|  Help  |  About  |  Contact Us

Search our database by keyword

Examples

  • Search this entire website. Enter identifiers, names or keywords for genes, diseases, strains, ontology terms, etc. (e.g. Pax6, Parkinson, ataxia)
  • Use OR to search for either of two terms (e.g. OR mus) or quotation marks to search for phrases (e.g. "dna binding").
  • Boolean search syntax is supported: e.g. Balb* for partial matches or mus AND NOT embryo to exclude a term

Search results 301 to 400 out of 427 for Sos1

<< First    < Previous  |  Next >    Last >>
0.039s

Categories

Hits by Pathway

Hits by Category

Hits by Strain

Type Details Score
Protein
E0CX54
Organism: Mus musculus/domesticus
Length: 429  
Fragment?: true
•
•
•
•
•
Protein
B7ZNG9
Organism: Mus musculus/domesticus
Length: 490  
Fragment?: false
•
•
•
•
•
Protein
E9QKB7
Organism: Mus musculus/domesticus
Length: 679  
Fragment?: false
•
•
•
•
•
Protein
A0A0N4SVR5
Organism: Mus musculus/domesticus
Length: 498  
Fragment?: false
•
•
•
•
•
Protein
D3Z2F9
Organism: Mus musculus/domesticus
Length: 231  
Fragment?: true
•
•
•
•
•
Protein
B2RX11
Organism: Mus musculus/domesticus
Length: 1742  
Fragment?: false
•
•
•
•
•
Protein
A0A0N4SVF2
Organism: Mus musculus/domesticus
Length: 489  
Fragment?: false
•
•
•
•
•
Publication
18235501 | -
First Author: Kim JE
Year: 2008
Journal: Nature
Title: DBC1 is a negative regulator of SIRT1.
Volume: 451
Issue: 7178
Pages: 583-6
•
•
•
•
•
Publication
23352644 | -
First Author: Kim W
Year: 2013
Journal: Cancer Lett
Title: Deleted in breast cancer 1 (DBC1) deficiency results in apoptosis of breast cancer cells through impaired responses to UV-induced DNA damage.
Volume: 333
Issue: 2
Pages: 180-6
•
•
•
•
•
Publication
19657230 | -
First Author: Kim JE
Year: 2009
Journal: Cell Cycle
Title: p30 DBC is a potential regulator of tumorigenesis.
Volume: 8
Issue: 18
Pages: 2932-5
•
•
•
•
•
Protein Domain
IPR036964 | RASGEF_cat_dom_sf
Type: Homologous_superfamily
Description: Ras proteins are membrane-associated molecular switches that bind GTP and GDP and slowly hydrolyze GTP to GDP []in fundamental events such as signal transduction, cytoskeleton dynamics and intracellular trafficking. The balance between the GTP bound (active) and GDP bound (inactive) states is regulated by the opposite action of proteins activating the GTPase activity and that of proteins which promote the loss of bound GDP and the uptake of fresh GTP [, ]. The latter proteins are known as guanine-nucleotide exchange (or releasing) factors (GEFs or GRFs) (or also as guanine-nucleotide dissociation stimulators (GDSs)). GEFs catalyze thedissociation of GDP from the inactive GTP-binding proteins. GTP can then bind and induce structural changes that allow interaction with effectors [, ].The crystal structure of the GEF region of human Sos1 complexes with Ras has been solved []. The structure consists of two distinct alpha helical structural domains: the N-terminal domain which seems to have a purely structural role and the C-terminal domain which is sufficient for catalytic activity and contains all residues that interact with Ras. A main feature of the catalytic domain is the protrusion of a helical hairpin important for the nucleotide-exchange mechanism. The N-terminal domain is likely to be important for the stability and correct placement of the hairpin structure.Some proteins known to contain a Ras-GEF domain are listed below:Cdc25 from yeast.Scd25 from yeast.Ste6 from fission yeast.Son of sevenless (gene sos) from Drosophila and mammals.p140-RAS GRF (cdc25Mm) from mammals. This protein possesses both a domain belonging to the CDC25 family and one belonging to the CDC24 family.Bud5 from yeast, that may interact with the ras-like protein RSR1/BUD1.Lte1 from yeast, whose target protein is not yet known.ralGDS from mammals, which interacts with the ras-like proteins ralA and ralB [].This entry represents the C-terminal catalytic domain of the Ras guanine-nucleotide exchange factors.
•
•
•
•
•
Protein Domain
IPR019804 | Ras_G-nucl-exch_fac_CS
Type: Conserved_site
Description: Ras proteins are membrane-associated molecular switches that bind GTP and GDP and slowly hydrolyse GTP to GDP []. The balance between the GTP bound (active) and GDP bound (inactive) states is regulated by the opposite action of proteins activating the GTPase activity and that of proteins which promote the loss of bound GDP and the uptake of fresh GTP [, ]. The latter proteins are known as guanine-nucleotide dissociation stimulators (GDSs) (or also as guanine-nucleotide releasing (or exchange) factors (GRFs)). Proteins that act as GDS can be classified into at least two families, on the basis of sequence similarities, the CDC24 family (see ) and the CDC25 family.The size of the proteins of the CDC25 family range from 309 residues (LTE1) to 1596 residues (sos). The sequence similarity shared by all these proteins is limited to a region of about 250 amino acids generally located in their C-terminal section (currently the only exceptions are sos and ralGDS where this domain makes up the central part of the protein). This domain has been shown, in CDC25 an SCD25, to be essential for the activity of these proteins.The crystal structure of the GEF region of human Sos1 complexes with Ras has been solved []. The structure consists of two distinct alpha helical structural domains: the N-terminal domain which seems to have a purely structural role and the C-terminal domain which is sufficient for catalytic activity and contains all residues that interact with Ras. A main feature of the catalytic domain is the protrusion of a helical hairpin important for the nucleotide-exchange mechanism. The N-terminal domain is likely to be important for the stability and correct placement of the hairpin structure. The signature pattern for this entry spans the helical hairpin.
•
•
•
•
•
Protein Domain
IPR001895 | RASGEF_cat_dom
Type: Domain
Description: Ras proteins are membrane-associated molecular switches that bind GTP and GDP and slowly hydrolyze GTP to GDP []in fundamental events such as signal transduction, cytoskeleton dynamics and intracellular trafficking. The balance between the GTP bound (active) and GDP bound (inactive) states is regulated by the opposite action of proteins activating the GTPase activity and that of proteins which promote the loss of bound GDP and the uptake of fresh GTP [, ]. The latter proteins are known as guanine-nucleotide exchange (or releasing) factors (GEFs or GRFs) (or also as guanine-nucleotide dissociation stimulators (GDSs)). GEFs catalyze the dissociation of GDP from the inactive GTP-binding proteins. GTP can then bind and induce structural changes that allow interaction with effectors [, ].The crystal structure of the GEF region of human Sos1 complexes with Ras has been solved []. The structure consists of two distinct alpha helical structural domains: the N-terminal domain which seems to have a purely structural role and the C-terminal domain which is sufficient for catalytic activity and contains all residues that interact with Ras. A main feature of the catalytic domain is the protrusion of a helical hairpin important for the nucleotide-exchange mechanism. The N-terminal domain is likely to be important for the stability and correct placement of the hairpin structure.Some proteins known to contain a Ras-GEF domain are listed below:Cdc25 from yeast.Scd25 from yeast.Ste6 from fission yeast.Son of sevenless (gene sos) from Drosophila and mammals.p140-RAS GRF (cdc25Mm) from mammals. This protein possesses both a domain belonging to the CDC25 family and one belonging to the CDC24 family.Bud5 from yeast, that may interact with the ras-like protein RSR1/BUD1.Lte1 from yeast, whose target protein is not yet known.ralGDS from mammals, which interacts with the ras-like proteins ralA and ralB [].This entry represents the catalytic domain of the Ras guanine-nucleotide exchange factors.
•
•
•
•
•
Publication
15335949 | -
First Author: Downward J
Year: 1992
Journal: Curr Biol
Title: Ras regulation: putting back the GTP.
Volume: 2
Issue: 6
Pages: 329-31
•
•
•
•
•
Protein
Q60695
Organism: Mus musculus/domesticus
Length: 768  
Fragment?: false
•
•
•
•
•
Protein
Q03385
Organism: Mus musculus/domesticus
Length: 852  
Fragment?: false
•
•
•
•
•
Protein
Q8JZL7
Organism: Mus musculus/domesticus
Length: 473  
Fragment?: false
•
•
•
•
•
Protein
Q9D300
Organism: Mus musculus/domesticus
Length: 466  
Fragment?: false
•
•
•
•
•
Protein
Q3UYI5
Organism: Mus musculus/domesticus
Length: 709  
Fragment?: false
•
•
•
•
•
Protein
Q3TWC1
Organism: Mus musculus/domesticus
Length: 907  
Fragment?: false
•
•
•
•
•
Protein
E9Q8N0
Organism: Mus musculus/domesticus
Length: 766  
Fragment?: false
•
•
•
•
•
Protein
Q3UHC1
Organism: Mus musculus/domesticus
Length: 1224  
Fragment?: false
•
•
•
•
•
Protein
Q3UY04
Organism: Mus musculus/domesticus
Length: 461  
Fragment?: true
•
•
•
•
•
Protein
Q6ZPU1
Organism: Mus musculus/domesticus
Length: 924  
Fragment?: true
•
•
•
•
•
Protein
A0A571BEH0
Organism: Mus musculus/domesticus
Length: 869  
Fragment?: false
•
•
•
•
•
Protein
F7B9R2
Organism: Mus musculus/domesticus
Length: 588  
Fragment?: true
•
•
•
•
•
Protein
Q8C5V7
Organism: Mus musculus/domesticus
Length: 642  
Fragment?: true
•
•
•
•
•
Protein
A2AK33
Organism: Mus musculus/domesticus
Length: 895  
Fragment?: false
•
•
•
•
•
Protein
A0A5F8MPI9
Organism: Mus musculus/domesticus
Length: 1087  
Fragment?: false
•
•
•
•
•
Protein
Q3TXZ3
Organism: Mus musculus/domesticus
Length: 895  
Fragment?: false
•
•
•
•
•
Protein
A0A1B0GSM5
Organism: Mus musculus/domesticus
Length: 559  
Fragment?: false
•
•
•
•
•
Protein
E9Q8M9
Organism: Mus musculus/domesticus
Length: 803  
Fragment?: false
•
•
•
•
•
Protein
F6ZDE5
Organism: Mus musculus/domesticus
Length: 643  
Fragment?: true
•
•
•
•
•
Protein
Q3UQY9
Organism: Mus musculus/domesticus
Length: 840  
Fragment?: false
•
•
•
•
•
Protein
A1L338
Organism: Mus musculus/domesticus
Length: 1185  
Fragment?: false
•
•
•
•
•
Protein
Q91ZZ2
Organism: Mus musculus/domesticus
Length: 1086  
Fragment?: false
•
•
•
•
•
Protein
Q3UGX8
Organism: Mus musculus/domesticus
Length: 1218  
Fragment?: false
•
•
•
•
•
Publication
8259209 | J:16033
First Author: Boguski MS
Year: 1993
Journal: Nature
Title: Proteins regulating Ras and its relatives.
Volume: 366
Issue: 6456
Pages: 643-54
•
•
•
•
•
Protein
B1ATE5
Organism: Mus musculus/domesticus
Length: 425  
Fragment?: false
•
•
•
•
•
Protein
Q9QYS6
Organism: Mus musculus/domesticus
Length: 537  
Fragment?: true
•
•
•
•
•
Protein
E9Q813
Organism: Mus musculus/domesticus
Length: 431  
Fragment?: false
•
•
•
•
•
Protein
H3BKA8
Organism: Mus musculus/domesticus
Length: 216  
Fragment?: false
•
•
•
•
•
Protein
Q3TSK1
Organism: Mus musculus/domesticus
Length: 260  
Fragment?: true
•
•
•
•
•
Protein
Q8BTM9
Organism: Mus musculus/domesticus
Length: 673  
Fragment?: false
•
•
•
•
•
Protein
Q9QUG9
Organism: Mus musculus/domesticus
Length: 608  
Fragment?: false
•
•
•
•
•
Protein
G3UZQ7
Organism: Mus musculus/domesticus
Length: 546  
Fragment?: false
•
•
•
•
•
Protein
Q5DTR1
Organism: Mus musculus/domesticus
Length: 1046  
Fragment?: true
•
•
•
•
•
Protein
A0A0G2JFC0
Organism: Mus musculus/domesticus
Length: 186  
Fragment?: true
•
•
•
•
•
Protein
A0A0N4SVV6
Organism: Mus musculus/domesticus
Length: 576  
Fragment?: false
•
•
•
•
•
Protein
A0A1W2P765
Organism: Mus musculus/domesticus
Length: 198  
Fragment?: true
•
•
•
•
•
Protein
A0A0N4SUQ3
Organism: Mus musculus/domesticus
Length: 639  
Fragment?: false
•
•
•
•
•
Protein
A0A5F8MPT3
Organism: Mus musculus/domesticus
Length: 1267  
Fragment?: false
•
•
•
•
•
Protein
A0A0N4SUN7
Organism: Mus musculus/domesticus
Length: 604  
Fragment?: false
•
•
•
•
•
Protein
E0CZ06
Organism: Mus musculus/domesticus
Length: 659  
Fragment?: false
•
•
•
•
•
Protein
G3UYP5
Organism: Mus musculus/domesticus
Length: 481  
Fragment?: false
•
•
•
•
•
Protein
Q3UPQ2
Organism: Mus musculus/domesticus
Length: 1131  
Fragment?: true
•
•
•
•
•
Protein
A0A0N4SW33
Organism: Mus musculus/domesticus
Length: 581  
Fragment?: false
•
•
•
•
•
Protein
Q68EF8
Organism: Mus musculus/domesticus
Length: 662  
Fragment?: false
•
•
•
•
•
Protein
A0A087WPL3
Organism: Mus musculus/domesticus
Length: 128  
Fragment?: true
•
•
•
•
•
Protein
A0A0N4SVP1
Organism: Mus musculus/domesticus
Length: 484  
Fragment?: false
•
•
•
•
•
Protein
Q3TYC0
Organism: Mus musculus/domesticus
Length: 344  
Fragment?: false
•
•
•
•
•
Protein
A0A087WQU0
Organism: Mus musculus/domesticus
Length: 489  
Fragment?: false
•
•
•
•
•
Protein
A0A3Q4EGY1
Organism: Mus musculus/domesticus
Length: 63  
Fragment?: true
•
•
•
•
•
Protein
A0A087WQ61
Organism: Mus musculus/domesticus
Length: 463  
Fragment?: false
•
•
•
•
•
Protein
Q02384
Organism: Mus musculus/domesticus
Length: 1333  
Fragment?: false
•
•
•
•
•
Protein
Q8VCC8
Organism: Mus musculus/domesticus
Length: 918  
Fragment?: false
•
•
•
•
•
Protein
Q61193
Organism: Mus musculus/domesticus
Length: 778  
Fragment?: false
•
•
•
•
•
Protein
Q8C0Q9
Organism: Mus musculus/domesticus
Length: 814  
Fragment?: false
•
•
•
•
•
Protein
Q9EQZ6
Organism: Mus musculus/domesticus
Length: 1011  
Fragment?: false
•
•
•
•
•
Protein
Q62245
Organism: Mus musculus/domesticus
Length: 1319  
Fragment?: false
•
•
•
•
•
Protein
Q3USK4
Organism: Mus musculus/domesticus
Length: 1119  
Fragment?: false
•
•
•
•
•
Protein
A2ASW8
Organism: Mus musculus/domesticus
Length: 867  
Fragment?: false
•
•
•
•
•
Protein
A0A0A0MQ87
Organism: Mus musculus/domesticus
Length: 1332  
Fragment?: false
•
•
•
•
•
Protein
Q571A8
Organism: Mus musculus/domesticus
Length: 1035  
Fragment?: true
•
•
•
•
•
Protein
H3BK39
Organism: Mus musculus/domesticus
Length: 884  
Fragment?: false
•
•
•
•
•
Protein
S4R2C4
Organism: Mus musculus/domesticus
Length: 1300  
Fragment?: false
•
•
•
•
•
Protein
E9Q2E5
Organism: Mus musculus/domesticus
Length: 909  
Fragment?: false
•
•
•
•
•
Protein
A2ASW4
Organism: Mus musculus/domesticus
Length: 1011  
Fragment?: false
•
•
•
•
•
Protein
Q2M4G6
Organism: Mus musculus/domesticus
Length: 1174  
Fragment?: true
•
•
•
•
•
Protein
A0A068BD34
Organism: Mus musculus/domesticus
Length: 778  
Fragment?: false
•
•
•
•
•
Protein
Q3TES7
Organism: Mus musculus/domesticus
Length: 909  
Fragment?: false
•
•
•
•
•
Protein
Q3UQC2
Organism: Mus musculus/domesticus
Length: 926  
Fragment?: false
•
•
•
•
•
Protein
Q3UEA9
Organism: Mus musculus/domesticus
Length: 555  
Fragment?: true
•
•
•
•
•
Protein
Q9QYS5
Organism: Mus musculus/domesticus
Length: 248  
Fragment?: true
•
•
•
•
•
Protein
Q9Z1S3
Organism: Mus musculus/domesticus
Length: 795  
Fragment?: false
•
•
•
•
•
Protein
Q8CHG7
Organism: Mus musculus/domesticus
Length: 1496  
Fragment?: false
•
•
•
•
•
Protein
Q6NZH9
Organism: Mus musculus/domesticus
Length: 691  
Fragment?: false
•
•
•
•
•
Protein
Q5NCJ0
Organism: Mus musculus/domesticus
Length: 1601  
Fragment?: false
•
•
•
•
•
Protein
Q69ZX7
Organism: Mus musculus/domesticus
Length: 693  
Fragment?: true
•
•
•
•
•
Protein
A0A0A6YWG7
Organism: Mus musculus/domesticus
Length: 1644  
Fragment?: false
•
•
•
•
•
Protein
Q2PHE9
Organism: Mus musculus/domesticus
Length: 691  
Fragment?: false
•
•
•
•
•
Protein
Q5NCJ4
Organism: Mus musculus/domesticus
Length: 1123  
Fragment?: false
•
•
•
•
•
Protein
G3UYC3
Organism: Mus musculus/domesticus
Length: 760  
Fragment?: false
•
•
•
•
•
Protein
Q5NCJ1
Organism: Mus musculus/domesticus
Length: 1609  
Fragment?: false
•
•
•
•
•
Protein
E9QNQ4
Organism: Mus musculus/domesticus
Length: 1494  
Fragment?: false
•
•
•
•
•
Protein
G3UWW4
Organism: Mus musculus/domesticus
Length: 597  
Fragment?: false
•
•
•
•
•
Protein
Q6NXI4
Organism: Mus musculus/domesticus
Length: 1511  
Fragment?: true
•
•
•
•
•
Protein
Q5NCJ5
Organism: Mus musculus/domesticus
Length: 1131  
Fragment?: false
•
•
•
•
•
Protein
A0A0G2JGV2
Organism: Mus musculus/domesticus
Length: 260  
Fragment?: true
•
•
•
•
•
Protein
B2RUJ6
Organism: Mus musculus/domesticus
Length: 1606  
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