Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O89090 (SP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription factor Sp1
Gene names
Name:Sp1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length784 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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 4and PBX1 isoform PBX1a Interacts with EGR1 By similarity.

Subcellular location

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

Post-translational modification

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.

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.

Ubiquitinated. Ubiquitination occurs on the C-terminal proteolytically-cleaved peptide and is triggered by phosphorylation 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.

Proteolytic cleavage in the N-terminal repressor domain is prevented by sumoylation. The C-terminal cleaved product is susceptible to degradation 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.

Sequence similarities

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

Contains 3 C2H2-type zinc fingers.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionActivator
Repressor
   PTMAcetylation
Glycoprotein
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdefinitive hemopoiesis

Inferred from genetic interaction PubMed 17584888. Source: MGI

embryonic camera-type eye morphogenesis

Inferred from genetic interaction PubMed 17584888. Source: MGI

embryonic placenta development

Inferred from genetic interaction PubMed 17584888. Source: MGI

embryonic process involved in female pregnancy

Inferred from genetic interaction PubMed 17584888. Source: MGI

embryonic skeletal system development

Inferred from genetic interaction PubMed 17584888. Source: MGI

enucleate erythrocyte differentiation

Inferred from genetic interaction PubMed 17584888. Source: MGI

in utero embryonic development

Inferred from genetic interaction PubMed 17584888. Source: MGI

liver development

Inferred from genetic interaction PubMed 17584888. Source: MGI

lung development

Inferred from genetic interaction PubMed 17584888. Source: MGI

megakaryocyte differentiation

Inferred from genetic interaction PubMed 17584888. Source: MGI

ossification

Inferred from genetic interaction PubMed 17584888. Source: MGI

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 21029371. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 15282343PubMed 15589828. Source: MGI

regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 12119294. Source: MGI

trophectodermal cell differentiation

Inferred from genetic interaction PubMed 17584888. Source: MGI

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear chromatin

Inferred from direct assay PubMed 21029371. Source: BHF-UCL

nucleus

Inferred from direct assay PubMed 11004506PubMed 12119294PubMed 15016652PubMed 15282343PubMed 15817708PubMed 16141233PubMed 9705320. Source: MGI

   Molecular_functionDNA binding

Inferred from direct assay PubMed 11004506PubMed 12119294PubMed 14630713PubMed 14667815PubMed 15094381PubMed 15589828PubMed 16886906PubMed 8617793PubMed 9738004. Source: MGI

RNA polymerase II core promoter proximal region sequence-specific DNA binding

Inferred from direct assay PubMed 12657651PubMed 21029371. Source: BHF-UCL

RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription

Inferred from direct assay PubMed 19943855. Source: MGI

RNA polymerase II core promoter sequence-specific DNA binding

Inferred from direct assay PubMed 17670746. Source: MGI

RNA polymerase II repressing transcription factor binding

Inferred from physical interaction PubMed 12657651. Source: BHF-UCL

bHLH transcription factor binding

Inferred from physical interaction PubMed 12657651. Source: BHF-UCL

core promoter proximal region sequence-specific DNA binding

Inferred from direct assay PubMed 15511642PubMed 19943855. Source: MGI

double-stranded DNA binding

Inferred from direct assay PubMed 15282343. Source: MGI

enhancer binding

Inferred from direct assay PubMed 9705320. Source: MGI

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 15282343PubMed 1909605. Source: MGI

sequence-specific DNA binding

Inferred from direct assay PubMed 11071760. Source: MGI

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 1524678PubMed 15282343PubMed 15589828PubMed 7565748. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O89090-1)

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.
Isoform 2 (identifier: O89090-2)

Also known as: Sp1-S;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 784783Transcription factor Sp1
PRO_0000047138

Regions

Zinc finger627 – 65630C2H2-type 1
Zinc finger657 – 68630C2H2-type 2
Zinc finger687 – 71428C2H2-type 3
Region2 – 8483Repressor domain By similarity
Region148 – 253106Transactivation domain A (Gln-rich) By similarity
Region263 – 497235Transactivation domain B (Gln-rich) By similarity
Region498 – 611114Transactivation domain C (highly charged) By similarity
Region620 – 784165VZV IE62-binding By similarity
Region709 – 78476Domain D By similarity
Compositional bias37 – 145109Ser/Thr-rich
Compositional bias273 – 381109Ser/Thr-rich

Sites

Site65 – 662Cleavage By similarity

Amino acid modifications

Modified residue21N-acetylserine Ref.5
Modified residue21Phosphoserine By similarity
Modified residue71Phosphoserine By similarity
Modified residue611Phosphoserine By similarity
Modified residue1031Phosphoserine; by ATM By similarity
Modified residue2801Phosphothreonine; by MAPK8 By similarity
Modified residue4551Phosphothreonine; by MAPK1 AND MAPK3 By similarity
Modified residue6131Phosphoserine; alternate By similarity
Modified residue6411Phosphothreonine; alternate By similarity
Modified residue6421Phosphoserine; by PKC/PRKCZ; alternate By similarity
Modified residue6521Phosphothreonine; by PKC/PRKCZ By similarity
Modified residue6691Phosphothreonine By similarity
Modified residue6711Phosphoserine; by PKC/PRKCZ By similarity
Modified residue6821Phosphothreonine; by PKC/PRKCZ By similarity
Modified residue7031Phosphoserine; alternate By similarity
Modified residue7041N6-acetyllysine By similarity
Modified residue7381Phosphothreonine; by MAPK1, MAPK3 AND MAPK8 By similarity
Glycosylation4931O-linked (GlcNAc) By similarity
Glycosylation6131O-linked (GlcNAc); alternate By similarity
Glycosylation6411O-linked (GlcNAc); alternate By similarity
Glycosylation6421O-linked (GlcNAc); alternate By similarity
Glycosylation6991O-linked (GlcNAc) By similarity
Glycosylation7031O-linked (GlcNAc); alternate By similarity
Cross-link16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence56 – 372317Missing in isoform 2.
VSP_007376

Experimental info

Sequence conflict1001T → A in AAC16484. Ref.1
Sequence conflict131 – 1333Missing in AAC16484. Ref.1
Sequence conflict2201R → E in AAC08527. Ref.3
Sequence conflict4621G → V in AAC16484. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 21, 2005. Version 2.
Checksum: B6B989F0A252CEE5

FASTA78480,732
        10         20         30         40         50         60 
MSDQDHSMDE VTAVVKIEKD VGGNNGGSGN GGGAAFSQTR SSSTGSSSSS GGGGGQESQP 

        70         80         90        100        110        120 
SPLALLAATC SRIESPNENS NNSQGPSQSG GTGELDLTAT QLSQGANGWQ IISSSSGATP 

       130        140        150        160        170        180 
TSKEQSGNST NGSNGSESSK NRTVSGGQYV VAATPNLQNQ QVLTGLPGVM PNIQYQVIPQ 

       190        200        210        220        230        240 
FQTVDGQQLQ FAATGAQVQQ DGSGQIQIIP GANQQIIPNR GSGGNIIAAM PNLLQQAVPL 

       250        260        270        280        290        300 
QGLANNVLSG QTQYVTNVPV ALNGNITLLP VNSVSAATLT PSSQAGTISS SGSQESSSQP 

       310        320        330        340        350        360 
VTSGTAISSA SLVSSQASSS SFFTNANSYS TTTTTSNMGI MNFTSSGSSG TSSQGQTPQR 

       370        380        390        400        410        420 
VGGLQGSDSL NIQQNQTSGG SLQGSQQKEG EQSQQTQQQQ ILIQPQLVQG GQALQALQAA 

       430        440        450        460        470        480 
PLSGQTFTTQ AISQETLQNL QLQAVQNSGP IIIRTPTVGP NGQVSWQTLQ LQNLQVQNPQ 

       490        500        510        520        530        540 
AQTITLAPMQ GVSLGQTSSS NTTLTPIASA ASIPAGTVTV NAAQLSSMPG LQTINLSALG 

       550        560        570        580        590        600 
TSGIQVHQLP GLPLAIANTP GDHGTQLGLH GSGGDGIHDE TAGGEGENSS DLQPQAGRRT 

       610        620        630        640        650        660 
RREACTCPYC KDSEGRASGD PGKKKQHICH IQGCGKVYGK TSHLRAHLRW HTGERPFMCN 

       670        680        690        700        710        720 
WSYCGKRFTR SDELQRHKRT HTGEKKFACP ECPKRFMRSD HLSKHIKTHQ NKKGGPGVAL 

       730        740        750        760        770        780 
SVGTLPLDSG AGSEGTATPS ALITTNMVAM EAICPEGIAR LANSGINVMQ VTELQSINIS 


GNGF 

« Hide

Isoform 2 (Sp1-S) [UniParc].

Checksum: 4A373D67E6128197
Show »

FASTA46748,749

References

« Hide 'large scale' references
[1]"Sp family transcription factors regulate expression of rat D2 dopamine receptor gene."
Yajima S., Lee S.H., Minowa T., Mouradian M.M.
DNA Cell Biol. 17:471-479(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Neuroblastoma.
[2]"An alternatively spliced form of the transcription factor Sp1 containing only a single glutamine-rich transactivation domain."
Persengiev S.P., Saffer J.D., Kilpatrick D.L.
Proc. Natl. Acad. Sci. U.S.A. 92:9107-9111(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]"Isolation of cDNA encoding transcription factor sp1 containing two glutamine-rich transactivation domain."
Park E.J., Kim J.H., Kim C.G., Park S.D., Hong S.S.
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Thymus.
[4]"Difference in the genomic organizations of the related transcription factors Sp1 and Krox-20; possible evolutionary significance."
Chestier A., Charnay P.
DNA Seq. 2:325-327(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 684-784.
[5]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF062566 mRNA. Translation: AAC16484.1.
S79832 mRNA. Translation: AAB35321.1.
AF022363 mRNA. Translation: AAC08527.1.
X60136 Genomic DNA. Translation: CAA42721.1.
PIRS30493.
RefSeqNP_038700.2. NM_013672.2.
UniGeneMm.4618.

3D structure databases

ProteinModelPortalO89090.
SMRO89090. Positions 583-713.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid203414. 26 interactions.
DIPDIP-35276N.
IntActO89090. 8 interactions.
MINTMINT-1550750.
STRING10090.ENSMUSP00000001326.

PTM databases

PhosphoSiteO89090.

Proteomic databases

MaxQBO89090.
PaxDbO89090.
PRIDEO89090.

Protocols and materials databases

DNASU20683.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000163709; ENSMUSP00000130747; ENSMUSG00000001280. [O89090-2]
GeneID20683.
KEGGmmu:20683.
UCSCuc012aab.1. mouse. [O89090-2]

Organism-specific databases

CTD6667.
MGIMGI:98372. Sp1.

Phylogenomic databases

eggNOGCOG5048.
GeneTreeENSGT00740000115126.
HOGENOMHOG000234295.
HOVERGENHBG008933.
InParanoidO89090.
KOK04684.
OrthoDBEOG76HQ15.

Gene expression databases

ArrayExpressO89090.
BgeeO89090.
CleanExMM_SP1.
GenevestigatorO89090.

Family and domain databases

Gene3D3.30.160.60. 3 hits.
InterProIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
SMARTSM00355. ZnF_C2H2. 3 hits.
[Graphical view]
PROSITEPS00028. ZINC_FINGER_C2H2_1. 3 hits.
PS50157. ZINC_FINGER_C2H2_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio299197.
PROO89090.
SOURCESearch...

Entry information

Entry nameSP1_MOUSE
AccessionPrimary (citable) accession number: O89090
Secondary accession number(s): O89087, Q62251, Q64167
Entry history
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: June 21, 2005
Last modified: June 11, 2014
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot