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UniProtKB - O89090 (SP1_MOUSE)

Protein

Transcription factor Sp1

Gene

Sp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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 (By similarity). Positively regulates the transcription of the core clock component ARNTL/BMAL1 (PubMed:24030830). Plays a role in protecting cells against oxidative stress following brain injury by regulating the expression of RNF112 (PubMed:27918959).By similarity2 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri627 – 656C2H2-type 1PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri657 – 686C2H2-type 2PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri687 – 714C2H2-type 3PROSITE-ProRule annotationAdd BLAST28

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionActivator, DNA-binding, Repressor
Biological processBiological rhythms, Transcription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-2173796 SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription
R-MMU-6807505 RNA polymerase II transcribes snRNA genes
R-MMU-9018519 Estrogen-dependent gene expression

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor Sp1
Alternative name(s):
Specificity protein 11 Publication
Gene namesi
Name:Sp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:98372 Sp1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000471382 – 784Transcription factor Sp1Add BLAST783

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei2PhosphoserineBy similarity1
Modified residuei7PhosphoserineBy similarity1
Cross-linki16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei61PhosphoserineCombined sources1
Modified residuei103Phosphoserine; by ATMBy similarity1
Modified residuei280Phosphothreonine; by MAPK8By similarity1
Modified residuei455Phosphothreonine; by MAPK1 and MAPK3By similarity1
Glycosylationi493O-linked (GlcNAc) serineBy similarity1
Modified residuei613Phosphoserine; alternateBy similarity1
Glycosylationi613O-linked (GlcNAc) serine; alternateBy similarity1
Modified residuei641Phosphothreonine; alternateBy similarity1
Glycosylationi641O-linked (GlcNAc) threonine; alternateBy similarity1
Modified residuei642Phosphoserine; by PKC/PRKCZ; alternateBy similarity1
Glycosylationi642O-linked (GlcNAc) serine; alternateBy similarity1
Modified residuei652Phosphothreonine; by PKC/PRKCZBy similarity1
Modified residuei669PhosphothreonineBy similarity1
Modified residuei671Phosphoserine; by PKC/PRKCZBy similarity1
Modified residuei682Phosphothreonine; by PKC/PRKCZBy similarity1
Modified residuei699Phosphoserine; alternateBy similarity1
Glycosylationi699O-linked (GlcNAc) serine; alternateBy similarity1
Modified residuei703Phosphoserine; alternateBy similarity1
Glycosylationi703O-linked (GlcNAc) serine; alternateBy similarity1
Modified residuei704N6-acetyllysineBy similarity1
Modified residuei738Phosphothreonine; by MAPK1, MAPK3 and MAPK8By similarity1

Post-translational modificationi

Phosphorylated on multiple serine and threonine residues. Phosphorylation is coupled to ubiquitination, sumoylation and proteolytic processing. Phosphorylation on Ser-61 enhances proteolytic cleavage. Phosphorylation on Ser-7 enhances ubiquitination and protein degradation. Hyperphosphorylation on Ser-103 in response to DNA damage has no effect on transcriptional activity. MAPK1/MAPK3-mediated phosphorylation on Thr-455 and Thr-738 enhances VEGF transcription but, represses FGF2-triggered PDGFR-alpha transcription. Also implicated in the repression of RECK by ERBB2. Hyperphosphorylated on Thr-280 and Thr-738 during mitosis by MAPK8 shielding SP1 from degradation by the ubiquitin-dependent pathway. Phosphorylated in the zinc-finger domain by calmodulin-activated PKCzeta. Phosphorylation on Ser-642 by PKCzeta is critical for TSA-activated LHR gene expression through release of its repressor, p107. Phosphorylation on Thr-669, Ser-671 and Thr-682 is stimulated by angiotensin II via the AT1 receptor inducing increased binding to the PDGF-D promoter. This phosphorylation is increased in injured artey wall. Ser-61 and Thr-682 can both be dephosphorylated by PP2A during cell-cycle interphase. Dephosphorylation on Ser-61 leads to increased chromatin association during interphase and increases the transcriptional activity. On insulin stimulation, sequentially glycosylated and phosphorylated on several C-terminal serine and threonine residues (By similarity).By similarity
Acetylated. Acetylation/deacetylation events affect transcriptional activity. Deacetylation leads to an increase in the expression the 12(s)-lipooxygenase gene though recruitment of p300 to the promoter (By similarity).By similarity
Ubiquitinated. Ubiquitination occurs on the C-terminal proteolytically-cleaved peptide and is triggered by phosphorylation (By similarity).By similarity
Sumoylated with SUMO1. Sumoylation modulates proteolytic cleavage of the N-terminal repressor domain. Sumoylation levels are attenuated during tumorigenesis. Phosphorylation mediates SP1 desumoylation (By similarity).By similarity
Proteolytic cleavage in the N-terminal repressor domain is prevented by sumoylation. The C-terminal cleaved product is susceptible to degradation (By similarity).By similarity
O-glycosylated; Contains 8 N-acetylglucosamine side chains. Levels are controlled by insulin and the SP1 phosphorylation states. Insulin-mediated O-glycosylation locates SP1 to the nucleus, where it is sequentially deglycosylated and phosphorylated. O-glycosylation affects transcriptional activity through disrupting the interaction with a number of transcription factors including ELF1 and NFYA. Inhibited by peroxisomome proliferator receptor gamma (PPARgamma) (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei65 – 66CleavageBy similarity2

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO89090
MaxQBiO89090
PaxDbiO89090
PeptideAtlasiO89090
PRIDEiO89090

PTM databases

iPTMnetiO89090
PhosphoSitePlusiO89090

Expressioni

Inductioni

Up-regulated by traumatic brain injury and hydrogen peroxide (at protein level)(PubMed:27918959).1 Publication

Gene expression databases

BgeeiENSMUSG00000001280 Expressed in 304 organ(s), highest expression level in rostral migratory stream
CleanExiMM_SP1
ExpressionAtlasiO89090 baseline and differential
GenevisibleiO89090 MM

Interactioni

Subunit structurei

Interacts with ATF7IP, ATF7IP2, BAHD1, POGZ, HCFC1, AATF and PHC2. Interacts with SV40 VP2/3 proteins. Interacts with SV40 major capsid protein VP1; this interaction leads to a cooperativity between the 2 proteins in DNA binding. Interacts with HLTF; the interaction may be required for basal transcriptional activity of HLTF. Interacts (deacetylated form) with EP300; the interaction enhances gene expression. Interacts with HDAC1 and JUN. Interacts with ELF1; the interaction is inhibited by glycosylation of SP1. Interaction with NFYA; the interaction is inhibited by glycosylation of SP1. Interacts with SMARCA4/BRG1. Interacts with ATF7IP and TBP. Interacts with MEIS2 isoform 4 and PBX1 isoform PBX1a. Interacts with EGR1 (By similarity). Interacts with RNF112 in an oxidative stress-regulated manner (PubMed:27918959). Interacts with ZBTB7A; ZBTB7A prevents the binding to GC-rich motifs in promoters and represses the transcriptional activity of SP1 (By similarity).By similarity1 Publication

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi203414, 28 interactors
CORUMiO89090
DIPiDIP-35276N
IntActiO89090, 10 interactors
MINTiO89090
STRINGi10090.ENSMUSP00000001326

Structurei

3D structure databases

ProteinModelPortaliO89090
SMRiO89090
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 84Repressor domainBy similarityAdd BLAST83
Regioni148 – 253Transactivation domain A (Gln-rich)By similarityAdd BLAST106
Regioni263 – 497Transactivation domain B (Gln-rich)By similarityAdd BLAST235
Regioni498 – 611Transactivation domain C (highly charged)By similarityAdd BLAST114
Regioni620 – 784VZV IE62-bindingBy similarityAdd BLAST165
Regioni709 – 784Domain DBy similarityAdd BLAST76

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi37 – 145Ser/Thr-richAdd BLAST109
Compositional biasi273 – 381Ser/Thr-richAdd BLAST109

Sequence similaritiesi

Belongs to the Sp1 C2H2-type zinc-finger protein family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri627 – 656C2H2-type 1PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri657 – 686C2H2-type 2PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri687 – 714C2H2-type 3PROSITE-ProRule annotationAdd BLAST28

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1721 Eukaryota
COG5048 LUCA
GeneTreeiENSGT00760000118984
HOGENOMiHOG000234295
HOVERGENiHBG008933
InParanoidiO89090
KOiK04684

Family and domain databases

InterProiView protein in InterPro
IPR030449 SP1
IPR036236 Znf_C2H2_sf
IPR013087 Znf_C2H2_type
PANTHERiPTHR23235:SF16 PTHR23235:SF16, 1 hit
PfamiView protein in Pfam
PF00096 zf-C2H2, 3 hits
SMARTiView protein in SMART
SM00355 ZnF_C2H2, 3 hits
SUPFAMiSSF57667 SSF57667, 1 hit
PROSITEiView protein in PROSITE
PS00028 ZINC_FINGER_C2H2_1, 3 hits
PS50157 ZINC_FINGER_C2H2_2, 3 hits

Sequences (2+)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: O89090-1) [UniParc]FASTAAdd to basket

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 VTAVVKIEKD VGGNNGGSGN GGGAAFSQTR SSSTGSSSSS 
        60         70         80         90        100
GGGGGQESQP SPLALLAATC SRIESPNENS NNSQGPSQSG GTGELDLTAT 
       110        120        130        140        150
QLSQGANGWQ IISSSSGATP TSKEQSGNST NGSNGSESSK NRTVSGGQYV 
       160        170        180        190        200
VAATPNLQNQ QVLTGLPGVM PNIQYQVIPQ FQTVDGQQLQ FAATGAQVQQ 
       210        220        230        240        250
DGSGQIQIIP GANQQIIPNR GSGGNIIAAM PNLLQQAVPL QGLANNVLSG 
       260        270        280        290        300
QTQYVTNVPV ALNGNITLLP VNSVSAATLT PSSQAGTISS SGSQESSSQP 
       310        320        330        340        350
VTSGTAISSA SLVSSQASSS SFFTNANSYS TTTTTSNMGI MNFTSSGSSG 
       360        370        380        390        400
TSSQGQTPQR VGGLQGSDSL NIQQNQTSGG SLQGSQQKEG EQSQQTQQQQ 
       410        420        430        440        450
ILIQPQLVQG GQALQALQAA PLSGQTFTTQ AISQETLQNL QLQAVQNSGP 
       460        470        480        490        500
IIIRTPTVGP NGQVSWQTLQ LQNLQVQNPQ AQTITLAPMQ GVSLGQTSSS 
       510        520        530        540        550
NTTLTPIASA ASIPAGTVTV NAAQLSSMPG LQTINLSALG TSGIQVHQLP 
       560        570        580        590        600
GLPLAIANTP GDHGTQLGLH GSGGDGIHDE TAGGEGENSS DLQPQAGRRT 
       610        620        630        640        650
RREACTCPYC KDSEGRASGD PGKKKQHICH IQGCGKVYGK TSHLRAHLRW 
       660        670        680        690        700
HTGERPFMCN WSYCGKRFTR SDELQRHKRT HTGEKKFACP ECPKRFMRSD 
       710        720        730        740        750
HLSKHIKTHQ NKKGGPGVAL SVGTLPLDSG AGSEGTATPS ALITTNMVAM 
       760        770        780 
EAICPEGIAR LANSGINVMQ VTELQSINIS GNGF
Length:784
Mass (Da):80,732
Last modified:June 21, 2005 - v2
Checksum:iB6B989F0A252CEE5
GO
Isoform 2 (identifier: O89090-2) [UniParc]FASTAAdd to basket
Also known as: Sp1-S

The sequence of this isoform differs from the canonical sequence as follows:
     56-372: Missing.

Show »
Length:467
Mass (Da):48,749
Checksum:i4A373D67E6128197
GO

Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G3X8Q0G3X8Q0_MOUSE
Trans-acting transcription factor 1
Sp1 mCG_17604
781Annotation score:
E9Q113E9Q113_MOUSE
Transcription factor Sp1
Sp1
183Annotation score:
E9Q2V3E9Q2V3_MOUSE
Transcription factor Sp1
Sp1
105Annotation score:
E9Q0S7E9Q0S7_MOUSE
Transcription factor Sp1
Sp1
55Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti100T → A in AAC16484 (PubMed:9628590).Curated1
Sequence conflicti131 – 133Missing in AAC16484 (PubMed:9628590).Curated3
Sequence conflicti220R → E in AAC08527 (Ref. 3) Curated1
Sequence conflicti462G → V in AAC16484 (PubMed:9628590).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_00737656 – 372Missing in isoform 2. 1 PublicationAdd BLAST317

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF062566 mRNA Translation: AAC16484.1
S79832 mRNA Translation: AAB35321.1
AF022363 mRNA Translation: AAC08527.1
X60136 Genomic DNA Translation: CAA42721.1
PIRiS30493
RefSeqiNP_038700.2, NM_013672.2
UniGeneiMm.4618

Genome annotation databases

EnsembliENSMUST00000163709; ENSMUSP00000130747; ENSMUSG00000001280 [O89090-2]
GeneIDi20683
KEGGimmu:20683
UCSCiuc012aab.1 mouse [O89090-2]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF062566 mRNA Translation: AAC16484.1
S79832 mRNA Translation: AAB35321.1
AF022363 mRNA Translation: AAC08527.1
X60136 Genomic DNA Translation: CAA42721.1
PIRiS30493
RefSeqiNP_038700.2, NM_013672.2
UniGeneiMm.4618

3D structure databases

ProteinModelPortaliO89090
SMRiO89090
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203414, 28 interactors
CORUMiO89090
DIPiDIP-35276N
IntActiO89090, 10 interactors
MINTiO89090
STRINGi10090.ENSMUSP00000001326

PTM databases

iPTMnetiO89090
PhosphoSitePlusiO89090

Proteomic databases

EPDiO89090
MaxQBiO89090
PaxDbiO89090
PeptideAtlasiO89090
PRIDEiO89090

Protocols and materials databases

DNASUi20683
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000163709; ENSMUSP00000130747; ENSMUSG00000001280 [O89090-2]
GeneIDi20683
KEGGimmu:20683
UCSCiuc012aab.1 mouse [O89090-2]

Organism-specific databases

CTDi6667
MGIiMGI:98372 Sp1

Phylogenomic databases

eggNOGiKOG1721 Eukaryota
COG5048 LUCA
GeneTreeiENSGT00760000118984
HOGENOMiHOG000234295
HOVERGENiHBG008933
InParanoidiO89090
KOiK04684

Enzyme and pathway databases

ReactomeiR-MMU-2173796 SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription
R-MMU-6807505 RNA polymerase II transcribes snRNA genes
R-MMU-9018519 Estrogen-dependent gene expression

Miscellaneous databases

PROiPR:O89090
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000001280 Expressed in 304 organ(s), highest expression level in rostral migratory stream
CleanExiMM_SP1
ExpressionAtlasiO89090 baseline and differential
GenevisibleiO89090 MM

Family and domain databases

InterProiView protein in InterPro
IPR030449 SP1
IPR036236 Znf_C2H2_sf
IPR013087 Znf_C2H2_type
PANTHERiPTHR23235:SF16 PTHR23235:SF16, 1 hit
PfamiView protein in Pfam
PF00096 zf-C2H2, 3 hits
SMARTiView protein in SMART
SM00355 ZnF_C2H2, 3 hits
SUPFAMiSSF57667 SSF57667, 1 hit
PROSITEiView protein in PROSITE
PS00028 ZINC_FINGER_C2H2_1, 3 hits
PS50157 ZINC_FINGER_C2H2_2, 3 hits
ProtoNetiSearch...

Entry informationi

Entry nameiSP1_MOUSE
AccessioniPrimary (citable) accession number: O89090
Secondary accession number(s): O89087, Q62251, Q64167
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: June 21, 2005
Last modified: October 10, 2018
This is version 167 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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