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Search results 101 to 200 out of 253 for Cdc16

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Type Details Score
Publication
30654941 | J:293228
First Author: Fujimoto T
Year: 2019
Journal: Biochem Biophys Res Commun
Title: Overexpression of Interleukin-15 exhibits improved glucose tolerance and promotes GLUT4 translocation via AMP-Activated protein kinase pathway in skeletal muscle.
Volume: 509
Issue: 4
Pages: 994-1000
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Publication
27307439 | J:234284
First Author: Chen L
Year: 2016
Journal: Proc Natl Acad Sci U S A
Title: Disruption of the AMPK-TBC1D1 nexus increases lipogenic gene expression and causes obesity in mice via promoting IGF1 secretion.
Volume: 113
Issue: 26
Pages: 7219-24
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Publication
10220406 | -
First Author: Li R
Year: 1999
Journal: Proc Natl Acad Sci U S A
Title: Bifurcation of the mitotic checkpoint pathway in budding yeast.
Volume: 96
Issue: 9
Pages: 4989-94
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Publication
10228157 | -
First Author: Fesquet D
Year: 1999
Journal: EMBO J
Title: A Bub2p-dependent spindle checkpoint pathway regulates the Dbf2p kinase in budding yeast.
Volume: 18
Issue: 9
Pages: 2424-34
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Publication
11084339 | -
First Author: Wang Y
Year: 2000
Journal: Curr Biol
Title: The Bfa1/Bub2 GAP complex comprises a universal checkpoint required to prevent mitotic exit.
Volume: 10
Issue: 21
Pages: 1379-82
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Publication
15147270 | -
First Author: Kim J
Year: 2004
Journal: Genes Cells
Title: The C-terminus of Bfa1p in budding yeast is essential to induce mitotic arrest in response to diverse checkpoint-activating signals.
Volume: 9
Issue: 5
Pages: 399-418
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Protein Domain
IPR034586 | Bfa1/Byr4
Type: Family
Description: Bfa1 is required for the spindle assembly checkpoint in budding yeast. It functions in the same pathway with Bub2 in one of the branches of the spindle assembly checkpoint which prevents cytokinesis before the completion of chromosome segregation [, ]. Bub2 and Bfa1 are also required for the maintenance of G2/M arrest in response to DNA damage and to spindle misorientation []. The homologue of Bfa1 in fission yeast is Byr4, which together with Cdc16 (homologue of Bub2) forms a two-component GTPase-activating protein for Spg1 GTPase [, ]. Spg1 GTPase positively regulates septation and constriction of the actomyosin ring for cell division.Bfa1 and Bub2 may function as a universal checkpoint in response to various checkpoint signals to avoid improper mitotic exit [].
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Protein
Q9D3N8
Organism: Mus musculus/domesticus
Length: 359  
Fragment?: false
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Protein
Q8BHL3
Organism: Mus musculus/domesticus
Length: 798  
Fragment?: false
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Protein
A1A5B6
Organism: Mus musculus/domesticus
Length: 742  
Fragment?: false
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Protein
Q9D9D3
Organism: Mus musculus/domesticus
Length: 336  
Fragment?: false
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Protein
Q80XQ2
Organism: Mus musculus/domesticus
Length: 815  
Fragment?: false
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Protein
Q8C9V1
Organism: Mus musculus/domesticus
Length: 444  
Fragment?: false
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Protein
Q80XC3
Organism: Mus musculus/domesticus
Length: 819  
Fragment?: false
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Protein
Q6A039
Organism: Mus musculus/domesticus
Length: 696  
Fragment?: false
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Protein
Q8CGA2
Organism: Mus musculus/domesticus
Length: 694  
Fragment?: false
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Protein
Q8R5A6
Organism: Mus musculus/domesticus
Length: 516  
Fragment?: false
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Protein
Q8R3D1
Organism: Mus musculus/domesticus
Length: 400  
Fragment?: false
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Publication
7566974 | -
First Author: Richardson PM
Year: 1995
Journal: Oncogene
Title: Molecular cloning of a cDNA with a novel domain present in the tre-2 oncogene and the yeast cell cycle regulators BUB2 and cdc16.
Volume: 11
Issue: 6
Pages: 1139-48
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Protein
P58802
Organism: Mus musculus/domesticus
Length: 500  
Fragment?: false
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Protein
Q80VE5
Organism: Mus musculus/domesticus
Length: 505  
Fragment?: false
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Protein
Q6PFC0
Organism: Mus musculus/domesticus
Length: 765  
Fragment?: false
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Protein
E9Q8K4
Organism: Mus musculus/domesticus
Length: 694  
Fragment?: false
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Protein
Q3TGE9
Organism: Mus musculus/domesticus
Length: 432  
Fragment?: false
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Protein
G3UVU5
Organism: Mus musculus/domesticus
Length: 714  
Fragment?: false
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Protein
A0A494BA22
Organism: Mus musculus/domesticus
Length: 623  
Fragment?: false
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Protein
Q8K257
Organism: Mus musculus/domesticus
Length: 146  
Fragment?: false
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Protein
G3UWY9
Organism: Mus musculus/domesticus
Length: 191  
Fragment?: true
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Protein
E9Q2V7
Organism: Mus musculus/domesticus
Length: 618  
Fragment?: false
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Protein
Q5SPX8
Organism: Mus musculus/domesticus
Length: 534  
Fragment?: false
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Protein
Q921M0
Organism: Mus musculus/domesticus
Length: 353  
Fragment?: false
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Protein
Q3TSE1
Organism: Mus musculus/domesticus
Length: 231  
Fragment?: true
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Protein
A0A0U1RPN1
Organism: Mus musculus/domesticus
Length: 189  
Fragment?: true
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Protein
A2ABG4
Organism: Mus musculus/domesticus
Length: 766  
Fragment?: false
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Protein
Q571E6
Organism: Mus musculus/domesticus
Length: 329  
Fragment?: true
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Protein
Q3US32
Organism: Mus musculus/domesticus
Length: 500  
Fragment?: false
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Protein
A2BD48
Organism: Mus musculus/domesticus
Length: 717  
Fragment?: true
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Protein
B7ZNA7
Organism: Mus musculus/domesticus
Length: 621  
Fragment?: false
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Protein
Q8BXI6
Organism: Mus musculus/domesticus
Length: 171  
Fragment?: false
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Protein
Q3U325
Organism: Mus musculus/domesticus
Length: 837  
Fragment?: false
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Protein
Q5U224
Organism: Mus musculus/domesticus
Length: 603  
Fragment?: false
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Protein
A0A1L1STB7
Organism: Mus musculus/domesticus
Length: 309  
Fragment?: false
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Protein
Q3TZ63
Organism: Mus musculus/domesticus
Length: 400  
Fragment?: false
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Protein
Q8BT80
Organism: Mus musculus/domesticus
Length: 305  
Fragment?: false
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Protein
Q8CC81
Organism: Mus musculus/domesticus
Length: 408  
Fragment?: false
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Protein
Q76LY3
Organism: Mus musculus/domesticus
Length: 413  
Fragment?: false
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Protein
Q9DAW8
Organism: Mus musculus/domesticus
Length: 332  
Fragment?: false
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Protein
A2VCT6
Organism: Mus musculus/domesticus
Length: 718  
Fragment?: true
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Protein
Q8K2U6
Organism: Mus musculus/domesticus
Length: 374  
Fragment?: true
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Protein
A0A494BA99
Organism: Mus musculus/domesticus
Length: 189  
Fragment?: false
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Protein
A0A286YDB3
Organism: Mus musculus/domesticus
Length: 837  
Fragment?: false
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Protein
E9QQ68
Organism: Mus musculus/domesticus
Length: 698  
Fragment?: false
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Protein
Q571D8
Organism: Mus musculus/domesticus
Length: 821  
Fragment?: true
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Protein
A0A1B0GSU4
Organism: Mus musculus/domesticus
Length: 197  
Fragment?: false
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Protein
Q6PAT2
Organism: Mus musculus/domesticus
Length: 163  
Fragment?: false
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Protein
A0A1B0GSA2
Organism: Mus musculus/domesticus
Length: 289  
Fragment?: false
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Protein
E9PWX7
Organism: Mus musculus/domesticus
Length: 723  
Fragment?: false
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Protein
S4R2S6
Organism: Mus musculus/domesticus
Length: 560  
Fragment?: false
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Protein
E9PZY7
Organism: Mus musculus/domesticus
Length: 305  
Fragment?: false
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Protein
Q8BXD8
Organism: Mus musculus/domesticus
Length: 766  
Fragment?: false
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Protein
A0A3Q4L343
Organism: Mus musculus/domesticus
Length: 198  
Fragment?: true
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Protein
Q4KMV6
Organism: Mus musculus/domesticus
Length: 653  
Fragment?: false
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Protein
A0A494BAA5
Organism: Mus musculus/domesticus
Length: 192  
Fragment?: false
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Protein
A0A6I8MX15
Organism: Mus musculus/domesticus
Length: 688  
Fragment?: false
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Protein
Q3UN43
Organism: Mus musculus/domesticus
Length: 544  
Fragment?: false
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Protein
Q8CI62
Organism: Mus musculus/domesticus
Length: 500  
Fragment?: false
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Protein
E9PYB1
Organism: Mus musculus/domesticus
Length: 413  
Fragment?: false
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Publication
9255064 | -
First Author: Neuwald AF
Year: 1997
Journal: Trends Biochem Sci
Title: A shared domain between a spindle assembly checkpoint protein and Ypt/Rab-specific GTPase-activators.
Volume: 22
Issue: 7
Pages: 243-4
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Publication
11013213 | -
First Author: Rak A
Year: 2000
Journal: EMBO J
Title: Crystal structure of the GAP domain of Gyp1p: first insights into interaction with Ypt/Rab proteins.
Volume: 19
Issue: 19
Pages: 5105-13
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Publication
10508155 | -
First Author: Albert S
Year: 1999
Journal: EMBO J
Title: Identification of the catalytic domains and their functionally critical arginine residues of two yeast GTPase-activating proteins specific for Ypt/Rab transport GTPases.
Volume: 18
Issue: 19
Pages: 5216-25
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Publication
8654926 | -
First Author: Zhang SD
Year: 1996
Journal: Genes Dev
Title: Pollux, a novel Drosophila adhesion molecule, belongs to a family of proteins expressed in plants, yeast, nematodes, and man.
Volume: 10
Issue: 9
Pages: 1108-19
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Protein
A0A1W2P853
Organism: Mus musculus/domesticus
Length: 240  
Fragment?: true
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Protein
Q8BW21
Organism: Mus musculus/domesticus
Length: 100  
Fragment?: true
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Protein
Q8K0Q9
Organism: Mus musculus/domesticus
Length: 121  
Fragment?: true
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Protein Domain
IPR000195 | Rab-GTPase-TBC_dom
Type: Domain
Description: The ~200 amino acid TBC/rab GTPase-activating protein (GAP) domain is well conserved across species and has been found in a wide range of different proteins from plant adhesion molecules to mammalian oncogenes. The name TBC derives from the name of the murine protein Tbc1 in which this domain was first identified based on its similarity to sequences in the tre-2 oncogene, and the yeast regulators of mitosis, BUB2 and cdc16 []. The connection of this domain with rab GTPase activation stems from subsequent in-depth sequence analyses and alignments []and recent work demonstrating that it appears to contain the catalytic activities of the yeast rab GAPs, GYP1, and GYP7 [].The TBC/rab GAP domain has also been named PTM after three proteins known to contain it: the Drosophila pollux, the human oncoprotein TRE17 (oncoTRE17), and a myeloid cell line-expressed protein []. The TBC/rab GAP domain contains six conserved motifs named A to F []. A conserved arginine residue in the sequence motif B has been shown to be critical for the full GAP activity []. Resolution of the 3D structure of the TBC/rab GAP domain of GYP1 has shown that it is a fully α-helical V-shaped molecule. The conserved arginine residue is positioned at the side of the narrow cleft on the concave site of the V-shaped molecule. It has been proposed that this cleft is the binding site for the GTPase. The conserved arginine residue probably functions as a catalytic arginine finger analogous to that seen in ras and Rho-GAPs. The two key features of the arginine finger activation mechanism appear to be (i) the positioning of the catalytically essential GTPase glutamine side chain via a hydrogen bonding interaction between the glutamine carbamoyl-NH2 group and the main chain carbonyl group of the GAP arginine, and (ii) the polarization of the gamma-phosphate group or the stabilization of charge on it via the interaction of the positively charged side chain guanidinoyl group of the GAP arginine [].
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Protein Domain
IPR035969 | Rab-GTPase_TBC_sf
Type: Homologous_superfamily
Description: The ~200 amino acid TBC/rab GTPase-activating protein (GAP) domain is well conserved across species and has been found in a wide range of different proteins from plant adhesion molecules to mammalian oncogenes. The name TBC derives from the name of the murine protein Tbc1 in which this domain was first identified based on its similarity to sequences in the tre-2 oncogene, and the yeast regulators of mitosis, BUB2 and cdc16 []. The connection of this domain with rab GTPase activation stems from subsequent in-depth sequence analyses and alignments []and recent work demonstrating that it appears to contain the catalytic activities of the yeast rab GAPs, GYP1, and GYP7 [].The TBC/rab GAP domain has also been named PTM after three proteins known to contain it: the Drosophila pollux, the human oncoprotein TRE17 (oncoTRE17), and a myeloid cell line-expressed protein []. The TBC/rab GAP domain contains six conserved motifs named A to F []. A conserved arginine residue in the sequence motif B has been shown to be critical for the full GAP activity []. Resolution of the 3D structure of the TBC/rab GAP domain of GYP1 has shown that it is a fully α-helical V-shaped molecule. The conserved arginine residue is positioned at the side of the narrow cleft on the concave site of the V-shaped molecule. It has been proposed that this cleft is the binding site for the GTPase. The conserved arginine residue probably functions as a catalytic arginine finger analogous to that seen in ras and Rho-GAPs. The two key features of the arginine finger activation mechanism appear to be (i) the positioning of the catalytically essential GTPase glutamine side chain via a hydrogen bonding interaction between the glutamine carbamoyl-NH2 group and the main chain carbonyl group of the GAP arginine, and (ii) the polarization of the gamma-phosphate group or the stabilization of charge on it via the interaction of the positively charged side chain guanidinoyl group of the GAP arginine [].
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Protein
Q3URV1
Organism: Mus musculus/domesticus
Length: 1296  
Fragment?: false
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Protein
A0A0A6YW18
Organism: Mus musculus/domesticus
Length: 107  
Fragment?: true
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Protein
B0R080
Organism: Mus musculus/domesticus
Length: 80  
Fragment?: true
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Protein
Q8C7X7
Organism: Mus musculus/domesticus
Length: 163  
Fragment?: false
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Protein
P97366
Organism: Mus musculus/domesticus
Length: 809  
Fragment?: false
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Protein
Q8BPQ7
Organism: Mus musculus/domesticus
Length: 1093  
Fragment?: false
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Protein
Q80U12
Organism: Mus musculus/domesticus
Length: 1005  
Fragment?: false
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Protein
Q3UUG6
Organism: Mus musculus/domesticus
Length: 561  
Fragment?: false
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Protein
Q9D0K0
Organism: Mus musculus/domesticus
Length: 293  
Fragment?: false
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Protein
Q69ZT9
Organism: Mus musculus/domesticus
Length: 766  
Fragment?: false
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Protein
Q9D9I4
Organism: Mus musculus/domesticus
Length: 402  
Fragment?: false
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Protein
Q8BYH7
Organism: Mus musculus/domesticus
Length: 645  
Fragment?: false
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Protein
Q9CXF4
Organism: Mus musculus/domesticus
Length: 671  
Fragment?: false
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Protein
Q3U5C0
Organism: Mus musculus/domesticus
Length: 645  
Fragment?: false
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Protein
H3BJX1
Organism: Mus musculus/domesticus
Length: 406  
Fragment?: false
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Protein
Q3UDU6
Organism: Mus musculus/domesticus
Length: 652  
Fragment?: false
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Protein
Q3TNX9
Organism: Mus musculus/domesticus
Length: 213  
Fragment?: true
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Protein
B0R081
Organism: Mus musculus/domesticus
Length: 155  
Fragment?: true
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Protein
Q8BRB6
Organism: Mus musculus/domesticus
Length: 325  
Fragment?: false
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Protein
Q8VDV7
Organism: Mus musculus/domesticus
Length: 526  
Fragment?: false
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Protein
Q3TMK4
Organism: Mus musculus/domesticus
Length: 376  
Fragment?: true
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Protein
Q3T9Q0
Organism: Mus musculus/domesticus
Length: 244  
Fragment?: true
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Protein
E9Q9B1
Organism: Mus musculus/domesticus
Length: 365  
Fragment?: true
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Protein
Q3UYX4
Organism: Mus musculus/domesticus
Length: 600  
Fragment?: true
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

Copyright © 2017 by The Jackson Laboratory. All Rights Reserved

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