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O89090

- SP1_MOUSE

UniProt

O89090 - SP1_MOUSE

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Protein

Transcription factor Sp1

Gene

Sp1

Organism
Mus musculus (Mouse)
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 (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. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: BHF-UCL
  9. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: MGI
  10. RNA polymerase II core promoter sequence-specific DNA binding Source: MGI
  11. RNA polymerase II repressing transcription factor binding Source: BHF-UCL
  12. sequence-specific DNA binding Source: MGI
  13. 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. rhythmic process Source: UniProtKB-KW
  16. trophectodermal cell differentiation Source: MGI
Complete GO annotation...

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-KW
  2. nuclear chromatin Source: BHF-UCL
  3. nucleus Source: MGI
Complete GO annotation...

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

BgeeiO89090.
CleanExiMM_SP1.
ExpressionAtlasiO89090. baseline and differential.
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.
GeneTreeiENSGT00760000118984.
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

        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

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 ENSGT00760000118984.
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

Bgeei O89090.
CleanExi MM_SP1.
ExpressionAtlasi O89090. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 133 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