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UniProtKB - O89090 (SP1_MOUSE)

Entry version 187 (23 Feb 2022)
Sequence version 2 (21 Jun 2005)
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Protein

Transcription factor Sp1

Gene

Sp1

Organism
Mus musculus (Mouse)
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 a role in the recruitment of SMARCA4/BRG1 on the c-FOS promoter Plays an essential role in the regulation of FE65 gene expression (By similarity).

Positively regulates the transcription of the core clock component ARNTL/BMAL1 (PubMed:24030830).

Plays a role in protecting cells against oxidative stress following brain injury by regulating the expression of RNF112 (PubMed:27918959).

By similarity2 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 fingeri627 – 656C2H2-type 1PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri657 – 686C2H2-type 2PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri687 – 714C2H2-type 3PROSITE-ProRule annotationAdd BLAST28

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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-MMU-2173796, SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription
R-MMU-6807505, RNA polymerase II transcribes snRNA genes
R-MMU-9018519, Estrogen-dependent gene expression

<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%5Fand%5Ftaxonomy%5Fsection">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
Alternative name(s):
Specificity protein 11 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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 15

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...MGIi		MGI:98372, Sp1

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSMUSG00000001280

<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

Keywords - Cellular componenti

Cytoplasm, Nucleus

<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%5Fprocessing%5Fsection">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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000471382 – 784Transcription factor Sp1Add BLAST783

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 residuei2PhosphoserineBy similarity1
Modified residuei7PhosphoserineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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); alternateBy similarity
Cross-linki16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei61PhosphoserineCombined sources1
Modified residuei103Phosphoserine; by ATMBy similarity1
Modified residuei280Phosphothreonine; by MAPK8By similarity1
Modified residuei455Phosphothreonine; by MAPK1 and MAPK3By similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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>Glycosylationi493O-linked (GlcNAc) serineBy similarity1
Modified residuei613Phosphoserine; alternateBy similarity1
Glycosylationi613O-linked (GlcNAc) serine; alternateBy similarity1
Modified residuei641Phosphothreonine; alternateBy similarity1
Glycosylationi641O-linked (GlcNAc) threonine; alternateBy similarity1
Modified residuei642Phosphoserine; by PKC/PRKCZ; alternateBy similarity1
Glycosylationi642O-linked (GlcNAc) serine; alternateBy similarity1
Modified residuei652Phosphothreonine; by PKC/PRKCZBy similarity1
Modified residuei669PhosphothreonineBy similarity1
Modified residuei671Phosphoserine; by PKC/PRKCZBy similarity1
Modified residuei682Phosphothreonine; by PKC/PRKCZBy similarity1
Modified residuei699Phosphoserine; alternateBy similarity1
Glycosylationi699O-linked (GlcNAc) serine; alternateBy similarity1
Modified residuei703Phosphoserine; alternateBy similarity1
Glycosylationi703O-linked (GlcNAc) serine; alternateBy similarity1
Modified residuei704N6-acetyllysineBy similarity1
Modified residuei738Phosphothreonine; by MAPK1, MAPK3 and MAPK8By similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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-61 enhances proteolytic cleavage. Phosphorylation on Ser-7 enhances ubiquitination and protein degradation. Hyperphosphorylation on Ser-103 in response to DNA damage has no effect on transcriptional activity. MAPK1/MAPK3-mediated phosphorylation on Thr-455 and Thr-738 enhances VEGF transcription but, represses FGF2-triggered PDGFR-alpha transcription. Also implicated in the repression of RECK by ERBB2. Hyperphosphorylated on Thr-280 and Thr-738 during mitosis by MAPK8 shielding SP1 from degradation by the ubiquitin-dependent pathway. Phosphorylated in the zinc-finger domain by calmodulin-activated PKCzeta. Phosphorylation on Ser-642 by PKCzeta is critical for TSA-activated LHR gene expression through release of its repressor, p107. Phosphorylation on Thr-669, Ser-671 and Thr-682 is stimulated by angiotensin II via the AT1 receptor inducing increased binding to the PDGF-D promoter. This phosphorylation is increased in injured artey wall. Ser-61 and Thr-682 can both be dephosphorylated by PP2A during cell-cycle interphase. Dephosphorylation on Ser-61 leads to increased chromatin association during interphase and increases the transcriptional activity. On insulin stimulation, sequentially glycosylated and phosphorylated on several C-terminal serine and threonine residues (By similarity).By similarity
Acetylated. Acetylation/deacetylation events affect transcriptional activity. Deacetylation leads to an increase in the expression the 12(s)-lipooxygenase gene though recruitment of p300 to the promoter (By similarity).By similarity
Ubiquitinated. Ubiquitination occurs on the C-terminal proteolytically-cleaved peptide and is triggered by phosphorylation (By similarity).By similarity
Sumoylated with SUMO1. Sumoylation modulates proteolytic cleavage of the N-terminal repressor domain. Sumoylation levels are attenuated during tumorigenesis. Phosphorylation mediates SP1 desumoylation (By similarity).By similarity
Proteolytic cleavage in the N-terminal repressor domain is prevented by sumoylation. The C-terminal cleaved product is susceptible to degradation (By similarity).By similarity
O-glycosylated; Contains 8 N-acetylglucosamine side chains. Levels are controlled by insulin and the SP1 phosphorylation states. Insulin-mediated O-glycosylation locates SP1 to the nucleus, where it is sequentially deglycosylated and phosphorylated. O-glycosylation affects transcriptional activity through disrupting the interaction with a number of transcription factors including ELF1 and NFYA. Inhibited by peroxisomome proliferator receptor gamma (PPARgamma) (By similarity).By similarity

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>Sitei65 – 66CleavageBy similarity2

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		O89090

MaxQB - The MaxQuant DataBase

More...MaxQBi		O89090

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

More...PaxDbi		O89090

PeptideAtlas

More...PeptideAtlasi		O89090

PRoteomics IDEntifications database

More...PRIDEi		O89090

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		261485 [O89090-1]
261486 [O89090-2]

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		O89090, 6 sites

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		O89090

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

More...PhosphoSitePlusi		O89090

<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 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

Up-regulated by traumatic brain injury and hydrogen peroxide (at protein level)(PubMed:27918959).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000001280, Expressed in rostral migratory stream and 323 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		O89090, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		O89090, MM

<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%5Fsection">'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%5Fsection">'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 SV40 VP2/3 proteins.

Interacts with SV40 major capsid protein VP1; this interaction leads to a cooperativity between the 2 proteins in DNA binding.

Interacts with HLTF; the interaction may be required for basal transcriptional activity of HLTF.

Interacts (deacetylated form) with EP300; the interaction enhances gene expression.

Interacts with HDAC1 and JUN.

Interacts with ELF1; the interaction is inhibited by glycosylation of SP1. Interaction with NFYA; the interaction is inhibited by glycosylation of SP1.

Interacts with SMARCA4/BRG1.

Interacts with ATF7IP and TBP.

Interacts with MEIS2 isoform 4 and PBX1 isoform PBX1a.

Interacts with EGR1 (By similarity).

Interacts with RNF112 in an oxidative stress-regulated manner (PubMed:27918959).

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

Interacts with DDX3X; this interaction potentiates SP1-induced CDKN1A/WAF1/CIP1 transcription (By similarity).

By similarity1 Publication

(Microbial infection) Interacts with murine minute virus NS1; this interaction allows high levels of viral P38 promoter transactivation by NS1.

2 Publications

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		203414, 29 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		O89090

Database of interacting proteins

More...DIPi		DIP-35276N

Protein interaction database and analysis system

More...IntActi		O89090, 11 interactors

Molecular INTeraction database

More...MINTi		O89090

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000001326

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		O89090, protein

<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

3D structure databases

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

More...SMRi		O89090

Database of comparative protein structure models

More...ModBasei		Search...

<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>Regioni1 – 95DisorderedSequence analysisAdd BLAST95
Regioni2 – 84Repressor domainBy similarityAdd BLAST83
Regioni111 – 144DisorderedSequence analysisAdd BLAST34
Regioni148 – 253Transactivation domain A (Gln-rich)By similarityAdd BLAST106
Regioni263 – 497Transactivation domain B (Gln-rich)By similarityAdd BLAST235
Regioni282 – 303DisorderedSequence analysisAdd BLAST22
Regioni333 – 398DisorderedSequence analysisAdd BLAST66
Regioni498 – 611Transactivation domain C (highly charged)By similarityAdd BLAST114
Regioni566 – 598DisorderedSequence analysisAdd BLAST33
Regioni620 – 784VZV IE62-bindingBy similarityAdd BLAST165
Regioni709 – 784Domain DBy similarityAdd BLAST76

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>Motifi464 – 4729aaTADBy similarity9

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 type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi1 – 16Basic and acidic residuesSequence analysisAdd BLAST16
Compositional biasi30 – 65Polar residuesSequence analysisAdd BLAST36
Compositional biasi72 – 95Polar residuesSequence analysisAdd BLAST24

<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.By similarity

<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

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri627 – 656C2H2-type 1PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri657 – 686C2H2-type 2PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri687 – 714C2H2-type 3PROSITE-ProRule annotationAdd BLAST28

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1721, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000157804

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_019688_1_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		O89090

Database of Orthologous Groups

More...OrthoDBi		1085860at2759

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR036236, Znf_C2H2_sf
IPR013087, Znf_C2H2_type

Pfam protein domain database

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

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00355, ZnF_C2H2, 3 hits

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF57667, SSF57667, 1 hit

PROSITE; a protein domain and family database

More...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%5Flength">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 (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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 2 <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 2 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: O89090-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <p><strong>What is the canonical sequence?</strong><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 VTAVVKIEKD VGGNNGGSGN GGGAAFSQTR SSSTGSSSSS 
        60         70         80         90        100
GGGGGQESQP SPLALLAATC SRIESPNENS NNSQGPSQSG GTGELDLTAT 
       110        120        130        140        150
QLSQGANGWQ IISSSSGATP TSKEQSGNST NGSNGSESSK NRTVSGGQYV 
       160        170        180        190        200
VAATPNLQNQ QVLTGLPGVM PNIQYQVIPQ FQTVDGQQLQ FAATGAQVQQ 
       210        220        230        240        250
DGSGQIQIIP GANQQIIPNR GSGGNIIAAM PNLLQQAVPL QGLANNVLSG 
       260        270        280        290        300
QTQYVTNVPV ALNGNITLLP VNSVSAATLT PSSQAGTISS SGSQESSSQP 
       310        320        330        340        350
VTSGTAISSA SLVSSQASSS SFFTNANSYS TTTTTSNMGI MNFTSSGSSG 
       360        370        380        390        400
TSSQGQTPQR VGGLQGSDSL NIQQNQTSGG SLQGSQQKEG EQSQQTQQQQ 
       410        420        430        440        450
ILIQPQLVQG GQALQALQAA PLSGQTFTTQ AISQETLQNL QLQAVQNSGP 
       460        470        480        490        500
IIIRTPTVGP NGQVSWQTLQ LQNLQVQNPQ AQTITLAPMQ GVSLGQTSSS 
       510        520        530        540        550
NTTLTPIASA ASIPAGTVTV NAAQLSSMPG LQTINLSALG TSGIQVHQLP 
       560        570        580        590        600
GLPLAIANTP GDHGTQLGLH GSGGDGIHDE TAGGEGENSS DLQPQAGRRT 
       610        620        630        640        650
RREACTCPYC KDSEGRASGD PGKKKQHICH IQGCGKVYGK TSHLRAHLRW 
       660        670        680        690        700
HTGERPFMCN WSYCGKRFTR SDELQRHKRT HTGEKKFACP ECPKRFMRSD 
       710        720        730        740        750
HLSKHIKTHQ NKKGGPGVAL SVGTLPLDSG AGSEGTATPS ALITTNMVAM 
       760        770        780 
EAICPEGIAR LANSGINVMQ VTELQSINIS GNGF
Length:784
Mass (Da):80,732
Last modified:June 21, 2005 - v2
<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:iB6B989F0A252CEE5
GO
Isoform 2 (identifier: O89090-2) [UniParc]FASTAAdd to basket
Also known as: Sp1-S

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

Show »
Length:467
Mass (Da):48,749
Checksum:i4A373D67E6128197
GO

<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 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G3X8Q0G3X8Q0_MOUSE
Transcription factor Sp1
Sp1
781Annotation score:

Annotation score:3 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>
E9Q113E9Q113_MOUSE
Transcription factor Sp1
Sp1
183Annotation 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>
E9Q2V3E9Q2V3_MOUSE
Transcription factor Sp1
Sp1
105Annotation 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>
E9Q0S7E9Q0S7_MOUSE
Transcription factor Sp1
Sp1
55Annotation 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>

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 conflicti100T → A in AAC16484 (PubMed:9628590).Curated1
Sequence conflicti131 – 133Missing in AAC16484 (PubMed:9628590).Curated3
Sequence conflicti220R → E in AAC08527 (Ref. 3) Curated1
Sequence conflicti462G → V in AAC16484 (PubMed:9628590).Curated1

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_00737656 – 372Missing in isoform 2. 1 PublicationAdd BLAST317

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
AF062566 mRNA Translation: AAC16484.1
S79832 mRNA Translation: AAB35321.1
AF022363 mRNA Translation: AAC08527.1
X60136 Genomic DNA Translation: CAA42721.1

Protein sequence database of the Protein Information Resource

More...PIRi		S30493

NCBI Reference Sequences

More...RefSeqi		NP_038700.2, NM_013672.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000163709; ENSMUSP00000130747; ENSMUSG00000001280 [O89090-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		20683

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:20683

UCSC genome browser

More...UCSCi		uc012aab.1, mouse [O89090-2]

Keywords - Coding sequence diversityi

Alternative splicing

<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
AF062566 mRNA Translation: AAC16484.1
S79832 mRNA Translation: AAB35321.1
AF022363 mRNA Translation: AAC08527.1
X60136 Genomic DNA Translation: CAA42721.1
PIRiS30493
RefSeqiNP_038700.2, NM_013672.2

3D structure databases

SMRiO89090
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi203414, 29 interactors
CORUMiO89090
DIPiDIP-35276N
IntActiO89090, 11 interactors
MINTiO89090
STRINGi10090.ENSMUSP00000001326

PTM databases

GlyGeniO89090, 6 sites
iPTMnetiO89090
PhosphoSitePlusiO89090

Proteomic databases

EPDiO89090
MaxQBiO89090
PaxDbiO89090
PeptideAtlasiO89090
PRIDEiO89090
ProteomicsDBi261485 [O89090-1]
261486 [O89090-2]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		892, 1068 antibodies from 47 providers

The DNASU plasmid repository

More...DNASUi		20683

Genome annotation databases

EnsembliENSMUST00000163709; ENSMUSP00000130747; ENSMUSG00000001280 [O89090-2]
GeneIDi20683
KEGGimmu:20683
UCSCiuc012aab.1, mouse [O89090-2]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		6667
MGIiMGI:98372, Sp1
VEuPathDBiHostDB:ENSMUSG00000001280

Phylogenomic databases

eggNOGiKOG1721, Eukaryota
GeneTreeiENSGT00940000157804
HOGENOMiCLU_019688_1_0_1
InParanoidiO89090
OrthoDBi1085860at2759

Enzyme and pathway databases

ReactomeiR-MMU-2173796, SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription
R-MMU-6807505, RNA polymerase II transcribes snRNA genes
R-MMU-9018519, Estrogen-dependent gene expression

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		20683, 21 hits in 68 CRISPR screens

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

More...ChiTaRSi		Sp1, mouse

Protein Ontology

More...PROi		PR:O89090
RNActiO89090, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000001280, Expressed in rostral migratory stream and 323 other tissues
ExpressionAtlasiO89090, baseline and differential
GenevisibleiO89090, MM

Family and domain databases

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

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_MOUSE
<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: O89090
Secondary accession number(s): O89087, Q62251, Q64167
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: June 21, 2005
Last modified: February 23, 2022
This is version 187 of the entry and version 2 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

<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

Reference proteome

Documents

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