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Search results 201 to 300 out of 335 for Rhd

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Type Details Score
Publication
- | J:53168
     
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
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Publication
- | J:91388
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
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Publication
- | J:90438
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
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Publication
- | J:144087
     
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
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Publication
15383466 | J:133234
First Author: Hall AM
Year: 2005
Journal: Blood
Title: Immune responses and tolerance to the RhD blood group protein in HLA-transgenic mice.
Volume: 105
Issue: 5
Pages: 2175-9
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Protein
Q3UME0
Organism: Mus musculus/domesticus
Length: 717  
Fragment?: false
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Protein
Q3UZ77
Organism: Mus musculus/domesticus
Length: 473  
Fragment?: false
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Protein
Q3U3Q8
Organism: Mus musculus/domesticus
Length: 549  
Fragment?: false
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Protein
Q3U0K7
Organism: Mus musculus/domesticus
Length: 558  
Fragment?: false
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Protein
Q8BTL4
Organism: Mus musculus/domesticus
Length: 549  
Fragment?: false
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Protein
Q3UG25
Organism: Mus musculus/domesticus
Length: 899  
Fragment?: false
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Protein
Q3U5V4
Organism: Mus musculus/domesticus
Length: 806  
Fragment?: true
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Protein
Q3UV15
Organism: Mus musculus/domesticus
Length: 899  
Fragment?: false
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Protein
Q3ULT8
Organism: Mus musculus/domesticus
Length: 899  
Fragment?: false
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Publication
1438298 | -
First Author: Le van Kim C
Year: 1992
Journal: Proc Natl Acad Sci U S A
Title: Molecular cloning and primary structure of the human blood group RhD polypeptide.
Volume: 89
Issue: 22
Pages: 10925-9
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Allele
Tg(RHD)65.08Goo | MGI:6148220
Name: transgene insertion 65.08, Dominique Goossens
Allele Type: Transgenic
Attribute String: Inserted expressed sequence
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Allele
Tg(RHD)1Goo | MGI:6148219
Name: transgene insertion 1, Dominique Goossens
Allele Type: Transgenic
Attribute String: Inserted expressed sequence
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Strain
MGI:6148921 | B6.CBA-Tg(RHD)65.08Goo/Orl
Attribute String: mutant strain, congenic, transgenic
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Strain
MGI:6148949 | B6;SJL-Tg(RHD)1Goo/Orl
Attribute String: mutant stock, transgenic
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Protein Domain
IPR011539 | RHD_DNA_bind_dom
Type: Domain
Description: The Rel homology domain (RHD) is found in a family of eukaryotic transcription factors, which includes NF-kappaB, Dorsal, Relish, NFAT, among others. The RHD is composed of two structural domains: the N-terminal DNA binding domain that is similar to that found in P53, the C-terminal domain has an immunoglobulin-like fold (See ) that functions as a dimerisation domain. This entry represents the N-terminal DNA binding domain []. Some of these transcription factors appear to form multi-protein DNA-bound complexes []. Phosphorylation of the RHD appears to play a role in the regulation of some of these transcription factors, acting to modulate the expression of their target genes []. The RHD is composed of two immunoglobulin-like β-barrel subdomains that grip the DNA in the major groove. The N-terminal specificity domain resembles the core domain of the p53 transcription factor, and contains a recognition loop that interacts with DNA bases; the C-terminal dimerisation domain contains the site for interaction with I-kappaB [].
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Protein Domain
IPR037059 | RHD_DNA_bind_dom_sf
Type: Homologous_superfamily
Description: The Rel homology domain (RHD) is found in a family of eukaryotic transcription factors, which includes NF-kappaB, Dorsal, Relish, NFAT, among others. The RHD is composed of two structural domains: the N-terminal DNA binding domain that is similar to that found in P53, the C-terminal domain has an immunoglobulin-like fold (See ) that functions as a dimerisation domain. This entry represents the N-terminal DNA binding domain superfamily []. Some of these transcription factors appear to form multi-protein DNA-bound complexes []. Phosphorylation of the RHD appears to play a role in the regulation of some of these transcription factors, acting to modulate the expression of their target genes []. The RHD is composed of two immunoglobulin-like β-barrel subdomains that grip the DNA in the major groove. The N-terminal specificity domain resembles the core domain of the p53 transcription factor, and contains a recognition loop that interacts with DNA bases; the C-terminal dimerisation domain contains the site for interaction with I-kappaB [].
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Publication
7830764 | -
First Author: Müller CW
Year: 1995
Journal: Nature
Title: Structure of the NF-kappa B p50 homodimer bound to DNA.
Volume: 373
Issue: 6512
Pages: 311-7
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Publication
9794820 | -
First Author: Wolberger C
Year: 1998
Journal: Curr Opin Genet Dev
Title: Combinatorial transcription factors.
Volume: 8
Issue: 5
Pages: 552-9
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Publication
15516339 | -
First Author: Anrather J
Year: 2005
Journal: J Biol Chem
Title: cis-acting, element-specific transcriptional activity of differentially phosphorylated nuclear factor-kappa B.
Volume: 280
Issue: 1
Pages: 244-52
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Publication
9426183 | -
First Author: Piette J
Year: 1997
Journal: Biol Chem
Title: Multiple redox regulation in NF-kappaB transcription factor activation.
Volume: 378
Issue: 11
Pages: 1237-45
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Publication
17431096 | -
First Author: Neumann M
Year: 2007
Journal: FASEB J
Title: Beyond IkappaBs: alternative regulation of NF-kappaB activity.
Volume: 21
Issue: 11
Pages: 2642-54
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Publication
18175145 | -
First Author: Gauthier M
Year: 2008
Journal: Dev Genes Evol
Title: The transcription factor NF-kappaB in the demosponge Amphimedon queenslandica: insights on the evolutionary origin of the Rel homology domain.
Volume: 218
Issue: 1
Pages: 23-32
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Publication
9416840 | J:44931
First Author: Huguet C
Year: 1997
Journal: Oncogene
Title: Rel/NF-kappa B transcription factors and I kappa B inhibitors: evolution from a unique common ancestor.
Volume: 15
Issue: 24
Pages: 2965-74
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Protein Domain
IPR042845 | RHD-n_c-Rel
Type: Domain
Description: NF-kappa B proteins are part of a protein complex that acts as a transcription factor, which is responsible for regulating a host of cellular responses to a variety of stimuli. This complex tightly regulates the expression of a large number of genes, and is involved in processes such as adaptive and innate immunity, stress response, inflammation, cell adhesion, proliferation and apoptosis. The cytosolic NF-kappa B complex is activated via phosphorylation of the ankyrin-repeat containing inhibitory protein I-kappa B, which dissociates from the complex and exposes the nuclear localization signal of the heterodimer (NF-kappa B and Rel) [, ]. c-Rel plays an important role in B cell proliferation and survival [].Proteins containing the Rel homology domain (RHD) are metazoan transcription factors. The RHD is composed of two structural sub-domains. This entry represents the N-terminal RHD sub-domain of the c-Rel family of transcription factors, categorized as a class II member of the NF-kappa B family. In class II NF-kappa Bs, the RHD domain co-occurs with a C-terminal transactivation domain (TAD) [, ].
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Publication
17869269 | -
First Author: Moorthy AK
Year: 2007
Journal: J Mol Biol
Title: X-ray structure of a NF-kappaB p50/RelB/DNA complex reveals assembly of multiple dimers on tandem kappaB sites.
Volume: 373
Issue: 3
Pages: 723-34
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Publication
14755244 | J:89745
First Author: Gilmore TD
Year: 2004
Journal: Oncogene
Title: The c-Rel transcription factor and B-cell proliferation: a deal with the devil.
Volume: 23
Issue: 13
Pages: 2275-86
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Publication
29100090 | J:262331
First Author: Sanna-Cherchi S
Year: 2017
Journal: Am J Hum Genet
Title: Exome-wide Association Study Identifies GREB1L Mutations in Congenital Kidney Malformations.
Volume: 101
Issue: 5
Pages: 789-802
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Publication
36189253 | J:334197
 
First Author: Qiu A
Year: 2022
Journal: Front Immunol
Title: FcγRIV is required for IgG2c mediated enhancement of RBC alloimmunization.
Volume: 13
Pages: 972723
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Publication
8528205 | J:26500
First Author: Schmitt I
Year: 1995
Journal: Hum Mol Genet
Title: Expression of the Huntington disease gene in rodents: cloning the rat homologue and evidence for downregulation in non-neuronal tissues during development.
Volume: 4
Issue: 7
Pages: 1173-82
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Protein
A4L9Q2
Organism: Mus musculus/domesticus
Length: 81  
Fragment?: true
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Protein
Q3U2V2
Organism: Mus musculus/domesticus
Length: 565  
Fragment?: false
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Protein
B5B2Q9
Organism: Mus musculus/domesticus
Length: 479  
Fragment?: false
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Protein
F6VCW7
Organism: Mus musculus/domesticus
Length: 135  
Fragment?: true
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Protein
B5B2Q8
Organism: Mus musculus/domesticus
Length: 459  
Fragment?: false
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Protein
Q6P3F6
Organism: Mus musculus/domesticus
Length: 624  
Fragment?: false
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Protein
B5B2U3
Organism: Mus musculus/domesticus
Length: 557  
Fragment?: false
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Protein
B5B2R0
Organism: Mus musculus/domesticus
Length: 258  
Fragment?: false
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Publication
22403241 | J:212523
First Author: Liu Q
Year: 2012
Journal: Circ Res
Title: Interaction between NFκB and NFAT coordinates cardiac hypertrophy and pathological remodeling.
Volume: 110
Issue: 8
Pages: 1077-86
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Publication
8662018 | J:34375
First Author: Westhoff CM
Year: 1996
Journal: J Mol Evol
Title: Investigation of the RH locus in gorillas and chimpanzees.
Volume: 42
Issue: 6
Pages: 658-68
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Publication
32765523 | J:341835
 
First Author: Shinde P
Year: 2020
Journal: Front Immunol
Title: IgG Subclass Determines Suppression Versus Enhancement of Humoral Alloimmunity to Kell RBC Antigens in Mice.
Volume: 11
Pages: 1516
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Protein
Q4U109
Organism: Mus musculus/domesticus
Length: 236  
Fragment?: false
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Protein
A0A140LJD6
Organism: Mus musculus/domesticus
Length: 147  
Fragment?: false
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Protein
Q4U112
Organism: Mus musculus/domesticus
Length: 147  
Fragment?: false
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Protein
A0A140LI24
Organism: Mus musculus/domesticus
Length: 116  
Fragment?: true
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Protein
A0A0G2JGK6
Organism: Mus musculus/domesticus
Length: 128  
Fragment?: false
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Protein
A0A494B901
Organism: Mus musculus/domesticus
Length: 67  
Fragment?: true
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Protein
A0A140LI46
Organism: Mus musculus/domesticus
Length: 138  
Fragment?: true
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Protein
Q4U111
Organism: Mus musculus/domesticus
Length: 237  
Fragment?: false
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Protein
Q4U113
Organism: Mus musculus/domesticus
Length: 121  
Fragment?: false
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Publication
7530332 | -
First Author: Ghosh G
Year: 1995
Journal: Nature
Title: Structure of NF-kappa B p50 homodimer bound to a kappa B site.
Volume: 373
Issue: 6512
Pages: 303-10
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Protein
G3UYA4
Organism: Mus musculus/domesticus
Length: 60  
Fragment?: true
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Publication
2018779 | -
First Author: Baeuerle PA
Year: 1991
Journal: Biochim Biophys Acta
Title: The inducible transcription activator NF-kappa B: regulation by distinct protein subunits.
Volume: 1072
Issue: 1
Pages: 63-80
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Publication
17114415 | -
First Author: Sen R
Year: 2006
Journal: J Immunol
Title: Multiple nuclear factors interact with the immunoglobulin enhancer sequences. Cell 1986. 46: 705-716.
Volume: 177
Issue: 11
Pages: 7485-96
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Publication
15371334 | -
First Author: Hayden MS
Year: 2004
Journal: Genes Dev
Title: Signaling to NF-kappaB.
Volume: 18
Issue: 18
Pages: 2195-224
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Publication
11062476 | -
First Author: Marini AM
Year: 2000
Journal: Nat Genet
Title: The human Rhesus-associated RhAG protein and a kidney homologue promote ammonium transport in yeast.
Volume: 26
Issue: 3
Pages: 341-4
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Publication
11861637 | -
First Author: Westhoff CM
Year: 2002
Journal: J Biol Chem
Title: Identification of the erythrocyte Rh blood group glycoprotein as a mammalian ammonium transporter.
Volume: 277
Issue: 15
Pages: 12499-502
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Protein Domain
IPR002229 | RhesusRHD
Type: Family
Description: Proteins in this group are responsible for the molecular basis of the blood group antigens, surface markers on the outside of the red blood cell membrane. Most of these markers are proteins, but some are carbohydrates attached to lipids or proteins [Reid M.E., Lomas-Francis C. The Blood Group Antigen Facts Book Academic Press, London / San Diego, (1997)]. The RH(CE) polypeptide (Rhesus C/E antigens) and RH(D) polypeptide (Rhesus D antigen) belong to the Rh blood group system and are associated with antigens that include C/c, E/e, D, f, C(e), C(w), C(x), V, E(w), G, Tar, VS, D(w), cE, amongst others.The Rh (Rhesus) blood group system is important in clinical medicine by virtue of being involved in haemolytic disease of the newborn, transfusion reactions, autoimmune haemolytic anaemias, and haemolytic reactions of non-immune origin []. The RH locus from RH(D)-positive donors contains 2 homologous structural genes, one of which encodes the D protein that carries the major antigen of the Rh system. Hydropathy analysis of the RhD gene product reveals 13 hydrophobic domains, all of which have been assumed to be transmembrane (TM) [].The proteins in this entry are related to ammonium transport [, ].
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Protein Domain
IPR000451 | NFkB/Dor
Type: Family
Description: The transcription factor NF-kB (Nuclear Factor-kappaB) was first identified as a DNA-binding protein specific for the 10-base pair kB site in the immunoglobulin k light-chain enhancer of B lymphocytes [], but has subsequently been found in many different cell types. NF-kB represents a group of structurally related proteins that share a 300 amino acid `Rel homology domain' (RHD) []: members include p50 (NF-kB1), p52 (NF-kB2), p65 (RelA), c-Rel, v-Rrel, RelB, and the Drosophila proteins Dorsal and Dif. These proteins exist as homo- and heterodimers that bind to kB sites in the enhancer regions of several target genes, most of which are involved in cellular defence mechanisms and differentiation.The RHD, which is located N-terminally, is responsible for proteindimerisation, DNA binding and nuclear localisation. The more variableC-terminal transactivation domain is found in RelA, RelB and c-Rel, but not in p50 or p52. Nevertheless, p50 and p52 play critical roles in modulatingthe specificity of NF-kB function. DNA binding requires the entire RHD, by contrast with other eukaryotic and prokaryotic transcription factors, where muchsmaller DNA-binding domains confer full specificity and bindingaffinity for the target []. The structure of the transcription factor NF-kB p50 homodimer bound to a palindromic kB site shows the RHD to fold into 2 distinct subdomains, similar to the β-sandwich structure of the immunoglobulins [].NF-kB is expressed in the cytoplasm of virtually all cell types, where its activity is controlled by a family of regulatory proteins, called inhibitors of NF-kB (IkB) [, ].
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Protein
P15307
Organism: Mus musculus/domesticus
Length: 587  
Fragment?: false
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Protein
A4QPD3
Organism: Mus musculus/domesticus
Length: 588  
Fragment?: false
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Protein
Q8K120
Organism: Mus musculus/domesticus
Length: 901  
Fragment?: false
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Protein
Q9WV30
Organism: Mus musculus/domesticus
Length: 1534  
Fragment?: false
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Protein
O88942
Organism: Mus musculus/domesticus
Length: 717  
Fragment?: false
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Protein
P97305
Organism: Mus musculus/domesticus
Length: 1075  
Fragment?: false
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Protein
Q60591
Organism: Mus musculus/domesticus
Length: 927  
Fragment?: false
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Protein
Q9JHD3
Organism: Mus musculus/domesticus
Length: 717  
Fragment?: false
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Protein
B5B2R5
Organism: Mus musculus/domesticus
Length: 673  
Fragment?: false
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Protein
B5B2N4
Organism: Mus musculus/domesticus
Length: 813  
Fragment?: false
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Protein
Q3UZ64
Organism: Mus musculus/domesticus
Length: 1076  
Fragment?: false
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Protein
Q3TTU8
Organism: Mus musculus/domesticus
Length: 473  
Fragment?: false
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Protein
B5B2Q6
Organism: Mus musculus/domesticus
Length: 477  
Fragment?: false
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Protein
B5B2U4
Organism: Mus musculus/domesticus
Length: 1068  
Fragment?: false
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Protein
A0A1U6URG8
Organism: Mus musculus/domesticus
Length: 1458  
Fragment?: false
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Protein
B5B2P6
Organism: Mus musculus/domesticus
Length: 903  
Fragment?: false
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Protein
B5B2Q2
Organism: Mus musculus/domesticus
Length: 907  
Fragment?: false
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Protein
Q571K2
Organism: Mus musculus/domesticus
Length: 748  
Fragment?: true
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Protein
B5B2P7
Organism: Mus musculus/domesticus
Length: 923  
Fragment?: false
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Protein
Q9JIH4
Organism: Mus musculus/domesticus
Length: 669  
Fragment?: false
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Protein
A0A2I3BRR0
Organism: Mus musculus/domesticus
Length: 831  
Fragment?: false
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Protein
Q9JIH5
Organism: Mus musculus/domesticus
Length: 409  
Fragment?: false
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Protein
Q8C443
Organism: Mus musculus/domesticus
Length: 452  
Fragment?: false
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Protein
B5B2N5
Organism: Mus musculus/domesticus
Length: 717  
Fragment?: false
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Protein
B5B2U1
Organism: Mus musculus/domesticus
Length: 1060  
Fragment?: false
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Protein
B5B2N2
Organism: Mus musculus/domesticus
Length: 939  
Fragment?: false
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Protein
Q6P7T9
Organism: Mus musculus/domesticus
Length: 827  
Fragment?: false
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Protein
A2AQC8
Organism: Mus musculus/domesticus
Length: 653  
Fragment?: false
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Protein
B5B2P8
Organism: Mus musculus/domesticus
Length: 702  
Fragment?: false
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Protein
B5B2R8
Organism: Mus musculus/domesticus
Length: 223  
Fragment?: false
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Protein
B5B2N7
Organism: Mus musculus/domesticus
Length: 925  
Fragment?: false
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Protein
B5B2U2
Organism: Mus musculus/domesticus
Length: 1068  
Fragment?: false
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Protein
B5B2Q4
Organism: Mus musculus/domesticus
Length: 706  
Fragment?: false
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Protein
Q8VHJ6
Organism: Mus musculus/domesticus
Length: 1458  
Fragment?: false
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Protein
Q9DBQ6
Organism: Mus musculus/domesticus
Length: 703  
Fragment?: false
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Protein
Q9QUT0
Organism: Mus musculus/domesticus
Length: 438  
Fragment?: false
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Protein
Q9QXP0
Organism: Mus musculus/domesticus
Length: 498  
Fragment?: false
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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

© 2002 - 2017 Department of Genetics, University of Cambridge, Downing Street,
Cambridge CB2 3EH, United Kingdom