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Protein

Transcription factor Sp1

Gene

SP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri626 – 650C2H2-type 1PROSITE-ProRule annotationAdd BLAST25
Zinc fingeri656 – 680C2H2-type 2PROSITE-ProRule annotationAdd BLAST25
Zinc fingeri686 – 708C2H2-type 3PROSITE-ProRule annotationAdd BLAST23

GO - Molecular functioni

  • bHLH transcription factor binding Source: BHF-UCL
  • core promoter sequence-specific DNA binding Source: UniProtKB
  • DNA binding Source: UniProtKB
  • double-stranded DNA binding Source: BHF-UCL
  • histone deacetylase binding Source: BHF-UCL
  • HMG box domain binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • protein C-terminus binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: BHF-UCL
  • RNA polymerase II regulatory region sequence-specific DNA binding Source: UniProtKB
  • RNA polymerase II repressing transcription factor binding Source: BHF-UCL
  • sequence-specific DNA binding Source: HGNC
  • transcription factor activity, RNA polymerase II core promoter proximal region sequence-specific binding Source: BHF-UCL
  • transcription factor activity, sequence-specific DNA binding Source: UniProtKB
  • transcription factor binding Source: UniProtKB
  • transcription regulatory region DNA binding Source: BHF-UCL

GO - Biological processi

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

BioCyciZFISH:ENSG00000181170-MONOMER.
ReactomeiR-HSA-1989781. PPARA activates gene expression.
R-HSA-2173796. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
R-HSA-2426168. Activation of gene expression by SREBF (SREBP).
R-HSA-2559585. Oncogene Induced Senescence.
R-HSA-6807505. RNA polymerase II transcribes snRNA genes.
SignaLinkiP08047.
SIGNORiP08047.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor Sp1
Gene namesi
Name:SP1
Synonyms:TSFP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: 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

  • cytoplasm Source: UniProtKB-SubCell
  • nuclear chromatin Source: BHF-UCL
  • nucleoplasm Source: ParkinsonsUK-UCL
  • nucleus Source: UniProtKB
  • protein-DNA complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi7S → A: Increase in protein stability. No change in sumoylation. 1 Publication1
Mutagenesisi15V → R: Enhanced transcriptional activity. 1
Mutagenesisi16K → R: Loss of sumoylation. No cleavage and reduced transcriptional activity. 1 Publication1
Mutagenesisi18E → A: Loss of sumoylation. Increased cleavage and enhanced transcriptional activity. 1 Publication1
Mutagenesisi19K → R: No effect on sumoylation nor on proteolytic cleavage. 1 Publication1
Mutagenesisi36S → A: No effect on phosphorylation on DNA damage. 1 Publication1
Mutagenesisi56S → A: No effect on phosphorylation on DNA damage. 1 Publication1
Mutagenesisi59S → A: Loss of phosphorylation. No effect on activated MAPK8-mediated phosphorylation. Similar loss of phosphorylation as by dephosphorylation by PP2AC. Reduced proteolytic processing. 3 Publications1
Mutagenesisi59S → E: Some association with chromatin, increased phosphorylation levels and decreased glycosylation. 3 Publications1
Mutagenesisi73S → A: Little effect on activated MAPK8-mediated phosphorylation. 1 Publication1
Mutagenesisi81S → A: No effect on phosphorylation on DNA damage. 1 Publication1
Mutagenesisi85S → A: No effect on phosphorylation on DNA damage. 1 Publication1
Mutagenesisi98T → A: No effect on phosphorylation on DNA damage. 1 Publication1
Mutagenesisi101S → A: Significant reduction of phosphorylation on DNA damage. 2 Publications1
Mutagenesisi101S → D: Increase in phosphorylation on DNA damage. 2 Publications1
Mutagenesisi117T → A: No effect on activated MAPK8-mediated phosphorylation. 1 Publication1
Mutagenesisi220S → A: No effect on dephosphorylation by PP2A. 1 Publication1
Mutagenesisi250T → A: No effect on phosphorylation on DNA damage. 1 Publication1
Mutagenesisi278T → 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 Publication1
Mutagenesisi278T → D: Increased protein stability during mitosis; when associated with D-739. 1 Publication1
Mutagenesisi281S → A: No effect on phosphorylation on DNA damage. 1 Publication1
Mutagenesisi291S → A: No effect on phosphorylation on DNA damage. 1 Publication1
Mutagenesisi296S → A: No effect on phosphorylation on DNA damage. 1 Publication1
Mutagenesisi313S → A: No effect on phosphorylation on DNA damage. 1 Publication1
Mutagenesisi351S → A: No effect on phosphorylation on DNA damage. 1 Publication1
Mutagenesisi355T → A: No effect on dephosphorylation by PP2A. 2 Publications1
Mutagenesisi394T → A: No effect on phosphorylation on DNA damage. 1 Publication1
Mutagenesisi427T → A: No effect on phosphorylation on DNA damage. 1 Publication1
Mutagenesisi431S → A: No effect on phosphorylation on DNA damage. 1 Publication1
Mutagenesisi453T → 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 Publications1
Mutagenesisi491S → A: Loss of O-glycosylation. Increase in transcriptional activity. 2 Publications1
Mutagenesisi612S → A: Diminished glycosylation. Inhibits transcriptional activity; when associated with A-640; A-641; A-698 and A-702. 1 Publication1
Mutagenesisi640T → A: Diminished glycosylation. Inhibits transcriptional activity; when associated with A-612; A-641; A-698 and A-702. 1 Publication1
Mutagenesisi641S → A: Abolishes PRKCzeta-mediated phosphorylation. Diminished glycosylation. Inhibits transcriptional activity; when associated with A-612; A-640; A-641 and A-702. 2 Publications1
Mutagenesisi651T → A: No effect on dephosphorylation by PP2A. 1 Publication1
Mutagenesisi668T → A: Abolishes PRKCzeta-mediated but not PKCdelta-mediated phosphorylation. No effect on DNA binding; when associated with A-670 and A-681. 1 Publication1
Mutagenesisi670S → A: Abolishes PRKCzeta-mediated but not PKCdelta-mediated phosphorylation. No effect on DNA binding; when associated with A-668 and A-681. 1 Publication1
Mutagenesisi681T → 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 Publications1
Mutagenesisi698S → A: Diminished glycosylation. Inhibits transcriptional activity; when associated with A-612; A-640; A-641 and A-702. 1 Publication1
Mutagenesisi702S → A: Diminished glycosylation. Inhibits transcriptional activity; when associated with A-612; A-640; A-641 and A-698. 1 Publication1
Mutagenesisi703K → A: Abolishes acetylation. Increases recruitment of p300 to the promoter and enhances gene transcription. 1 Publication1
Mutagenesisi728S → A: Exhibits attenuated endoproteolytic cleavage; when associated with A-732. 1 Publication1
Mutagenesisi732S → A: Exhibits attenuated endoproteolytic cleavage; when associated with A-728. 1 Publication1
Mutagenesisi739T → 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 Publications1
Mutagenesisi739T → D: Increased protein stability during mitosis; when associated with D-278. 4 Publications1

Organism-specific databases

DisGeNETi6667.
OpenTargetsiENSG00000185591.
PharmGKBiPA36042.

Chemistry databases

ChEMBLiCHEMBL6103.

Polymorphism and mutation databases

BioMutaiSP1.
DMDMi13638437.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000471372 – 785Transcription factor Sp1Add BLAST784

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei2PhosphoserineCombined sources1
Modified residuei7PhosphoserineCombined sources1 Publication1
Cross-linki16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Cross-linki16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei59PhosphoserineCombined sources3 Publications1
Modified residuei101Phosphoserine; by ATM2 Publications1
Modified residuei278Phosphothreonine; by MAPK81 Publication1
Modified residuei453Phosphothreonine; by MAPK1 AND MAPK33 Publications1
Glycosylationi491O-linked (GlcNAc)2 Publications1
Modified residuei612Phosphoserine; alternate1 Publication1
Glycosylationi612O-linked (GlcNAc); alternate1 Publication1
Modified residuei640Phosphothreonine; alternate1 Publication1
Glycosylationi640O-linked (GlcNAc); alternate1 Publication1
Modified residuei641Phosphoserine; by PKC/PRKCZ; alternate1 Publication1
Glycosylationi641O-linked (GlcNAc); alternate1 Publication1
Modified residuei651Phosphothreonine; by PKC/PRKCZCombined sources1
Modified residuei668Phosphothreonine1 Publication1
Modified residuei670Phosphoserine; by PKC/PRKCZ1 Publication1
Modified residuei681Phosphothreonine; by PKC/PRKCZ2 Publications1
Glycosylationi698O-linked (GlcNAc)1 Publication1
Modified residuei702Phosphoserine; alternate1 Publication1
Glycosylationi702O-linked (GlcNAc); alternate1 Publication1
Modified residuei703N6-acetyllysine1 Publication1
Modified residuei739Phosphothreonine; by MAPK1, MAPK3 AND MAPK83 Publications1

Post-translational modificationi

Phosphorylated on multiple serine and threonine residues. Phosphorylation is coupled to ubiquitination, sumoylation and proteolytic processing. Phosphorylation on Ser-59 enhances proteolytic cleavage. Phosphorylation on Ser-7 enhances ubiquitination and protein degradation. Hyperphosphorylation on Ser-101 in response to DNA damage has no effect on transcriptional activity. MAPK1/MAPK3-mediated phosphorylation on Thr-453 and Thr-739 enhances VEGF transcription but, represses FGF2-triggered PDGFR-alpha transcription. Also implicated in the repression of RECK by ERBB2. Hyperphosphorylated on Thr-278 and Thr-739 during mitosis by MAPK8 shielding SP1 from degradation by the ubiquitin-dependent pathway. Phosphorylated in the zinc-finger domain by calmodulin-activated PKCzeta. Phosphorylation on Ser-641 by PKCzeta is critical for TSA-activated LHR gene expression through release of its repressor, p107. Phosphorylation on Thr-668, Ser-670 and Thr-681 is stimulated by angiotensin II via the AT1 receptor inducing increased binding to the PDGF-D promoter. This phosphorylation is increased in injured artey wall. Ser-59 and Thr-681 can both be dephosphorylated by PP2A during cell-cycle interphase. Dephosphorylation on Ser-59 leads to increased chromatin association during interphase and increases the transcriptional activity. On insulin stimulation, sequentially glycosylated and phosphorylated on several C-terminal serine and threonine residues.11 Publications
Acetylated. Acetylation/deacetylation events affect transcriptional activity. Deacetylation leads to an increase in the expression the 12(s)-lipooxygenase gene though recruitment of p300 to the promoter.1 Publication
Ubiquitinated. Ubiquitination occurs on the C-terminal proteolytically-cleaved peptide and is triggered by phosphorylation.1 Publication
Sumoylated with SUMO1. Sumoylation modulates proteolytic cleavage of the N-terminal repressor domain. Sumoylation levels are attenuated during tumorigenesis. Phosphorylation mediates SP1 desumoylation.
Proteolytic cleavage in the N-terminal repressor domain is prevented by sumoylation. The C-terminal cleaved product is susceptible to degradation.
O-glycosylated; Contains 8 N-acetylglucosamine side chains. Levels are controlled by insulin and the SP1 phosphorylation states. Insulin-mediated O-glycosylation locates SP1 to the nucleus, where it is sequentially deglycosylated and phosphorylated. O-glycosylation affects transcriptional activity through disrupting the interaction with a number of transcription factors including ELF1 and NFYA. Also inhibits interaction with the HIV1 promoter. Inhibited by peroxisomome proliferator receptor gamma (PPARgamma).

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei63 – 64CleavageCurated2

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP08047.
MaxQBiP08047.
PaxDbiP08047.
PeptideAtlasiP08047.
PRIDEiP08047.

PTM databases

iPTMnetiP08047.
PhosphoSitePlusiP08047.
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

BgeeiENSG00000185591.
CleanExiHS_SP1.
ExpressionAtlasiP08047. baseline and differential.
GenevisibleiP08047. HS.

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
AATFQ9NY612EBI-298336,EBI-372428
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
STAT3P407634EBI-298336,EBI-518675
ZBTB2Q8N6804EBI-298336,EBI-2515601

GO - Molecular functioni

  • bHLH transcription factor binding Source: BHF-UCL
  • histone deacetylase binding Source: BHF-UCL
  • HMG box domain binding Source: UniProtKB
  • protein C-terminus binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • RNA polymerase II repressing transcription factor binding Source: BHF-UCL
  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi112550. 229 interactors.
DIPiDIP-36N.
IntActiP08047. 66 interactors.
MINTiMINT-98326.
STRINGi9606.ENSP00000329357.

Structurei

Secondary structure

1785
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi620 – 622Combined sources3
Beta strandi636 – 638Combined sources3
Helixi640 – 651Combined sources12
Turni661 – 663Combined sources3
Beta strandi666 – 668Combined sources3
Helixi670 – 677Combined sources8
Turni678 – 680Combined sources3
Turni689 – 692Combined sources4
Helixi699 – 706Combined sources8
Helixi707 – 709Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SP1NMR-A684-712[»]
1SP2NMR-A654-684[»]
1VA1NMR-A619-654[»]
1VA2NMR-A654-684[»]
1VA3NMR-A684-712[»]
DisProtiDP00378.
ProteinModelPortaliP08047.
SMRiP08047.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08047.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 82Repressor domainAdd BLAST81
Regioni146 – 251Transactivation domain A (Gln-rich)Add BLAST106
Regioni261 – 495Transactivation domain B (Gln-rich)Add BLAST235
Regioni496 – 610Transactivation domain C (highly charged)Add BLAST115
Regioni619 – 785VZV IE62-bindingAdd BLAST167
Regioni708 – 785Domain DAdd BLAST78

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi36 – 143Ser/Thr-richAdd BLAST108
Compositional biasi271 – 379Ser/Thr-richAdd BLAST109

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri626 – 650C2H2-type 1PROSITE-ProRule annotationAdd BLAST25
Zinc fingeri656 – 680C2H2-type 2PROSITE-ProRule annotationAdd BLAST25
Zinc fingeri686 – 708C2H2-type 3PROSITE-ProRule annotationAdd BLAST23

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00760000118984.
HOGENOMiHOG000234295.
HOVERGENiHBG008933.
InParanoidiP08047.
KOiK04684.
OMAiGWQIISS.
OrthoDBiEOG091G0HX6.
PhylomeDBiP08047.
TreeFamiTF350150.

Family and domain databases

Gene3Di3.30.160.60. 3 hits.
InterProiIPR030450. Sp1_fam.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PANTHERiPTHR23235. PTHR23235. 1 hit.
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. AlignAdd to basket

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

        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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti366D → G AA sequence (PubMed:3319186).Curated1
Sequence conflicti670S → F AA sequence (PubMed:3319186).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_019971737T → A.Corresponds to variant rs3741665dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0539341 – 7Missing in isoform 2. Curated7
Alternative sequenceiVSP_05393554 – 101Missing in isoform 3. 1 PublicationAdd BLAST48

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FN908228 mRNA. Translation: CBM42955.1.
AC068889 Genomic DNA. No translation available.
AC073611 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW96699.1.
BC043224 mRNA. Translation: AAH43224.1. Different initiation.
BC062539 mRNA. Translation: AAH62539.1.
AF252284 mRNA. Translation: AAF67726.1.
AB039286 Genomic DNA. Translation: BAB13476.1.
J03133 mRNA. Translation: AAA61154.1.
AF255682 mRNA. Translation: AAF78781.1.
AJ272134 mRNA. Translation: CAB75345.1.
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]
XP_011536998.1. XM_011538696.2. [P08047-2]
UniGeneiHs.620754.
Hs.649191.

Genome annotation databases

EnsembliENST00000327443; ENSP00000329357; ENSG00000185591. [P08047-1]
ENST00000426431; ENSP00000404263; ENSG00000185591. [P08047-2]
GeneIDi6667.
KEGGihsa:6667.
UCSCiuc001scw.4. human. [P08047-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FN908228 mRNA. Translation: CBM42955.1.
AC068889 Genomic DNA. No translation available.
AC073611 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW96699.1.
BC043224 mRNA. Translation: AAH43224.1. Different initiation.
BC062539 mRNA. Translation: AAH62539.1.
AF252284 mRNA. Translation: AAF67726.1.
AB039286 Genomic DNA. Translation: BAB13476.1.
J03133 mRNA. Translation: AAA61154.1.
AF255682 mRNA. Translation: AAF78781.1.
AJ272134 mRNA. Translation: CAB75345.1.
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]
XP_011536998.1. XM_011538696.2. [P08047-2]
UniGeneiHs.620754.
Hs.649191.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SP1NMR-A684-712[»]
1SP2NMR-A654-684[»]
1VA1NMR-A619-654[»]
1VA2NMR-A654-684[»]
1VA3NMR-A684-712[»]
DisProtiDP00378.
ProteinModelPortaliP08047.
SMRiP08047.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112550. 229 interactors.
DIPiDIP-36N.
IntActiP08047. 66 interactors.
MINTiMINT-98326.
STRINGi9606.ENSP00000329357.

Chemistry databases

ChEMBLiCHEMBL6103.

PTM databases

iPTMnetiP08047.
PhosphoSitePlusiP08047.
UniCarbKBiP08047.

Polymorphism and mutation databases

BioMutaiSP1.
DMDMi13638437.

Proteomic databases

EPDiP08047.
MaxQBiP08047.
PaxDbiP08047.
PeptideAtlasiP08047.
PRIDEiP08047.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000327443; ENSP00000329357; ENSG00000185591. [P08047-1]
ENST00000426431; ENSP00000404263; ENSG00000185591. [P08047-2]
GeneIDi6667.
KEGGihsa:6667.
UCSCiuc001scw.4. human. [P08047-1]

Organism-specific databases

CTDi6667.
DisGeNETi6667.
GeneCardsiSP1.
HGNCiHGNC:11205. SP1.
HPAiCAB000330.
HPA001853.
HPA012292.
MIMi189906. gene.
neXtProtiNX_P08047.
OpenTargetsiENSG00000185591.
PharmGKBiPA36042.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00760000118984.
HOGENOMiHOG000234295.
HOVERGENiHBG008933.
InParanoidiP08047.
KOiK04684.
OMAiGWQIISS.
OrthoDBiEOG091G0HX6.
PhylomeDBiP08047.
TreeFamiTF350150.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000181170-MONOMER.
ReactomeiR-HSA-1989781. PPARA activates gene expression.
R-HSA-2173796. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
R-HSA-2426168. Activation of gene expression by SREBF (SREBP).
R-HSA-2559585. Oncogene Induced Senescence.
R-HSA-6807505. RNA polymerase II transcribes snRNA genes.
SignaLinkiP08047.
SIGNORiP08047.

Miscellaneous databases

ChiTaRSiSP1. human.
EvolutionaryTraceiP08047.
GeneWikiiSp1_transcription_factor.
GenomeRNAii6667.
PMAP-CutDBP08047.
PROiP08047.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000185591.
CleanExiHS_SP1.
ExpressionAtlasiP08047. baseline and differential.
GenevisibleiP08047. HS.

Family and domain databases

Gene3Di3.30.160.60. 3 hits.
InterProiIPR030450. Sp1_fam.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PANTHERiPTHR23235. PTHR23235. 1 hit.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 209 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.