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P08047 (SP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 179. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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
Synonyms:TSFP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length785 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. 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. Ref.1 Ref.16 Ref.18 Ref.19 Ref.23 Ref.26 Ref.28 Ref.29 Ref.30 Ref.33 Ref.34 Ref.35 Ref.36 Ref.38 Ref.43 Ref.46

Subunit structure

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 4and PBX1 isoform PBX1a Interacts with EGR1. Ref.12 Ref.15 Ref.16 Ref.17 Ref.20 Ref.21 Ref.22 Ref.24 Ref.29 Ref.40 Ref.41 Ref.42 Ref.44 Ref.45 Ref.49

Subcellular location

Nucleus. Cytoplasm. Note: Nuclear location is governed by glycosylated/phosphorylated states. Insulin promotes nuclear location, while glucagon favors cytoplasmic location. Ref.25 Ref.38

Tissue specificity

Up-regulated in adenocarcinomas of the stomach (at protein level). Isoform 3 is ubiquitously expressed at low levels. Ref.1

Induction

By insulin. Ref.25

Post-translational modification

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. Ref.19 Ref.23 Ref.25 Ref.26 Ref.28 Ref.30 Ref.33 Ref.35 Ref.36 Ref.37 Ref.38

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. Ref.29

Ubiquitinated. Ubiquitination occurs on the C-terminal proteolytically-cleaved peptide and is triggered by phosphorylation. Ref.35

Sumoylated with SUMO1. Sumoylation modulates proteolytic cleavage of the N-terminal repressor domain. Sumoylation levels are attenuated during tumorigenesis. Phosphorylation mediates SP1 desumoylation. Ref.27 Ref.35

Proteolytic cleavage in the N-terminal repressor domain is prevented by sumoylation. The C-terminal cleaved product is susceptible to degradation. Ref.27 Ref.35

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). Ref.19 Ref.23 Ref.25 Ref.26 Ref.28 Ref.30 Ref.33 Ref.35 Ref.36 Ref.37 Ref.38

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.

Sequence similarities

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

Contains 3 C2H2-type zinc fingers.

Sequence caution

The sequence AAH43224.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processHost-virus interaction
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionActivator
Repressor
   PTMAcetylation
Glycoprotein
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular lipid metabolic process

Traceable author statement. Source: Reactome

definitive hemopoiesis

Inferred from electronic annotation. Source: Ensembl

embryonic camera-type eye morphogenesis

Inferred from electronic annotation. Source: Ensembl

embryonic placenta development

Inferred from electronic annotation. Source: Ensembl

embryonic process involved in female pregnancy

Inferred from electronic annotation. Source: Ensembl

embryonic skeletal system development

Inferred from electronic annotation. Source: Ensembl

enucleate erythrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

gene expression

Traceable author statement. Source: Reactome

liver development

Inferred from electronic annotation. Source: Ensembl

lung development

Inferred from electronic annotation. Source: Ensembl

megakaryocyte differentiation

Inferred from electronic annotation. Source: Ensembl

ossification

Inferred from electronic annotation. Source: Ensembl

positive regulation by host of viral transcription

Inferred from direct assay PubMed 2833704. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 19263243PubMed 2833704. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 12771217. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from direct assay PubMed 12560508. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription, DNA-templated

Traceable author statement. Source: Reactome

transforming growth factor beta receptor signaling pathway

Traceable author statement. Source: Reactome

trophectodermal cell differentiation

Inferred from electronic annotation. Source: Ensembl

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred by curator Ref.10. Source: UniProtKB

protein-DNA complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionDNA binding

Inferred from direct assay PubMed 12560508. Source: UniProtKB

HMG box domain binding

Inferred from physical interaction PubMed 16582099. Source: UniProtKB

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

Inferred from sequence or structural similarity. 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 electronic annotation. Source: Ensembl

RNA polymerase II core promoter sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

RNA polymerase II repressing transcription factor binding

Inferred from sequence or structural similarity. Source: BHF-UCL

bHLH transcription factor binding

Inferred from sequence or structural similarity. Source: BHF-UCL

double-stranded DNA binding

Inferred from direct assay PubMed 20371611. Source: BHF-UCL

enhancer binding

Inferred from electronic annotation. Source: Ensembl

histone deacetylase binding

Inferred from physical interaction PubMed 17827154PubMed 18850004. Source: BHF-UCL

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein C-terminus binding

Inferred from physical interaction PubMed 10816420. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay PubMed 10393239. Source: UniProtKB

sequence-specific DNA binding

Inferred from direct assay PubMed 12169688. Source: HGNC

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 12560508. Source: UniProtKB

transcription factor binding

Inferred from physical interaction PubMed 14988427PubMed 20716579. Source: UniProtKB

transcription regulatory region DNA binding

Inferred from direct assay PubMed 18293083PubMed 18850004. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P08047-1)

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.
Isoform 2 (identifier: P08047-2)

Also known as: Sp1b;

The sequence of this isoform differs from the canonical sequence as follows:
     1-7: Missing.
Isoform 3 (identifier: P08047-3)

Also known as: Sp1c;

The sequence of this isoform differs from the canonical sequence as follows:
     54-101: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.47
Chain2 – 785784Transcription factor Sp1
PRO_0000047137

Regions

Zinc finger626 – 65025C2H2-type 1
Zinc finger656 – 68025C2H2-type 2
Zinc finger686 – 70823C2H2-type 3
Region2 – 8281Repressor domain
Region146 – 251106Transactivation domain A (Gln-rich)
Region261 – 495235Transactivation domain B (Gln-rich)
Region496 – 610115Transactivation domain C (highly charged)
Region619 – 785167VZV IE62-binding
Region708 – 78578Domain D
Compositional bias36 – 143108Ser/Thr-rich
Compositional bias271 – 379109Ser/Thr-rich

Sites

Site63 – 642Cleavage Probable

Amino acid modifications

Modified residue21N-acetylserine Ref.47 Ref.50
Modified residue21Phosphoserine Ref.47
Modified residue71Phosphoserine Ref.35 Ref.47 Ref.50
Modified residue591Phosphoserine Ref.28 Ref.32 Ref.35 Ref.38
Modified residue1011Phosphoserine; by ATM Ref.33 Ref.36
Modified residue2781Phosphothreonine; by MAPK8
Modified residue4531Phosphothreonine; by MAPK1 AND MAPK3 Ref.19 Ref.23 Ref.26
Modified residue6121Phosphoserine; alternate
Modified residue6401Phosphothreonine; alternate
Modified residue6411Phosphoserine; by PKC/PRKCZ; alternate Ref.30
Modified residue6511Phosphothreonine; by PKC/PRKCZ Ref.39
Modified residue6681Phosphothreonine Ref.37
Modified residue6701Phosphoserine; by PKC/PRKCZ Ref.37
Modified residue6811Phosphothreonine; by PKC/PRKCZ Ref.28 Ref.37
Modified residue7021Phosphoserine; alternate
Modified residue7031N6-acetyllysine Ref.29
Modified residue7391Phosphothreonine; by MAPK1, MAPK3 AND MAPK8 Ref.19 Ref.23 Ref.26
Glycosylation4911O-linked (GlcNAc) Ref.14 Ref.18
Glycosylation6121O-linked (GlcNAc); alternate Ref.25
Glycosylation6401O-linked (GlcNAc); alternate Ref.25
Glycosylation6411O-linked (GlcNAc); alternate Ref.25
Glycosylation6981O-linked (GlcNAc) Ref.25
Glycosylation7021O-linked (GlcNAc); alternate Ref.25
Cross-link16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.27 Ref.35

Natural variations

Alternative sequence1 – 77Missing in isoform 2.
VSP_053934
Alternative sequence54 – 10148Missing in isoform 3.
VSP_053935
Natural variant7371T → A.
Corresponds to variant rs3741665 [ dbSNP | Ensembl ].
VAR_019971

Experimental info

Mutagenesis71S → A: Increase in protein stability. No change in sumoylation. Ref.35
Mutagenesis151V → R: Enhanced transcriptional activity.
Mutagenesis161K → R: Loss of sumoylation. No cleavage and reduced transcriptional activity. Ref.27
Mutagenesis181E → A: Loss of sumoylation. Increased cleavage and enhanced transcriptional activity. Ref.27
Mutagenesis191K → R: No effect on sumoylation nor on proteolytic cleavage. Ref.27
Mutagenesis361S → A: No effect on phosphorylation on DNA damage. Ref.36
Mutagenesis561S → A: No effect on phosphorylation on DNA damage. Ref.36
Mutagenesis591S → A: Loss of phosphorylation. No effect on activated MAPK8-mediated phosphorylation. Similar loss of phosphorylation as by dephosphorylation by PP2AC. Reduced proteolytic processing. Ref.28 Ref.35 Ref.38
Mutagenesis591S → E: Some association with chromatin, increased phosphorylation levels and decreased glycosylation. Ref.28 Ref.35 Ref.38
Mutagenesis731S → A: Little effect on activated MAPK8-mediated phosphorylation. Ref.38
Mutagenesis811S → A: No effect on phosphorylation on DNA damage. Ref.36
Mutagenesis851S → A: No effect on phosphorylation on DNA damage. Ref.36
Mutagenesis981T → A: No effect on phosphorylation on DNA damage. Ref.36
Mutagenesis1011S → A: Significant reduction of phosphorylation on DNA damage. Ref.33 Ref.36
Mutagenesis1011S → D: Increase in phosphorylation on DNA damage. Ref.33 Ref.36
Mutagenesis1171T → A: No effect on activated MAPK8-mediated phosphorylation. Ref.38
Mutagenesis2201S → A: No effect on dephosphorylation by PP2A. Ref.28
Mutagenesis2501T → A: No effect on phosphorylation on DNA damage. Ref.36
Mutagenesis2781T → 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. Ref.38
Mutagenesis2781T → D: Increased protein stability during mitosis; when associated with D-739. Ref.38
Mutagenesis2811S → A: No effect on phosphorylation on DNA damage. Ref.36
Mutagenesis2911S → A: No effect on phosphorylation on DNA damage. Ref.36
Mutagenesis2961S → A: No effect on phosphorylation on DNA damage. Ref.36
Mutagenesis3131S → A: No effect on phosphorylation on DNA damage. Ref.36
Mutagenesis3511S → A: No effect on phosphorylation on DNA damage. Ref.36
Mutagenesis3551T → A: No effect on dephosphorylation by PP2A. Ref.19 Ref.28
Mutagenesis3941T → A: No effect on phosphorylation on DNA damage. Ref.36
Mutagenesis4271T → A: No effect on phosphorylation on DNA damage. Ref.36
Mutagenesis4311S → A: No effect on phosphorylation on DNA damage. Ref.36
Mutagenesis4531T → 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. Ref.19 Ref.23 Ref.28
Mutagenesis4911S → A: Loss of O-glycosylation. Increase in transcriptional activity. Ref.14 Ref.18
Mutagenesis6121S → A: Diminished glycosylation. Inhibits transcriptional activity; when associated with A-640; A-641; A-698 and A-702. Ref.34
Mutagenesis6401T → A: Diminished glycosylation. Inhibits transcriptional activity; when associated with A-612; A-641; A-698 and A-702. Ref.34
Mutagenesis6411S → A: Abolishes PRKCzeta-mediated phosphorylation. Diminished glycosylation. Inhibits transcriptional activity; when associated with A-612; A-640; A-641 and A-702. Ref.30 Ref.34
Mutagenesis6511T → A: No effect on dephosphorylation by PP2A. Ref.28
Mutagenesis6681T → A: Abolishes PRKCzeta-mediated but not PKCdelta-mediated phosphorylation. No effect on DNA binding; when associated with A-670 and A-681. Ref.37
Mutagenesis6701S → A: Abolishes PRKCzeta-mediated but not PKCdelta-mediated phosphorylation. No effect on DNA binding; when associated with A-668 and A-681. Ref.37
Mutagenesis6811T → 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. Ref.28 Ref.37
Mutagenesis6981S → A: Diminished glycosylation. Inhibits transcriptional activity; when associated with A-612; A-640; A-641 and A-702. Ref.34
Mutagenesis7021S → A: Diminished glycosylation. Inhibits transcriptional activity; when associated with A-612; A-640; A-641 and A-698. Ref.34
Mutagenesis7031K → A: Abolishes acetylation. Increases recruitment of p300 to the promoter and enhances gene transcription. Ref.29
Mutagenesis7281S → A: Exhibits attenuated endoproteolytic cleavage; when associated with A-732. Ref.35
Mutagenesis7321S → A: Exhibits attenuated endoproteolytic cleavage; when associated with A-728. Ref.35
Mutagenesis7391T → 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. Ref.19 Ref.23 Ref.28 Ref.38
Mutagenesis7391T → D: Increased protein stability during mitosis; when associated with D-278. Ref.19 Ref.23 Ref.28 Ref.38
Sequence conflict3661D → G AA sequence Ref.7
Sequence conflict6701S → F AA sequence Ref.7

Secondary structure

................... 785
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Sp1a) [UniParc].

Last modified April 27, 2001. Version 3.
Checksum: 43893DBF6518B9EA

FASTA78580,693
        10         20         30         40         50         60 
MSDQDHSMDE MTAVVKIEKG VGGNNGGNGN GGGAFSQARS SSTGSSSSTG GGGQESQPSP 

        70         80         90        100        110        120 
LALLAATCSR IESPNENSNN SQGPSQSGGT GELDLTATQL SQGANGWQII SSSSGATPTS 

       130        140        150        160        170        180 
KEQSGSSTNG SNGSESSKNR TVSGGQYVVA AAPNLQNQQV LTGLPGVMPN IQYQVIPQFQ 

       190        200        210        220        230        240 
TVDGQQLQFA ATGAQVQQDG SGQIQIIPGA NQQIITNRGS GGNIIAAMPN LLQQAVPLQG 

       250        260        270        280        290        300 
LANNVLSGQT QYVTNVPVAL NGNITLLPVN SVSAATLTPS SQAVTISSSG SQESGSQPVT 

       310        320        330        340        350        360 
SGTTISSASL VSSQASSSSF FTNANSYSTT TTTSNMGIMN FTTSGSSGTN SQGQTPQRVS 

       370        380        390        400        410        420 
GLQGSDALNI QQNQTSGGSL QAGQQKEGEQ NQQTQQQQIL IQPQLVQGGQ ALQALQAAPL 

       430        440        450        460        470        480 
SGQTFTTQAI SQETLQNLQL QAVPNSGPII IRTPTVGPNG QVSWQTLQLQ NLQVQNPQAQ 

       490        500        510        520        530        540 
TITLAPMQGV SLGQTSSSNT TLTPIASAAS IPAGTVTVNA AQLSSMPGLQ TINLSALGTS 

       550        560        570        580        590        600 
GIQVHPIQGL PLAIANAPGD HGAQLGLHGA GGDGIHDDTA GGEEGENSPD AQPQAGRRTR 

       610        620        630        640        650        660 
REACTCPYCK DSEGRGSGDP GKKKQHICHI QGCGKVYGKT SHLRAHLRWH TGERPFMCTW 

       670        680        690        700        710        720 
SYCGKRFTRS DELQRHKRTH TGEKKFACPE CPKRFMRSDH LSKHIKTHQN KKGGPGVALS 

       730        740        750        760        770        780 
VGTLPLDSGA GSEGSGTATP SALITTNMVA MEAICPEGIA RLANSGINVM QVADLQSINI 


SGNGF 

« Hide

Isoform 2 (Sp1b) [UniParc].

Checksum: 74D5DA9A1F8DC8EA
Show »

FASTA77879,892
Isoform 3 (Sp1c) [UniParc].

Checksum: D830B2947A96C8B9
Show »

FASTA73775,824

References

« Hide 'large scale' references
[1]"Identification of a novel Sp1 splice variant as a strong transcriptional activator."
Infantino V., Convertini P., Iacobazzi F., Pisano I., Scarcia P., Iacobazzi V.
Biochem. Biophys. Res. Commun. 412:86-91(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, TISSUE SPECIFICITY.
[2]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain and Testis.
[5]Haggart M.H., Ladurner A.G.
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-785 (ISOFORM 1).
Tissue: Cervix carcinoma.
[6]"Heterogeneous Sp1 mRNAs in human HepG2 cells include a product of homotypic trans-splicing."
Takahara T., Kanazu S., Yanagisawa S., Akanuma H.
J. Biol. Chem. 275:38067-38072(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-558 (ISOFORM 1), TRANS-SPLICING.
[7]"Isolation of cDNA encoding transcription factor Sp1 and functional analysis of the DNA binding domain."
Kadonaga J.T., Carner K.R., Masiarz F.R., Tjian R.
Cell 51:1079-1090(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 90-785 (ISOFORM 1/2), PROTEIN SEQUENCE OF 359-375 AND 670-675.
[8]"Expression of transcription factor Sp1 mRNA in mammalian cells."
Nicolas M., Noe V., Ciudad C.J.
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-109 (ISOFORM 1).
[9]"Sequencing of the 5' end of human transcription factor SP1 mRNA."
Handschug K., Huebner A.
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-98 (ISOFORM 1).
[10]"O-glycosylation of eukaryotic transcription factors: implications for mechanisms of transcriptional regulation."
Jackson S.P., Tjian R.
Cell 55:125-133(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION.
[11]"Analysis of Sp1 in vivo reveals multiple transcriptional domains, including a novel glutamine-rich activation motif."
Courey A.J., Tjian R.
Cell 55:887-898(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: TRANSACTIVATION DOMAINS.
[12]"Interaction of virion protein Vpr of human immunodeficiency virus type 1 with cellular transcription factor Sp1 and trans-activation of viral long terminal repeat."
Wang L., Mukherjee S., Jia F., Narayan O., Zhao L.J.
J. Biol. Chem. 270:25564-25569(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIV-1 VPR.
[13]"The serotonin 1a receptor gene contains a TATA-less promoter that responds to MAZ and Sp1."
Parks C.L., Shenk T.
J. Biol. Chem. 271:4417-4430(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF SEROTONIN 1A RECEPTOR PROMOTER BINDING SITES.
[14]"O glycosylation of an Sp1-derived peptide blocks known Sp1 protein interactions."
Roos M.D., Su K., Baker J.R., Kudlow J.E.
Mol. Cell. Biol. 17:6472-6480(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT SER-491, MUTAGENESIS OF SER-491, IDENTIFICATION BY MASS SPECTROMETRY.
[15]"The SV40 capsid protein VP3 cooperates with the cellular transcription factor Sp1 in DNA-binding and in regulating viral promoter activity."
Gordon-Shaag A., Ben-Nun-Shaul O., Kasamatsu H., Oppenheim A.B., Oppenheim A.
J. Mol. Biol. 275:187-195(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SV40 VP2/3.
[16]"Functional interactions between Sp1 or Sp3 and the helicase-like transcription factor mediate basal expression from the human plasminogen activator inhibitor-1 gene."
Ding H., Benotmane A.M., Suske G., Collen D., Belayew A.
J. Biol. Chem. 274:19573-19580(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HLTF.
[17]"A set of proteins interacting with transcription factor Sp1 identified in a two-hybrid screening."
Gunther M., Laithier M., Brison O.
Mol. Cell. Biochem. 210:131-142(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATF7IP; PHC2; POGZ AND HCFC1.
Tissue: Colon.
[18]"O-linkage of N-acetylglucosamine to Sp1 activation domain inhibits its transcriptional capability."
Yang X., Su K., Roos M.D., Chang Q., Paterson A.J., Kudlow J.E.
Proc. Natl. Acad. Sci. U.S.A. 98:6611-6616(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT SER-491, FUNCTION, MUTAGENESIS OF SER-491.
[19]"Identification of two Sp1 phosphorylation sites for p42/p44 mitogen-activated protein kinases: their implication in vascular endothelial growth factor gene transcription."
Milanini-Mongiat J., Pouyssegur J., Pages G.
J. Biol. Chem. 277:20631-20639(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-453 AND THR-739, FUNCTION, MUTAGENESIS OF THR-355; THR-453 AND THR-739.
[20]"Cellular transcription factor Sp1 recruits simian virus 40 capsid proteins to the viral packaging signal, ses."
Gordon-Shaag A., Ben-Nun-Shaul O., Roitman V., Yosef Y., Oppenheim A.
J. Virol. 76:5915-5924(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SV40 VP1.
[21]"Che-1 arrests human colon carcinoma cell proliferation by displacing HDAC1 from the p21WAF1/CIP1 promoter."
Di Padova M., Bruno T., De Nicola F., Iezzi S., D'Angelo C., Gallo R., Nicosia D., Corbi N., Biroccio A., Floridi A., Passananti C., Fanciulli M.
J. Biol. Chem. 278:36496-36504(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AATF.
[22]"Interaction between the varicella zoster virus IE62 major transactivator and cellular transcription factor Sp1."
Peng H., He H., Hay J., Ruyechan W.T.
J. Biol. Chem. 278:38068-38075(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH VARICELLA-ZOSTER VIRUS IE62 PROTEIN.
[23]"Fibroblast growth factor-2 represses platelet-derived growth factor receptor-alpha (PDGFR-alpha) transcription via ERK1/2-dependent Sp1 phosphorylation and an atypical cis-acting element in the proximal PDGFR-alpha promoter."
Bonello M.R., Khachigian L.M.
J. Biol. Chem. 279:2377-2382(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-453 AND THR-739, FUNCTION, MUTAGENESIS OF THR-453 AND THR-739.
[24]"Transcriptional repression and heterochromatin formation by MBD1 and MCAF/AM family proteins."
Ichimura T., Watanabe S., Sakamoto Y., Aoto T., Fujita N., Nakao M.
J. Biol. Chem. 280:13928-13935(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATF7IP AND ATF7IP2.
[25]"Insulin dynamically regulates calmodulin gene expression by sequential O-glycosylation and phosphorylation of SP1 and its subcellular compartmentalization in liver cells."
Majumdar G., Harrington A., Hungerford J., Martinez-Hernandez A., Gerling I.C., Raghow R., Solomon S.
J. Biol. Chem. 281:3642-3650(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT SER-612; THR-640; SER-641; SER-698 AND SER-702, PHOSPHORYLATION, INDUCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[26]"HER-2/neu represses the metastasis suppressor RECK via ERK and Sp transcription factors to promote cell invasion."
Hsu M.C., Chang H.C., Hung W.C.
J. Biol. Chem. 281:4718-4725(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-453 AND THR-739, FUNCTION.
[27]"Sumoylation inhibits cleavage of Sp1 N-terminal negative regulatory domain and inhibits Sp1-dependent transcription."
Spengler M.L., Brattain M.G.
J. Biol. Chem. 281:5567-5574(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-16, PROTEOLYTIC PROCESSING, MUTAGENESIS OF LYS-16; GLU-18 AND LYS-19.
[28]"Increased chromatin association of Sp1 in interphase cells by PP2A-mediated dephosphorylations."
Vicart A., Lefebvre T., Imbert J., Fernandez A., Kahn-Perles B.
J. Mol. Biol. 364:897-908(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-59 AND THR-681, DEPHOSPHORYLATION, GLYCOSYLATION, FUNCTION, MUTAGENESIS OF SER-59; SER-220; THR-355; THR-453; THR-651; THR-681 AND THR-739.
[29]"Sp1 deacetylation induced by phorbol ester recruits p300 to activate 12(S)-lipoxygenase gene transcription."
Hung J.J., Wang Y.T., Chang W.C.
Mol. Cell. Biol. 26:1770-1785(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-703, INTERACTION WITH HDAC1; EP300 AND JUN, FUNCTION, MUTAGENESIS OF LYS-703.
[30]"Phosphatidylinositol 3-kinase/protein kinase Czeta-induced phosphorylation of Sp1 and p107 repressor release have a critical role in histone deacetylase inhibitor-mediated derepression of transcription of the luteinizing hormone receptor gene."
Zhang Y., Liao M., Dufau M.L.
Mol. Cell. Biol. 26:6748-6761(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-641, FUNCTION, MUTAGENESIS OF SER-641.
[31]Erratum
Zhang Y., Liao M., Dufau M.L.
Mol. Cell. Biol. 26:8214-8214(2006)
[32]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[33]"Phosphorylation of Sp1 in response to DNA damage by ataxia telangiectasia-mutated kinase."
Olofsson B.A., Kelly C.M., Kim J., Hornsby S.M., Azizkhan-Clifford J.
Mol. Cancer Res. 5:1319-1330(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-101, FUNCTION, MUTAGENESIS OF SER-101.
[34]"Activation of PPARgamma negatively regulates O-GlcNAcylation of Sp1."
Chung S.S., Kim J.H., Park H.S., Choi H.H., Lee K.W., Cho Y.M., Lee H.K., Park K.S.
Biochem. Biophys. Res. Commun. 372:713-718(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION, FUNCTION, MUTAGENESIS OF SER-612; THR-640; SER-641; SER-698 AND SER-702.
[35]"Phosphorylation mediates Sp1 coupled activities of proteolytic processing, desumoylation and degradation."
Spengler M.L., Guo L.W., Brattain M.G.
Cell Cycle 7:623-630(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-7 AND SER-59, SUMOYLATION AT LYS-16, PROTEOLYTIC PROCESSING, UBIQUITINATION, FUNCTION, MUTAGENESIS OF SER-7; SER-59; SER-728 AND SER-732.
[36]"Identification of phosphorylation sites on transcription factor Sp1 in response to DNA damage and its accumulation at damaged sites."
Iwahori S., Yasui Y., Kudoh A., Sato Y., Nakayama S., Murata T., Isomura H., Tsurumi T.
Cell. Signal. 20:1795-1803(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-101, FUNCTION, MUTAGENESIS OF SER-36; SER-56; SER-81; SER-85; THR-98; SER-101; THR-250; SER-281; SER-291; SER-296; SER-313; SER-351; THR-394; THR-427 AND SER-431.
[37]"Angiotensin II-inducible platelet-derived growth factor-D transcription requires specific Ser/Thr residues in the second zinc finger region of Sp1."
Tan N.Y., Midgley V.C., Kavurma M.M., Santiago F.S., Luo X., Peden R., Fahmy R.G., Berndt M.C., Molloy M.P., Khachigian L.M.
Circ. Res. 102:38-51(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-668; SER-670 AND THR-681, MUTAGENESIS OF THR-668; SER-670 AND THR-681.
[38]"Phosphorylation by c-Jun NH2-terminal kinase 1 regulates the stability of transcription factor Sp1 during mitosis."
Chuang J.-Y., Wang Y.-T., Yeh S.-H., Liu Y.-W., Chang W.-C., Hung J.-J.
Mol. Biol. Cell 19:1139-1151(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-59, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-59; SER-73; THR-117; THR-278 AND THR-739.
[39]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-651, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[40]"O-GlcNAc inhibits interaction between Sp1 and Elf-1 transcription factors."
Lim K., Chang H.I.
Biochem. Biophys. Res. Commun. 380:569-574(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION, INTERACTION WITH ELF1.
[41]"O-GlcNAcylation of Sp1 interrupts Sp1 interaction with NF-Y."
Lim K., Chang H.I.
Biochem. Biophys. Res. Commun. 382:593-597(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION, INTERACTION WITH NFYA.
[42]"MCAF1/AM is involved in Sp1-mediated maintenance of cancer-associated telomerase activity."
Liu L., Ishihara K., Ichimura T., Fujita N., Hino S., Tomita S., Watanabe S., Saitoh N., Ito T., Nakao M.
J. Biol. Chem. 284:5165-5174(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATF7IP AND TBP.
[43]"O-linked N-acetylglucosaminylation of Sp1 inhibits the human immunodeficiency virus type 1 promoter."
Jochmann R., Thurau M., Jung S., Hofmann C., Naschberger E., Kremmer E., Harrer T., Miller M., Schaft N., Stuerzl M.
J. Virol. 83:3704-3718(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION, FUNCTION.
[44]"Human BAHD1 promotes heterochromatic gene silencing."
Bierne H., Tham T.N., Batsche E., Dumay A., Leguillou M., Kerneis-Golsteyn S., Regnault B., Seeler J.S., Muchardt C., Feunteun J., Cossart P.
Proc. Natl. Acad. Sci. U.S.A. 106:13826-13831(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BAHD1.
[45]"Snail associates with EGR-1 and SP-1 to upregulate transcriptional activation of p15INK4b."
Hu C.T., Chang T.Y., Cheng C.C., Liu C.S., Wu J.R., Li M.C., Wu W.S.
FEBS J. 277:1202-1218(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EGR1.
[46]"Transcriptional regulation of human FE65, a ligand of Alzheimer's disease amyloid precursor protein, by Sp1."
Yu H.T., Chan W.W., Chai K.H., Lee C.W., Chang R.C., Yu M.S., McLoughlin D.M., Miller C.C., Lau K.F.
J. Cell. Biochem. 109:782-793(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[47]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-7, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[48]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[49]"Cooperative transcriptional activation by Klf4, Meis2, and Pbx1."
Bjerke G.A., Hyman-Walsh C., Wotton D.
Mol. Cell. Biol. 31:3723-3733(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MEIS2 AND PBX1.
[50]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[51]"Structures of zinc finger domains from transcription factor Sp1. Insights into sequence-specific protein-DNA recognition."
Narayan V.A., Kriwacki R.W., Caradonna J.P.
J. Biol. Chem. 272:7801-7809(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 654-684 AND 684-712.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA29635.
RefSeqNP_001238754.1. NM_001251825.1.
NP_003100.1. NM_003109.1.
NP_612482.2. NM_138473.2.
UniGeneHs.620754.
Hs.649191.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SP1NMR-A684-712[»]
1SP2NMR-A654-684[»]
1VA1NMR-A619-654[»]
1VA2NMR-A654-684[»]
1VA3NMR-A684-712[»]
DisProtDP00378.
ProteinModelPortalP08047.
SMRP08047. Positions 578-712.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112550. 222 interactions.
DIPDIP-36N.
IntActP08047. 62 interactions.
MINTMINT-98326.
STRING9606.ENSP00000329357.

Chemistry

ChEMBLCHEMBL6103.

PTM databases

PhosphoSiteP08047.
UniCarbKBP08047.

Polymorphism databases

DMDM13638437.

Proteomic databases

PaxDbP08047.
PeptideAtlasP08047.
PRIDEP08047.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000327443; ENSP00000329357; ENSG00000185591.
ENST00000426431; ENSP00000404263; ENSG00000185591.
GeneID6667.
KEGGhsa:6667.
UCSCuc001scw.3. human.

Organism-specific databases

CTD6667.
GeneCardsGC12P053773.
HGNCHGNC:11205. SP1.
HPACAB000330.
HPA001853.
HPA012292.
MIM189906. gene.
neXtProtNX_P08047.
PharmGKBPA36042.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5048.
HOGENOMHOG000234295.
HOVERGENHBG008933.
InParanoidP08047.
KOK04684.
OMAGWQIISS.
OrthoDBEOG76HQ15.
PhylomeDBP08047.
TreeFamTF350150.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_116125. Disease.
REACT_120956. Cellular responses to stress.
REACT_71. Gene Expression.
SignaLinkP08047.

Gene expression databases

ArrayExpressP08047.
BgeeP08047.
CleanExHS_SP1.
GenevestigatorP08047.

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]
PfamPF00096. zf-C2H2. 1 hit.
[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

ChiTaRSSP1. human.
EvolutionaryTraceP08047.
GeneWikiSp1_transcription_factor.
GenomeRNAi6667.
NextBio25995.
PMAP-CutDBP08047.
PROP08047.
SOURCESearch...

Entry information

Entry nameSP1_HUMAN
AccessionPrimary (citable) accession number: P08047
Secondary accession number(s): E4Z9M7 expand/collapse secondary AC list , G5E9M8, Q86TN8, Q9H3Q5, Q9NR51, Q9NY21, Q9NYE7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: April 27, 2001
Last modified: April 16, 2014
This is version 179 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM