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Search results 1501 to 1600 out of 2004 for Arc

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Type Details Score
Publication
2176636 | -
First Author: Rothberg JM
Year: 1990
Journal: Genes Dev
Title: slit: an extracellular protein necessary for development of midline glia and commissural axon pathways contains both EGF and LRR domains.
Volume: 4
Issue: 12A
Pages: 2169-87
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Publication
32244188 | J:310050
 
First Author: Yu H
Year: 2020
Journal: Mol Metab
Title: Hypothalamic POMC deficiency increases circulating adiponectin despite obesity.
Volume: 35
Pages: 100957
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Protein
Q80TH2
Organism: Mus musculus/domesticus
Length: 1402  
Fragment?: false
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Protein
Q9QZN1
Organism: Mus musculus/domesticus
Length: 701  
Fragment?: false
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Protein
Q5BJ29
Organism: Mus musculus/domesticus
Length: 491  
Fragment?: false
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Protein
Q91W61
Organism: Mus musculus/domesticus
Length: 300  
Fragment?: false
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Protein
Q8C2S5
Organism: Mus musculus/domesticus
Length: 690  
Fragment?: false
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Protein
Q8CDU4
Organism: Mus musculus/domesticus
Length: 790  
Fragment?: false
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Protein
Q8K3P5
Organism: Mus musculus/domesticus
Length: 557  
Fragment?: false
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Protein
Q8BXA7
Organism: Mus musculus/domesticus
Length: 1320  
Fragment?: false
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Protein
Q505F5
Organism: Mus musculus/domesticus
Length: 581  
Fragment?: false
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Protein
Q8BID8
Organism: Mus musculus/domesticus
Length: 400  
Fragment?: false
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Protein
Q8VEG6
Organism: Mus musculus/domesticus
Length: 555  
Fragment?: false
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Protein
Q80U72
Organism: Mus musculus/domesticus
Length: 1612  
Fragment?: false
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Protein
Q80TE7
Organism: Mus musculus/domesticus
Length: 1490  
Fragment?: false
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Protein
Q6P9N3
Organism: Mus musculus/domesticus
Length: 929  
Fragment?: false
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Protein
B2RUJ2
Organism: Mus musculus/domesticus
Length: 1294  
Fragment?: false
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Protein
B7ZNX6
Organism: Mus musculus/domesticus
Length: 1411  
Fragment?: false
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Protein
J3QM82
Organism: Mus musculus/domesticus
Length: 1355  
Fragment?: false
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Protein
F6W6I1
Organism: Mus musculus/domesticus
Length: 611  
Fragment?: true
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Protein
D3Z584
Organism: Mus musculus/domesticus
Length: 673  
Fragment?: false
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Protein
E9PV22
Organism: Mus musculus/domesticus
Length: 603  
Fragment?: false
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Protein
A0A571BEA5
Organism: Mus musculus/domesticus
Length: 1488  
Fragment?: false
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Protein
B7ZNK2
Organism: Mus musculus/domesticus
Length: 745  
Fragment?: false
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Protein
D3Z399
Organism: Mus musculus/domesticus
Length: 632  
Fragment?: false
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Protein
A0A0G2JDT9
Organism: Mus musculus/domesticus
Length: 1495  
Fragment?: false
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Protein
E9Q6L9
Organism: Mus musculus/domesticus
Length: 1542  
Fragment?: false
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Protein
B1AX98
Organism: Mus musculus/domesticus
Length: 581  
Fragment?: false
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Protein
A0A1B0GQY9
Organism: Mus musculus/domesticus
Length: 621  
Fragment?: false
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Protein
B7ZNY4
Organism: Mus musculus/domesticus
Length: 1402  
Fragment?: false
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Protein
F7BZC4
Organism: Mus musculus/domesticus
Length: 679  
Fragment?: false
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Protein
B7ZNK1
Organism: Mus musculus/domesticus
Length: 778  
Fragment?: false
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Protein
B2RUK2
Organism: Mus musculus/domesticus
Length: 1450  
Fragment?: false
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Protein
Q8C2X8
Organism: Mus musculus/domesticus
Length: 180  
Fragment?: true
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Protein
D3Z6S4
Organism: Mus musculus/domesticus
Length: 690  
Fragment?: false
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Protein
A0A0G2JFZ5
Organism: Mus musculus/domesticus
Length: 1531  
Fragment?: true
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Protein
Q3U407
Organism: Mus musculus/domesticus
Length: 391  
Fragment?: true
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Publication
22051675 | J:281818
First Author: Xue T
Year: 2011
Journal: Nature
Title: Melanopsin signalling in mammalian iris and retina.
Volume: 479
Issue: 7371
Pages: 67-73
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Publication
35809573 | J:328588
First Author: Hwang FJ
Year: 2022
Journal: Neuron
Title: Motor learning selectively strengthens cortical and striatal synapses of motor engram neurons.
Volume: 110
Issue: 17
Pages: 2790-2801.e5
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Protein
Q3UVD5
Organism: Mus musculus/domesticus
Length: 967  
Fragment?: false
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Protein
Q9EPX5
Organism: Mus musculus/domesticus
Length: 326  
Fragment?: false
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Protein
Q5RKR3
Organism: Mus musculus/domesticus
Length: 745  
Fragment?: false
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Protein
Q8BFZ4
Organism: Mus musculus/domesticus
Length: 434  
Fragment?: false
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Protein
C3VPR6
Organism: Mus musculus/domesticus
Length: 1915  
Fragment?: false
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Protein
Q8C4V4
Organism: Mus musculus/domesticus
Length: 428  
Fragment?: false
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Protein
Q6NS60
Organism: Mus musculus/domesticus
Length: 873  
Fragment?: false
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Protein
Q8VE08
Organism: Mus musculus/domesticus
Length: 562  
Fragment?: false
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Protein
Q5NBU5
Organism: Mus musculus/domesticus
Length: 443  
Fragment?: false
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Protein
Q8CIG9
Organism: Mus musculus/domesticus
Length: 374  
Fragment?: false
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Protein
Q8BMI0
Organism: Mus musculus/domesticus
Length: 1194  
Fragment?: false
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Protein
P49813
Organism: Mus musculus/domesticus
Length: 359  
Fragment?: false
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Protein
Q9DBY4
Organism: Mus musculus/domesticus
Length: 809  
Fragment?: false
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Protein
P58681
Organism: Mus musculus/domesticus
Length: 1050  
Fragment?: false
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Protein
E0CZ81
Organism: Mus musculus/domesticus
Length: 428  
Fragment?: false
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Protein
E9Q9N7
Organism: Mus musculus/domesticus
Length: 789  
Fragment?: false
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Protein
Q3U4A0
Organism: Mus musculus/domesticus
Length: 707  
Fragment?: false
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Protein
Q3UGY7
Organism: Mus musculus/domesticus
Length: 873  
Fragment?: false
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Protein
Q3TD55
Organism: Mus musculus/domesticus
Length: 374  
Fragment?: false
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Protein
U5LLB3
Organism: Mus musculus/domesticus
Length: 1049  
Fragment?: true
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Protein
A4VCH8
Organism: Mus musculus/domesticus
Length: 358  
Fragment?: true
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Protein
D3YWZ0
Organism: Mus musculus/domesticus
Length: 177  
Fragment?: true
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Protein
A2A533
Organism: Mus musculus/domesticus
Length: 110  
Fragment?: true
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Protein
A0A0R4J1M5
Organism: Mus musculus/domesticus
Length: 154  
Fragment?: false
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Protein
Q14BU8
Organism: Mus musculus/domesticus
Length: 360  
Fragment?: true
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Protein
A0A1B0GS40
Organism: Mus musculus/domesticus
Length: 306  
Fragment?: true
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Protein
A0A2I3BQG6
Organism: Mus musculus/domesticus
Length: 72  
Fragment?: false
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Protein
A0A3Q4EH58
Organism: Mus musculus/domesticus
Length: 251  
Fragment?: false
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Protein
F8VQK6
Organism: Mus musculus/domesticus
Length: 707  
Fragment?: false
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Protein
A0A2K6EDL0
Organism: Mus musculus/domesticus
Length: 297  
Fragment?: false
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Protein
Q3TJJ7
Organism: Mus musculus/domesticus
Length: 428  
Fragment?: false
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Protein
D3YWZ8
Organism: Mus musculus/domesticus
Length: 86  
Fragment?: false
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Protein
A0A2R8W753
Organism: Mus musculus/domesticus
Length: 144  
Fragment?: true
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Protein
A0A0U1RNZ6
Organism: Mus musculus/domesticus
Length: 101  
Fragment?: true
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Protein
A0A0N4SVC9
Organism: Mus musculus/domesticus
Length: 54  
Fragment?: false
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Protein
G3X9Y3
Organism: Mus musculus/domesticus
Length: 460  
Fragment?: false
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Protein
E9PYR1
Organism: Mus musculus/domesticus
Length: 771  
Fragment?: false
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Protein
U5LLA9
Organism: Mus musculus/domesticus
Length: 1049  
Fragment?: true
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Protein
Q811T4
Organism: Mus musculus/domesticus
Length: 86  
Fragment?: false
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Protein
U5LI18
Organism: Mus musculus/domesticus
Length: 1049  
Fragment?: true
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Protein
Q5PRF6
Organism: Mus musculus/domesticus
Length: 428  
Fragment?: false
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Protein
Q548J0
Organism: Mus musculus/domesticus
Length: 1050  
Fragment?: false
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Publication
11967365 | -
First Author: Kajava AV
Year: 2002
Journal: Protein Sci
Title: Assessment of the ability to model proteins with leucine-rich repeats in light of the latest structural information.
Volume: 11
Issue: 5
Pages: 1082-90
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Publication
21606681 | -
First Author: Ng A
Year: 2011
Journal: Autophagy
Title: Leucine-rich repeat (LRR) proteins: integrators of pattern recognition and signaling in immunity.
Volume: 7
Issue: 9
Pages: 1082-4
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Publication
15808743 | -
First Author: Aravind L
Year: 2005
Journal: FEMS Microbiol Rev
Title: The many faces of the helix-turn-helix domain: transcription regulation and beyond.
Volume: 29
Issue: 2
Pages: 231-62
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Publication
8946850 | -
First Author: Peters JW
Year: 1996
Journal: Nat Struct Biol
Title: A leucine-rich repeat variant with a novel repetitive protein structural motif.
Volume: 3
Issue: 12
Pages: 991-4
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Publication
8264799 | -
First Author: Kobe B
Year: 1993
Journal: Nature
Title: Crystal structure of porcine ribonuclease inhibitor, a protein with leucine-rich repeats.
Volume: 366
Issue: 6457
Pages: 751-6
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Protein Domain
IPR006553 | Leu-rich_rpt_Cys-con_subtyp
Type: Repeat
Description: Leucine-rich repeats (LRR) consist of 2-45 motifs of 20-30 amino acids in length that generally folds into an arc or horseshoe shape []. LRRs occur in proteins ranging from viruses to eukaryotes, and appear to provide a structural framework for the formation of protein-protein interactions [, ].Proteins containing LRRs include tyrosine kinase receptors, cell-adhesion molecules, virulence factors, and extracellular matrix-binding glycoproteins, and are involved in a variety of biological processes, including signal transduction, cell adhesion, DNA repair, recombination, transcription, RNA processing, disease resistance, apoptosis, and the immune response [, ].Sequence analyses of LRR proteins suggested the existence of several different subfamilies of LRRs. The significance of this classification is that repeats from different subfamilies never occur simultaneously and have most probably evolved independently. It is, however, now clear that all major classes of LRR have curved horseshoe structures with a parallel beta sheet on the concave side and mostly helical elements on the convex side. At least six families of LRR proteins, characterised by different lengths and consensus sequences of the repeats, have been identified. Eleven-residue segments of the LRRs (LxxLxLxxN/CxL), corresponding to the β-strand and adjacent loop regions, are conserved in LRR proteins, whereas the remaining parts of the repeats (herein termed variable) may be very different. Despite the differences, each of the variable parts contains two half-turns at both ends and a "linear"segment (as the chain follows a linear path overall), usually formed by a helix, in the middle. The concave face and the adjacent loops are the most common protein interaction surfaces on LRR proteins. 3D structure of some LRR proteins-ligand complexes show that the concave surface of LRR domain is ideal for interaction with α-helix, thus supporting earlier conclusions that the elongated and curved LRR structure provides an outstanding framework for achieving diverse protein-protein interactions []. Molecular modeling suggests that the conserved pattern LxxLxL, which is shorter than the previously proposed LxxLxLxxN/CxL is sufficient to impart the characteristic horseshoe curvature to proteins with 20- to 30-residue repeats []. This is a cysteine-containing, leucine-rich repeat which is wide spread amongsteukaryotes proteins but does not appear to be found in archae, bacteria or viruses.
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Protein Domain
IPR004830 | LRR_variant
Type: Repeat
Description: Leucine-rich repeats (LRR) consist of 2-45 motifs of 20-30 amino acids in length that generally folds into an arc or horseshoe shape []. LRRs occur in proteins ranging from viruses to eukaryotes, and appear to provide a structural framework for the formation of protein-protein interactions [, ].Proteins containing LRRs include tyrosine kinase receptors, cell-adhesion molecules, virulence factors, and extracellular matrix-binding glycoproteins, and are involved in a variety of biological processes, including signal transduction, cell adhesion, DNA repair, recombination, transcription, RNA processing, disease resistance, apoptosis, and the immune response [, ].Sequence analyses of LRR proteins suggested the existence of several different subfamilies of LRRs. The significance of this classification is that repeats from different subfamilies never occur simultaneously and have most probably evolved independently. It is, however, now clear that all major classes of LRR have curved horseshoe structures with a parallel beta sheet on the concave side and mostly helical elements on the convex side. At least six families of LRR proteins, characterised by different lengths and consensus sequences of the repeats, have been identified. Eleven-residue segments of the LRRs (LxxLxLxxN/CxL), corresponding to the β-strand and adjacent loop regions, are conserved in LRR proteins, whereas the remaining parts of the repeats (herein termed variable) may be very different. Despite the differences, each of the variable parts contains two half-turns at both ends and a "linear"segment (as the chain follows a linear path overall), usually formed by a helix, in the middle. The concave face and the adjacent loops are the most common protein interaction surfaces on LRR proteins. 3D structure of some LRR proteins-ligand complexes show that the concave surface of LRR domain is ideal for interaction with α-helix, thus supporting earlier conclusions that the elongated and curved LRR structure provides an outstanding framework for achieving diverse protein-protein interactions []. Molecular modeling suggests that the conserved pattern LxxLxL, which is shorter than the previously proposed LxxLxLxxN/CxL is sufficient to impart the characteristic horseshoe curvature to proteins with 20- to 30-residue repeats []. This signature describes a leucine-rich repeat variant (LRV), which has a novel repetitive structural motif consisting of alternating alpha- and 3(10)-helices arranged in a right-handed superhelix, with the absence of the β-sheets present in other LRRs [].
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Protein Domain
IPR000372 | LRRNT
Type: Domain
Description: Leucine-rich repeats (LRR) consist of 2-45 motifs of 20-30 amino acids in length that generally folds into an arc or horseshoe shape []. LRRs occur in proteins ranging from viruses to eukaryotes, and appear to provide a structural framework for the formation of protein-protein interactions [, ].Proteins containing LRRs include tyrosine kinase receptors, cell-adhesion molecules, virulence factors, and extracellular matrix-binding glycoproteins, and are involved in a variety of biological processes, including signal transduction, cell adhesion, DNA repair, recombination, transcription, RNA processing, disease resistance, apoptosis, and the immune response [, ].Sequence analyses of LRR proteins suggested the existence of several different subfamilies of LRRs. The significance of this classification is that repeats from different subfamilies never occur simultaneously and have most probably evolved independently. It is, however, now clear that all major classes of LRR have curved horseshoe structures with a parallel beta sheet on the concave side and mostly helical elements on the convex side. At least six families of LRR proteins, characterised by different lengths and consensus sequences of the repeats, have been identified. Eleven-residue segments of the LRRs (LxxLxLxxN/CxL), corresponding to the β-strand and adjacent loop regions, are conserved in LRR proteins, whereas the remaining parts of the repeats (herein termed variable) may be very different. Despite the differences, each of the variable parts contains two half-turns at both ends and a "linear"segment (as the chain follows a linear path overall), usually formed by a helix, in the middle. The concave face and the adjacent loops are the most common protein interaction surfaces on LRR proteins. 3D structure of some LRR proteins-ligand complexes show that the concave surface of LRR domain is ideal for interaction with α-helix, thus supporting earlier conclusions that the elongated and curved LRR structure provides an outstanding framework for achieving diverse protein-protein interactions []. Molecular modeling suggests that the conserved pattern LxxLxL, which is shorter than the previously proposed LxxLxLxxN/CxL is sufficient to impart the characteristic horseshoe curvature to proteins with 20- to 30-residue repeats []. LRRs are often flanked by cysteine-rich domains: an N-terminal LRR domain and a C-terminal LRR domain (). This entry represents the N-terminal LRR domain.
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Protein Domain
IPR003591 | Leu-rich_rpt_typical-subtyp
Type: Repeat
Description: Leucine-rich repeats (LRR) consist of 2-45 motifs of 20-30 amino acids in length that generally folds into an arc or horseshoe shape []. LRRs occur in proteins ranging from viruses to eukaryotes, and appear to provide a structural framework for the formation of protein-protein interactions [, ].Proteins containing LRRs include tyrosine kinase receptors, cell-adhesion molecules, virulence factors, and extracellular matrix-binding glycoproteins, and are involved in a variety of biological processes, including signal transduction, cell adhesion, DNA repair, recombination, transcription, RNA processing, disease resistance, apoptosis, and the immune response [, ].Sequence analyses of LRR proteins suggested the existence of several different subfamilies of LRRs. The significance of this classification is that repeats from different subfamilies never occur simultaneously and have most probably evolved independently. It is, however, now clear that all major classes of LRR have curved horseshoe structures with a parallel beta sheet on the concave side and mostly helical elements on the convex side. At least six families of LRR proteins, characterised by different lengths and consensus sequences of the repeats, have been identified. Eleven-residue segments of the LRRs (LxxLxLxxN/CxL), corresponding to the β-strand and adjacent loop regions, are conserved in LRR proteins, whereas the remaining parts of the repeats (herein termed variable) may be very different. Despite the differences, each of the variable parts contains two half-turns at both ends and a "linear"segment (as the chain follows a linear path overall), usually formed by a helix, in the middle. The concave face and the adjacent loops are the most common protein interaction surfaces on LRR proteins. 3D structure of some LRR proteins-ligand complexes show that the concave surface of LRR domain is ideal for interaction with α-helix, thus supporting earlier conclusions that the elongated and curved LRR structure provides an outstanding framework for achieving diverse protein-protein interactions []. Molecular modeling suggests that the conserved pattern LxxLxL, which is shorter than the previously proposed LxxLxLxxN/CxL is sufficient to impart the characteristic horseshoe curvature to proteins with 20- to 30-residue repeats []. This entry represents a most populated subfamily of leucine-rich repeats.
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Protein Domain
IPR013210 | LRR_N_plant-typ
Type: Domain
Description: Leucine-rich repeats (LRR) consist of 2-45 motifs of 20-30 amino acids in length that generally folds into an arc or horseshoe shape []. LRRs occur in proteins ranging from viruses to eukaryotes, and appear to provide a structural framework for the formation of protein-protein interactions [, ].Proteins containing LRRs include tyrosine kinase receptors, cell-adhesion molecules, virulence factors, and extracellular matrix-binding glycoproteins, and are involved in a variety of biological processes, including signal transduction, cell adhesion, DNA repair, recombination, transcription, RNA processing, disease resistance, apoptosis, and the immune response [, ].Sequence analyses of LRR proteins suggested the existence of several different subfamilies of LRRs. The significance of this classification is that repeats from different subfamilies never occur simultaneously and have most probably evolved independently. It is, however, now clear that all major classes of LRR have curved horseshoe structures with aparallel beta sheet on the concave side and mostly helical elements on the convex side. At least six families of LRR proteins, characterised by different lengths and consensus sequences of the repeats, have been identified. Eleven-residue segments of the LRRs (LxxLxLxxN/CxL), corresponding to the β-strand and adjacent loop regions, are conserved in LRR proteins, whereas the remaining parts of the repeats (herein termed variable) may be very different. Despite the differences, each of the variable parts contains two half-turns at both ends and a "linear"segment (as the chain follows a linear path overall), usually formed by a helix, in the middle. The concave face and the adjacent loops are the most common protein interaction surfaces on LRR proteins. 3D structure of some LRR proteins-ligand complexes show that the concave surface of LRR domain is ideal for interaction with α-helix, thus supporting earlier conclusions that the elongated and curved LRR structure provides an outstanding framework for achieving diverse protein-protein interactions []. Molecular modeling suggests that the conserved pattern LxxLxL, which is shorter than the previously proposed LxxLxLxxN/CxL is sufficient to impart the characteristic horseshoe curvature to proteins with 20- to 30-residue repeats []. This domain is often found at the N terminus of tandem leucine rich repeats, mainly in plant proteins.
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Protein Domain
IPR013101 | Leu-rich_rpt_2
Type: Repeat
Description: Leucine-rich repeats (LRR) consist of 2-45 motifs of 20-30 amino acids in length that generally folds into an arc or horseshoe shape []. LRRs occur in proteins ranging from viruses to eukaryotes, and appear to provide a structural framework for the formation of protein-protein interactions [, ].Proteins containing LRRs include tyrosine kinase receptors, cell-adhesion molecules, virulence factors, and extracellular matrix-binding glycoproteins, and are involved in a variety of biological processes, including signal transduction, cell adhesion, DNA repair, recombination, transcription, RNA processing, disease resistance, apoptosis, and the immune response [, ].Sequence analyses of LRR proteins suggested the existence of several different subfamilies of LRRs. The significance of this classification is that repeats from different subfamilies never occur simultaneously and have most probably evolved independently. It is, however, now clear that all major classes of LRR have curved horseshoe structures with a parallel beta sheet on the concave side and mostly helical elements on the convex side. At least six families of LRR proteins, characterised by different lengths and consensus sequences of the repeats, have been identified. Eleven-residue segments of the LRRs (LxxLxLxxN/CxL), corresponding to the β-strand and adjacent loop regions, are conserved in LRR proteins, whereas the remaining parts of the repeats (herein termed variable) may be very different. Despite the differences, each of the variable parts contains two half-turns at both ends and a "linear"segment (as the chain follows a linear path overall), usually formed by a helix, in the middle. The concave face and the adjacent loops are the most common protein interaction surfaces on LRR proteins. 3D structure of some LRR proteins-ligand complexes show that the concave surface of LRR domain is ideal for interaction with α-helix, thus supporting earlier conclusions that the elongated and curved LRR structure provides an outstanding framework for achieving diverse protein-protein interactions []. Molecular modeling suggests that the conserved pattern LxxLxL, which is shorter than the previously proposed LxxLxLxxN/CxL is sufficient to impart the characteristic horseshoe curvature to proteins with 20- to 30-residue repeats []. This entry includes some LRRs that fail to be detected by [, ].
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Protein Domain
IPR011713 | Leu-rich_rpt_3
Type: Repeat
Description: Leucine-rich repeats (LRR) consist of 2-45 motifs of 20-30 amino acids in length that generally folds into an arc or horseshoe shape []. LRRs occur in proteins ranging from viruses to eukaryotes, and appear to provide a structural framework for the formation of protein-protein interactions [, ].Proteins containing LRRs include tyrosine kinase receptors, cell-adhesion molecules, virulence factors, and extracellular matrix-binding glycoproteins, and are involved in a variety of biological processes, including signal transduction, cell adhesion, DNA repair, recombination, transcription, RNA processing, disease resistance, apoptosis, and the immune response [, ].Sequence analyses of LRR proteins suggested the existence of several different subfamilies of LRRs. The significance of this classification is that repeats from different subfamilies never occur simultaneously and have most probably evolved independently. It is, however, now clear that all major classes of LRR have curved horseshoe structures with a parallel beta sheet on the concave side and mostly helical elements on the convex side. At least six families of LRR proteins, characterised by different lengths and consensus sequences of the repeats, have been identified. Eleven-residue segments of the LRRs (LxxLxLxxN/CxL), corresponding to the β-strand and adjacent loop regions, are conserved in LRR proteins, whereas the remaining parts of the repeats (herein termed variable) may be very different. Despite the differences, each of the variable parts contains two half-turns at both ends and a "linear"segment (as the chain follows a linear path overall), usually formed by a helix, in the middle. The concave face and the adjacent loops are the most common protein interaction surfaces on LRR proteins. 3D structure of some LRR proteins-ligand complexes show that the concave surface of LRR domain is ideal for interaction with α-helix, thus supporting earlier conclusions that the elongated and curved LRR structure provides an outstanding framework for achieving diverse protein-protein interactions []. Molecular modeling suggests that the conserved pattern LxxLxL, which is shorter than the previously proposed LxxLxLxxN/CxL is sufficient to impart the characteristic horseshoe curvature to proteins with 20- to 30-residue repeats []. This entry includes some LRRs that fail to be detected by the model.
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Protein
Q6EDY6
Organism: Mus musculus/domesticus
Length: 1374  
Fragment?: false
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Protein
Q9EST5
Organism: Mus musculus/domesticus
Length: 272  
Fragment?: false
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Protein
Q9QXW0
Organism: Mus musculus/domesticus
Length: 535  
Fragment?: false
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Protein
Q3V3V9
Organism: Mus musculus/domesticus
Length: 1296  
Fragment?: false
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Protein
P46061
Organism: Mus musculus/domesticus
Length: 589  
Fragment?: false
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Protein
Q9D5S7
Organism: Mus musculus/domesticus
Length: 820  
Fragment?: false
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Protein
Q5DU56
Organism: Mus musculus/domesticus
Length: 1064  
Fragment?: false
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