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Search results 1 to 100 out of 152 for Sbp

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0.045s
Type Details Score
Gene
Type: gene
Organism: rat
Interaction Term
Protein Domain
Type: Family
Description: Bacterial high affinity transport systems are involved in active transport of solutes across the cytoplasmic membrane. Most of the bacterial ABC (ATP-binding cassette) importers are composed of one or two transmembrane permease proteins, one or two nucleotide-binding proteins and a highly specific periplasmic solute-binding protein. In Gram-negative bacteria the solute-binding proteins are dissolved in the periplasm, while in archaea and Gram-positive bacteria, their solute-binding proteins are membrane-anchored lipoproteins [, ]. On the basis of sequence similarities, the vast majority of these solute-binding proteins can be grouped into eight family clusters [], which generally correlate with the nature of the solute bound. This entry represents the family 1. Family 1 members include:Maltose/maltodextrin-binding proteins of Enterobacteriaceae (gene malE) []and Streptococcus pneumoniae malXMultiple oligosaccharide binding protein of Streptococcus mutans (gene msmE)Escherichia coli glycerol-3-phosphate-binding proteinSerratia marcescens iron-binding protein (gene sfuA) and the homologous proteins (gene fbp) from Haemophilus influenzae and NeisseriaE. coli thiamine-binding protein (gene tbpA) Interestingly, these thiamin-binding proteins share protein structural similarity with thiaminase-I. They may be evolved from a common ancestor []. This entry also includes thiaminase-1 from Paenibacillus thiaminolyticus (Bacillus thiaminolyticus).
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Publication
First Author: Tam R
Year: 1993
Journal: Microbiol Rev
Title: Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria.
Volume: 57
Issue: 2
Pages: 320-46
Publication
First Author: Singh B
Year: 2008
Journal: Microbiology
Title: Characterization of a Pseudomonas putida ABC transporter (AatJMQP) required for acidic amino acid uptake: biochemical properties and regulation by the Aau two-component system.
Volume: 154
Issue: Pt 3
Pages: 797-809
Publication
First Author: Saurin W
Year: 1994
Journal: Protein Sci
Title: Sequence relationships between integral inner membrane proteins of binding protein-dependent transport systems: evolution by recurrent gene duplications.
Volume: 3
Issue: 2
Pages: 325-44
Publication
First Author: Soriano EV
Year: 2008
Journal: Biochemistry
Title: Structural similarities between thiamin-binding protein and thiaminase-I suggest a common ancestor.
Volume: 47
Issue: 5
Pages: 1346-57
Publication
First Author: Sharff AJ
Year: 1995
Journal: J Mol Biol
Title: Refined structures of two insertion/deletion mutants probe function of the maltodextrin binding protein.
Volume: 246
Issue: 1
Pages: 8-13
Protein
Organism: Mus musculus/domesticus
Length: 197  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 217  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 217  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 217  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 232  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 217  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 147  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 232  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 217  
Fragment?: false
Publication
First Author: Mills JS
Year: 1987
Journal: Nucleic Acids Res
Title: Androgen regulated expression of a spermine binding protein gene in mouse ventral prostate.
Volume: 15
Issue: 19
Pages: 7709-24
Protein Domain
Type: Domain
Description: SBP (for SQUAMOSA-pROMOTER BINDING PROTEIN) domain is a sequence specific DNA-binding domain found in plant proteins []. Members of family probably function as transcription factors involved in the control of early flower development []. They share a highly conserved DNA-binding domain that contains two zinc-binding sites. Among the 11 possible ligands for the zinc atoms that are conserved in the SBP zinc finger, only 8 are used. The SBP zinc finger follows the general pattern C-x4-C-x16-C-x2-[HC]-x15-C-x2-C-x3-H-x11-C. Three other histidines are well conserved but not involved in zinc binding [, ].In vitro experiments show that the SBP zinc finger preferentially binds theconsensus sequence -TNCGTACAA- []. However, little is known of the physiological functions of these putative transcriptional regulators beyond their ability to bind DNA.The solution structure of the SBP zinc finger has been solved[]. The first four Cys or His coordinate one zinc ion and the last four coordinate the other. It can be viewed as two structural subdomains, each subdomain containing a single zinc-binding pocket. The N-terminal subdomain consists of two short alpha helices whereas the C-terminal one contains a three-stranded antiparallel β-sheet.
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus caroli
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus pahari
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus spretus
Publication
First Author: Abbott DE
Year: 2003
Journal: Genome Biol
Title: Expressed sequence tag profiling identifies developmental and anatomic partitioning of gene expression in the mouse prostate.
Volume: 4
Issue: 12
Pages: R79
Publication
First Author: Okazaki Y
Year: 2002
Journal: Nature
Title: Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs.
Volume: 420
Issue: 6915
Pages: 563-73
Publication
First Author: Fischer A
Year: 2005
Journal: Neuron
Title: Opposing roles of transient and prolonged expression of p25 in synaptic plasticity and hippocampus-dependent memory.
Volume: 48
Issue: 5
Pages: 825-38
Publication      
First Author: Shanghai Model Organisms Center
Year: 2017
Journal: MGI Direct Data Submission
Title: Information obtained from the Shanghai Model Organisms Center (SMOC), Shanghai, China
Publication
First Author: Joesting MS
Year: 2008
Journal: Dev Biol
Title: Secreted frizzled related protein 1 is a paracrine modulator of epithelial branching morphogenesis, proliferation, and secretory gene expression in the prostate.
Volume: 317
Issue: 1
Pages: 161-73
Publication        
First Author: The Gene Ontology Consortium
Year: 2010
Title: Automated transfer of experimentally-verified manual GO annotation data to mouse-human orthologs
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Function or Process or Component Unknown following Literature Review
Publication        
First Author: UniProt-GOA
Year: 2012
Title: Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Publication        
First Author: Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas
Year: 2010
Title: Annotation inferences using phylogenetic trees
Publication  
First Author: Timmermans S
Year: 2018
Journal: JCI Insight
Title: Overview of inactivating mutations in the protein-coding genome of the mouse reference strain C57BL/6J.
Volume: 3
Issue: 13
GXD Expression    
Probe: MGI:3055856
Assay Type: RT-PCR
Annotation Date: 2004-11-02
Strength: Present
Sex: Male
Emaps: EMAPS:2983628
Stage: TS28
Assay Id: MGI:3055876
Age: postnatal adult
Image: 4
Specimen Label: VP
Detected: true
Specimen Num: 1
GXD Expression      
Probe: MGI:3055856
Assay Type: RT-PCR
Annotation Date: 2004-11-02
Strength: Not Specified
Sex: Male
Emaps: EMAPS:2979428
Stage: TS28
Assay Id: MGI:3055876
Age: postnatal adult
Image: 4
Specimen Label: AP
Specimen Num: 2
GXD Expression    
Probe: MGI:3055856
Assay Type: RT-PCR
Annotation Date: 2004-11-02
Strength: Present
Sex: Male
Emaps: EMAPS:3571028
Stage: TS28
Assay Id: MGI:3055876
Age: postnatal adult
Image: 4
Specimen Label: DLP
Detected: true
Specimen Num: 3
GXD Expression      
Probe: MGI:3846133
Assay Type: RT-PCR
Annotation Date: 2009-06-02
Strength: Not Specified
Sex: Male
Emaps: EMAPS:2979428
Stage: TS28
Assay Id: MGI:3846415
Age: postnatal
Image: 6
Specimen Label: WT AP
Specimen Num: 1
GXD Expression      
Probe: MGI:3846133
Assay Type: RT-PCR
Annotation Date: 2009-06-02
Strength: Not Specified
Sex: Male
Emaps: EMAPS:2979428
Stage: TS28
Assay Id: MGI:3846415
Age: postnatal
Image: 6
Specimen Label: KO AP
Specimen Num: 2
GXD Expression    
Probe: MGI:3846133
Assay Type: RT-PCR
Annotation Date: 2009-06-02
Strength: Present
Sex: Male
Emaps: EMAPS:2983628
Stage: TS28
Assay Id: MGI:3846415
Age: postnatal
Image: 6
Specimen Label: WT VP
Detected: true
Specimen Num: 3
GXD Expression    
Probe: MGI:3846133
Assay Type: RT-PCR
Annotation Date: 2009-06-02
Strength: Present
Sex: Male
Emaps: EMAPS:2983628
Stage: TS28
Assay Id: MGI:3846415
Age: postnatal
Image: 6
Specimen Label: KO VP
Detected: true
Specimen Num: 4
GXD Expression      
Probe: MGI:3846133
Assay Type: RT-PCR
Annotation Date: 2009-06-02
Strength: Not Specified
Sex: Male
Emaps: EMAPS:3571028
Stage: TS28
Assay Id: MGI:3846415
Age: postnatal
Image: 6
Specimen Label: WT DLP
Specimen Num: 5
GXD Expression      
Probe: MGI:3846133
Assay Type: RT-PCR
Annotation Date: 2009-06-02
Strength: Not Specified
Sex: Male
Emaps: EMAPS:3571028
Stage: TS28
Assay Id: MGI:3846415
Age: postnatal
Image: 6
Specimen Label: KO DLP
Specimen Num: 6
GXD Expression      
Probe: MGI:3846133
Assay Type: RT-PCR
Annotation Date: 2009-06-02
Strength: Not Specified
Sex: Male
Emaps: EMAPS:2979428
Stage: TS28
Assay Id: MGI:3846420
Age: postnatal year 1
Image: 7
Specimen Label: WT AP
Specimen Num: 1
GXD Expression    
Probe: MGI:3846133
Assay Type: RT-PCR
Annotation Date: 2009-06-02
Strength: Present
Sex: Male
Emaps: EMAPS:2983628
Stage: TS28
Assay Id: MGI:3846420
Age: postnatal year 1
Image: 7
Specimen Label: WT VP
Detected: true
Specimen Num: 3
GXD Expression      
Probe: MGI:3846133
Assay Type: RT-PCR
Annotation Date: 2009-06-02
Strength: Not Specified
Sex: Male
Emaps: EMAPS:3571028
Stage: TS28
Assay Id: MGI:3846420
Age: postnatal year 1
Image: 7
Specimen Label: WT DLP
Specimen Num: 5
Publication      
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Mouse Synonym Curation
Publication      
First Author: The Jackson Laboratory Mouse Radiation Hybrid Database
Year: 2004
Journal: Database Release
Title: Mouse T31 Radiation Hybrid Data Load
Publication      
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform
Publication      
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
Publication      
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
Publication      
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome U74 Array Platform (A, B, C v2).
Publication      
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2003
Title: MGI Sequence Curation Reference
Protein Domain
Type: Homologous_superfamily
Description: SBP (for SQUAMOSA-pROMOTER BINDING PROTEIN) domain is a sequence specific DNA-binding domain found in plant proteins []. Members of family probably function as transcription factors involved in the control of early flower development []. They share a highly conserved DNA-binding domain that contains two zinc-binding sites. Among the 11 possible ligands for the zinc atoms that are conserved in the SBP zinc finger, only 8 are used. The SBP zinc finger follows the general pattern C-x4-C-x16-C-x2-[HC]-x15-C-x2-C-x3-H-x11-C. Three other histidines are well conserved but not involved in zinc binding [, ].In vitro experiments show that the SBP zinc finger preferentially binds theconsensus sequence -TNCGTACAA- []. However, little is known of the physiological functions of these putative transcriptional regulators beyond their ability to bind DNA.The solution structure of the SBP zinc finger has been solved[]. The first four Cys or His coordinate one zinc ion and the last four coordinate the other. It can be viewed as two structural subdomains, each subdomain containing a single zinc-binding pocket. The N-terminal subdomain consists of two short alpha helices whereas the C-terminal one contains a three-stranded antiparallel β-sheet.
Publication
First Author: Yamasaki K
Year: 2004
Journal: J Mol Biol
Title: A novel zinc-binding motif revealed by solution structures of DNA-binding domains of Arabidopsis SBP-family transcription factors.
Volume: 337
Issue: 1
Pages: 49-63
Publication
First Author: Cardon G
Year: 1999
Journal: Gene
Title: Molecular characterisation of the Arabidopsis SBP-box genes.
Volume: 237
Issue: 1
Pages: 91-104
Publication
First Author: Klein J
Year: 1996
Journal: Mol Gen Genet
Title: A new family of DNA binding proteins includes putative transcriptional regulators of the Antirrhinum majus floral meristem identity gene SQUAMOSA.
Volume: 250
Issue: 1
Pages: 7-16
Protein
Organism: Mus musculus/domesticus
Length: 199  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 403  
Fragment?: false
DO Term
Gene
Type: gene
Organism: human
Protein Domain
Type: Family
Description: The tripartite ATP-independent periplasmic (TRAP) transporters are substrate-binding protein (SBP)-dependent secondary transporters ubiquitous in prokaryotes, but absent from eukaryotes. Theyare comprised of an SBP of the DctP or TAXI families and two integral membrane proteins of unequal sizes that form the DctQ and DctM protein families (the small and large membrane components respectively). The TRAP transporter for sialic acid consists of the SBP siaP, and siaQM (termed siaT in some cases), encoding the fused integral membrane protein [].This family consists of DctQ homologues found in TRAP transporters [].
Protein Domain
Type: Family
Description: This entry represents a group of DNA binding proteins, known as SBP (SQUAMOSA-PROMOTER BINDING PROTEIN) family. They are putative transcription factors characterised by a highly conserved SBP-box of 76 amino acids involved in DNA binding and nuclear localisation []. They are involved in the control of early flower development [].
Gene
Type: gene
Organism: human
Publication
First Author: Preston JC
Year: 2010
Journal: Plant J
Title: SQUAMOSA-PROMOTER BINDING PROTEIN 1 initiates flowering in Antirrhinum majus through the activation of meristem identity genes.
Volume: 62
Issue: 4
Pages: 704-12
Publication
First Author: Wu G
Year: 2006
Journal: Development
Title: Temporal regulation of shoot development in Arabidopsis thaliana by miR156 and its target SPL3.
Volume: 133
Issue: 18
Pages: 3539-47
Publication  
First Author: Jorgensen SA
Year: 2014
Journal: Mol Phylogenet Evol
Title: Differential SPL gene expression patterns reveal candidate genes underlying flowering time and architectural differences in Mimulus and Arabidopsis.
Volume: 73
Pages: 129-39
Protein Domain
Type: Family
Description: This entry represents a group of DNA binding proteins, known as SBP (SQUAMOSA-pROMOTER BINDING PROTEIN) family. They are putative transcription factors characterised by a highly conserved SBP-box of 76 amino acids involved in DNA binding and nuclear localisation []. They are involved in the control of early flower development []. This entry includes Arabidopsis SPL3 and SPL4 []. SPL3/SPL4 promote vegetative phase change and flowering, and are strongly repressed by miR156 [].
Protein Domain
Type: Conserved_site
Description: Sulphate-binding protein (gene sbp or sbpA) and thiosulphate-binding protein (gene cysP) are two structurally related periplasmic bacterial proteins which specifically bind sulphate and thiosulphate and are involved in the transport systems for these nutrients [, ]. There are two conserved regions in the protein, one located in the N-terminal region and the other in the central part of these proteins. The second region includes two adjacent amino acids (Ser-Gly) that, in sbp, are known to be essential for sulphate binding [].This entry represents a conserved site located in the N-terminal region of these proteins.
Protein Domain
Type: Binding_site
Description: Sulphate-binding protein (gene sbp or sbpA) and thiosulphate-binding protein (gene cysP) are two structurally related periplasmic bacterial proteins which specifically bind sulphate and thiosulphate and are involved in the transport systems for these nutrients [, ]. There are two conserved regions in the protein, one located in the N-terminal region and the other in the central part of these proteins. The second region includes two adjacent amino acids (Ser-Gly) that, in sbp, are knownto be essential for sulphate binding [].This entry represents the second conserved region that includes two adjacent amino acids (Ser-Gly) known to be essential for sulfate binding [].
Publication
First Author: Hryniewicz M
Year: 1990
Journal: J Bacteriol
Title: Sulfate and thiosulfate transport in Escherichia coli K-12: identification of a gene encoding a novel protein involved in thiosulfate binding.
Volume: 172
Issue: 6
Pages: 3358-66
Publication
First Author: Pflugrath JW
Year: 1988
Journal: J Mol Biol
Title: The 2 A resolution structure of the sulfate-binding protein involved in active transport in Salmonella typhimurium.
Volume: 200
Issue: 1
Pages: 163-80
Publication
First Author: Laudenbach DE
Year: 1991
Journal: J Bacteriol
Title: Characterization and mutagenesis of sulfur-regulated genes in a cyanobacterium: evidence for function in sulfate transport.
Volume: 173
Issue: 9
Pages: 2739-50
Publication  
First Author: Rabus R
Year: 1999
Journal: Microbiology
Title: TRAP transporters: an ancient family of extracytoplasmic solute-receptor-dependent secondary active transporters.
Volume: 145 ( Pt 12)
Pages: 3431-45
Publication
First Author: Teixeira SK
Year: 2024
Journal: Sci Adv
Title: Genetic determinants of blood pressure and heart rate identified through ENU-induced mutagenesis with automated meiotic mapping.
Volume: 10
Issue: 9
Pages: eadj9797
HT Experiment
Series Id: GSE19817
Experiment Type: transcription profiling by array
Study Type: Baseline
Source: ArrayExpress
Publication
First Author: Mulligan C
Year: 2011
Journal: FEMS Microbiol Rev
Title: Tripartite ATP-independent periplasmic (TRAP) transporters in bacteria and archaea.
Volume: 35
Issue: 1
Pages: 68-86
Publication
First Author: Fujiwara A
Year: 2014
Journal: J Hypertens
Title: Impaired nitric oxide production and increased blood pressure in systemic heterozygous ATP2B1 null mice.
Volume: 32
Issue: 7
Pages: 1415-23; discussion 1423