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Search results 2901 to 3000 out of 4706 for Coil

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0.031s

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Hits by Strain

Type Details Score
Protein
D3Z118
Organism: Mus musculus/domesticus
Length: 465  
Fragment?: false
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Protein
Q8R0Z4
Organism: Mus musculus/domesticus
Length: 172  
Fragment?: false
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Protein
V9GX85
Organism: Mus musculus/domesticus
Length: 368  
Fragment?: false
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Protein
A0A1B0GSM3
Organism: Mus musculus/domesticus
Length: 267  
Fragment?: false
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Protein
A0A0G2JEL5
Organism: Mus musculus/domesticus
Length: 272  
Fragment?: true
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Protein
J3QNA0
Organism: Mus musculus/domesticus
Length: 530  
Fragment?: false
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Protein
J3KMP6
Organism: Mus musculus/domesticus
Length: 355  
Fragment?: false
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Protein
Q6PIE1
Organism: Mus musculus/domesticus
Length: 831  
Fragment?: true
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Protein
F6VZK2
Organism: Mus musculus/domesticus
Length: 216  
Fragment?: true
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Protein
M0QWM1
Organism: Mus musculus/domesticus
Length: 295  
Fragment?: true
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Protein
A0A1B0GQY8
Organism: Mus musculus/domesticus
Length: 111  
Fragment?: true
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Protein
D3Z2F3
Organism: Mus musculus/domesticus
Length: 209  
Fragment?: true
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Protein
F8WJ48
Organism: Mus musculus/domesticus
Length: 539  
Fragment?: false
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Protein
Q0V927
Organism: Mus musculus/domesticus
Length: 563  
Fragment?: false
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Protein
A0JLM6
Organism: Mus musculus/domesticus
Length: 679  
Fragment?: true
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Protein
G5E874
Organism: Mus musculus/domesticus
Length: 1193  
Fragment?: false
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Publication
9218783 | -
First Author: Biou V
Year: 1997
Journal: EMBO J
Title: The crystal structure of plant acetohydroxy acid isomeroreductase complexed with NADPH, two magnesium ions and a herbicidal transition state analog determined at 1.65 A resolution.
Volume: 16
Issue: 12
Pages: 3405-15
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Publication
12691757 | -
First Author: Ahn HJ
Year: 2003
Journal: J Mol Biol
Title: Crystal structure of class I acetohydroxy acid isomeroreductase from Pseudomonas aeruginosa.
Volume: 328
Issue: 2
Pages: 505-15
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Publication
11352718 | -
First Author: Dumas R
Year: 2001
Journal: Acc Chem Res
Title: Enzymology, structure, and dynamics of acetohydroxy acid isomeroreductase.
Volume: 34
Issue: 5
Pages: 399-408
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Publication
25849365 | -
First Author: Cahn JK
Year: 2015
Journal: Biochem J
Title: Cofactor specificity motifs and the induced fit mechanism in class I ketol-acid reductoisomerases.
Volume: 468
Issue: 3
Pages: 475-84
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Publication
26644020 | -
First Author: Cahn JK
Year: 2016
Journal: Protein Sci
Title: Artificial domain duplication replicates evolutionary history of ketol-acid reductoisomerases.
Volume: 25
Issue: 7
Pages: 1241-8
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Publication
11448994 | -
First Author: Caplan S
Year: 2001
Journal: J Cell Biol
Title: Human Vam6p promotes lysosome clustering and fusion in vivo.
Volume: 154
Issue: 1
Pages: 109-22
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Publication
2666164 | -
First Author: Engel J
Year: 1989
Journal: FEBS Lett
Title: EGF-like domains in extracellular matrix proteins: localized signals for growth and differentiation?
Volume: 251
Issue: 1-2
Pages: 1-7
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Publication
8349613 | -
First Author: Yurchenco PD
Year: 1993
Journal: J Biol Chem
Title: Self-assembly and calcium-binding sites in laminin. A three-arm interaction model.
Volume: 268
Issue: 23
Pages: 17286-99
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Publication
10429180 | -
First Author: Strunnikov AV
Year: 1999
Journal: Eur J Biochem
Title: Structural maintenance of chromosomes (SMC) proteins: conserved molecular properties for multiple biological functions.
Volume: 263
Issue: 1
Pages: 6-13
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Publication
10363373 | -
First Author: Cubas P
Year: 1999
Journal: Plant J
Title: The TCP domain: a motif found in proteins regulating plant growth and development.
Volume: 18
Issue: 2
Pages: 215-22
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Publication
15902272 | -
First Author: Fennell-Fezzie R
Year: 2005
Journal: EMBO J
Title: The MukF subunit of Escherichia coli condensin: architecture and functional relationship to kleisins.
Volume: 24
Issue: 11
Pages: 1921-30
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Publication
11346801 | -
First Author: Tarricone C
Year: 2001
Journal: Nature
Title: The structural basis of Arfaptin-mediated cross-talk between Rac and Arf signalling pathways.
Volume: 411
Issue: 6834
Pages: 215-9
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Publication
10623590 | J:59399
First Author: Takeya R
Year: 2000
Journal: Biochem Biophys Res Commun
Title: Interaction of the PDZ domain of human PICK1 with class I ADP-ribosylation factors.
Volume: 267
Issue: 1
Pages: 149-55
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Publication
12411491 | -
First Author: Hirano M
Year: 2002
Journal: EMBO J
Title: Hinge-mediated dimerization of SMC protein is essential for its dynamic interaction with DNA.
Volume: 21
Issue: 21
Pages: 5733-44
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Publication
16472755 | J:247420
First Author: Kühnel K
Year: 2006
Journal: Structure
Title: Crystal structure of the human retinitis pigmentosa 2 protein and its interaction with Arl3.
Volume: 14
Issue: 2
Pages: 367-78
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Publication
8606779 | -
First Author: Kull FJ
Year: 1996
Journal: Nature
Title: Crystal structure of the kinesin motor domain reveals a structural similarity to myosin.
Volume: 380
Issue: 6574
Pages: 550-5
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Protein Domain
IPR036961 | Kinesin_motor_dom_sf
Type: Homologous_superfamily
Description: Kinesin [, , ]is a microtubule-associated force-producing protein that may play a role in organelle transport. The kinesin motor activity is directed toward the microtubule's plus end. Kinesin is an oligomeric complex composed of two heavy chains and two light chains. The maintenance of the quaternary structure does not require interchain disulphide bonds.The heavy chain is composed of three structural domains: a large globular N-terminal domain which is responsible for the motor activity of kinesin (it is known to hydrolyse ATP, to bind and move on microtubules), a central α-helical coiled coil domain that mediates the heavy chain dimerisation; and a small globular C-terminal domain which interacts with other proteins (such as the kinesin light chains), vesicles and membranous organelles.The kinesin motor domain comprises five motifs, namely N1 (P-loop), N2 (Switch I), N3 (Switch II), N4 and L2 (KVD finger) []. It has a mixed eight stranded β-sheet core with flanking solvent exposed α-helices and a small three-stranded antiparallel β-sheet in the N-terminal region [].A number of proteins have been recently found that contain a domain similar to that of the kinesin 'motor' domain [, ]:Drosophila melanogaster claret segregational protein (ncd). Ncd is required for normal chromosomal segregation in meiosis, in females, and in early mitotic divisions of the embryo. The ncd motor activity is directed toward the microtubule's minus end.Homo sapiens CENP-E []. CENP-E is a protein that associates with kinetochores during chromosome congression, relocates to the spindle midzone at anaphase, and is quantitatively discarded at the end of the cell division. CENP-E is probably an important motor molecule in chromosome movement and/or spindle elongation.H. sapiens mitotic kinesin-like protein-1 (MKLP-1), a motor protein whose activity is directed toward the microtubule's plus end.Saccharomyces cerevisiae KAR3 protein, which is essential for nuclear fusion during mating. KAR3 may mediate microtubule sliding during nuclear fusion and possibly mitosis.S. cerevisiae CIN8 and KIP1 proteins which are required for the assembly of the mitotic spindle. Both proteins seem to interact with spindle microtubules to produce anoutwardly directed force acting upon the poles.Emericella nidulans (Aspergillus nidulans) bimC, which plays an important role in nuclear division.A. nidulans klpA.Caenorhabditis elegans unc-104, which may be required for the transport of substances needed for neuronal cell differentiation.C. elegans osm-3.Xenopus laevis Eg5, which may be involved in mitosis.Arabidopsis thaliana KatA, KatB and katC.Chlamydomonas reinhardtii FLA10/KHP1 and KLP1. Both proteins seem to play a role in the rotation or twisting of the microtubules of the flagella.C. elegans hypothetical protein T09A5.2.The kinesin motor domain is located in the N-terminal part of most of the above proteins, with the exception of KAR3, klpA, and ncd where it is located in the C-terminal section.The kinesin motor domain contains about 330 amino acids. An ATP-binding motif of type A is found near position 80 to 90, the C-terminal half of the domain is involved in microtubule-binding.Interestingly, kinesin motor domain has a striking structural similarity to the core of the catalytic domain of the actin-based motor myosin [].
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Protein Domain
IPR022642 | CheR_C
Type: Domain
Description: Methyl transfer from the ubiquitous S-adenosyl-L-methionine (AdoMet) to either nitrogen, oxygen or carbon atoms is frequently employed in diverse organisms ranging from bacteria to plants and mammals. The reaction is catalysed by methyltransferases (Mtases) and modifies DNA, RNA, proteins and small molecules, such as catechol for regulatory purposes. The various aspects ofthe role of DNA methylation in prokaryotic restriction-modification systems and in a number of cellular processes in eukaryotes including gene regulation and differentiation is well documented.Three classes of DNA Mtases transfer the methyl group from AdoMet to the target base to form either N-6-methyladenine, or N-4-methylcytosine, or C-5- methylcytosine. In C-5-cytosine Mtases, ten conserved motifs are arranged in the same order []. Motif I (a glycine-rich or closely related consensus sequence; FAGxGG in M.HhaI []), shared by other AdoMet-Mtases [], is part of the cofactor binding site and motif IV (PCQ) is part of the catalytic site. In contrast, sequence comparison among N-6-adenine and N-4-cytosine Mtases indicated two of the conserved segments [], although more conserved segments may be present. One of them corresponds to motif I in C-5-cytosine Mtases, and the other is named (D/N/S)PP(Y/F). Crystal structures are known for a number of Mtases [, , , ]. The cofactor binding sites are almost identical and the essential catalytic amino acids coincide. The comparable protein folding and the existence of equivalent amino acids in similar secondary and tertiary positions indicate that many (if not all) AdoMet-Mtases have a common catalytic domain structure. This permits tertiary structure prediction of other DNA, RNA, protein, and small-molecule AdoMet-Mtases from their amino acid sequences [].CheR proteins are part of the chemotaxis signaling mechanism in bacteria. Flagellated bacteria swim towards favourable chemicals and away from deleterious ones. Sensing of chemoeffector gradients involves chemotaxis receptors, transmembrane (TM) proteins that detect stimuli through their periplasmic domains and transduce the signals via their cytoplasmic domains []. Signalling outputs from these receptors are influenced both by the binding of the chemoeffector ligand to their periplasmic domains and by methylation of specific glutamate residues on their cytoplasmic domains. Methylation is catalysed by CheR, an S-adenosylmethionine-dependent methyltransferase [], which reversibly methylates specific glutamate residues within a coiled coil region, to form gamma-glutamyl methyl ester residues [, ].The structure of the Salmonella typhimurium chemotaxis receptor methyltransferase CheR, bound to S-adenosylhomocysteine, has been determined to a resolution of 2.0 A []. The structure reveals CheR to be a two-domain protein, with a smaller N-terminal helical domain linked via a single polypeptide connection to a larger C-terminal alpha/beta domain. The C-terminal domain has the characteristics of a nucleotide-binding fold, with an insertion of a small anti-parallel β-sheet subdomain. The S-adenosylhomocysteine-binding site is formed mainly by the large domain, with contributions from residues within the N-terminal domain and the linker region [].CheR proteins are part of the chemotaxis signaling mechanism which methylates the chemotaxis receptor at specific glutamate residues. This entry refers to the C-terminal SAM-binding domain of the CherR-type MCP methyltransferases, which are found in bacteria, archaea and green plants. This entry is found in association with .
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Protein Domain
IPR019821 | Kinesin_motor_CS
Type: Conserved_site
Description: Kinesin [, , ]is a microtubule-associated force-producing protein that may play a role in organelle transport. The kinesin motor activity is directed toward the microtubule's plus end. Kinesin is an oligomeric complex composed of two heavy chains and two light chains. The maintenance of the quaternary structure does not require interchain disulphide bonds.The heavy chain is composed of three structural domains: a large globular N-terminal domain which is responsible for the motor activity of kinesin (it is known to hydrolyse ATP, to bind and move on microtubules), a central α-helical coiled coil domain that mediates the heavy chain dimerisation; and a small globular C-terminal domain which interacts with other proteins (such as the kinesin light chains), vesicles and membranous organelles.The kinesin motor domain comprises five motifs, namely N1 (P-loop), N2 (Switch I), N3 (Switch II), N4 and L2 (KVD finger) []. It has a mixed eight stranded β-sheet core with flanking solvent exposed α-helices and a small three-stranded antiparallel β-sheet in the N-terminal region [].A number of proteins have been recently found that contain a domain similar to that of the kinesin 'motor' domain [, ]:Drosophila melanogaster claret segregational protein (ncd). Ncd is required for normal chromosomal segregation in meiosis, in females, and in early mitotic divisions of the embryo. The ncd motor activity is directed toward the microtubule's minus end.Homo sapiens CENP-E []. CENP-E is a protein that associates with kinetochores during chromosome congression, relocates to the spindle midzone at anaphase, and is quantitatively discarded at the end of the cell division. CENP-E is probably an important motor molecule in chromosome movement and/or spindle elongation.H. sapiens mitotic kinesin-like protein-1 (MKLP-1), a motor protein whose activity is directed toward the microtubule's plus end.Saccharomyces cerevisiae KAR3 protein, which is essential for nuclear fusion during mating. KAR3 may mediate microtubule sliding during nuclear fusion and possibly mitosis.S. cerevisiae CIN8 and KIP1 proteins which are required for the assembly of the mitotic spindle. Both proteins seem to interact with spindle microtubules to produce an outwardly directed force acting upon the poles.Emericella nidulans (Aspergillus nidulans) bimC, which plays an important role in nuclear division.A. nidulans klpA.Caenorhabditis elegans unc-104, which may be required for the transport of substances needed for neuronal cell differentiation.C. elegans osm-3.Xenopus laevis Eg5, which may be involved in mitosis.Arabidopsis thaliana KatA, KatB and katC.Chlamydomonas reinhardtii FLA10/KHP1 and KLP1. Both proteins seem to play a role in the rotation or twisting of the microtubules of the flagella.C. elegans hypothetical protein T09A5.2.The kinesin motor domain is located in the N-terminal part of most of the above proteins, with the exception of KAR3, klpA, and ncd where it is located in the C-terminal section.The kinesin motor domain contains about 330 amino acids. An ATP-binding motif of type A is found near position 80 to 90, the C-terminal half of the domain is involved in microtubule-binding.The signature pattern for this entry is derived from a conserved decapeptide inside the microtubule-binding region.
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Protein Domain
IPR001752 | Kinesin_motor_dom
Type: Domain
Description: Kinesin [, , ]is a microtubule-associated force-producing protein that may play a role in organelle transport. The kinesin motor activity is directed toward the microtubule's plus end. Kinesin is an oligomeric complex composed of two heavy chains and two light chains. The maintenance of the quaternary structure does not require interchain disulphide bonds.The heavy chain is composed of three structural domains: a large globular N-terminal domain which is responsible for the motor activity of kinesin (it is known to hydrolyse ATP, to bind and move on microtubules), a central α-helical coiled coil domain that mediates the heavy chain dimerisation; and a small globular C-terminal domain which interacts with other proteins (such as the kinesin light chains), vesicles and membranous organelles.The kinesin motor domain comprises five motifs, namely N1 (P-loop), N2 (Switch I), N3 (Switch II), N4 and L2 (KVD finger) []. It has a mixed eight stranded β-sheet core with flanking solvent exposed α-helices and a small three-stranded antiparallel β-sheet in the N-terminal region [].A number of proteins have been recently found that contain a domain similar to that of the kinesin 'motor' domain [, ]:Drosophila melanogaster claret segregational protein (ncd). Ncd is required for normal chromosomal segregation in meiosis, in females, and in early mitotic divisions of the embryo. The ncd motor activity is directed toward the microtubule's minus end.Homo sapiens CENP-E []. CENP-E is a protein that associates with kinetochores during chromosome congression, relocates to the spindle midzone at anaphase, and is quantitatively discarded at the end of the cell division. CENP-E is probably an important motor molecule in chromosome movement and/or spindle elongation.H. sapiens mitotic kinesin-like protein-1 (MKLP-1), a motor protein whose activity is directed toward the microtubule's plus end.Saccharomyces cerevisiae KAR3 protein, which is essential for nuclear fusion during mating. KAR3 may mediatemicrotubule sliding during nuclear fusion and possibly mitosis.S. cerevisiae CIN8 and KIP1 proteins which are required for the assembly of the mitotic spindle. Both proteins seem to interact with spindle microtubules to produce an outwardly directed force acting upon the poles.Emericella nidulans (Aspergillus nidulans) bimC, which plays an important role in nuclear division.A. nidulans klpA.Caenorhabditis elegans unc-104, which may be required for the transport of substances needed for neuronal cell differentiation.C. elegans osm-3.Xenopus laevis Eg5, which may be involved in mitosis.Arabidopsis thaliana KatA, KatB and katC.Chlamydomonas reinhardtii FLA10/KHP1 and KLP1. Both proteins seem to play a role in the rotation or twisting of the microtubules of the flagella.C. elegans hypothetical protein T09A5.2.The kinesin motor domain is located in the N-terminal part of most of the above proteins, with the exception of KAR3, klpA, and ncd where it is located in the C-terminal section.The kinesin motor domain contains about 330 amino acids. An ATP-binding motif of type A is found near position 80 to 90, the C-terminal half of the domain is involved in microtubule-binding.
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Protein
Q80TM9
Organism: Mus musculus/domesticus
Length: 1593  
Fragment?: false
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Protein
Q7TNC6
Organism: Mus musculus/domesticus
Length: 2112  
Fragment?: false
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Protein
P51942
Organism: Mus musculus/domesticus
Length: 500  
Fragment?: false
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Protein
Q6P9L6
Organism: Mus musculus/domesticus
Length: 1387  
Fragment?: false
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Protein
Q52KG5
Organism: Mus musculus/domesticus
Length: 1881  
Fragment?: false
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Publication
16434393 | -
First Author: Short KM
Year: 2006
Journal: J Biol Chem
Title: Subclassification of the RBCC/TRIM superfamily reveals a novel motif necessary for microtubule binding.
Volume: 281
Issue: 13
Pages: 8970-80
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Protein
Q99M15
Organism: Mus musculus/domesticus
Length: 334  
Fragment?: false
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Protein
Q9JK48
Organism: Mus musculus/domesticus
Length: 365  
Fragment?: false
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Protein
Q8R3V5
Organism: Mus musculus/domesticus
Length: 400  
Fragment?: false
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Protein
Q62420
Organism: Mus musculus/domesticus
Length: 352  
Fragment?: false
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Protein
Q61085
Organism: Mus musculus/domesticus
Length: 643  
Fragment?: false
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Protein
B1AUS7
Organism: Mus musculus/domesticus
Length: 101  
Fragment?: false
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Protein
A0A1Y7VN53
Organism: Mus musculus/domesticus
Length: 176  
Fragment?: false
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Protein
B0LDS3
Organism: Mus musculus/domesticus
Length: 395  
Fragment?: false
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Protein
C4MLI0
Organism: Mus musculus/domesticus
Length: 118  
Fragment?: false
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Protein
C4MLH9
Organism: Mus musculus/domesticus
Length: 133  
Fragment?: false
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Protein
Q6XAS4
Organism: Mus musculus/domesticus
Length: 170  
Fragment?: false
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Protein
B1AY40
Organism: Mus musculus/domesticus
Length: 170  
Fragment?: false
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Protein
Q9CPU1
Organism: Mus musculus/domesticus
Length: 170  
Fragment?: false
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Protein
Q6XAR7
Organism: Mus musculus/domesticus
Length: 170  
Fragment?: false
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Protein
Q3TG20
Organism: Mus musculus/domesticus
Length: 98  
Fragment?: true
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Protein
Q6ZQ98
Organism: Mus musculus/domesticus
Length: 937  
Fragment?: true
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Protein
Q5M8N5
Organism: Mus musculus/domesticus
Length: 212  
Fragment?: true
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Protein
Q8BT68
Organism: Mus musculus/domesticus
Length: 97  
Fragment?: false
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Protein
F6V6Z9
Organism: Mus musculus/domesticus
Length: 178  
Fragment?: true
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Protein
E0CXK4
Organism: Mus musculus/domesticus
Length: 84  
Fragment?: false
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Protein
Q2A657
Organism: Mus musculus/domesticus
Length: 119  
Fragment?: true
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Protein
Q8CES7
Organism: Mus musculus/domesticus
Length: 266  
Fragment?: false
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Protein
O35064
Organism: Mus musculus/domesticus
Length: 166  
Fragment?: true
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Protein
A0A286YD28
Organism: Mus musculus/domesticus
Length: 151  
Fragment?: true
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Protein
Q3UQ55
Organism: Mus musculus/domesticus
Length: 283  
Fragment?: false
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Protein
A0A1L1SQ84
Organism: Mus musculus/domesticus
Length: 303  
Fragment?: false
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Protein
Q8BIT4
Organism: Mus musculus/domesticus
Length: 248  
Fragment?: false
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Protein
Q99PU2
Organism: Mus musculus/domesticus
Length: 130  
Fragment?: true
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Protein
O35067
Organism: Mus musculus/domesticus
Length: 165  
Fragment?: true
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Protein
Q5BJ94
Organism: Mus musculus/domesticus
Length: 497  
Fragment?: false
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Protein
Q99PT6
Organism: Mus musculus/domesticus
Length: 155  
Fragment?: true
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Protein
Q99PU1
Organism: Mus musculus/domesticus
Length: 151  
Fragment?: true
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Protein
A0A286YDI7
Organism: Mus musculus/domesticus
Length: 144  
Fragment?: false
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Protein
Q6XAR6
Organism: Mus musculus/domesticus
Length: 170  
Fragment?: false
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Protein
Q5DTT9
Organism: Mus musculus/domesticus
Length: 668  
Fragment?: true
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Protein
A0A0A6YWT1
Organism: Mus musculus/domesticus
Length: 355  
Fragment?: true
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Protein
A0A286YCI2
Organism: Mus musculus/domesticus
Length: 207  
Fragment?: true
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Protein
Q8R248
Organism: Mus musculus/domesticus
Length: 343  
Fragment?: false
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Protein
A2AWI7
Organism: Mus musculus/domesticus
Length: 404  
Fragment?: false
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Protein
Q6XAR5
Organism: Mus musculus/domesticus
Length: 170  
Fragment?: false
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Protein
A0A1L1SU97
Organism: Mus musculus/domesticus
Length: 711  
Fragment?: true
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Protein
Q8C901
Organism: Mus musculus/domesticus
Length: 481  
Fragment?: true
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Protein
Q6XAS1
Organism: Mus musculus/domesticus
Length: 140  
Fragment?: true
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Protein
B7ZNZ3
Organism: Mus musculus/domesticus
Length: 170  
Fragment?: false
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Protein
E9PX64
Organism: Mus musculus/domesticus
Length: 1665  
Fragment?: false
•
•
•
•
•
Protein
A0A286YCJ8
Organism: Mus musculus/domesticus
Length: 51  
Fragment?: true
•
•
•
•
•
Protein
F6QAV8
Organism: Mus musculus/domesticus
Length: 227  
Fragment?: true
•
•
•
•
•
Protein
E9Q628
Organism: Mus musculus/domesticus
Length: 382  
Fragment?: false
•
•
•
•
•
Protein
A0A0J9YUN5
Organism: Mus musculus/domesticus
Length: 497  
Fragment?: false
•
•
•
•
•
Protein
Q3U4E4
Organism: Mus musculus/domesticus
Length: 334  
Fragment?: false
•
•
•
•
•
Protein
A0A494BBG6
Organism: Mus musculus/domesticus
Length: 312  
Fragment?: false
•
•
•
•
•
Protein
A0A1W2P7M3
Organism: Mus musculus/domesticus
Length: 194  
Fragment?: true
•
•
•
•
•
Protein
Q6XAR4
Organism: Mus musculus/domesticus
Length: 127  
Fragment?: true
•
•
•
•
•
Protein
A2AHC8
Organism: Mus musculus/domesticus
Length: 147  
Fragment?: true
•
•
•
•
•
Protein
A2BI73
Organism: Mus musculus/domesticus
Length: 179  
Fragment?: false
•
•
•
•
•
Protein
A0A286YE35
Organism: Mus musculus/domesticus
Length: 230  
Fragment?: true
•
•
•
•
•
Protein
Q5RJ53
Organism: Mus musculus/domesticus
Length: 298  
Fragment?: false
•
•
•
•
•
Protein
A0A0G2JEC4
Organism: Mus musculus/domesticus
Length: 394  
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