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O89090

- SP1_MOUSE

UniProt

O89090 - SP1_MOUSE

Protein

Transcription factor Sp1

Gene

Sp1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 2 (21 Jun 2005)
      Previous versions | rss
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    Functioni

    Transcription factor that can activate or repress transcription in response to physiological and pathological stimuli. Binds with high affinity to GC-rich motifs and regulates the expression of a large number of genes involved in a variety of processes such as cell growth, apoptosis, differentiation and immune responses. Highly regulated by post-translational modifications (phosphorylations, sumoylation, proteolytic cleavage, glycosylation and acetylation). Binds also the PDGFR-alpha G-box promoter. May have a role in modulating the cellular response to DNA damage. Implicated in chromatin remodeling. Plays a role in the recruitment of SMARCA4/BRG1 on the c-FOS promoter Plays an essential role in the regulation of FE65 gene expression By similarity. Positively regulates the transcription of the core clock component ARNTL/BMAL1.By similarity1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei65 – 662CleavageBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri627 – 65630C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri657 – 68630C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri687 – 71428C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. bHLH transcription factor binding Source: BHF-UCL
    2. core promoter proximal region sequence-specific DNA binding Source: MGI
    3. core promoter sequence-specific DNA binding Source: UniProtKB
    4. DNA binding Source: MGI
    5. double-stranded DNA binding Source: MGI
    6. enhancer binding Source: MGI
    7. metal ion binding Source: UniProtKB-KW
    8. protein binding Source: MGI
    9. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: BHF-UCL
    10. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: MGI
    11. RNA polymerase II core promoter sequence-specific DNA binding Source: MGI
    12. RNA polymerase II repressing transcription factor binding Source: BHF-UCL
    13. sequence-specific DNA binding Source: MGI
    14. sequence-specific DNA binding transcription factor activity Source: MGI

    GO - Biological processi

    1. definitive hemopoiesis Source: MGI
    2. embryonic camera-type eye morphogenesis Source: MGI
    3. embryonic placenta development Source: MGI
    4. embryonic process involved in female pregnancy Source: MGI
    5. embryonic skeletal system development Source: MGI
    6. enucleate erythrocyte differentiation Source: MGI
    7. in utero embryonic development Source: MGI
    8. liver development Source: MGI
    9. lung development Source: MGI
    10. megakaryocyte differentiation Source: MGI
    11. ossification Source: MGI
    12. positive regulation of transcription, DNA-templated Source: UniProtKB
    13. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    14. regulation of transcription, DNA-templated Source: MGI
    15. trophectodermal cell differentiation Source: MGI

    Keywords - Molecular functioni

    Activator, Repressor

    Keywords - Biological processi

    Biological rhythms, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_198602. PPARA activates gene expression.
    REACT_198969. Activation of gene expression by SREBF (SREBP).
    REACT_203903. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcription factor Sp1
    Gene namesi
    Name:Sp1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 15

    Organism-specific databases

    MGIiMGI:98372. Sp1.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nuclear chromatin Source: BHF-UCL
    3. nucleus Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 784783Transcription factor Sp1PRO_0000047138Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei2 – 21PhosphoserineBy similarity
    Modified residuei7 – 71PhosphoserineBy similarity
    Cross-linki16 – 16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
    Modified residuei61 – 611PhosphoserineBy similarity
    Modified residuei103 – 1031Phosphoserine; by ATMBy similarity
    Modified residuei280 – 2801Phosphothreonine; by MAPK8By similarity
    Modified residuei455 – 4551Phosphothreonine; by MAPK1 AND MAPK3By similarity
    Glycosylationi493 – 4931O-linked (GlcNAc)By similarity
    Modified residuei613 – 6131Phosphoserine; alternateBy similarity
    Glycosylationi613 – 6131O-linked (GlcNAc); alternateBy similarity
    Modified residuei641 – 6411Phosphothreonine; alternateBy similarity
    Glycosylationi641 – 6411O-linked (GlcNAc); alternateBy similarity
    Modified residuei642 – 6421Phosphoserine; by PKC/PRKCZ; alternateBy similarity
    Glycosylationi642 – 6421O-linked (GlcNAc); alternateBy similarity
    Modified residuei652 – 6521Phosphothreonine; by PKC/PRKCZBy similarity
    Modified residuei669 – 6691PhosphothreonineBy similarity
    Modified residuei671 – 6711Phosphoserine; by PKC/PRKCZBy similarity
    Modified residuei682 – 6821Phosphothreonine; by PKC/PRKCZBy similarity
    Glycosylationi699 – 6991O-linked (GlcNAc)By similarity
    Modified residuei703 – 7031Phosphoserine; alternateBy similarity
    Glycosylationi703 – 7031O-linked (GlcNAc); alternateBy similarity
    Modified residuei704 – 7041N6-acetyllysineBy similarity
    Modified residuei738 – 7381Phosphothreonine; by MAPK1, MAPK3 AND MAPK8By similarity

    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

    Keywords - PTMi

    Acetylation, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiO89090.
    PaxDbiO89090.
    PRIDEiO89090.

    PTM databases

    PhosphoSiteiO89090.

    Expressioni

    Gene expression databases

    ArrayExpressiO89090.
    BgeeiO89090.
    CleanExiMM_SP1.
    GenevestigatoriO89090.

    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.By similarity

    Protein-protein interaction databases

    BioGridi203414. 26 interactions.
    DIPiDIP-35276N.
    IntActiO89090. 8 interactions.
    MINTiMINT-1550750.
    STRINGi10090.ENSMUSP00000001326.

    Structurei

    3D structure databases

    ProteinModelPortaliO89090.
    SMRiO89090. Positions 583-713.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 8483Repressor domainBy similarityAdd
    BLAST
    Regioni148 – 253106Transactivation domain A (Gln-rich)By similarityAdd
    BLAST
    Regioni263 – 497235Transactivation domain B (Gln-rich)By similarityAdd
    BLAST
    Regioni498 – 611114Transactivation domain C (highly charged)By similarityAdd
    BLAST
    Regioni620 – 784165VZV IE62-bindingBy similarityAdd
    BLAST
    Regioni709 – 78476Domain DBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi37 – 145109Ser/Thr-richAdd
    BLAST
    Compositional biasi273 – 381109Ser/Thr-richAdd
    BLAST

    Sequence similaritiesi

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

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri627 – 65630C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri657 – 68630C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri687 – 71428C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5048.
    GeneTreeiENSGT00740000115126.
    HOGENOMiHOG000234295.
    HOVERGENiHBG008933.
    InParanoidiO89090.
    KOiK04684.
    OrthoDBiEOG76HQ15.

    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]
    SMARTiSM00355. ZnF_C2H2. 3 hits.
    [Graphical view]
    PROSITEiPS00028. ZINC_FINGER_C2H2_1. 3 hits.
    PS50157. ZINC_FINGER_C2H2_2. 3 hits.
    [Graphical view]

    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. Align

    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

    MSDQDHSMDE VTAVVKIEKD VGGNNGGSGN GGGAAFSQTR SSSTGSSSSS    50
    GGGGGQESQP SPLALLAATC SRIESPNENS NNSQGPSQSG GTGELDLTAT 100
    QLSQGANGWQ IISSSSGATP TSKEQSGNST NGSNGSESSK NRTVSGGQYV 150
    VAATPNLQNQ QVLTGLPGVM PNIQYQVIPQ FQTVDGQQLQ FAATGAQVQQ 200
    DGSGQIQIIP GANQQIIPNR GSGGNIIAAM PNLLQQAVPL QGLANNVLSG 250
    QTQYVTNVPV ALNGNITLLP VNSVSAATLT PSSQAGTISS SGSQESSSQP 300
    VTSGTAISSA SLVSSQASSS SFFTNANSYS TTTTTSNMGI MNFTSSGSSG 350
    TSSQGQTPQR VGGLQGSDSL NIQQNQTSGG SLQGSQQKEG EQSQQTQQQQ 400
    ILIQPQLVQG GQALQALQAA PLSGQTFTTQ AISQETLQNL QLQAVQNSGP 450
    IIIRTPTVGP NGQVSWQTLQ LQNLQVQNPQ AQTITLAPMQ GVSLGQTSSS 500
    NTTLTPIASA ASIPAGTVTV NAAQLSSMPG LQTINLSALG TSGIQVHQLP 550
    GLPLAIANTP GDHGTQLGLH GSGGDGIHDE TAGGEGENSS DLQPQAGRRT 600
    RREACTCPYC KDSEGRASGD PGKKKQHICH IQGCGKVYGK TSHLRAHLRW 650
    HTGERPFMCN WSYCGKRFTR SDELQRHKRT HTGEKKFACP ECPKRFMRSD 700
    HLSKHIKTHQ NKKGGPGVAL SVGTLPLDSG AGSEGTATPS ALITTNMVAM 750
    EAICPEGIAR LANSGINVMQ VTELQSINIS GNGF 784
    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti100 – 1001T → A in AAC16484. (PubMed:9628590)Curated
    Sequence conflicti131 – 1333Missing in AAC16484. (PubMed:9628590)Curated
    Sequence conflicti220 – 2201R → E in AAC08527. 1 PublicationCurated
    Sequence conflicti462 – 4621G → V in AAC16484. (PubMed:9628590)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei56 – 372317Missing in isoform 2. 1 PublicationVSP_007376Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF062566 mRNA. Translation: AAC16484.1 .
    S79832 mRNA. Translation: AAB35321.1 .
    AF022363 mRNA. Translation: AAC08527.1 .
    X60136 Genomic DNA. Translation: CAA42721.1 .
    PIRi S30493.
    RefSeqi NP_038700.2. NM_013672.2.
    UniGenei Mm.4618.

    3D structure databases

    ProteinModelPortali O89090.
    SMRi O89090. Positions 583-713.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 203414. 26 interactions.
    DIPi DIP-35276N.
    IntActi O89090. 8 interactions.
    MINTi MINT-1550750.
    STRINGi 10090.ENSMUSP00000001326.

    PTM databases

    PhosphoSitei O89090.

    Proteomic databases

    MaxQBi O89090.
    PaxDbi O89090.
    PRIDEi O89090.

    Protocols and materials databases

    DNASUi 20683.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000163709 ; ENSMUSP00000130747 ; ENSMUSG00000001280 . [O89090-2 ]
    GeneIDi 20683.
    KEGGi mmu:20683.
    UCSCi uc012aab.1. mouse. [O89090-2 ]

    Organism-specific databases

    CTDi 6667.
    MGIi MGI:98372. Sp1.

    Phylogenomic databases

    eggNOGi COG5048.
    GeneTreei ENSGT00740000115126.
    HOGENOMi HOG000234295.
    HOVERGENi HBG008933.
    InParanoidi O89090.
    KOi K04684.
    OrthoDBi EOG76HQ15.

    Enzyme and pathway databases

    Reactomei REACT_198602. PPARA activates gene expression.
    REACT_198969. Activation of gene expression by SREBF (SREBP).
    REACT_203903. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.

    Miscellaneous databases

    NextBioi 299197.
    PROi O89090.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O89090.
    Bgeei O89090.
    CleanExi MM_SP1.
    Genevestigatori O89090.

    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 ]
    SMARTi SM00355. ZnF_C2H2. 3 hits.
    [Graphical view ]
    PROSITEi PS00028. ZINC_FINGER_C2H2_1. 3 hits.
    PS50157. ZINC_FINGER_C2H2_2. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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. 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.
    6. "Transcription factor NF-Y is a functional regulator of the transcription of core clock gene Bmal1."
      Xiao J., Zhou Y., Lai H., Lei S., Chi L.H., Mo X.
      J. Biol. Chem. 288:31930-31936(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiSP1_MOUSE
    AccessioniPrimary (citable) accession number: O89090
    Secondary accession number(s): O89087, Q62251, Q64167
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 9, 2003
    Last sequence update: June 21, 2005
    Last modified: October 1, 2014
    This is version 132 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3