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Entry version 238 (13 Nov 2019)
Sequence version 3 (27 Apr 2001)
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Protein

Transcription factor Sp1

Gene

SP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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 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. Positively regulates the transcription of the core clock component ARNTL/BMAL1 (PubMed:10391891, PubMed:11371615, PubMed:11904305, PubMed:14593115, PubMed:16377629, PubMed:16478997, PubMed:16943418, PubMed:17049555, PubMed:18171990, PubMed:18199680, PubMed:18239466, PubMed:18513490, PubMed:18619531, PubMed:19193796, PubMed:20091743, PubMed:21798247, PubMed:21046154). Plays a role in the recruitment of SMARCA4/BRG1 on the c-FOS promoter. Plays a role in protecting cells against oxidative stress following brain injury by regulating the expression of RNF112 (By similarity).By similarity17 Publications

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.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri626 – 650C2H2-type 1PROSITE-ProRule annotationAdd BLAST25
Zinc fingeri656 – 680C2H2-type 2PROSITE-ProRule annotationAdd BLAST25
Zinc fingeri686 – 708C2H2-type 3PROSITE-ProRule annotationAdd BLAST23

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-1989781 PPARA activates gene expression
R-HSA-2173796 SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription
R-HSA-2426168 Activation of gene expression by SREBF (SREBP)
R-HSA-2559585 Oncogene Induced Senescence
R-HSA-6807505 RNA polymerase II transcribes snRNA genes
R-HSA-9018519 Estrogen-dependent gene expression

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
P08047

SIGNOR Signaling Network Open Resource

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SIGNORi
P08047

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Transcription factor Sp1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:SP1
Synonyms:TSFP1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 12

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:11205 SP1

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
189906 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P08047

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi7S → A: Increase in protein stability. No change in sumoylation. 1 Publication1
Mutagenesisi15V → R: Enhanced transcriptional activity. 1
Mutagenesisi16K → R: Loss of sumoylation. No cleavage and reduced transcriptional activity. 1 Publication1
Mutagenesisi18E → A: Loss of sumoylation. Increased cleavage and enhanced transcriptional activity. 1 Publication1
Mutagenesisi19K → R: No effect on sumoylation nor on proteolytic cleavage. 1 Publication1
Mutagenesisi36S → A: No effect on phosphorylation on DNA damage. 1 Publication1
Mutagenesisi56S → A: No effect on phosphorylation on DNA damage. 1 Publication1
Mutagenesisi59S → A: Loss of phosphorylation. No effect on activated MAPK8-mediated phosphorylation. Similar loss of phosphorylation as by dephosphorylation by PP2AC. Reduced proteolytic processing. 3 Publications1
Mutagenesisi59S → E: Some association with chromatin, increased phosphorylation levels and decreased glycosylation. 3 Publications1
Mutagenesisi73S → A: Little effect on activated MAPK8-mediated phosphorylation. 1 Publication1
Mutagenesisi81S → A: No effect on phosphorylation on DNA damage. 1 Publication1
Mutagenesisi85S → A: No effect on phosphorylation on DNA damage. 1 Publication1
Mutagenesisi98T → A: No effect on phosphorylation on DNA damage. 1 Publication1
Mutagenesisi101S → A: Significant reduction of phosphorylation on DNA damage. 2 Publications1
Mutagenesisi101S → D: Increase in phosphorylation on DNA damage. 2 Publications1
Mutagenesisi117T → A: No effect on activated MAPK8-mediated phosphorylation. 1 Publication1
Mutagenesisi220S → A: No effect on dephosphorylation by PP2A. 1 Publication1
Mutagenesisi250T → A: No effect on phosphorylation on DNA damage. 1 Publication1
Mutagenesisi278T → 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. 1 Publication1
Mutagenesisi278T → D: Increased protein stability during mitosis; when associated with D-739. 1 Publication1
Mutagenesisi281S → A: No effect on phosphorylation on DNA damage. 1 Publication1
Mutagenesisi291S → A: No effect on phosphorylation on DNA damage. 1 Publication1
Mutagenesisi296S → A: No effect on phosphorylation on DNA damage. 1 Publication1
Mutagenesisi313S → A: No effect on phosphorylation on DNA damage. 1 Publication1
Mutagenesisi351S → A: No effect on phosphorylation on DNA damage. 1 Publication1
Mutagenesisi355T → A: No effect on dephosphorylation by PP2A. 2 Publications1
Mutagenesisi394T → A: No effect on phosphorylation on DNA damage. 1 Publication1
Mutagenesisi427T → A: No effect on phosphorylation on DNA damage. 1 Publication1
Mutagenesisi431S → A: No effect on phosphorylation on DNA damage. 1 Publication1
Mutagenesisi453T → 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. 3 Publications1
Mutagenesisi491S → A: Loss of O-glycosylation. Increase in transcriptional activity. 2 Publications1
Mutagenesisi612S → A: Diminished glycosylation. Inhibits transcriptional activity; when associated with A-640; A-641; A-698 and A-702. 1 Publication1
Mutagenesisi640T → A: Diminished glycosylation. Inhibits transcriptional activity; when associated with A-612; A-641; A-698 and A-702. 1 Publication1
Mutagenesisi641S → A: Abolishes PRKCzeta-mediated phosphorylation. Diminished glycosylation. Inhibits transcriptional activity; when associated with A-612; A-640; A-641 and A-702. 2 Publications1
Mutagenesisi651T → A: No effect on dephosphorylation by PP2A. 1 Publication1
Mutagenesisi668T → A: Abolishes PRKCzeta-mediated but not PKCdelta-mediated phosphorylation. No effect on DNA binding; when associated with A-670 and A-681. 1 Publication1
Mutagenesisi670S → A: Abolishes PRKCzeta-mediated but not PKCdelta-mediated phosphorylation. No effect on DNA binding; when associated with A-668 and A-681. 1 Publication1
Mutagenesisi681T → 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. 2 Publications1
Mutagenesisi698S → A: Diminished glycosylation. Inhibits transcriptional activity; when associated with A-612; A-640; A-641 and A-702. 1 Publication1
Mutagenesisi702S → A: Diminished glycosylation. Inhibits transcriptional activity; when associated with A-612; A-640; A-641 and A-698. 1 Publication1
Mutagenesisi703K → A: Abolishes acetylation. Increases recruitment of p300 to the promoter and enhances gene transcription. 1 Publication1
Mutagenesisi728S → A: Exhibits attenuated endoproteolytic cleavage; when associated with A-732. 1 Publication1
Mutagenesisi732S → A: Exhibits attenuated endoproteolytic cleavage; when associated with A-728. 1 Publication1
Mutagenesisi739T → 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. 4 Publications1
Mutagenesisi739T → D: Increased protein stability during mitosis; when associated with D-278. 4 Publications1

Organism-specific databases

DisGeNET

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DisGeNETi
6667

Open Targets

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OpenTargetsi
ENSG00000185591

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA36042

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
P08047

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL6103

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
SP1

Domain mapping of disease mutations (DMDM)

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DMDMi
13638437

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000471372 – 785Transcription factor Sp1Add BLAST784

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylserineCombined sources1
Modified residuei2PhosphoserineCombined sources1
Modified residuei7PhosphoserineCombined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Cross-linki16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei59PhosphoserineCombined sources3 Publications1
Modified residuei101Phosphoserine; by ATM2 Publications1
Modified residuei278Phosphothreonine; by MAPK81 Publication1
Modified residuei453Phosphothreonine; by MAPK1 and MAPK33 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi491O-linked (GlcNAc) serine2 Publications1
Modified residuei612Phosphoserine; alternate1 Publication1
Glycosylationi612O-linked (GlcNAc) serine; alternate1 Publication1
Modified residuei640Phosphothreonine; alternate1 Publication1
Glycosylationi640O-linked (GlcNAc) threonine; alternate1 Publication1
Modified residuei641Phosphoserine; by PKC/PRKCZ; alternate2 Publications1
Glycosylationi641O-linked (GlcNAc) serine; alternate1 Publication1
Modified residuei651Phosphothreonine; by PKC/PRKCZCombined sources1
Modified residuei668Phosphothreonine1 Publication1
Modified residuei670Phosphoserine; by PKC/PRKCZ1 Publication1
Modified residuei681Phosphothreonine; by PKC/PRKCZ2 Publications1
Modified residuei698Phosphoserine; alternate1 Publication1
Glycosylationi698O-linked (GlcNAc) serine; alternate1 Publication1
Modified residuei702Phosphoserine; alternate1 Publication1 Publication1
Glycosylationi702O-linked (GlcNAc) serine; alternate1 Publication1
Modified residuei703N6-acetyllysine1 Publication1
Modified residuei739Phosphothreonine; by MAPK1, MAPK3 and MAPK83 Publications1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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.11 Publications
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.1 Publication
Ubiquitinated. Ubiquitination occurs on the C-terminal proteolytically-cleaved peptide and is triggered by phosphorylation.1 Publication
Sumoylated with SUMO1. Sumoylation modulates proteolytic cleavage of the N-terminal repressor domain. Sumoylation levels are attenuated during tumorigenesis. Phosphorylation mediates SP1 desumoylation.
Proteolytic cleavage in the N-terminal repressor domain is prevented by sumoylation. The C-terminal cleaved product is susceptible to degradation.
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).

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei63 – 64CleavageCurated2

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P08047

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P08047

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
P08047

MaxQB - The MaxQuant DataBase

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MaxQBi
P08047

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P08047

PeptideAtlas

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PeptideAtlasi
P08047

PRoteomics IDEntifications database

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PRIDEi
P08047

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
33987
52061 [P08047-1]

PTM databases

GlyConnect protein glycosylation platform

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GlyConnecti
605

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P08047

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P08047

UniCarbKB; an annotated and curated database of glycan structures

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UniCarbKBi
P08047

Miscellaneous databases

CutDB - Proteolytic event database

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PMAP-CutDBi
P08047

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

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

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By insulin.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000185591 Expressed in 208 organ(s), highest expression level in nipple

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P08047 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P08047 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB000330
HPA001853
HPA012292

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with ATF7IP, ATF7IP2, BAHD1, POGZ, HCFC1, AATF and PHC2.

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 ATF7IP and TBP.

Interacts with MEIS2 isoform 4 and PBX1 isoform PBX1a.

Interacts with EGR1 (PubMed:10391891, PubMed:10976766, PubMed:12021324, PubMed:12847090, PubMed:12855699, PubMed:15691849, PubMed:16478997, PubMed:19106100, PubMed:19285002, PubMed:19302979, PubMed:19666599, PubMed:20121949, PubMed:21746878, PubMed:7592727, PubMed:9466902).

Interacts with SMARCA4/BRG1.

Interacts with RNF112 in an oxidative stress-regulated manner (By similarity).

Interacts with ZBTB7A; ZBTB7A prevents the binding to GC-rich motifs in promoters and represses the transcriptional activity of SP1 (PubMed:12004059).

By similarity12 Publications

(Microbial infection) Interacts with varicella-zoster virus IE62 protein.

1 Publication

(Microbial infection) 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.

2 Publications

(Microbial infection) Interacts with HIV-1 Vpr; the interaction is inhibited by SP1 O-glycosylation.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
112550, 242 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P08047

Database of interacting proteins

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DIPi
DIP-36N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
P08047

Protein interaction database and analysis system

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IntActi
P08047, 73 interactors

Molecular INTeraction database

More...
MINTi
P08047

STRING: functional protein association networks

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STRINGi
9606.ENSP00000329357

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1785
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P08047

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P08047

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni2 – 82Repressor domainAdd BLAST81
Regioni146 – 251Transactivation domain A (Gln-rich)Add BLAST106
Regioni261 – 495Transactivation domain B (Gln-rich)Add BLAST235
Regioni496 – 610Transactivation domain C (highly charged)Add BLAST115
Regioni619 – 785VZV IE62-bindingAdd BLAST167
Regioni708 – 785Domain DAdd BLAST78

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi462 – 4709aaTAD1 Publication9

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi36 – 143Ser/Thr-richAdd BLAST108
Compositional biasi271 – 379Ser/Thr-richAdd BLAST109

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.1 Publication

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri626 – 650C2H2-type 1PROSITE-ProRule annotationAdd BLAST25
Zinc fingeri656 – 680C2H2-type 2PROSITE-ProRule annotationAdd BLAST25
Zinc fingeri686 – 708C2H2-type 3PROSITE-ProRule annotationAdd BLAST23

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG1721 Eukaryota
COG5048 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000157804

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000234295

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P08047

KEGG Orthology (KO)

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KOi
K04684

Identification of Orthologs from Complete Genome Data

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OMAi
MGIMNFS

Database of Orthologous Groups

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OrthoDBi
1085860at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P08047

TreeFam database of animal gene trees

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TreeFami
TF350150

Family and domain databases

Database of protein disorder

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DisProti
DP00378

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR036236 Znf_C2H2_sf
IPR013087 Znf_C2H2_type

Pfam protein domain database

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Pfami
View protein in Pfam
PF00096 zf-C2H2, 3 hits

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00355 ZnF_C2H2, 3 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF57667 SSF57667, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00028 ZINC_FINGER_C2H2_1, 3 hits
PS50157 ZINC_FINGER_C2H2_2, 3 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P08047-1) [UniParc]FASTAAdd to basket
Also known as: Sp1a

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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 MTAVVKIEKG VGGNNGGNGN GGGAFSQARS SSTGSSSSTG
60 70 80 90 100
GGGQESQPSP LALLAATCSR IESPNENSNN SQGPSQSGGT GELDLTATQL
110 120 130 140 150
SQGANGWQII SSSSGATPTS KEQSGSSTNG SNGSESSKNR TVSGGQYVVA
160 170 180 190 200
AAPNLQNQQV LTGLPGVMPN IQYQVIPQFQ TVDGQQLQFA ATGAQVQQDG
210 220 230 240 250
SGQIQIIPGA NQQIITNRGS GGNIIAAMPN LLQQAVPLQG LANNVLSGQT
260 270 280 290 300
QYVTNVPVAL NGNITLLPVN SVSAATLTPS SQAVTISSSG SQESGSQPVT
310 320 330 340 350
SGTTISSASL VSSQASSSSF FTNANSYSTT TTTSNMGIMN FTTSGSSGTN
360 370 380 390 400
SQGQTPQRVS GLQGSDALNI QQNQTSGGSL QAGQQKEGEQ NQQTQQQQIL
410 420 430 440 450
IQPQLVQGGQ ALQALQAAPL SGQTFTTQAI SQETLQNLQL QAVPNSGPII
460 470 480 490 500
IRTPTVGPNG QVSWQTLQLQ NLQVQNPQAQ TITLAPMQGV SLGQTSSSNT
510 520 530 540 550
TLTPIASAAS IPAGTVTVNA AQLSSMPGLQ TINLSALGTS GIQVHPIQGL
560 570 580 590 600
PLAIANAPGD HGAQLGLHGA GGDGIHDDTA GGEEGENSPD AQPQAGRRTR
610 620 630 640 650
REACTCPYCK DSEGRGSGDP GKKKQHICHI QGCGKVYGKT SHLRAHLRWH
660 670 680 690 700
TGERPFMCTW SYCGKRFTRS DELQRHKRTH TGEKKFACPE CPKRFMRSDH
710 720 730 740 750
LSKHIKTHQN KKGGPGVALS VGTLPLDSGA GSEGSGTATP SALITTNMVA
760 770 780
MEAICPEGIA RLANSGINVM QVADLQSINI SGNGF
Length:785
Mass (Da):80,693
Last modified:April 27, 2001 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i43893DBF6518B9EA
GO
Isoform 2 (identifier: P08047-2) [UniParc]FASTAAdd to basket
Also known as: Sp1b

The sequence of this isoform differs from the canonical sequence as follows:
     1-7: Missing.

Show »
Length:778
Mass (Da):79,892
Checksum:i74D5DA9A1F8DC8EA
GO
Isoform 3 (identifier: P08047-3) [UniParc]FASTAAdd to basket
Also known as: Sp1c

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

Show »
Length:737
Mass (Da):75,824
Checksum:iD830B2947A96C8B9
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H3BVI2H3BVI2_HUMAN
Transcription factor Sp1
SP1
230Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H3BUU5H3BUU5_HUMAN
Transcription factor Sp1
SP1
162Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAH43224 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti366D → G AA sequence (PubMed:3319186).Curated1
Sequence conflicti670S → F AA sequence (PubMed:3319186).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_019971737T → A. Corresponds to variant dbSNP:rs3741665Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0539341 – 7Missing in isoform 2. Curated7
Alternative sequenceiVSP_05393554 – 101Missing in isoform 3. 1 PublicationAdd BLAST48

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
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

The Consensus CDS (CCDS) project

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CCDSi
CCDS44898.1 [P08047-2]
CCDS8857.1 [P08047-1]

Protein sequence database of the Protein Information Resource

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PIRi
A29635

NCBI Reference Sequences

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RefSeqi
NP_001238754.1, NM_001251825.1 [P08047-3]
NP_003100.1, NM_003109.1 [P08047-2]
NP_612482.2, NM_138473.2 [P08047-1]
XP_011536998.1, XM_011538696.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000327443; ENSP00000329357; ENSG00000185591 [P08047-1]
ENST00000426431; ENSP00000404263; ENSG00000185591 [P08047-2]

Database of genes from NCBI RefSeq genomes

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GeneIDi
6667

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:6667

UCSC genome browser

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UCSCi
uc001scw.4 human [P08047-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
CCDSiCCDS44898.1 [P08047-2]
CCDS8857.1 [P08047-1]
PIRiA29635
RefSeqiNP_001238754.1, NM_001251825.1 [P08047-3]
NP_003100.1, NM_003109.1 [P08047-2]
NP_612482.2, NM_138473.2 [P08047-1]
XP_011536998.1, XM_011538696.2

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SP1NMR-A684-712[»]
1SP2NMR-A654-684[»]
1VA1NMR-A619-654[»]
1VA2NMR-A654-684[»]
1VA3NMR-A684-712[»]
SMRiP08047
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi112550, 242 interactors
CORUMiP08047
DIPiDIP-36N
ELMiP08047
IntActiP08047, 73 interactors
MINTiP08047
STRINGi9606.ENSP00000329357

Chemistry databases

ChEMBLiCHEMBL6103

PTM databases

GlyConnecti605
iPTMnetiP08047
PhosphoSitePlusiP08047
UniCarbKBiP08047

Polymorphism and mutation databases

BioMutaiSP1
DMDMi13638437

Proteomic databases

EPDiP08047
jPOSTiP08047
MassIVEiP08047
MaxQBiP08047
PaxDbiP08047
PeptideAtlasiP08047
PRIDEiP08047
ProteomicsDBi33987
52061 [P08047-1]

Genome annotation databases

EnsembliENST00000327443; ENSP00000329357; ENSG00000185591 [P08047-1]
ENST00000426431; ENSP00000404263; ENSG00000185591 [P08047-2]
GeneIDi6667
KEGGihsa:6667
UCSCiuc001scw.4 human [P08047-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
6667
DisGeNETi6667

GeneCards: human genes, protein and diseases

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GeneCardsi
SP1
HGNCiHGNC:11205 SP1
HPAiCAB000330
HPA001853
HPA012292
MIMi189906 gene
neXtProtiNX_P08047
OpenTargetsiENSG00000185591
PharmGKBiPA36042

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1721 Eukaryota
COG5048 LUCA
GeneTreeiENSGT00940000157804
HOGENOMiHOG000234295
InParanoidiP08047
KOiK04684
OMAiMGIMNFS
OrthoDBi1085860at2759
PhylomeDBiP08047
TreeFamiTF350150

Enzyme and pathway databases

ReactomeiR-HSA-1989781 PPARA activates gene expression
R-HSA-2173796 SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription
R-HSA-2426168 Activation of gene expression by SREBF (SREBP)
R-HSA-2559585 Oncogene Induced Senescence
R-HSA-6807505 RNA polymerase II transcribes snRNA genes
R-HSA-9018519 Estrogen-dependent gene expression
SignaLinkiP08047
SIGNORiP08047

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
SP1 human
EvolutionaryTraceiP08047

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Sp1_transcription_factor

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
6667
PharosiP08047
PMAP-CutDBiP08047

Protein Ontology

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PROi
PR:P08047

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000185591 Expressed in 208 organ(s), highest expression level in nipple
ExpressionAtlasiP08047 baseline and differential
GenevisibleiP08047 HS

Family and domain databases

DisProtiDP00378
InterProiView protein in InterPro
IPR036236 Znf_C2H2_sf
IPR013087 Znf_C2H2_type
PfamiView protein in Pfam
PF00096 zf-C2H2, 3 hits
SMARTiView protein in SMART
SM00355 ZnF_C2H2, 3 hits
SUPFAMiSSF57667 SSF57667, 1 hit
PROSITEiView protein in PROSITE
PS00028 ZINC_FINGER_C2H2_1, 3 hits
PS50157 ZINC_FINGER_C2H2_2, 3 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSP1_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P08047
Secondary accession number(s): E4Z9M7
, G5E9M8, Q86TN8, Q9H3Q5, Q9NR51, Q9NY21, Q9NYE7
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: April 27, 2001
Last modified: November 13, 2019
This is version 238 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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