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P08047

- SP1_HUMAN

UniProt

P08047 - SP1_HUMAN

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Protein

Transcription factor Sp1

Gene

SP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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 C-terminus binding Source: UniProtKB
  10. protein homodimerization activity Source: UniProtKB
  11. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: BHF-UCL
  12. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: Ensembl
  13. RNA polymerase II core promoter sequence-specific DNA binding Source: Ensembl
  14. RNA polymerase II repressing transcription factor binding Source: BHF-UCL
  15. sequence-specific DNA binding Source: HGNC
  16. sequence-specific DNA binding transcription factor activity Source: UniProtKB
  17. transcription factor binding Source: UniProtKB
  18. 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. rhythmic process Source: UniProtKB-KW
  18. small molecule metabolic process Source: Reactome
  19. transcription, DNA-templated Source: Reactome
  20. transcription initiation from RNA polymerase II promoter Source: Reactome
  21. transforming growth factor beta receptor signaling pathway Source: Reactome
  22. trophectodermal cell differentiation Source: Ensembl
  23. viral process Source: UniProtKB-KW
Complete GO annotation...

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-KW
  2. nucleoplasm Source: Reactome
  3. nucleus Source: UniProtKB
  4. protein-DNA complex Source: Ensembl
Complete GO annotation...

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 – 21Phosphoserine1 Publication
Modified residuei7 – 71Phosphoserine3 Publications
Cross-linki16 – 16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei59 – 591Phosphoserine4 Publications
Modified residuei101 – 1011Phosphoserine; by ATM2 Publications
Modified residuei278 – 2781Phosphothreonine; by MAPK81 Publication
Modified residuei453 – 4531Phosphothreonine; by MAPK1 AND MAPK33 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; alternate1 Publication
Glycosylationi641 – 6411O-linked (GlcNAc); alternate1 Publication
Modified residuei651 – 6511Phosphothreonine; by PKC/PRKCZ1 Publication
Modified residuei668 – 6681Phosphothreonine1 Publication
Modified residuei670 – 6701Phosphoserine; by PKC/PRKCZ1 Publication
Modified residuei681 – 6811Phosphothreonine; by PKC/PRKCZ2 Publications
Glycosylationi698 – 6981O-linked (GlcNAc)1 Publication
Modified residuei702 – 7021Phosphoserine; alternate1 Publication
Glycosylationi702 – 7021O-linked (GlcNAc); alternate1 Publication
Modified residuei703 – 7031N6-acetyllysine1 Publication
Modified residuei739 – 7391Phosphothreonine; by MAPK1, MAPK3 AND MAPK83 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

BgeeiP08047.
CleanExiHS_SP1.
ExpressionAtlasiP08047. baseline and differential.
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.
GeneTreeiENSGT00760000118984.
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) [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

        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
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.
GeneTreei ENSGT00760000118984.
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

Bgeei P08047.
CleanExi HS_SP1.
ExpressionAtlasi P08047. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 185 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