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Search results 1 to 100 out of 134 for Phb

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0.052s
Type Details Score
Gene
Type: gene
Organism: Not Specified
Gene
Type: gene
Organism: chicken
Gene
Type: gene
Organism: zebrafish
Protein Domain
Type: Domain
Description: This domain can be found in many bacterial hypothetical proteins. The structures of , PDB:3hsa, and , PDB:3dcx, show similarities to the PH or pleckstrin homology domain. First evidence of PH-like domains in bacteria suggests role in cell envelope stress response [].
Publication
First Author: Xu Q
Year: 2010
Journal: J Mol Biol
Title: Bacterial pleckstrin homology domains: a prokaryotic origin for the PH domain.
Volume: 396
Issue: 1
Pages: 31-46
Ontology Term
Author
Publication
First Author: Zhang LF
Year: 2020
Journal: Nucleic Acids Res
Title: PHB regulates meiotic recombination via JAK2-mediated histone modifications in spermatogenesis.
Volume: 48
Issue: 9
Pages: 4780-4796
Protein Domain
Type: Domain
Description: This entry represents the C terminus of bacterial poly(3-hydroxybutyrate) (PHB) de-polymerase. This degrades PHB granules to oligomers and monomers of 3-hydroxy-butyric acid.
Protein
Organism: Mus musculus/domesticus
Length: 399  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 282  
Fragment?: false
Publication
First Author: Prieto MA
Year: 1999
Journal: J Bacteriol
Title: PhaF, a polyhydroxyalkanoate-granule-associated protein of Pseudomonas oleovorans GPo1 involved in the regulatory expression system for pha genes.
Volume: 181
Issue: 3
Pages: 858-68
Publication
First Author: Gordillo F
Year: 2006
Journal: Mycol Res
Title: Penicillium purpurogenum produces a family 1 acetyl xylan esterase containing a carbohydrate-binding module: characterization of the protein and its gene.
Volume: 110
Issue: Pt 10
Pages: 1129-39
Publication
First Author: Garcia-Conesa MT
Year: 2004
Journal: J Biotechnol
Title: The feruloyl esterase system of Talaromyces stipitatus: production of three discrete feruloyl esterases, including a novel enzyme, TsFaeC, with a broad substrate specificity.
Volume: 108
Issue: 3
Pages: 227-41
Publication
First Author: Saito T
Year: 1989
Journal: J Bacteriol
Title: Cloning, nucleotide sequence, and expression in Escherichia coli of the gene for poly(3-hydroxybutyrate) depolymerase from Alcaligenes faecalis.
Volume: 171
Issue: 1
Pages: 184-9
Protein Domain
Type: Family
Description: This entry describes a group of lipases, including bacterial depolymerases for poly(3-hydroxybutyrate) (PHB) []and related polyhydroxyalkanoates (PHA), as well as acetyl xylan esterases [], and feruloyl esterases from fungi [].
Protein Domain
Type: Domain
Description: The proteins this domain is found in are typically involved in regulating polymer accumulation in bacteria, for example the production of poly-beta-hydroxybutyrate (PHB) which is formed via the polymerisation of D(-)-3-hydroxybutyryl-CoA []. The function ofthis domain is unknown.
GO Term
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein
Organism: Mus musculus/domesticus
Length: 272  
Fragment?: false
GO Term
Publication
First Author: Sugiyama A
Year: 2004
Journal: Curr Microbiol
Title: Roles of poly(3-hydroxybutyrate) depolymerase and 3HB-oligomer hydrolase in bacterial PHB metabolism.
Volume: 48
Issue: 6
Pages: 424-7
GO Term
GO Term
Publication
First Author: Cai GQ
Year: 2000
Journal: J Bacteriol
Title: Requirement for the enzymes acetoacetyl coenzyme A synthetase and poly-3-hydroxybutyrate (PHB) synthase for growth of Sinorhizobium meliloti on PHB cycle intermediates.
Volume: 182
Issue: 8
Pages: 2113-8
GO Term
GO Term
Allele
Name: transgene insertion KL287, GENSAT Project at Rockefeller University
Allele Type: Transgenic
Attribute String: Reporter
Strain
Attribute String: mutant stock, transgenic
Protein Domain
Type: Family
Description: Members of this family are transcriptional regulatory proteins found in the vicinity of poly-beta-hydroxybutyrate (PHB) operons in several species of Bacillus. This protein appears to have repressor activity modulated by PHB itself. This protein belongs to the larger PadR family.
Publication
First Author: Garzia L
Year: 2018
Journal: Cell
Title: A Hematogenous Route for Medulloblastoma Leptomeningeal Metastases.
Volume: 172
Issue: 5
Pages: 1050-1062.e14
Publication
First Author: Richter-Dennerlein R
Year: 2014
Journal: Cell Metab
Title: DNAJC19, a mitochondrial cochaperone associated with cardiomyopathy, forms a complex with prohibitins to regulate cardiolipin remodeling.
Volume: 20
Issue: 1
Pages: 158-71
Publication
First Author: Fernandez DC
Year: 2018
Journal: Cell
Title: Light Affects Mood and Learning through Distinct Retina-Brain Pathways.
Volume: 175
Issue: 1
Pages: 71-84.e18
Publication
First Author: Weil T
Year: 2022
Journal: Sci Adv
Title: Daily changes in light influence mood via inhibitory networks within the thalamic perihabenular nucleus.
Volume: 8
Issue: 23
Pages: eabn3567
Publication
First Author: Li Y
Year: 2016
Journal: Immunity
Title: Analysis of the Rab GTPase Interactome in Dendritic Cells Reveals Anti-microbial Functions of the Rab32 Complex in Bacterial Containment.
Volume: 44
Issue: 2
Pages: 422-37
Publication
First Author: Ande SR
Year: 2009
Journal: Biochem Biophys Res Commun
Title: Prohibitin interacts with phosphatidylinositol 3,4,5-triphosphate (PIP3) and modulates insulin signaling.
Volume: 390
Issue: 3
Pages: 1023-8
Protein Domain
Type: Homologous_superfamily
Description: The band-7 protein family comprises a diverse set of membrane-bound proteins characterised by the presence of a conserved domain, the band-7 domain, also known as SPFH or PHB domain []. The exact function of the band-7 domain is not known, but examples from animal and bacterial stomatin-type proteins demonstrate binding to lipids and the ability to assemble into membrane-bound oligomers that form putative scaffolds []. A variety of proteins belong to this family. These include the prohibitins, cytoplasmic anti-proliferative proteins and stomatin, an erythrocyte membrane protein. Bacterial HflC protein also belongs to this family.Note: Band 4.1 and Band 7 proteins refer to human erythrocyte membrane proteins separated by SDS polyacrylamide gels and stained with coomassie blue [].
Protein Domain
Type: Domain
Description: The band-7 protein family comprises a diverse set of membrane-bound proteins characterised by the presence of a conserved domain, the band-7 domain, also known as SPFH or PHB domain []. The exact function of the band-7 domain is not known, but examples from animal and bacterial stomatin-type proteins demonstrate binding to lipids and the ability to assemble into membrane-bound oligomers that form putative scaffolds []. A variety of proteins belong to this family. These include the prohibitins, cytoplasmic anti-proliferative proteins and stomatin, an erythrocyte membrane protein. Bacterial HflC protein also belongs to this family.Note: Band 4.1 and Band 7 proteins refer to human erythrocyte membrane proteins separated by SDS polyacrylamide gels and stained with coomassie blue [].
Protein
Organism: Mus musculus/domesticus
Length: 340  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 348  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 158  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 185  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 220  
Fragment?: true
Publication
First Author: Ande SR
Year: 2014
Journal: Diabetes
Title: Prohibitin overexpression in adipocytes induces mitochondrial biogenesis, leads to obesity development, and affects glucose homeostasis in a sex-specific manner.
Volume: 63
Issue: 11
Pages: 3734-41
Publication
First Author: He B
Year: 2008
Journal: Mol Endocrinol
Title: A repressive role for prohibitin in estrogen signaling.
Volume: 22
Issue: 2
Pages: 344-60
Publication
First Author: He B
Year: 2011
Journal: Endocrinology
Title: Estrogen-regulated prohibitin is required for mouse uterine development and adult function.
Volume: 152
Issue: 3
Pages: 1047-56
Publication
First Author: Savulescu D
Year: 2013
Journal: Mol Endocrinol
Title: Gonadotropin-releasing hormone-regulated prohibitin mediates apoptosis of the gonadotrope cells.
Volume: 27
Issue: 11
Pages: 1856-70
Publication
First Author: Yang C
Year: 2012
Journal: Genetics
Title: Targeting of >1.5 Mb of human DNA into the mouse X chromosome reveals presence of cis-acting regulators of epigenetic silencing.
Volume: 192
Issue: 4
Pages: 1281-93
Publication
First Author: Nguyen KH
Year: 2016
Journal: Biochem Biophys Res Commun
Title: Obesity-related abnormalities couple environmental triggers with genetic susceptibility in adult-onset T1D.
Volume: 470
Issue: 1
Pages: 94-100
Publication
First Author: Rao CV
Year: 2020
Journal: Aging Cell
Title: GSK3-ARC/Arg3.1 and GSK3-Wnt signaling axes trigger amyloid-β accumulation and neuroinflammation in middle-aged Shugoshin 1 mice.
Volume: 19
Issue: 10
Pages: e13221
Publication
First Author: Kathiria AS
Year: 2013
Journal: Am J Physiol Gastrointest Liver Physiol
Title: Nrf2 is not required for epithelial prohibitin-dependent attenuation of experimental colitis.
Volume: 304
Issue: 10
Pages: G885-96
Publication
First Author: Goo HG
Year: 2014
Journal: Exp Cell Res
Title: HtrA2/Omi influences the stability of LON protease 1 and prohibitin, proteins involved in mitochondrial homeostasis.
Volume: 328
Issue: 2
Pages: 456-65
Publication
First Author: Ande SR
Year: 2016
Journal: Oncogene
Title: Expression of a mutant prohibitin from the aP2 gene promoter leads to obesity-linked tumor development in insulin resistance-dependent manner.
Volume: 35
Issue: 34
Pages: 4459-70
Publication
First Author: Morrow IC
Year: 2002
Journal: J Biol Chem
Title: Flotillin-1/reggie-2 traffics to surface raft domains via a novel golgi-independent pathway. Identification of a novel membrane targeting domain and a role for palmitoylation.
Volume: 277
Issue: 50
Pages: 48834-41
Publication
First Author: Laviola G
Year: 1994
Journal: Psychopharmacology (Berl)
Title: A mouse model of early social interactions after prenatal drug exposure: a genetic investigation.
Volume: 113
Issue: 3-4
Pages: 388-94
Publication
First Author: Huber TB
Year: 2006
Journal: Proc Natl Acad Sci U S A
Title: Podocin and MEC-2 bind cholesterol to regulate the activity of associated ion channels.
Volume: 103
Issue: 46
Pages: 17079-86
Publication
First Author: Theiss AL
Year: 2007
Journal: J Biol Chem
Title: Interleukin-6 transcriptionally regulates prohibitin expression in intestinal epithelial cells.
Volume: 282
Issue: 17
Pages: 12804-12
Publication
First Author: Theiss AL
Year: 2009
Journal: Mol Biol Cell
Title: Prohibitin inhibits tumor necrosis factor alpha-induced nuclear factor-kappa B nuclear translocation via the novel mechanism of decreasing importin alpha3 expression.
Volume: 20
Issue: 20
Pages: 4412-23
Publication
First Author: Kathiria AS
Year: 2012
Journal: Cancer Res
Title: Prohibitin attenuates colitis-associated tumorigenesis in mice by modulating p53 and STAT3 apoptotic responses.
Volume: 72
Issue: 22
Pages: 5778-89
Publication  
First Author: Zi Xu YX
Year: 2018
Journal: Cancer Lett
Title: Prohibitin: A new player in immunometabolism and in linking obesity and inflammation with cancer.
Volume: 415
Pages: 208-216
Publication
First Author: Theiss AL
Year: 2009
Journal: Gastroenterology
Title: Prohibitin is a novel regulator of antioxidant response that attenuates colonic inflammation in mice.
Volume: 137
Issue: 1
Pages: 199-208, 208.e1-6
Protein
Organism: Mus musculus/domesticus
Length: 353  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 212  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 286  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 287  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 299  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 428  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 241  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 428  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 104  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 428  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 207  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 217  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 428  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 196  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 271  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 299  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 192  
Fragment?: true
Publication
First Author: Too IHK
Year: 2018
Journal: PLoS Pathog
Title: Prohibitin plays a critical role in Enterovirus 71 neuropathogenesis.
Volume: 14
Issue: 1
Pages: e1006778
Protein
Organism: Mus musculus/domesticus
Length: 385  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 395  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 85  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 385  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 150  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 395  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 265  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 159  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 395  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 251  
Fragment?: true
Publication  
First Author: Gehl B
Year: 2014
Journal: Front Plant Sci
Title: Mitochondrial Band-7 family proteins: scaffolds for respiratory chain assembly?
Volume: 5
Pages: 141
Publication
First Author: de Almeida A
Year: 2007
Journal: Appl Environ Microbiol
Title: Effects of granule-associated protein PhaP on glycerol-dependent growth and polymer production in poly(3-hydroxybutyrate)-producing Escherichia coli.
Volume: 73
Issue: 24
Pages: 7912-6
Publication
First Author: Neumann L
Year: 2008
Journal: J Bacteriol
Title: Binding of the major phasin, PhaP1, from Ralstonia eutropha H16 to poly(3-hydroxybutyrate) granules.
Volume: 190
Issue: 8
Pages: 2911-9
Publication
First Author: Pötter M
Year: 2004
Journal: Microbiology
Title: The complex structure of polyhydroxybutyrate (PHB) granules: four orthologous and paralogous phasins occur in Ralstonia eutropha.
Volume: 150
Issue: Pt 7
Pages: 2301-11
Publication
First Author: Korotkova N
Year: 2002
Journal: J Bacteriol
Title: Poly-beta-hydroxybutyrate biosynthesis in the facultative methylotroph methylobacterium extorquens AM1: identification and mutation of gap11, gap20, and phaR.
Volume: 184
Issue: 22
Pages: 6174-81
Protein Domain
Type: Domain
Description: Phasins (or granule-associate proteins) are surface proteins found covering Polyhydroxyalkanoate (PHA) storage granules in bacteria. Polyhydroxyalkanoates are linear polyesters produced by bacterial fermentation of sugar or lipids for the purpose of storing carbon and energy, and are accumulated as intracellular granules by many bacteria under unfavorable conditions, enhancing their fitness and stress resistance []. The layer of phasins stabilises the granules and prevents coalescence of separated granules in the cytoplasm and nonspecific binding of other proteins to the hydrophobic surfaces of the granules. For example, in Ralstonia eutropha (strain ATCC 17699/H16/DSM 428/Stanier 337) (Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)), the major surface protein of polyhydroxybutyrate (PHB) granules is phasin PhaP1(Reu), which occurs along with three homologues (PhaP2, PhaP3, and PhaP4) that have the capacity to bind to PHB granules but are present at minor levels [, ]. These four phasins lack a highly conserved domain but share homologous hydrophobic regions. This entry describes a group of phasins that associate with polyhydroxyalkanoate (PHA) inclusions, the most common of which consist of polyhydroxybutyrate (PHB).
Protein Domain
Type: Family
Description: Phasins (or granule-associate proteins) are surface proteins found covering Polyhydroxyalkanoate (PHA) storage granules in bacteria. Polyhydroxyalkanoates are linear polyesters produced by bacterial fermentation of sugar or lipids for the purpose of storing carbon and energy, and are accumulated as intracellular granules by many bacteria under unfavorable conditions, enhancing their fitness and stress resistance []. The layer of phasins stabilises the granules and prevents coalescence of separated granules in the cytoplasm and nonspecific binding of other proteins to the hydrophobic surfaces of the granules. For example, in Ralstonia eutropha (strain ATCC 17699/H16/DSM 428/Stanier 337) (Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)), the major surface protein of polyhydroxybutyrate (PHB) granules is phasin PhaP1(Reu), which occurs along with three homologues (PhaP2, PhaP3, and PhaP4) that have the capacity to bind to PHB granules but are present at minor levels [, ]. These four phasins lack a highly conserved domain but share homologous hydrophobic regions. Members of this entry are encoded in polyhydroxyalkanoic acid storage system regions in a number of Vibrio species, including Vibrio cholerae V52, Photobacterium profundum SS9, Acinetobacter sp., and Aeromonas hydrophila. Members appear distantly related to the phasin family, see: and .
Protein Domain
Type: Family
Description: Phasins (or granule-associate proteins) are surface proteins found covering Polyhydroxyalkanoate (PHA) storage granules in bacteria. Polyhydroxyalkanoates are linear polyesters produced by bacterial fermentation of sugar or lipids for the purpose of storing carbon and energy, and are accumulated as intracellular granules by many bacteria under unfavorable conditions, enhancing their fitness and stress resistance []. The layer of phasins stabilises the granules and prevents coalescence of separated granules in the cytoplasm and nonspecific binding of other proteins to the hydrophobic surfaces of the granules. For example, in Ralstonia eutropha (strain ATCC 17699/H16/DSM 428/Stanier 337) (Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)), the major surface protein of polyhydroxybutyrate (PHB) granules is phasin PhaP1(Reu), which occurs along with three homologues (PhaP2, PhaP3, and PhaP4) that have the capacity to bind to PHB granules but are present at minor levels [, ]. These four phasins lack a highly conserved domain but share homologous hydrophobic regions. This entry describes a group of phasins associated with polyhydroxyalkanoate (PHA) inclusions, the most common of which consist of polyhydroxybutyrate (PHB). However, the member from Magnetospirillum sp. (strain AMB-1) is called a magnetic particle membrane-specific GTPase.
Protein Domain
Type: Family
Description: Phasins (or granule-associate proteins) are surface proteins found covering Polyhydroxyalkanoate (PHA) storage granules in bacteria. Polyhydroxyalkanoates are linear polyesters produced by bacterial fermentation of sugar or lipids for the purpose of storing carbon and energy, and are accumulated as intracellular granules by many bacteria under unfavorable conditions, enhancing their fitness and stress resistance []. The layer of phasins stabilises the granules and prevents coalescence of separated granules in the cytoplasm and nonspecific binding of other proteins to the hydrophobic surfaces of the granules. For example, in Ralstonia eutropha (strain ATCC 17699/H16/DSM 428/Stanier 337) (Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)), the major surface protein of polyhydroxybutyrate (PHB) granules is phasin PhaP1(Reu), which occurs along with three homologues (PhaP2, PhaP3, and PhaP4) that have the capacity to bind to PHB granules but are present at minor levels [, ]. These four phasins lack a highly conserved domain but share homologous hydrophobic regions. This entry represents a family of phasins that are part of the polyhydroxyalkanoate synthesis machinery []. Members of this family are related to .
Protein
Organism: Mus musculus/domesticus
Length: 428  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 428  
Fragment?: false