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Search results 101 to 135 out of 135 for Phb

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Type Details Score
Protein
Q540I4
Organism: Mus musculus/domesticus
Length: 428  
Fragment?: false
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Protein
Q3UEG9
Organism: Mus musculus/domesticus
Length: 456  
Fragment?: false
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Protein
Q3TJS0
Organism: Mus musculus/domesticus
Length: 428  
Fragment?: false
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Protein
G3UYU4
Organism: Mus musculus/domesticus
Length: 380  
Fragment?: false
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Publication
10542406 | -
First Author: Tavernarakis N
Year: 1999
Journal: Trends Biochem Sci
Title: The SPFH domain: implicated in regulating targeted protein turnover in stomatins and other membrane-associated proteins.
Volume: 24
Issue: 11
Pages: 425-7
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Publication
4326772 | -
First Author: Fairbanks G
Year: 1971
Journal: Biochemistry
Title: Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane.
Volume: 10
Issue: 13
Pages: 2606-17
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Protein
Q6PE84
Organism: Mus musculus/domesticus
Length: 287  
Fragment?: false
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Protein
Q8CI66
Organism: Mus musculus/domesticus
Length: 399  
Fragment?: false
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Protein
F6QPR1
Organism: Mus musculus/domesticus
Length: 157  
Fragment?: true
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Protein
Q3V2V2
Organism: Mus musculus/domesticus
Length: 180  
Fragment?: false
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Protein
Q99L68
Organism: Mus musculus/domesticus
Length: 197  
Fragment?: false
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Protein
A0A0B4J1F1
Organism: Mus musculus/domesticus
Length: 399  
Fragment?: false
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Protein
B2RS16
Organism: Mus musculus/domesticus
Length: 287  
Fragment?: false
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Protein
P54116
Organism: Mus musculus/domesticus
Length: 284  
Fragment?: false
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Protein
A0A1L1STP7
Organism: Mus musculus/domesticus
Length: 68  
Fragment?: true
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Protein
A0A1L1STX8
Organism: Mus musculus/domesticus
Length: 94  
Fragment?: false
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Protein Domain
IPR043202 | Band-7_stomatin-like
Type: Family
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 the band-7 family. These include the stomatins, prohibitins, flottins and the HflK/C bacterial proteins. Eukaryotic band 7 proteins tend to be oligomeric and are involved in membrane-associated processes. Stomatins are involved in ion channel function, prohibitins are involved in modulating the activity of a membrane-bound FtsH protease and the assembly of mitochondrial respiratory complexes, and flotillins are involved in signal transduction and vesicle trafficking [].Stomatin, also known as human erythrocyte membrane protein band 7.2b [], was first identified in the band 7 region of human erythrocyte membrane proteins. It is an oligomeric, monotopic membrane protein associated with cholesterol-rich membranes/lipid rafts. Human stomatin is ubiquitously expressed in all tissues; highly in hematopoietic cells, relatively low in brain. It is associated with the plasma membrane and cytoplasmic vesicles of fibroblasts, epithelial and endothelial cells [].Stomatin is believed to be involved in regulating monovalent cation transport through lipid membranes. Absence of the protein in hereditary stomatocytosis is believed to be the reason for the leakage of Na+and K+ions into and from erythrocytes []. Stomatin is also expressed in mechanosensory neurons, where it may interact directly with transduction components, including cation channels [].Stomatin proteins have been identified in various organisms, including Caenorhabditis elegans. There are nine stomatin-like proteins in C. elegans, MEC-2 being the one best characterised []. In mammals, other stomatin family members are stomatin-like proteins SLP1, SLP2 and SLP3, and NPHS2 (podocin), which display selective expression patterns []. Stomatin family members are oligomeric, they mostly localise to membrane domains, and in many cases have been shown to modulate ion channel activity.The stomatins and prohibitins, and to a lesser extent flotillins, are highly conserved protein families and are found in a variety of organisms ranging from prokaryotes to higher eukaryotes, whereas HflK and HflC homologues are only present in bacteria [].This entry represents the stomatins and stomatin-like proteins, including podicin, from a wide range of eukaryotes, bacteria, archaea and viruses. It excludes the HflK and HflC proteins, prohibitins and flotillins.
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Protein Domain
IPR001972 | Stomatin_HflK_HflKC_fam
Type: Family
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 the band-7 family. These include the stomatins, prohibitins, flottins and the HflK/C bacterial proteins. Eukaryotic band 7 proteins tend to be oligomeric and are involved in membrane-associated processes. Stomatins are involved in ion channel function, prohibitins are involved in modulating the activity of a membrane-bound FtsH protease and the assembly of mitochondrial respiratory complexes, and flotillins are involved in signal transduction and vesicle trafficking [].Stomatin, also known as human erythrocyte membrane protein band 7.2b [], was first identified in the band 7 region of human erythrocyte membrane proteins. It is an oligomeric, monotopic membrane protein associated with cholesterol-rich membranes/lipid rafts. Human stomatin is ubiquitously expressed in all tissues; highly in hematopoietic cells, relatively low in brain. It is associated with the plasma membrane and cytoplasmic vesicles of fibroblasts, epithelial and endothelial cells [].Stomatin is believed to be involved in regulating monovalent cation transport through lipid membranes. Absence of the protein in hereditary stomatocytosis is believed to be the reason for the leakage of Na+and K+ions into and from erythrocytes []. Stomatin is also expressed in mechanosensory neurons, where it may interact directly with transduction components, including cation channels [].Stomatin proteins have been identified in various organisms, including Caenorhabditis elegans. There are nine stomatin-like proteins in C. elegans, MEC-2 being the one best characterised []. In mammals, other stomatin family members are stomatin-like proteins SLP1, SLP2 and SLP3, and NPHS2 (podocin), which display selective expression patterns []. Stomatin family members are oligomeric, they mostly localise to membrane domains, and in many cases have been shown to modulate ion channel activity.The stomatins and prohibitins, and to a lesser extent flotillins, are highly conserved protein families and are found in a variety of organisms ranging from prokaryotes to higher eukaryotes, whereas HflK and HflC homologues are only present in bacteria [].This entry matches Stomatin, HflK and HflC proteins.
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Publication
15471860 | -
First Author: Price MP
Year: 2004
Journal: J Biol Chem
Title: Stomatin modulates gating of acid-sensing ion channels.
Volume: 279
Issue: 51
Pages: 53886-91
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Publication
12239636 | J:174835
First Author: Goldstein BJ
Year: 2003
Journal: J Assoc Res Otolaryngol
Title: Cloning and characterization of SLP3: a novel member of the stomatin family expressed by olfactory receptor neurons.
Volume: 4
Issue: 1
Pages: 74-82
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Publication
21501885 | -
First Author: Lapatsina L
Year: 2012
Journal: Eur J Cell Biol
Title: Stomatin-domain proteins.
Volume: 91
Issue: 4
Pages: 240-5
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Publication
28575093 | -
First Author: Rungaldier S
Year: 2017
Journal: PLoS One
Title: Structure-function analysis of human stomatin: A mutation study.
Volume: 12
Issue: 6
Pages: e0178646
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Publication
19684140 | -
First Author: Boehm M
Year: 2009
Journal: J Bacteriol
Title: Structural and mutational analysis of band 7 proteins in the cyanobacterium Synechocystis sp. strain PCC 6803.
Volume: 191
Issue: 20
Pages: 6425-35
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Publication
9147127 | -
First Author: Stewart GW
Year: 1997
Journal: Int J Biochem Cell Biol
Title: Stomatin.
Volume: 29
Issue: 2
Pages: 271-4
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Protein
Q9EQK5
Organism: Mus musculus/domesticus
Length: 861  
Fragment?: false
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Protein
Q8C2S9
Organism: Mus musculus/domesticus
Length: 870  
Fragment?: false
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Protein
E9Q3X0
Organism: Mus musculus/domesticus
Length: 870  
Fragment?: false
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Protein
Q3THX5
Organism: Mus musculus/domesticus
Length: 870  
Fragment?: false
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Publication
12466851 | J:80000
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
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Publication
11217851 | J:65060
First Author: Kawai J
Year: 2001
Journal: Nature
Title: Functional annotation of a full-length mouse cDNA collection.
Volume: 409
Issue: 6821
Pages: 685-90
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Publication
11042159 | J:68323
First Author: Carninci P
Year: 2000
Journal: Genome Res
Title: Normalization and subtraction of cap-trapper-selected cDNAs to prepare full-length cDNA libraries for rapid discovery of new genes.
Volume: 10
Issue: 10
Pages: 1617-30
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Publication
10349636 | J:80645
 
First Author: Carninci P
Year: 1999
Journal: Methods Enzymol
Title: High-efficiency full-length cDNA cloning.
Volume: 303
Pages: 19-44
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Publication
11076861 | J:68324
First Author: Shibata K
Year: 2000
Journal: Genome Res
Title: RIKEN integrated sequence analysis (RISA) system--384-format sequencing pipeline with 384 multicapillary sequencer.
Volume: 10
Issue: 11
Pages: 1757-71
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Publication
16141073 | -
First Author: Katayama S
Year: 2005
Journal: Science
Title: Antisense transcription in the mammalian transcriptome.
Volume: 309
Issue: 5740
Pages: 1564-6
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Publication
- | J:100256
     
First Author: The Gene Expression Nervous System Atlas (GENSAT) Project, The Rockefeller University (New York, NY)
Year: 2005
Journal: Database Download
Title: MGI download of GENSAT transgene data
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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