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Search results 1901 to 2000 out of 2972 for Ca2

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0.017s

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Type Details Score
Publication
17644967 | -
 
First Author: Gibbs GM
Year: 2007
Journal: Soc Reprod Fertil Suppl
Title: Cysteine rich secretory proteins in reproduction and venom.
Volume: 65
Pages: 261-7
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Publication
16414181 | -
First Author: Roberts KP
Year: 2006
Journal: Mol Cell Endocrinol
Title: Epididymal secreted protein Crisp-1 and sperm function.
Volume: 250
Issue: 1-2
Pages: 122-7
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Publication
16872593 | -
First Author: Ellerman DA
Year: 2006
Journal: Dev Biol
Title: Sperm protein "DE" mediates gamete fusion through an evolutionarily conserved site of the CRISP family.
Volume: 297
Issue: 1
Pages: 228-37
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Publication
7647234 | -
First Author: Morrissette J
Year: 1995
Journal: Biophys J
Title: Primary structure and properties of helothermine, a peptide toxin that blocks ryanodine receptors.
Volume: 68
Issue: 6
Pages: 2280-8
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Publication
15477360 | J:93692
First Author: Iida H
Year: 2004
Journal: J Androl
Title: Molecular cloning of rat Spergen-3, a spermatogenic cell-specific gene-3, encoding a novel 75-kDa protein bearing EF-hand motifs.
Volume: 25
Issue: 6
Pages: 885-92
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Protein Domain
IPR043520 | SPT21/EFCAB3
Type: Family
Description: This entry includes a group of EF-hand calcium-binding domain-containing proteins, including EFCAB3 and SPT21 (spermatogenesis-associated protein 21). The function of EFCAB3 is not clear. SPT21 is involved in the differentiation of haploid spermatids [].Many calcium-binding proteins belong to the same evolutionary family and share a type of calcium-binding domain known as the EF-hand. This type of domain consists of a twelve residue loop flanked on both sides by a twelve residue α-helical domain. In an EF-hand loop the calcium ion is coordinated in a pentagonal bipyramidal configuration. The six residues involved in the binding are in positions 1, 3, 5, 7, 9 and 12; these residues are denoted by X, Y, Z, -Y, -X and -Z. The invariant Glu or Asp at position 12 provides two oxygens for liganding Ca (bidentate ligand). Ca2 binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers [, , , , ].
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Protein Domain
IPR016134 | Dockerin_dom
Type: Domain
Description: Plant cell wall polysaccharides comprise the most abundant reservoir of organic carbon in the biosphere. The cellulosome is a large multienzymecomplex used by many anaerobic bacteria for the efficient degradation of plant-cell wall polysaccharides. The principal component of the cellulosome is a scaffolding subunit, a large enzyme-integrating protein, that contains cohesin modules (usually in multiple copies) for incorporation of thedifferent enzymes and other cellulosomal components. The enzymes contain a complementary type of module, the dockerin domain, that binds tenaciously to the cohesin modules of the scaffoldin subunit [, , , ].The dockerin domains consist of about 70 amino acid residues and contain two duplicated segments, each of about 22 amino acid residues. The first 12 residues of these duplicated sequences bear remarkable resemblance to the calcium-binding loop of the EF-hand motif, in which all thecalcium-binding residues (i.e., aspartic acids and asparagines) are highly conserved. The second halves of the duplicated sequences appear to form alpha helices. These helices would be analogous to the F helix of the EF-hand motif [, , , ].The dockerin domain comprises three α-helices. Helices H1 and H3, which are antiparallel to one another, and the two calcium-binding loops (Ca1 and Ca2) correspond to the tandem duplicated sequences that form the two F-hand motifs. A short loop region and helix H2 connect the F-hand motifs. The 12-residue Ca(2+)-binding loop of each motif coordinates one Ca2 ion in the typical pentagonal bipyramid configuration of EF-handCa2-binding proteins [, ].
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Protein Domain
IPR004010 | Double_Cache_2
Type: Domain
Description: Cache is an extracellular domain that is predicted to have a role in small-molecule recognition in a wide range of proteins, including the animal dihydropyridine-sensitive voltage-gated Ca2 channel alpha-2delta subunit, and various bacterial chemotaxis receptors. The name Cache comes from CAlcium channels and CHEmotaxis receptors. The Cache domain, also known as the extracellular PAS domain, consists of an N-terminal part with three predicted strands and an α-helix, and a C-terminal part with a strand dyad followed by a relatively unstructured region. The N-terminal portion of the Cache domain containing the three predicted strands could form a sheet analogous to that present in the core of the PAS domain structure. Cache domains are particularly widespread in bacteria, such as Vibrio cholerae. The animal calcium channel alpha-2delta subunits might have acquired a part of their extracellular domains from a bacterial source []. The Cache domain appears to have arisen from the GAF-PAS fold, despite their divergent functions [, ].This entry represents the double Cache domain 2 (dCache_2), which may be a result of single Cache domain 2 (sCache_2) duplication [].
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Protein Domain
IPR031967 | PhoR_single_Cache-like_dom
Type: Domain
Description: This entry represents the N-terminal Cache-like domain of the alkaline phosphatase synthesis sensor protein PhoR. It covers part of the PAS-like fold that share a central five-stranded β-sheet of identical topology to other PAS domains [].Cache is an extracellular domain that is predicted to have a role in small-molecule recognition in a wide range of proteins, including the animal dihydropyridine-sensitive voltage-gated Ca2 channel alpha-2delta subunit, and various bacterial chemotaxis receptors. The name Cache comes from CAlcium channels and CHEmotaxis receptors. The Cache domain, also known as the extracellular PAS domain, consists of an N-terminal part with three predicted strands and an α-helix, and a C-terminal part with a strand dyad followed by a relatively unstructured region. The N-terminal portion of the Cache domain containing the three predicted strands could form a sheet analogous to that present in the core of the PAS domain structure. Cache domains are particularly widespread in bacteria, such as Vibrio cholerae. The animal calcium channel alpha-2delta subunits might have acquired a part of their extracellular domains from a bacterial source []. The Cache domain appears to have arisen from the GAF-PAS fold, despite their divergent functions [, ].
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Protein Domain
IPR034117 | SCP_CRISP
Type: Domain
Description: This SCP-like extracellular protein domain is found in cysteine-rich secretory proteins (CRISPs). Involvement of CRISP in response to pathogens, fertilization, and sperm maturation have been proposed [, , ]. One member, Tex31 from the venom duct of Conus textile, has been shown to possess proteolytic activity sensitive to serine protease inhibitors []. SCP has also been proposed to be a Ca2 chelating serine protease. The Ca2-chelating function would fit with various signaling processes that members of this family, such as the CRISPs, are involved in, and is supported by sequence and structural evidence of a conserved pocket containing two histidines and a glutamate. It also may explain how helothermine, a toxic peptide secreted by the beaded lizard, blocks Ca++ transporting ryanodine receptors []. One member, DE or CRISP-1, has been shown to mediate gamete fusion by binding to the egg surface; a sequence motif in the SCP domain plays a role in that binding [].The SCP domain is also known as CAP domain []. The wider family of SCP containing proteins includes plant pathogenesis-related protein 1 (PR-1), CRISPs, mammalian cysteine-rich secretory proteins, which combine SCP with a C-terminal cysteine rich domain, and allergen 5 from vespid venom. It has been proposed that SCP domains may function as endopeptidases.
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Protein Domain
IPR036439 | Dockerin_dom_sf
Type: Homologous_superfamily
Description: Plant cell wall polysaccharides comprise the most abundant reservoir of organic carbon in the biosphere. The cellulosome is a large multienzymecomplex used by many anaerobic bacteria for the efficient degradation of plant-cell wall polysaccharides. The principal component of the cellulosome is a scaffolding subunit, a large enzyme-integrating protein, that contains cohesin modules (usually in multiple copies) for incorporation of thedifferent enzymes and other cellulosomal components. The enzymes contain a complementary type of module, the dockerin domain, that binds tenaciously to the cohesin modules of the scaffoldin subunit [, , , ].The dockerin domains consist of about 70 amino acid residues and contain two duplicated segments, each of about 22 amino acid residues. The first 12 residues of these duplicated sequences bear remarkable resemblance to the calcium-binding loop of the EF-hand motif, in which all thecalcium-binding residues (i.e., aspartic acids and asparagines) are highly conserved. The second halves of the duplicated sequences appear to form alpha helices. These helices would be analogous to the F helix of the EF-hand motif [, , , ].The dockerin domain comprises three α-helices. Helices H1 and H3, which are antiparallel to one another, and the two calcium-binding loops (Ca1 and Ca2) correspond to the tandem duplicated sequences that form the two F-hand motifs. A short loop region and helix H2 connect the F-hand motifs. The 12-residue Ca(2+)-binding loop of each motif coordinates one Ca2 ion in the typical pentagonal bipyramid configuration of EF-handCa2-binding proteins [, ].
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Protein Domain
IPR029150 | dCache_3
Type: Domain
Description: Cache is an extracellular domain that is predicted to have a role in small-molecule recognition in a wide range of proteins, including the animal dihydropyridine-sensitive voltage-gated Ca2 channel alpha-2delta subunit, and various bacterial chemotaxis receptors. The name Cache comes from CAlcium channels and CHEmotaxis receptors. The Cache domain, also known as the extracellular PAS domain, consists of an N-terminal part with three predicted strands and an α-helix, and a C-terminal part with a strand dyad followed by a relatively unstructured region. The N-terminal portion of the Cache domain containing the three predicted strands could form a sheet analogous to that present in the core of the PAS domain structure. Cache domains are particularly widespread in bacteria, such as Vibrio cholerae. The animal calcium channel alpha-2delta subunits might have acquired a part of their extracellular domains from a bacterial source []. The Cache domain appears to have arisen from the GAF-PAS fold, despite their divergent functions [, ].This entry represents the double Cache domain 3 (dCache_3), which may be a result of single Cache domain 3 (sCache_3) duplication [].
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Protein Domain
IPR033480 | sCache_2
Type: Domain
Description: Cache is an extracellular domain that is predicted to have a role in small-molecule recognition in a wide range of proteins, including the animal dihydropyridine-sensitive voltage-gated Ca2 channel alpha-2delta subunit, and various bacterial chemotaxis receptors. The name Cache comes from CAlcium channels and CHEmotaxis receptors. The Cache domain, also known as the extracellular PAS domain, consists of an N-terminal part with three predicted strands and an α-helix, and a C-terminal part with a strand dyad followed by a relatively unstructured region. The N-terminal portion of the Cache domain containing the three predicted strands could form a sheet analogous to that present in the core of the PAS domain structure. Cache domains are particularly widespread in bacteria, such as Vibrio cholerae. The animal calcium channel alpha-2delta subunits might have acquired a part of their extracellular domains from a bacterial source []. The Cache domain appears to have arisen from the GAF-PAS fold, despite their divergent functions [, ].This entry represents the single Cache domain 2 (sCache_2), which contains the long N-terminal helix domain [].
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Protein Domain
IPR033479 | dCache_1
Type: Domain
Description: Cache is an extracellular domain that is predicted to have a role in small-molecule recognition in a wide range of proteins, including the animal dihydropyridine-sensitive voltage-gated Ca2 channel alpha-2delta subunit, and various bacterial chemotaxis receptors. The name Cache comes from CAlcium channels and CHEmotaxis receptors. The Cache domain, also known as the extracellular PAS domain, consists of an N-terminal part with three predicted strands and an α-helix, and a C-terminal part with a strand dyad followed by a relatively unstructured region. The N-terminal portion of the Cache domain containing the three predicted strands could form a sheet analogous to that present in the core of the PAS domain structure. Cache domains are particularly widespread in bacteria, such as Vibrio cholerae. The animal calcium channel alpha-2delta subunits might have acquired a part of their extracellular domains from a bacterial source []. The Cache domain appears to have arisen from the GAF-PAS fold, despite their divergent functions [, ].This entry represents double cache domain 1, which covers the last three strands from the membrane distal PAS-like domain, the first two strands of the membrane proximal domain, and the connecting elements between the two domains [].
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Protein Domain
IPR033463 | sCache_3
Type: Domain
Description: Cache is an extracellular domain that is predicted to have a role in small-molecule recognition in a wide range of proteins, including the animal dihydropyridine-sensitive voltage-gated Ca2 channel alpha-2delta subunit, and various bacterial chemotaxis receptors. The name Cache comes from CAlcium channels and CHEmotaxis receptors. The Cache domain, also known as the extracellular PAS domain, consists of an N-terminal part with three predicted strands and an α-helix, and a C-terminal part with a strand dyad followed by a relatively unstructured region. The N-terminal portion of the Cache domain containing the three predicted strands could form a sheet analogous to that present in the core of the PAS domain structure. Cache domains are particularly widespread in bacteria, such as Vibrio cholerae. The animal calcium channel alpha-2delta subunits might have acquired a part of their extracellular domains from a bacterial source []. The Cache domain appears to have arisen from the GAF-PAS fold, despite their divergent functions [, ].This entry represents the single cache domain 3 (sCache_3) [].
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Protein Domain
IPR033462 | Cache_3-Cache_2
Type: Domain
Description: Cache is an extracellular domain that is predicted to have a role in small-molecule recognition in a wide range of proteins, including the animal dihydropyridine-sensitive voltage-gated Ca2 channel alpha-2delta subunit, and various bacterial chemotaxis receptors. The name Cache comes from CAlcium channels and CHEmotaxis receptors. The Cache domain, also known as the extracellular PAS domain, consists of an N-terminal part with three predicted strands and an α-helix, and a C-terminal part with a strand dyad followed by a relatively unstructured region. The N-terminal portion of the Cache domain containing the three predicted strands could form a sheet analogous to that present in the core of the PAS domain structure. Cache domains are particularly widespread in bacteria, such as Vibrio cholerae. The animal calcium channel alpha-2delta subunits might have acquired a part of their extracellular domains from a bacterial source []. The Cache domain appears to have arisen from the GAF-PAS fold, despite their divergent functions [, ].This entry represents a type of Cache domain that likely originated asa fusion of sCache_3 and sCache_2 domains [].
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Protein Domain
IPR035940 | CAP_sf
Type: Homologous_superfamily
Description: The cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins (CAP) superfamily proteins are found in a wide range of organisms, including prokaryotes []and non-vertebrate eukaryotes [], The nine subfamilies of the mammalian CAP superfamily include: the human glioma pathogenesis-related 1 (GLIPR1), Golgi associated pathogenesis related-1 (GAPR1) proteins, peptidase inhibitor 15 (PI15), peptidase inhibitor 16 (PI16), cysteine-rich secretory proteins (CRISPs), CRISP LCCL domain containing 1 (CRISPLD1), CRISP LCCL domain containing 2 (CRISPLD2), mannose receptor like and the R3H domain containing like proteins. Members are most often secreted and have an extracellular endocrine or paracrine function and are involved in processes including the regulation of extracellular matrix and branching morphogenesis, potentially as either proteases or protease inhibitors; in ion channel regulation in fertility; as tumour suppressor or pro-oncogenic genes in tissues including the prostate; and in cell-cell adhesion during fertilisation. The overall protein structural conservation within the CAP superfamily results in fundamentally similar functions for the CAP domain in all members, yet the diversity outside of this core region dramatically alters the target specificity and, thus, the biological consequences []. The Ca2-chelating function []would fit with the various signalling processes (e.g. the CRISP proteins) that members of this family are involved in, and also the sequence and structural evidence of a conserved pocket containing two histidines and a glutamate. It also may explain how blocks the Ca2 transporting ryanodine receptors. The CAP domain forms a unique 3 layer α-β-α fold with some, though not all, of the structural elements found in proteases [].
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Protein Domain
IPR018247 | EF_Hand_1_Ca_BS
Type: Binding_site
Description: Many calcium-binding proteins belong to the same evolutionary family and share a type of calcium-binding domain known as the EF-hand. This type of domain consists of a twelve residue loop flanked on both sides by a twelve residue α-helical domain. In an EF-hand loop the calcium ion is coordinated in a pentagonal bipyramidal configuration. The six residues involved in the binding are in positions 1, 3, 5, 7, 9 and 12; these residues are denoted by X, Y, Z, -Y, -X and -Z. The invariant Glu or Asp at position 12 provides two oxygens for liganding Ca (bidentate ligand). Ca2 binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers [, , , , ].This signature pattern includes the complete EF-hand loop as well as the first residue which follows the loop and which seem to always be hydrophobic. Note: positions 1 (X), 3 (Y) and 12 (-Z) are the most conserved. The 6th residue in an EF-hand loop is, inmost cases a Gly, but the number of exceptions to this 'rule' has gradually increased, therefore, this signature pattern includes all the different residues which have been shown to exist in this position in functional Ca-binding sites. The pattern is known, in some cases, to miss one of the EF-hand regions in some proteins with multiple EF-hand domains.
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Protein Coding Gene
MGI:88276 | Ctnnb1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:109520 | Pafah1b1
Type: protein_coding_gene
Organism: mouse, laboratory
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Publication
2995362 | J:8030
First Author: Venta PJ
Year: 1985
Journal: J Biol Chem
Title: Structure and exon to protein domain relationships of the mouse carbonic anhydrase II gene.
Volume: 260
Issue: 22
Pages: 12130-5
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Publication
17702944 | J:123535
First Author: Hu J
Year: 2007
Journal: Science
Title: Detection of near-atmospheric concentrations of CO2 by an olfactory subsystem in the mouse.
Volume: 317
Issue: 5840
Pages: 953-7
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Publication
20637621 | J:163768
First Author: Munger SD
Year: 2010
Journal: Curr Biol
Title: An olfactory subsystem that detects carbon disulfide and mediates food-related social learning.
Volume: 20
Issue: 16
Pages: 1438-44
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Publication
7616606 | J:23601
First Author: Cammer W
Year: 1995
Journal: J Neurosci Res
Title: Effects of carbonic anhydrase II (CAII) deficiency on CNS structure and function in the myelin-deficient CAII-deficient double mutant mouse.
Volume: 40
Issue: 4
Pages: 451-7
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Publication
9027408 | J:37700
First Author: Nógrádi A
Year: 1997
Journal: Brain Res Dev Brain Res
Title: Carbonic anhydrase II and carbonic anhydrase-related protein in the cerebellar cortex of normal and lurcher mice.
Volume: 98
Issue: 1
Pages: 91-101
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Publication
16396925 | J:289036
First Author: Pan P
Year: 2006
Journal: J Physiol
Title: Carbonic anhydrase gene expression in CA II-deficient (Car2-/-) and CA IX-deficient (Car9-/-) mice.
Volume: 571
Issue: Pt 2
Pages: 319-27
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Publication
27526715 | J:236724
First Author: Henry EK
Year: 2016
Journal: J Exp Med
Title: Carbonic anhydrase enzymes regulate mast cell-mediated inflammation.
Volume: 213
Issue: 9
Pages: 1663-73
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Publication
29124201 | J:260088
 
First Author: Ueda T
Year: 2015
Journal: Biochem Biophys Rep
Title: Basal cells express functional TRPV4 channels in the mouse nasal epithelium.
Volume: 4
Pages: 169-174
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Publication
10792952 | J:63366
First Author: Kadison AS
Year: 2000
Journal: J Surg Res
Title: In vitro validation of duct differentiation in developing embryonic mouse pancreas.
Volume: 90
Issue: 2
Pages: 126-30
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Publication
2040456 | J:11217
First Author: von Deimling OH
Year: 1991
Journal: Genet Res
Title: Biochemical and genetic characterization of esterase-27 (ES-27), the major plasma cholinesterase of the house mouse (Mus musculus).
Volume: 57
Issue: 1
Pages: 61-70
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Protein
O88456
Organism: Mus musculus/domesticus
Length: 268  
Fragment?: false
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Protein
P12658
Organism: Mus musculus/domesticus
Length: 261  
Fragment?: false
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Protein
P0DP27
Organism: Mus musculus/domesticus
Length: 149  
Fragment?: false
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Protein
P0DP28
Organism: Mus musculus/domesticus
Length: 149  
Fragment?: false
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Protein
Q08331
Organism: Mus musculus/domesticus
Length: 271  
Fragment?: false
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Protein
Q8R1U2
Organism: Mus musculus/domesticus
Length: 281  
Fragment?: false
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Protein
Q8K4K1
Organism: Mus musculus/domesticus
Length: 168  
Fragment?: false
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Protein
Q63810
Organism: Mus musculus/domesticus
Length: 170  
Fragment?: false
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Protein
Q6P8Y1
Organism: Mus musculus/domesticus
Length: 208  
Fragment?: false
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Protein
Q8VHC5
Organism: Mus musculus/domesticus
Length: 271  
Fragment?: false
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Protein
Q9QXT8
Organism: Mus musculus/domesticus
Length: 256  
Fragment?: false
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Protein
Q9D0E5
Organism: Mus musculus/domesticus
Length: 162  
Fragment?: false
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Protein
Q9D3N2
Organism: Mus musculus/domesticus
Length: 212  
Fragment?: false
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Protein
Q91X97
Organism: Mus musculus/domesticus
Length: 193  
Fragment?: false
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Protein
Q8BP92
Organism: Mus musculus/domesticus
Length: 320  
Fragment?: false
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Protein
Q05186
Organism: Mus musculus/domesticus
Length: 325  
Fragment?: false
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Protein
Q8BH97
Organism: Mus musculus/domesticus
Length: 328  
Fragment?: false
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Protein
Q8VE28
Organism: Mus musculus/domesticus
Length: 461  
Fragment?: false
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Protein
Q9Z176
Organism: Mus musculus/domesticus
Length: 491  
Fragment?: false
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Protein
P51667
Organism: Mus musculus/domesticus
Length: 166  
Fragment?: false
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Protein
P81117
Organism: Mus musculus/domesticus
Length: 420  
Fragment?: false
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Protein
Q63811
Organism: Mus musculus/domesticus
Length: 179  
Fragment?: false
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Protein
Q8BYI6
Organism: Mus musculus/domesticus
Length: 544  
Fragment?: false
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Protein
Q3TFD2
Organism: Mus musculus/domesticus
Length: 534  
Fragment?: false
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Protein
Q6P1E8
Organism: Mus musculus/domesticus
Length: 1516  
Fragment?: false
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Protein
Q8BNY6
Organism: Mus musculus/domesticus
Length: 190  
Fragment?: false
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Protein
Q9JM83
Organism: Mus musculus/domesticus
Length: 148  
Fragment?: false
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Protein
Q9JLK3
Organism: Mus musculus/domesticus
Length: 173  
Fragment?: false
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Protein
P84075
Organism: Mus musculus/domesticus
Length: 193  
Fragment?: false
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Protein
Q8BGZ1
Organism: Mus musculus/domesticus
Length: 191  
Fragment?: false
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Protein
Q9D5U0
Organism: Mus musculus/domesticus
Length: 516  
Fragment?: false
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Protein
P12815
Organism: Mus musculus/domesticus
Length: 191  
Fragment?: false
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Protein
Q9JJ69
Organism: Mus musculus/domesticus
Length: 270  
Fragment?: false
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Protein
P97457
Organism: Mus musculus/domesticus
Length: 169  
Fragment?: false
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Protein
Q3THE2
Organism: Mus musculus/domesticus
Length: 172  
Fragment?: false
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Protein
P59024
Organism: Mus musculus/domesticus
Length: 211  
Fragment?: false
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Protein
Q62082
Organism: Mus musculus/domesticus
Length: 202  
Fragment?: false
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Protein
Q99MH6
Organism: Mus musculus/domesticus
Length: 471  
Fragment?: false
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Protein
Q8VCX5
Organism: Mus musculus/domesticus
Length: 477  
Fragment?: false
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Protein
Q9JJ57
Organism: Mus musculus/domesticus
Length: 227  
Fragment?: false
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Protein
Q6PHZ8
Organism: Mus musculus/domesticus
Length: 250  
Fragment?: false
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Protein
Q6ZQ12
Organism: Mus musculus/domesticus
Length: 1394  
Fragment?: false
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Protein
Q9Z247
Organism: Mus musculus/domesticus
Length: 570  
Fragment?: false
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Protein
Q9JLK7
Organism: Mus musculus/domesticus
Length: 227  
Fragment?: false
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Protein
O35648
Organism: Mus musculus/domesticus
Length: 167  
Fragment?: false
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Protein
A0JP43
Organism: Mus musculus/domesticus
Length: 1406  
Fragment?: false
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Protein
Q8VDY4
Organism: Mus musculus/domesticus
Length: 628  
Fragment?: false
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Protein
Q61576
Organism: Mus musculus/domesticus
Length: 581  
Fragment?: false
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Protein
O54998
Organism: Mus musculus/domesticus
Length: 218  
Fragment?: false
•
•
•
•
•
Protein
Q61112
Organism: Mus musculus/domesticus
Length: 361  
Fragment?: false
•
•
•
•
•
Protein
Q8BUG5
Organism: Mus musculus/domesticus
Length: 550  
Fragment?: false
•
•
•
•
•
Protein
Q9D6P8
Organism: Mus musculus/domesticus
Length: 149  
Fragment?: false
•
•
•
•
•
Protein
P0DP26
Organism: Mus musculus/domesticus
Length: 149  
Fragment?: false
•
•
•
•
•
Protein
Q8CDU5
Organism: Mus musculus/domesticus
Length: 853  
Fragment?: false
•
•
•
•
•
Protein
Q8VC88
Organism: Mus musculus/domesticus
Length: 220  
Fragment?: false
•
•
•
•
•
Protein
P62748
Organism: Mus musculus/domesticus
Length: 193  
Fragment?: false
•
•
•
•
•
Protein
Q8K5B2
Organism: Mus musculus/domesticus
Length: 145  
Fragment?: false
•
•
•
•
•
Protein
Q02819
Organism: Mus musculus/domesticus
Length: 459  
Fragment?: false
•
•
•
•
•
Protein
Q9CTY5
Organism: Mus musculus/domesticus
Length: 523  
Fragment?: false
•
•
•
•
•
Protein
Q9CQ19
Organism: Mus musculus/domesticus
Length: 172  
Fragment?: false
•
•
•
•
•
Protein
P34057
Organism: Mus musculus/domesticus
Length: 202  
Fragment?: false
•
•
•
•
•
Protein
O35887
Organism: Mus musculus/domesticus
Length: 315  
Fragment?: false
•
•
•
•
•
Protein
Q9Z0F4
Organism: Mus musculus/domesticus
Length: 191  
Fragment?: false
•
•
•
•
•
Protein
Q9Z309
Organism: Mus musculus/domesticus
Length: 187  
Fragment?: false
•
•
•
•
•
Protein
Q0P523
Organism: Mus musculus/domesticus
Length: 160  
Fragment?: false
•
•
•
•
•
Protein
Q9D9N5
Organism: Mus musculus/domesticus
Length: 185  
Fragment?: false
•
•
•
•
•
Protein
P61022
Organism: Mus musculus/domesticus
Length: 195  
Fragment?: false
•
•
•
•
•
Protein
Q9D869
Organism: Mus musculus/domesticus
Length: 196  
Fragment?: false
•
•
•
•
•
Protein
Q9JKL5
Organism: Mus musculus/domesticus
Length: 214  
Fragment?: false
•
•
•
•
•
Protein
Q6P069
Organism: Mus musculus/domesticus
Length: 198  
Fragment?: false
•
•
•
•
•




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