB
    10. protein C-terminus binding Source: UniProtKB
    11. protein homodimerization activity Source: UniProtKB
    12. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: BHF-UCL
    13. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: Ensembl
    14. RNA polymerase II core promoter sequence-specific DNA binding Source: Ensembl
    15. RNA polymerase II repressing transcription factor binding Source: BHF-UCL
    16. sequence-specific DNA binding Source: HGNC
    17. sequence-specific DNA binding transcription factor activity Source: UniProtKB
    18. transcription factor binding Source: UniProtKB
    19. transcription regulatory region DNA binding Source: BHF-UCL

    GO - Biological processi

    1. cellular lipid metabolic process Source: Reactome
    2. definitive hemopoiesis Source: Ensembl
    3. embryonic camera-type eye morphogenesis Source: Ensembl
    4. embryonic placenta development Source: Ensembl
    5. embryonic process involved in female pregnancy Source: Ensembl
    6. embryonic skeletal system development Source: Ensembl
    7. enucleate erythrocyte differentiation Source: Ensembl
    8. gene expression Source: Reactome
    9. liver development Source: Ensembl
    10. lung development Source: Ensembl
    11. megakaryocyte differentiation Source: Ensembl
    12. ossification Source: Ensembl
    13. positive regulation by host of viral transcription Source: UniProtKB
    14. positive regulation of transcription, DNA-templated Source: UniProtKB
    15. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    16. regulation of transcription, DNA-templated Source: UniProtKB
    17. small molecule metabolic process Source: Reactome
    18. transcription, DNA-templated Source: Reactome
    19. transcription initiation from RNA polymerase II promoter Source: Reactome
    20. transforming growth factor beta receptor signaling pathway Source: Reactome
    21. trophectodermal cell differentiation Source: Ensembl
    22. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Repressor

    Keywords - Biological processi

    Biological rhythms, Host-virus interaction, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_116145. PPARA activates gene expression.
    REACT_120734. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
    REACT_147904. Activation of gene expression by SREBF (SREBP).
    REACT_169325. Oncogene Induced Senescence.
    SignaLinkiP08047.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcription factor Sp1
    Gene namesi
    Name:SP1
    Synonyms:TSFP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:11205. SP1.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: Nuclear location is governed by glycosylated/phosphorylated states. Insulin promotes nuclear location, while glucagon favors cytoplasmic location.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleoplasm Source: Reactome
    3. nucleus Source: UniProtKB
    4. protein-DNA complex Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi7 – 71S → A: Increase in protein stability. No change in sumoylation. 1 Publication
    Mutagenesisi15 – 151V → R: Enhanced transcriptional activity.
    Mutagenesisi16 – 161K → R: Loss of sumoylation. No cleavage and reduced transcriptional activity. 1 Publication
    Mutagenesisi18 – 181E → A: Loss of sumoylation. Increased cleavage and enhanced transcriptional activity. 1 Publication
    Mutagenesisi19 – 191K → R: No effect on sumoylation nor on proteolytic cleavage. 1 Publication
    Mutagenesisi36 – 361S → A: No effect on phosphorylation on DNA damage. 1 Publication
    Mutagenesisi56 – 561S → A: No effect on phosphorylation on DNA damage. 1 Publication
    Mutagenesisi59 – 591S → 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
    Mutagenesisi59 – 591S → E: Some association with chromatin, increased phosphorylation levels and decreased glycosylation. 3 Publications
    Mutagenesisi73 – 731S → A: Little effect on activated MAPK8-mediated phosphorylation. 1 Publication
    Mutagenesisi81 – 811S → A: No effect on phosphorylation on DNA damage. 1 Publication
    Mutagenesisi85 – 851S → A: No effect on phosphorylation on DNA damage. 1 Publication
    Mutagenesisi98 – 981T → A: No effect on phosphorylation on DNA damage. 1 Publication
    Mutagenesisi101 – 1011S → A: Significant reduction of phosphorylation on DNA damage. 2 Publications
    Mutagenesisi101 – 1011S → D: Increase in phosphorylation on DNA damage. 2 Publications
    Mutagenesisi117 – 1171T → A: No effect on activated MAPK8-mediated phosphorylation. 1 Publication
    Mutagenesisi220 – 2201S → A: No effect on dephosphorylation by PP2A. 1 Publication
    Mutagenesisi250 – 2501T → A: No effect on phosphorylation on DNA damage. 1 Publication
    Mutagenesisi278 – 2781T → 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
    Mutagenesisi278 – 2781T → D: Increased protein stability during mitosis; when associated with D-739. 1 Publication
    Mutagenesisi281 – 2811S → A: No effect on phosphorylation on DNA damage. 1 Publication
    Mutagenesisi291 – 2911S → A: No effect on phosphorylation on DNA damage. 1 Publication
    Mutagenesisi296 – 2961S → A: No effect on phosphorylation on DNA damage. 1 Publication
    Mutagenesisi313 – 3131S → A: No effect on phosphorylation on DNA damage. 1 Publication
    Mutagenesisi351 – 3511S → A: No effect on phosphorylation on DNA damage. 1 Publication
    Mutagenesisi355 – 3551T → A: No effect on dephosphorylation by PP2A. 2 Publications
    Mutagenesisi394 – 3941T → A: No effect on phosphorylation on DNA damage. 1 Publication
    Mutagenesisi427 – 4271T → A: No effect on phosphorylation on DNA damage. 1 Publication
    Mutagenesisi431 – 4311S → A: No effect on phosphorylation on DNA damage. 1 Publication
    Mutagenesisi453 – 4531T → 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
    Mutagenesisi491 – 4911S → A: Loss of O-glycosylation. Increase in transcriptional activity. 2 Publications
    Mutagenesisi612 – 6121S → A: Diminished glycosylation. Inhibits transcriptional activity; when associated with A-640; A-641; A-698 and A-702. 1 Publication
    Mutagenesisi640 – 6401T → A: Diminished glycosylation. Inhibits transcriptional activity; when associated with A-612; A-641; A-698 and A-702. 1 Publication
    Mutagenesisi641 – 6411S → A: Abolishes PRKCzeta-mediated phosphorylation. Diminished glycosylation. Inhibits transcriptional activity; when associated with A-612; A-640; A-641 and A-702. 2 Publications
    Mutagenesisi651 – 6511T → A: No effect on dephosphorylation by PP2A. 1 Publication
    Mutagenesisi668 – 6681T → A: Abolishes PRKCzeta-mediated but not PKCdelta-mediated phosphorylation. No effect on DNA binding; when associated with A-670 and A-681. 1 Publication
    Mutagenesisi670 – 6701S → A: Abolishes PRKCzeta-mediated but not PKCdelta-mediated phosphorylation. No effect on DNA binding; when associated with A-668 and A-681. 1 Publication
    Mutagenesisi681 – 6811T → 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
    Mutagenesisi698 – 6981S → A: Diminished glycosylation. Inhibits transcriptional activity; when associated with A-612; A-640; A-641 and A-702. 1 Publication
    Mutagenesisi702 – 7021S → A: Diminished glycosylation. Inhibits transcriptional activity; when associated with A-612; A-640; A-641 and A-698. 1 Publication
    Mutagenesisi703 – 7031K → A: Abolishes acetylation. Increases recruitment of p300 to the promoter and enhances gene transcription. 1 Publication
    Mutagenesisi728 – 7281S → A: Exhibits attenuated endoproteolytic cleavage; when associated with A-732. 1 Publication
    Mutagenesisi732 – 7321S → A: Exhibits attenuated endoproteolytic cleavage; when associated with A-728. 1 Publication
    Mutagenesisi739 – 7391T → 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
    Mutagenesisi739 – 7391T → D: Increased protein stability during mitosis; when associated with D-278. 4 Publications

    Organism-specific databases

    PharmGKBiPA36042.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 785784Transcription factor Sp1PRO_0000047137Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications
    Modified residuei2 – 21Phosphoserine2 Publications
    Modified residuei7 – 71Phosphoserine4 Publications
    Cross-linki16 – 16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei59 – 591Phosphoserine5 Publications
    Modified residuei101 – 1011Phosphoserine; by ATM3 Publications
    Modified residuei278 – 2781Phosphothreonine; by MAPK82 Publications
    Modified residuei453 – 4531Phosphothreonine; by MAPK1 AND MAPK34 Publications
    Glycosylationi491 – 4911O-linked (GlcNAc)2 Publications
    Modified residuei612 – 6121Phosphoserine; alternate1 Publication
    Glycosylationi612 – 6121O-linked (GlcNAc); alternate1 Publication
    Modified residuei640 – 6401Phosphothreonine; alternate1 Publication
    Glycosylationi640 – 6401O-linked (GlcNAc); alternate1 Publication
    Modified residuei641 – 6411Phosphoserine; by PKC/PRKCZ; alternate2 Publications
    Glycosylationi641 – 6411O-linked (GlcNAc); alternate1 Publication
    Modified residuei651 – 6511Phosphothreonine; by PKC/PRKCZ2 Publications
    Modified residuei668 – 6681Phosphothreonine2 Publications
    Modified residuei670 – 6701Phosphoserine; by PKC/PRKCZ2 Publications
    Modified residuei681 – 6811Phosphothreonine; by PKC/PRKCZ3 Publications
    Glycosylationi698 – 6981O-linked (GlcNAc)1 Publication
    Modified residuei702 – 7021Phosphoserine; alternate2 Publications
    Glycosylationi702 – 7021O-linked (GlcNAc); alternate1 Publication
    Modified residuei703 – 7031N6-acetyllysine1 Publication
    Modified residuei739 – 7391Phosphothreonine; by MAPK1, MAPK3 AND MAPK84 Publications

    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.14 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.3 Publications
    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).

    Keywords - PTMi

    Acetylation, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP08047.
    PaxDbiP08047.
    PeptideAtlasiP08047.
    PRIDEiP08047.

    PTM databases

    PhosphoSiteiP08047.
    UniCarbKBiP08047.

    Miscellaneous databases

    PMAP-CutDBP08047.

    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

    ArrayExpressiP08047.
    BgeeiP08047.
    CleanExiHS_SP1.
    GenevestigatoriP08047.

    Organism-specific databases

    HPAiCAB000330.
    HPA001853.
    HPA012292.

    Interactioni

    Subunit structurei

    Interacts with ATF7IP, ATF7IP2, BAHD1, POGZ, HCFC1, AATF and PHC2. Interacts with varicella-zoster virus IE62 protein. Interacts with HIV-1 Vpr; the interaction is inhibited by SP1 O-glycosylation. 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. Interacts with SMARCA4/BRG1 By similarity. Interacts with ATF7IP and TBP. Interacts with MEIS2 isoform 4 and PBX1 isoform PBX1a. Interacts with EGR1.By similarity15 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DLX4Q929884EBI-298336,EBI-1752755
    E2F1Q010942EBI-298336,EBI-448924
    ELF1P325192EBI-298336,EBI-765526
    EPAS1Q998142EBI-298336,EBI-447470
    ESR1P033722EBI-298336,EBI-78473
    HCFC1P516104EBI-298336,EBI-396176
    HIF1AQ166653EBI-298336,EBI-447269
    KLF10Q131182EBI-298336,EBI-1389509
    MYCP011064EBI-298336,EBI-447544
    NCK1P163332EBI-298336,EBI-389883
    NfyaP2370818EBI-298336,EBI-862337From a different organism.
    PHC2Q8IXK02EBI-298336,EBI-713786
    POGZQ7Z3K32EBI-298336,EBI-1389308
    POU2F1P148597EBI-298336,EBI-624770
    RUNX1T1Q064552EBI-298336,EBI-743342
    SF3A1Q154592EBI-298336,EBI-1054743
    SMAD4Q134852EBI-298336,EBI-347263
    SREBF2Q127723EBI-298336,EBI-465059

    Protein-protein interaction databases

    BioGridi112550. 222 interactions.
    DIPiDIP-36N.
    IntActiP08047. 62 interactions.
    MINTiMINT-98326.
    STRINGi9606.ENSP00000329357.

    Structurei

    Secondary structure

    1
    785
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi620 – 6223
    Beta strandi636 – 6383
    Helixi640 – 65112
    Turni661 – 6633
    Beta strandi666 – 6683
    Helixi670 – 6778
    Turni678 – 6803
    Turni689 – 6924
    Helixi699 – 7068
    Helixi707 – 7093

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1SP1NMR-A684-712[»]
    1SP2NMR-A654-684[»]
    1VA1NMR-A619-654[»]
    1VA2NMR-A654-684[»]
    1VA3NMR-A684-712[»]
    DisProtiDP00378.
    ProteinModelPortaliP08047.
    SMRiP08047. Positions 606-712.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08047.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 8281Repressor domainAdd
    BLAST
    Regioni146 – 251106Transactivation domain A (Gln-rich)Add
    BLAST
    Regioni261 – 495235Transactivation domain B (Gln-rich)Add
    BLAST
    Regioni496 – 610115Transactivation domain C (highly charged)Add
    BLAST
    Regioni619 – 785167VZV IE62-bindingAdd
    BLAST
    Regioni708 – 78578Domain DAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi36 – 143108Ser/Thr-richAdd
    BLAST
    Compositional biasi271 – 379109Ser/Thr-richAdd
    BLAST

    Sequence similaritiesi

    Contains 3 C2H2-type zinc fingers.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri626 – 65025C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri656 – 68025C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri686 – 70823C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5048.
    HOGENOMiHOG000234295.
    HOVERGENiHBG008933.
    InParanoidiP08047.
    KOiK04684.
    OMAiGWQIISS.
    OrthoDBiEOG76HQ15.
    PhylomeDBiP08047.
    TreeFamiTF350150.

    Family and domain databases

    Gene3Di3.30.160.60. 3 hits.
    InterProiIPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view]
    PfamiPF00096. zf-C2H2. 1 hit.
    [Graphical view]
    SMARTiSM00355. ZnF_C2H2. 3 hits.
    [Graphical view]
    PROSITEiPS00028. ZINC_FINGER_C2H2_1. 3 hits.
    PS50157. ZINC_FINGER_C2H2_2. 3 hits.
    [Graphical view]

    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. Align

    Isoform 1 (identifier: P08047-1) [UniParc]FASTAAdd to Basket

    Also known as: Sp1a

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSDQDHSMDE MTAVVKIEKG VGGNNGGNGN GGGAFSQARS SSTGSSSSTG    50
    GGGQESQPSP LALLAATCSR IESPNENSNN SQGPSQSGGT GELDLTATQL 100
    SQGANGWQII SSSSGATPTS KEQSGSSTNG SNGSESSKNR TVSGGQYVVA 150
    AAPNLQNQQV LTGLPGVMPN IQYQVIPQFQ TVDGQQLQFA ATGAQVQQDG 200
    SGQIQIIPGA NQQIITNRGS GGNIIAAMPN LLQQAVPLQG LANNVLSGQT 250
    QYVTNVPVAL NGNITLLPVN SVSAATLTPS SQAVTISSSG SQESGSQPVT 300
    SGTTISSASL VSSQASSSSF FTNANSYSTT TTTSNMGIMN FTTSGSSGTN 350
    SQGQTPQRVS GLQGSDALNI QQNQTSGGSL QAGQQKEGEQ NQQTQQQQIL 400
    IQPQLVQGGQ ALQALQAAPL SGQTFTTQAI SQETLQNLQL QAVPNSGPII 450
    IRTPTVGPNG QVSWQTLQLQ NLQVQNPQAQ TITLAPMQGV SLGQTSSSNT 500
    TLTPIASAAS IPAGTVTVNA AQLSSMPGLQ TINLSALGTS GIQVHPIQGL 550
    PLAIANAPGD HGAQLGLHGA GGDGIHDDTA GGEEGENSPD AQPQAGRRTR 600
    REACTCPYCK DSEGRGSGDP GKKKQHICHI QGCGKVYGKT SHLRAHLRWH 650
    TGERPFMCTW SYCGKRFTRS DELQRHKRTH TGEKKFACPE CPKRFMRSDH 700
    LSKHIKTHQN KKGGPGVALS VGTLPLDSGA GSEGSGTATP SALITTNMVA 750
    MEAICPEGIA RLANSGINVM QVADLQSINI SGNGF 785
    Length:785
    Mass (Da):80,693
    Last modified:April 27, 2001 - v3
    Checksum:i43893DBF6518B9EA
    GO
    Isoform 2 (identifier: P08047-2) [UniParc]FASTAAdd to Basket

    Also known as: Sp1b

    The sequence of this isoform differs from the canonical sequence as follows:
         1-7: Missing.

    Show »
    Length:778
    Mass (Da):79,892
    Checksum:i74D5DA9A1F8DC8EA
    GO
    Isoform 3 (identifier: P08047-3) [UniParc]FASTAAdd to Basket

    Also known as: Sp1c

    The sequence of this isoform differs from the canonical sequence as follows:
         54-101: Missing.

    Show »
    Length:737
    Mass (Da):75,824
    Checksum:iD830B2947A96C8B9
    GO

    Sequence cautioni

    The sequence AAH43224.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti366 – 3661D → G AA sequence (PubMed:3319186)Curated
    Sequence conflicti670 – 6701S → F AA sequence (PubMed:3319186)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti737 – 7371T → A.
    Corresponds to variant rs3741665 [ dbSNP | Ensembl ].
    VAR_019971

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 77Missing in isoform 2. CuratedVSP_053934
    Alternative sequencei54 – 10148Missing in isoform 3. 1 PublicationVSP_053935Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    CCDSiCCDS44898.1. [P08047-2]
    CCDS8857.1. [P08047-1]
    PIRiA29635.
    RefSeqiNP_001238754.1. NM_001251825.1. [P08047-3]
    NP_003100.1. NM_003109.1. [P08047-2]
    NP_612482.2. NM_138473.2. [P08047-1]
    UniGeneiHs.620754.
    Hs.649191.

    Genome annotation databases

    EnsembliENST00000327443; ENSP00000329357; ENSG00000185591. [P08047-1]
    ENST00000426431; ENSP00000404263; ENSG00000185591. [P08047-2]
    GeneIDi6667.
    KEGGihsa:6667.
    UCSCiuc001scw.3. human. [P08047-1]

    Polymorphism databases

    DMDMi13638437.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 ]
    UniGenei Hs.620754.
    Hs.649191.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    DisProti DP00378.
    ProteinModelPortali P08047.
    SMRi P08047. Positions 606-712.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112550. 222 interactions.
    DIPi DIP-36N.
    IntActi P08047. 62 interactions.
    MINTi MINT-98326.
    STRINGi 9606.ENSP00000329357.

    Chemistry

    ChEMBLi CHEMBL6103.

    PTM databases

    PhosphoSitei P08047.
    UniCarbKBi P08047.

    Polymorphism databases

    DMDMi 13638437.

    Proteomic databases

    MaxQBi P08047.
    PaxDbi P08047.
    PeptideAtlasi P08047.
    PRIDEi P08047.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000327443 ; ENSP00000329357 ; ENSG00000185591 . [P08047-1 ]
    ENST00000426431 ; ENSP00000404263 ; ENSG00000185591 . [P08047-2 ]
    GeneIDi 6667.
    KEGGi hsa:6667.
    UCSCi uc001scw.3. human. [P08047-1 ]

    Organism-specific databases

    CTDi 6667.
    GeneCardsi GC12P053773.
    HGNCi HGNC:11205. SP1.
    HPAi CAB000330.
    HPA001853.
    HPA012292.
    MIMi 189906. gene.
    neXtProti NX_P08047.
    PharmGKBi PA36042.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5048.
    HOGENOMi HOG000234295.
    HOVERGENi HBG008933.
    InParanoidi P08047.
    KOi K04684.
    OMAi GWQIISS.
    OrthoDBi EOG76HQ15.
    PhylomeDBi P08047.
    TreeFami TF350150.

    Enzyme and pathway databases

    Reactomei REACT_116145. PPARA activates gene expression.
    REACT_120734. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
    REACT_147904. Activation of gene expression by SREBF (SREBP).
    REACT_169325. Oncogene Induced Senescence.
    SignaLinki P08047.

    Miscellaneous databases

    ChiTaRSi SP1. human.
    EvolutionaryTracei P08047.
    GeneWikii Sp1_transcription_factor.
    GenomeRNAii 6667.
    NextBioi 25995.
    PMAP-CutDB P08047.
    PROi P08047.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P08047.
    Bgeei P08047.
    CleanExi HS_SP1.
    Genevestigatori P08047.

    Family and domain databases

    Gene3Di 3.30.160.60. 3 hits.
    InterProi IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view ]
    Pfami PF00096. zf-C2H2. 1 hit.
    [Graphical view ]
    SMARTi SM00355. ZnF_C2H2. 3 hits.
    [Graphical view ]
    PROSITEi PS00028. ZINC_FINGER_C2H2_1. 3 hits.
    PS50157. ZINC_FINGER_C2H2_2. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a novel Sp1 splice variant as a strong transcriptional activator."
      Infantino V., Convertini P., Iacobazzi F., Pisano I., Scarcia P., Iacobazzi V.
      Biochem. Biophys. Res. Commun. 412:86-91(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, TISSUE SPECIFICITY.
    2. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain and Testis.
    5. Haggart M.H., Ladurner A.G.
      Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-785 (ISOFORM 1).
      Tissue: Cervix carcinoma.
    6. "Heterogeneous Sp1 mRNAs in human HepG2 cells include a product of homotypic trans-splicing."
      Takahara T., Kanazu S., Yanagisawa S., Akanuma H.
      J. Biol. Chem. 275:38067-38072(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-558 (ISOFORM 1), TRANS-SPLICING.
    7. "Isolation of cDNA encoding transcription factor Sp1 and functional analysis of the DNA binding domain."
      Kadonaga J.T., Carner K.R., Masiarz F.R., Tjian R.
      Cell 51:1079-1090(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 90-785 (ISOFORM 1/2), PROTEIN SEQUENCE OF 359-375 AND 670-675.
    8. "Expression of transcription factor Sp1 mRNA in mammalian cells."
      Nicolas M., Noe V., Ciudad C.J.
      Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-109 (ISOFORM 1).
    9. "Sequencing of the 5' end of human transcription factor SP1 mRNA."
      Handschug K., Huebner A.
      Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-98 (ISOFORM 1).
    10. "O-glycosylation of eukaryotic transcription factors: implications for mechanisms of transcriptional regulation."
      Jackson S.P., Tjian R.
      Cell 55:125-133(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION.
    11. "Analysis of Sp1 in vivo reveals multiple transcriptional domains, including a novel glutamine-rich activation motif."
      Courey A.J., Tjian R.
      Cell 55:887-898(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: TRANSACTIVATION DOMAINS.
    12. "Interaction of virion protein Vpr of human immunodeficiency virus type 1 with cellular transcription factor Sp1 and trans-activation of viral long terminal repeat."
      Wang L., Mukherjee S., Jia F., Narayan O., Zhao L.J.
      J. Biol. Chem. 270:25564-25569(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIV-1 VPR.
    13. "The serotonin 1a receptor gene contains a TATA-less promoter that responds to MAZ and Sp1."
      Parks C.L., Shenk T.
      J. Biol. Chem. 271:4417-4430(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF SEROTONIN 1A RECEPTOR PROMOTER BINDING SITES.
    14. "O glycosylation of an Sp1-derived peptide blocks known Sp1 protein interactions."
      Roos M.D., Su K., Baker J.R., Kudlow J.E.
      Mol. Cell. Biol. 17:6472-6480(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT SER-491, MUTAGENESIS OF SER-491, IDENTIFICATION BY MASS SPECTROMETRY.
    15. "The SV40 capsid protein VP3 cooperates with the cellular transcription factor Sp1 in DNA-binding and in regulating viral promoter activity."
      Gordon-Shaag A., Ben-Nun-Shaul O., Kasamatsu H., Oppenheim A.B., Oppenheim A.
      J. Mol. Biol. 275:187-195(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SV40 VP2/3.
    16. "Functional interactions between Sp1 or Sp3 and the helicase-like transcription factor mediate basal expression from the human plasminogen activator inhibitor-1 gene."
      Ding H., Benotmane A.M., Suske G., Collen D., Belayew A.
      J. Biol. Chem. 274:19573-19580(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HLTF.
    17. "A set of proteins interacting with transcription factor Sp1 identified in a two-hybrid screening."
      Gunther M., Laithier M., Brison O.
      Mol. Cell. Biochem. 210:131-142(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ATF7IP; PHC2; POGZ AND HCFC1.
      Tissue: Colon.
    18. "O-linkage of N-acetylglucosamine to Sp1 activation domain inhibits its transcriptional capability."
      Yang X., Su K., Roos M.D., Chang Q., Paterson A.J., Kudlow J.E.
      Proc. Natl. Acad. Sci. U.S.A. 98:6611-6616(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT SER-491, FUNCTION, MUTAGENESIS OF SER-491.
    19. "Identification of two Sp1 phosphorylation sites for p42/p44 mitogen-activated protein kinases: their implication in vascular endothelial growth factor gene transcription."
      Milanini-Mongiat J., Pouyssegur J., Pages G.
      J. Biol. Chem. 277:20631-20639(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-453 AND THR-739, FUNCTION, MUTAGENESIS OF THR-355; THR-453 AND THR-739.
    20. "Cellular transcription factor Sp1 recruits simian virus 40 capsid proteins to the viral packaging signal, ses."
      Gordon-Shaag A., Ben-Nun-Shaul O., Roitman V., Yosef Y., Oppenheim A.
      J. Virol. 76:5915-5924(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SV40 VP1.
    21. "Che-1 arrests human colon carcinoma cell proliferation by displacing HDAC1 from the p21WAF1/CIP1 promoter."
      Di Padova M., Bruno T., De Nicola F., Iezzi S., D'Angelo C., Gallo R., Nicosia D., Corbi N., Biroccio A., Floridi A., Passananti C., Fanciulli M.
      J. Biol. Chem. 278:36496-36504(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AATF.
    22. "Interaction between the varicella zoster virus IE62 major transactivator and cellular transcription factor Sp1."
      Peng H., He H., Hay J., Ruyechan W.T.
      J. Biol. Chem. 278:38068-38075(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VARICELLA-ZOSTER VIRUS IE62 PROTEIN.
    23. "Fibroblast growth factor-2 represses platelet-derived growth factor receptor-alpha (PDGFR-alpha) transcription via ERK1/2-dependent Sp1 phosphorylation and an atypical cis-acting element in the proximal PDGFR-alpha promoter."
      Bonello M.R., Khachigian L.M.
      J. Biol. Chem. 279:2377-2382(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-453 AND THR-739, FUNCTION, MUTAGENESIS OF THR-453 AND THR-739.
    24. "Transcriptional repression and heterochromatin formation by MBD1 and MCAF/AM family proteins."
      Ichimura T., Watanabe S., Sakamoto Y., Aoto T., Fujita N., Nakao M.
      J. Biol. Chem. 280:13928-13935(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ATF7IP AND ATF7IP2.
    25. "Insulin dynamically regulates calmodulin gene expression by sequential O-glycosylation and phosphorylation of SP1 and its subcellular compartmentalization in liver cells."
      Majumdar G., Harrington A., Hungerford J., Martinez-Hernandez A., Gerling I.C., Raghow R., Solomon S.
      J. Biol. Chem. 281:3642-3650(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT SER-612; THR-640; SER-641; SER-698 AND SER-702, PHOSPHORYLATION, INDUCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    26. "HER-2/neu represses the metastasis suppressor RECK via ERK and Sp transcription factors to promote cell invasion."
      Hsu M.C., Chang H.C., Hung W.C.
      J. Biol. Chem. 281:4718-4725(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-453 AND THR-739, FUNCTION.
    27. "Sumoylation inhibits cleavage of Sp1 N-terminal negative regulatory domain and inhibits Sp1-dependent transcription."
      Spengler M.L., Brattain M.G.
      J. Biol. Chem. 281:5567-5574(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-16, PROTEOLYTIC PROCESSING, MUTAGENESIS OF LYS-16; GLU-18 AND LYS-19.
    28. "Increased chromatin association of Sp1 in interphase cells by PP2A-mediated dephosphorylations."
      Vicart A., Lefebvre T., Imbert J., Fernandez A., Kahn-Perles B.
      J. Mol. Biol. 364:897-908(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-59 AND THR-681, DEPHOSPHORYLATION, GLYCOSYLATION, FUNCTION, MUTAGENESIS OF SER-59; SER-220; THR-355; THR-453; THR-651; THR-681 AND THR-739.
    29. "Sp1 deacetylation induced by phorbol ester recruits p300 to activate 12(S)-lipoxygenase gene transcription."
      Hung J.J., Wang Y.T., Chang W.C.
      Mol. Cell. Biol. 26:1770-1785(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-703, INTERACTION WITH HDAC1; EP300 AND JUN, FUNCTION, MUTAGENESIS OF LYS-703.
    30. "Phosphatidylinositol 3-kinase/protein kinase Czeta-induced phosphorylation of Sp1 and p107 repressor release have a critical role in histone deacetylase inhibitor-mediated derepression of transcription of the luteinizing hormone receptor gene."
      Zhang Y., Liao M., Dufau M.L.
      Mol. Cell. Biol. 26:6748-6761(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-641, FUNCTION, MUTAGENESIS OF SER-641.
    31. Erratum
      Zhang Y., Liao M., Dufau M.L.
      Mol. Cell. Biol. 26:8214-8214(2006)
    32. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    33. "Phosphorylation of Sp1 in response to DNA damage by ataxia telangiectasia-mutated kinase."
      Olofsson B.A., Kelly C.M., Kim J., Hornsby S.M., Azizkhan-Clifford J.
      Mol. Cancer Res. 5:1319-1330(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-101, FUNCTION, MUTAGENESIS OF SER-101.
    34. Cited for: GLYCOSYLATION, FUNCTION, MUTAGENESIS OF SER-612; THR-640; SER-641; SER-698 AND SER-702.
    35. "Phosphorylation mediates Sp1 coupled activities of proteolytic processing, desumoylation and degradation."
      Spengler M.L., Guo L.W., Brattain M.G.
      Cell Cycle 7:623-630(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-7 AND SER-59, SUMOYLATION AT LYS-16, PROTEOLYTIC PROCESSING, UBIQUITINATION, FUNCTION, MUTAGENESIS OF SER-7; SER-59; SER-728 AND SER-732.
    36. "Identification of phosphorylation sites on transcription factor Sp1 in response to DNA damage and its accumulation at damaged sites."
      Iwahori S., Yasui Y., Kudoh A., Sato Y., Nakayama S., Murata T., Isomura H., Tsurumi T.
      Cell. Signal. 20:1795-1803(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-101, FUNCTION, MUTAGENESIS OF SER-36; SER-56; SER-81; SER-85; THR-98; SER-101; THR-250; SER-281; SER-291; SER-296; SER-313; SER-351; THR-394; THR-427 AND SER-431.
    37. "Angiotensin II-inducible platelet-derived growth factor-D transcription requires specific Ser/Thr residues in the second zinc finger region of Sp1."
      Tan N.Y., Midgley V.C., Kavurma M.M., Santiago F.S., Luo X., Peden R., Fahmy R.G., Berndt M.C., Molloy M.P., Khachigian L.M.
      Circ. Res. 102:38-51(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-668; SER-670 AND THR-681, MUTAGENESIS OF THR-668; SER-670 AND THR-681.
    38. "Phosphorylation by c-Jun NH2-terminal kinase 1 regulates the stability of transcription factor Sp1 during mitosis."
      Chuang J.-Y., Wang Y.-T., Yeh S.-H., Liu Y.-W., Chang W.-C., Hung J.-J.
      Mol. Biol. Cell 19:1139-1151(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-59 AND THR-278, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-59; SER-73; THR-117; THR-278 AND THR-739.
    39. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-651, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    40. "O-GlcNAc inhibits interaction between Sp1 and Elf-1 transcription factors."
      Lim K., Chang H.I.
      Biochem. Biophys. Res. Commun. 380:569-574(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION, INTERACTION WITH ELF1.
    41. "O-GlcNAcylation of Sp1 interrupts Sp1 interaction with NF-Y."
      Lim K., Chang H.I.
      Biochem. Biophys. Res. Commun. 382:593-597(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION, INTERACTION WITH NFYA.
    42. "MCAF1/AM is involved in Sp1-mediated maintenance of cancer-associated telomerase activity."
      Liu L., Ishihara K., Ichimura T., Fujita N., Hino S., Tomita S., Watanabe S., Saitoh N., Ito T., Nakao M.
      J. Biol. Chem. 284:5165-5174(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ATF7IP AND TBP.
    43. "O-linked N-acetylglucosaminylation of Sp1 inhibits the human immunodeficiency virus type 1 promoter."
      Jochmann R., Thurau M., Jung S., Hofmann C., Naschberger E., Kremmer E., Harrer T., Miller M., Schaft N., Stuerzl M.
      J. Virol. 83:3704-3718(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION, FUNCTION.
    44. Cited for: INTERACTION WITH BAHD1.
    45. "Snail associates with EGR-1 and SP-1 to upregulate transcriptional activation of p15INK4b."
      Hu C.T., Chang T.Y., Cheng C.C., Liu C.S., Wu J.R., Li M.C., Wu W.S.
      FEBS J. 277:1202-1218(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EGR1.
    46. "Transcriptional regulation of human FE65, a ligand of Alzheimer's disease amyloid precursor protein, by Sp1."
      Yu H.T., Chan W.W., Chai K.H., Lee C.W., Chang R.C., Yu M.S., McLoughlin D.M., Miller C.C., Lau K.F.
      J. Cell. Biochem. 109:782-793(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    47. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-7, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    48. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    49. "Transforming growth factor-beta-inducible early response gene 1 is a novel substrate for atypical protein kinase Cs."
      Alemu E.A., Sjoettem E., Outzen H., Larsen K.B., Holm T., Bjoerkoey G., Johansen T.
      Cell. Mol. Life Sci. 68:1953-1968(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-702.
    50. "Cooperative transcriptional activation by Klf4, Meis2, and Pbx1."
      Bjerke G.A., Hyman-Walsh C., Wotton D.
      Mol. Cell. Biol. 31:3723-3733(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MEIS2 AND PBX1.
    51. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    52. "Structures of zinc finger domains from transcription factor Sp1. Insights into sequence-specific protein-DNA recognition."
      Narayan V.A., Kriwacki R.W., Caradonna J.P.
      J. Biol. Chem. 272:7801-7809(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 654-684 AND 684-712.

    Entry informationi

    Entry nameiSP1_HUMAN
    AccessioniPrimary (citable) accession number: P08047
    Secondary accession number(s): E4Z9M7
    , G5E9M8, Q86TN8, Q9H3Q5, Q9NR51, Q9NY21, Q9NYE7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: April 27, 2001
    Last modified: October 1, 2014
    This is version 184 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny 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

    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.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3