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Search results 101 to 195 out of 195 for Rp1

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Hits by Strain

Type Details Score
Protein
P56716
Organism: Mus musculus/domesticus
Length: 2095  
Fragment?: false
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Allele
Rp1<tm1Jnz> | MGI:2179129
 
Name: retinitis pigmentosa 1 (human); targeted mutation 1, Jian Zuo
Allele Type: Targeted
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Allele
Rp1<m1Jdun> | MGI:5604910
 
Name: retinitis pigmentosa 1 (human); mutation 1, Joshua L Dunaief
Allele Type: Spontaneous
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Publication
2559940 | -
First Author: Fong ST
Year: 1989
Journal: J Gen Microbiol
Title: Location and characterization of two functions on RP1 that inhibit the fertility of the IncW plasmid R388.
Volume: 135
Issue: 3
Pages: 499-502
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Allele
Rp1<em1Smoc> | MGI:7292105
Name: retinitis pigmentosa 1 (human); endonuclease-mediated mutation 1, Shanghai Model Organisms Center
Allele Type: Endonuclease-mediated
Attribute String: Null/knockout
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Genotype
Genotype
Symbol: Rp1/Rp1
Background: involves: 129S7/SvEvBrd
Zygosity: hm
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Rp1/Rp1
Background: C57BL/6-Rp1
Zygosity: hm
Has Mutant Allele: true
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Strain
MGI:6355159 | C57BL/6JSmoc-Rp1<em1Smoc>/Smoc
Attribute String: coisogenic, mutant strain, endonuclease-mediated mutation
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Protein Coding Gene
MGI:106271 | Mapre2
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:88611 | Cyp4a10
Type: protein_coding_gene
Organism: mouse, laboratory
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HT Experiment
GSE127 | P21 knockout
 
Experiment Type: transcription profiling by array
Study Type: WT vs. Mutant
Source: GEO
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HT Experiment
GSE126 | P18 knockout
 
Experiment Type: transcription profiling by array
Study Type: WT vs. Mutant
Source: GEO
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HT Experiment
GSE123 | P7 knockout
 
Experiment Type: transcription profiling by array
Study Type: WT vs. Mutant
Source: GEO
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HT Experiment
GSE124 | P10 knockout
 
Experiment Type: transcription profiling by array
Study Type: WT vs. Mutant
Source: GEO
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HT Experiment
GSE125 | P14 knockout
 
Experiment Type: transcription profiling by array
Study Type: WT vs. Mutant
Source: GEO
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Protein Domain
IPR021915 | RP1-2
Type: Domain
Description: Spiders use fibroins to make silk strands. This family includes tubuliform silk fibroins which are used to protect egg cases. This domain is a structural domain which is found in repeats of up to 20 in many individuals (although this is not necessarily the case). RP1 makes up structural domains in the N-terminal while RP2 makes up structural domains in the C-terminal [].
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Protein Domain
IPR026565 | PPDK_reg
Type: Family
Description: This is a family of proteins which are putative bifunctional serine/threonine kinase/phosphorylases involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalysing its phosphorylation/dephosphorylation [, ]. In plants, the pyruvate, phosphate dikinase regulatory protein 1 (RP1) is a bifunctional serine/threonine kinase and phosphorylase involved in the dark/light-mediated regulation of PPDK by catalysing its phosphorylation/dephosphorylation. In the dark, RP1 phosphorylates the catalytic intermediate of PPDK (PPDK-HisP), inactivating it. Light exposure induces the phosphorolysis reaction that reactivates PPDK [, , , ].
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Protein Domain
IPR027735 | RP1/EB2_vertebrate
Type: Family
Description: Microtubule-associated protein RP/EB family member 2 (also known as RP1 or EB2) belongs to the RP/EB family, which consists of MAPRE1 (EB1), MAPRE2 (RP1, also known as EB2) and MAPRE3 (EBF3, also known as EB3). Unlike EB1 and EB3, EB2 does not promote persistent microtubule growth by suppressing catastrophes []. It has been shown that MAPRE2 is highly expressed in pancreatic cancer cells, and seems to be involved in perineural invasion [].
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Publication
16614481 | J:115839
First Author: Kumar A
Year: 2006
Journal: Biofactors
Title: Evaluation of chemopreventive action of Ginsenoside Rp1.
Volume: 26
Issue: 1
Pages: 29-43
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Publication
17996018 | -
First Author: Chastain CJ
Year: 2008
Journal: Plant J
Title: The pyruvate, orthophosphate dikinase regulatory proteins of Arabidopsis possess a novel, unprecedented Ser/Thr protein kinase primary structure.
Volume: 53
Issue: 5
Pages: 854-63
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Publication
15489437 | -
First Author: Lee LY
Year: 2004
Journal: J Bacteriol
Title: Osa protein constitutes a strong oncogenic suppression system that can block vir-dependent transfer of IncQ plasmids between Agrobacterium cells and the establishment of IncQ plasmids in plant cells.
Volume: 186
Issue: 21
Pages: 7254-61
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Publication
1832152 | -
First Author: Close SM
Year: 1991
Journal: J Bacteriol
Title: The osa gene of pSa encodes a 21.1-kilodalton protein that suppresses Agrobacterium tumefaciens oncogenicity.
Volume: 173
Issue: 17
Pages: 5449-56
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Publication
15547285 | -
First Author: Mohd-Zain Z
Year: 2004
Journal: J Bacteriol
Title: Transferable antibiotic resistance elements in Haemophilus influenzae share a common evolutionary origin with a diverse family of syntenic genomic islands.
Volume: 186
Issue: 23
Pages: 8114-22
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Publication
16194240 | -
First Author: Cascales E
Year: 2005
Journal: Mol Microbiol
Title: Agrobacterium tumefaciens oncogenic suppressors inhibit T-DNA and VirE2 protein substrate binding to the VirD4 coupling protein.
Volume: 58
Issue: 2
Pages: 565-79
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Protein Domain
IPR035615 | FiwA/Osa
Type: Family
Description: Osa and FiwA are fertility inhibition factors (FIN), which are employed by plasmids to block import of rival plasmids []. Osa (oncogenic suppressive activity) of IncW group plasmid pSa gene inhibits the oncogenic properties of Agrobacterium tumefaciens. Osa is structurally similar to the ParB N-terminal domain/Srx superfamily of proteins: ParB acts in the bacterial and plasmid parABS partitioning systems []. Osa has been shown to have ATPase and DNAse activities, and can block T-DNA transfer into plants [, ]. FiwA is encoded by plasmid RP1 and blocks the transfer of plasmid R388 []. The gene product of Haemophilus influenzae p1056.10c also blocks T-DNA transfer [].
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Publication
19458259 | -
First Author: Lin Z
Year: 2009
Journal: Proc Natl Acad Sci U S A
Title: Solution structure of eggcase silk protein and its implications for silk fiber formation.
Volume: 106
Issue: 22
Pages: 8906-11
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Publication
8185929 | J:17141
First Author: Green GR
Year: 1994
Journal: Mol Reprod Dev
Title: Synthesis and processing of mammalian protamines and transition proteins.
Volume: 37
Issue: 3
Pages: 255-63
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Publication
10391212 | J:75362
First Author: Sullivan LS
Year: 1999
Journal: Nat Genet
Title: Mutations in a novel retina-specific gene cause autosomal dominant retinitis pigmentosa.
Volume: 22
Issue: 3
Pages: 255-9
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Publication
9233623 | J:41637
First Author: Renner C
Year: 1997
Journal: J Immunol
Title: RP1, a new member of the adenomatous polyposis coli-binding EB1-like gene family, is differentially expressed in activated T cells.
Volume: 159
Issue: 3
Pages: 1276-83
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Publication
12724644 | J:83424
 
First Author: Bowne SJ
Year: 2003
Journal: Mol Vis
Title: Characterization of RP1L1, a highly polymorphic paralog of the retinitis pigmentosa 1 (RP1) gene.
Volume: 9
Pages: 129-37
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Publication
10686478 | J:68853
First Author: Yang Z
Year: 2000
Journal: Exp Clin Immunogenet
Title: Organizations and gene duplications of the human and mouse MHC complement gene clusters.
Volume: 17
Issue: 1
Pages: 1-17
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Publication
10533048 | J:65156
First Author: Burgess HA
Year: 1999
Journal: J Neurosci Res
Title: KIAA0369, doublecortin-like kinase, is expressed during brain development.
Volume: 58
Issue: 4
Pages: 567-75
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Publication
16684769 | J:114886
First Author: Ohmae S
Year: 2006
Journal: J Biol Chem
Title: Molecular identification and characterization of a family of kinases with homology to Ca2+/calmodulin-dependent protein kinases I/IV.
Volume: 281
Issue: 29
Pages: 20427-39
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Protein
Q9D1B8
Organism: Mus musculus/domesticus
Length: 347  
Fragment?: false
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Protein
J3KML0
Organism: Mus musculus/domesticus
Length: 287  
Fragment?: false
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Protein
K3W4L8
Organism: Mus musculus/domesticus
Length: 347  
Fragment?: false
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Protein
A0A1Y7VIY3
Organism: Mus musculus/domesticus
Length: 622  
Fragment?: true
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Protein
F7BCK0
Organism: Mus musculus/domesticus
Length: 340  
Fragment?: true
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Protein
A0A1Y7VLK4
Organism: Mus musculus/domesticus
Length: 376  
Fragment?: false
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Publication
10749977 | -
First Author: Sapir T
Year: 2000
Journal: Hum Mol Genet
Title: Doublecortin mutations cluster in evolutionarily conserved functional domains.
Volume: 9
Issue: 5
Pages: 703-12
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Publication
10441322 | -
First Author: Horesh D
Year: 1999
Journal: Hum Mol Genet
Title: Doublecortin, a stabilizer of microtubules.
Volume: 8
Issue: 9
Pages: 1599-610
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Protein
Q3UEX7
Organism: Mus musculus/domesticus
Length: 302  
Fragment?: true
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Protein
Q9QZY0
Organism: Mus musculus/domesticus
Length: 1026  
Fragment?: true
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Publication
16696949 | -
First Author: Burnell JN
Year: 2006
Journal: Biochem Biophys Res Commun
Title: Cloning and expression of maize-leaf pyruvate, Pi dikinase regulatory protein gene.
Volume: 345
Issue: 2
Pages: 675-80
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Publication
10683263 | -
First Author: Chastain CJ
Year: 2000
Journal: Arch Biochem Biophys
Title: Further analysis of maize C(4) pyruvate,orthophosphate dikinase phosphorylation by its bifunctional regulatory protein using selective substitutions of the regulatory Thr-456 and catalytic His-458 residues.
Volume: 375
Issue: 1
Pages: 165-70
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Publication
6326674 | -
First Author: Burnell JN
Year: 1984
Journal: Arch Biochem Biophys
Title: Regulation of C4 photosynthesis: identification of a catalytically important histidine residue and its role in the regulation of pyruvate,Pi dikinase.
Volume: 231
Issue: 1
Pages: 175-82
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Publication
2834385 | -
First Author: Roeske CA
Year: 1988
Journal: J Biol Chem
Title: Sequence of the phosphothreonyl regulatory site peptide from inactive maize leaf pyruvate, orthophosphate dikinase.
Volume: 263
Issue: 14
Pages: 6683-7
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Publication
25358815 | -
 
First Author: Maindola P
Year: 2014
Journal: Nat Commun
Title: Multiple enzymatic activities of ParB/Srx superfamily mediate sexual conflict among conjugative plasmids.
Volume: 5
Pages: 5322
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Publication
20826268 | -
First Author: Akahori M
Year: 2010
Journal: Am J Hum Genet
Title: Dominant mutations in RP1L1 are responsible for occult macular dystrophy.
Volume: 87
Issue: 3
Pages: 424-9
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Publication
23129012 | -
First Author: Wang S
Year: 2012
Journal: J Biomol NMR
Title: NMR structure note: repetitive domain of aciniform spidroin 1 from Nephila antipodiana.
Volume: 54
Issue: 4
Pages: 415-20
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Protein Domain
IPR036572 | Doublecortin_dom_sf
Type: Homologous_superfamily
Description: X-linked lissencephaly is a severe brain malformation affecting males. Recently it has been demonstrated that the doublecortin gene is implicated in this disorder []. Doublecortin was found to bind to the microtubule cytoskeleton. In vivo and in vitro assays show that Doublecortin stabilises microtubules and causes bundling []. Doublecortin is a basic protein with an iso-electric point of 10, typical of microtubule-binding proteins. However, its sequence contains no known microtubule-binding domain(s).The detailed sequence analysis of Doublecortin and Doublecortin-like proteins allowed the identification of an evolutionarily conserved Doublecortin (DC) domain, which is ubiquitin-like. This domain is found in the N terminus of proteins and consists of one or two tandemly repeated copies of an around 80 amino acids region. It has been suggested that the first DC domain of Doublecortin binds tubulin and enhances microtubule polymerisation [].Some proteins known to contain a DC domain are listed below:Doublecortin. It is required for neuronal migration []. A large number of point mutations in the human DCX gene leading to lissencephaly are located within the DC domains [].Human serine/threonine-protein kinase DCAMKL1. It is a probable kinase that may be involved in a calcium-signaling pathway controlling neuronal migration in the developing brain [, ].Retinitis pigmentosa 1 protein. It is required for the differentiation of photoreceptor cells. Mutation in the human RP1 gene cause retinitis pigmentosa of type 1 [, ].
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Protein Domain
IPR040163 | RP1/RP1L1/DCX
Type: Family
Description: This entry includes oxygen-regulated protein 1 (RP1), retinitis pigmentosa 1-like 1 (RP1L1) and neuronal migration protein doublecortin (DCX).Oxygen-regulated protein 1 (also known as retinitis pigmentosa 1, RP1) is a photoreceptor-specific, microtubule-associated ciliary protein containing the doublecortin (DCX) domain. Together with RP1L1, they play essential and synergistic roles in affecting photosensitivity and outer segment morphogenesis of rod photoreceptors [].Mutations in the RP1 gene account for 5-10% of cases of autosomal dominant retinitis pigmentosa, a disease characterised by late-onset night blindness, loss of peripheral vision, and diminished or absent electroretinogram (ERG) responses [].Mutations in the RP1L1 gene cause occult macular dystrophy (OCMD), an inherited macular dystrophy characterised by progressive loss of macular function but normal ophthalmoscopic appearance []. Neuronal migration protein doublecortin (DCX; also known as Lissencephalin-X) seems to be required for the initial steps of neuronal dispersion and cortex lamination during cerebral cortex development []. This protein may act by competing with the putative neuronal protein kinase DCAMKL1 in binding to a target protein, and thereby participate in a signalling pathway that is crucial for neuronal interaction before and during migration, possibly as part of a calcium ion-dependent signal transduction pathway. It may also be involved with LIS-1 in an overlapping, but distinct, signalling pathways that promotes neuronal migration. Defects in neuronal migration protein doublecortin are the cause of lissencephaly X-linked type 1 (LISX1), a classic lissencephaly characterised by mental retardation and seizures that are more severe in male patients [, ].
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Protein Domain
IPR003533 | Doublecortin_dom
Type: Domain
Description: X-linked lissencephaly is a severe brain malformation affecting males. Recently it has been demonstrated that the doublecortin gene is implicated in this disorder []. Doublecortin was found to bind to the microtubule cytoskeleton. In vivo and in vitro assays show that Doublecortin stabilises microtubules and causes bundling []. Doublecortin is a basic protein with an iso-electric point of 10, typical of microtubule-binding proteins. However, its sequence contains no known microtubule-binding domain(s).The detailed sequence analysis of Doublecortin and Doublecortin-like proteins allowed the identification of an evolutionarily conserved Doublecortin (DC) domain, which is ubiquitin-like. This domain is found in the N terminus of proteins and consists of one or two tandemly repeated copies of an around 80 amino acids region. It has been suggested that the first DC domain of Doublecortin binds tubulin and enhances microtubule polymerisation [].Some proteins known to contain a DC domain are listed below:Doublecortin. It is required for neuronal migration []. A large number of point mutations in the human DCX gene leading to lissencephaly are located within the DC domains [].Human serine/threonine-protein kinase DCAMKL1. It is a probable kinase that may be involved in a calcium-signaling pathway controlling neuronal migration in the developing brain [, ].Retinitis pigmentosa 1 protein. It is required for the differentiation of photoreceptor cells. Mutation in the human RP1 gene cause retinitis pigmentosa of type 1 [, ].
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Protein Domain
IPR043070 | Spidroin_repeat
Type: Homologous_superfamily
Description: Spidroins are large silk proteins which display relatively conserved terminal domains and a characteristic core repetitive region that amounts to around 90 % of the full length sequence and is believed to dominate the mechanical properties of spider silk. Spidroins are secreted into silk glands and then stably stored where their concentration increases up to 50 % (w/w) allowing them to self-assemble into silk fibres. Spider silks are renowned for their excellent mechanical properties and biomimetic and industrial potentials. The orb-web spiders employ up to seven types of abdominal glands to produce silks for various purposes, ranging from prey capture to offspring protection in egg cases. Egg-case silk fibroins are synthesised only in female tubuliform (cylindrical) silk glands for the construction of protective egg cases, where eggs undergo development. Two spidroins, tubliform spidroin (TuSp1), the major component of egg-case silk, and the recently characterised aciniform spidroin (AcSp1) participate in the egg case formation: AcSp1 forms the inner egg case, while TuSp1 forms the outer egg case. Studies on both proteins have revealed poor sequence similarity between their respective repetitive (RP) domains but a remarkable structural identity. The latter suggests that these two spidroins may share some common characters in fibre formation mechanism and silk fibre properties [, ].This superfamily represents a structural domain which is found in repeats of up to 20 in many individuals (although this is not necessarily the case). RP1 makes up structural domains in the N terminus while RP2 makes up structural domains in the C terminus [].
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Protein
Q5DU00
Organism: Mus musculus/domesticus
Length: 475  
Fragment?: false
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Protein
Q8VDT3
Organism: Mus musculus/domesticus
Length: 363  
Fragment?: false
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Protein
Q3UGP0
Organism: Mus musculus/domesticus
Length: 363  
Fragment?: false
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Protein
R4GML1
Organism: Mus musculus/domesticus
Length: 475  
Fragment?: false
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Protein
Q8BRN4
Organism: Mus musculus/domesticus
Length: 379  
Fragment?: false
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Protein
Q80VB6
Organism: Mus musculus/domesticus
Length: 363  
Fragment?: false
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Protein
A2BHQ5
Organism: Mus musculus/domesticus
Length: 186  
Fragment?: false
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Protein
Q8CEB0
Organism: Mus musculus/domesticus
Length: 148  
Fragment?: false
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Publication
19787265 | -
First Author: Abiatari I
Year: 2009
Journal: Int J Oncol
Title: The microtubule-associated protein MAPRE2 is involved in perineural invasion of pancreatic cancer cells.
Volume: 35
Issue: 5
Pages: 1111-6
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Protein
O88809
Organism: Mus musculus/domesticus
Length: 366  
Fragment?: false
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Protein
Q8CGM2
Organism: Mus musculus/domesticus
Length: 1859  
Fragment?: false
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Protein
Q8C852
Organism: Mus musculus/domesticus
Length: 379  
Fragment?: false
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Protein
Q3V349
Organism: Mus musculus/domesticus
Length: 331  
Fragment?: false
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Protein
A1L340
Organism: Mus musculus/domesticus
Length: 1859  
Fragment?: false
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Protein
A0A0G2JGR9
Organism: Mus musculus/domesticus
Length: 111  
Fragment?: true
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Protein
Q8BXR8
Organism: Mus musculus/domesticus
Length: 769  
Fragment?: true
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Protein
Q6PGI2
Organism: Mus musculus/domesticus
Length: 365  
Fragment?: false
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Protein
Q9CXL6
Organism: Mus musculus/domesticus
Length: 360  
Fragment?: false
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Publication
9489699 | -
First Author: des Portes V
Year: 1998
Journal: Cell
Title: A novel CNS gene required for neuronal migration and involved in X-linked subcortical laminar heterotopia and lissencephaly syndrome.
Volume: 92
Issue: 1
Pages: 51-61
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Protein
D6RH42
Organism: Mus musculus/domesticus
Length: 135  
Fragment?: false
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Publication
9489700 | -
First Author: Gleeson JG
Year: 1998
Journal: Cell
Title: Doublecortin, a brain-specific gene mutated in human X-linked lissencephaly and double cortex syndrome, encodes a putative signaling protein.
Volume: 92
Issue: 1
Pages: 63-72
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Publication
18231966 | J:134646
First Author: Boekhoorn K
Year: 2008
Journal: J Comp Neurol
Title: Doublecortin (DCX) and doublecortin-like (DCL) are differentially expressed in the early but not late stages of murine neocortical development.
Volume: 507
Issue: 4
Pages: 1639-52
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Publication
19255245 | -
First Author: Komarova Y
Year: 2009
Journal: J Cell Biol
Title: Mammalian end binding proteins control persistent microtubule growth.
Volume: 184
Issue: 5
Pages: 691-706
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Protein
A0A140LHJ6
Organism: Mus musculus/domesticus
Length: 1371  
Fragment?: false
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Protein
Q9JLM7
Organism: Mus musculus/domesticus
Length: 527  
Fragment?: false
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Protein
Q9JLM8
Organism: Mus musculus/domesticus
Length: 756  
Fragment?: false
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Protein
Q6PGN3
Organism: Mus musculus/domesticus
Length: 756  
Fragment?: false
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Protein
Q8BWQ5
Organism: Mus musculus/domesticus
Length: 790  
Fragment?: false
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Protein
Q8CHG1
Organism: Mus musculus/domesticus
Length: 791  
Fragment?: true
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Protein
A0A0A6YX71
Organism: Mus musculus/domesticus
Length: 711  
Fragment?: false
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Protein
A0A0A6YWI6
Organism: Mus musculus/domesticus
Length: 641  
Fragment?: false
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Protein
A3KN70
Organism: Mus musculus/domesticus
Length: 740  
Fragment?: false
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Protein
A0A0A6YX33
Organism: Mus musculus/domesticus
Length: 591  
Fragment?: false
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Protein
A0A0G2JGQ6
Organism: Mus musculus/domesticus
Length: 739  
Fragment?: false
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Protein
Q80UN1
Organism: Mus musculus/domesticus
Length: 339  
Fragment?: false
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Protein
E9PUA6
Organism: Mus musculus/domesticus
Length: 389  
Fragment?: false
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Protein
Q3TG90
Organism: Mus musculus/domesticus
Length: 171  
Fragment?: false
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Protein
Q8R001
Organism: Mus musculus/domesticus
Length: 326  
Fragment?: false
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Protein
E9Q6X0
Organism: Mus musculus/domesticus
Length: 284  
Fragment?: false
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Protein
D3YYK8
Organism: Mus musculus/domesticus
Length: 260  
Fragment?: true
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Publication
15489334 | -
First Author: Gerhard DS
Year: 2004
Journal: Genome Res
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Volume: 14
Issue: 10B
Pages: 2121-7
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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.

Copyright © 2017 by The Jackson Laboratory. All Rights Reserved

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Cambridge CB2 3EH, United Kingdom