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Search results 101 to 180 out of 180 for Dennd1a

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Hits by Strain

Type Details Score
Protein
F6QZ02
Organism: Mus musculus/domesticus
Length: 198  
Fragment?: true
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Protein
F6RPS8
Organism: Mus musculus/domesticus
Length: 158  
Fragment?: true
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Protein
F7AWK3
Organism: Mus musculus/domesticus
Length: 257  
Fragment?: true
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Protein
Q9D8N2
Organism: Mus musculus/domesticus
Length: 357  
Fragment?: false
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Protein
D3YUG1
Organism: Mus musculus/domesticus
Length: 136  
Fragment?: true
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Protein
D6RG52
Organism: Mus musculus/domesticus
Length: 403  
Fragment?: false
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Protein
E9Q372
Organism: Mus musculus/domesticus
Length: 408  
Fragment?: false
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Protein
F6QG63
Organism: Mus musculus/domesticus
Length: 177  
Fragment?: true
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Protein
F6UAX9
Organism: Mus musculus/domesticus
Length: 236  
Fragment?: false
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Protein
Q3TH34
Organism: Mus musculus/domesticus
Length: 236  
Fragment?: false
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Protein
Q6NZD6
Organism: Mus musculus/domesticus
Length: 283  
Fragment?: true
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Protein
Q80ZM6
Organism: Mus musculus/domesticus
Length: 456  
Fragment?: true
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Protein
Q8BX53
Organism: Mus musculus/domesticus
Length: 572  
Fragment?: false
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Protein
Q8C8V8
Organism: Mus musculus/domesticus
Length: 390  
Fragment?: false
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Protein Domain
IPR005112 | dDENN_dom
Type: Domain
Description: This entry represents the dDENN domain.The tripartite DENN (Differentially Expressed in Normal and Neoplastic Cells) domain is an evolutionarily conserved protein module found in several proteins involved in Rab-mediated processes and, in some cases, regulation of MAPK (Mitogen-Activated Protein Kinase) signalling pathways and related proteins in eukaryotic organisms. The DENN domain consists of three subdomains: uDENN (upstream DENN) , the core DENN domain , and dDENN (downstream DENN) , which are structurally distinct but functionally interconnected due to their roles in Rab GTPase activation. Recent studies have confirmed the DENN domain's function as a guanine nucleotide exchange factor (GEF) for Rab GTPases, facilitating the exchange of GDP for GTP to activate Rabs. This activity has been demonstrated for various DENN proteins, such as DENND1A and DENND1B, which specifically activate Rab35, and DENND2B, which serves as a GEF for Rab10 and Rab13, influencing processes like primary ciliogenesis and epithelial cancer development [, , ].The tripartite structure of the DENN domain, comprising uDENN, DENN itself, and dDENN, features distinct patterns of sequence conservation and variable interdomain lengths that suggest functional specialisation. Structural studies have revealed conserved residues critical for Rab binding and catalytic activity, emphasising the role of DENN domains in spatially and temporally regulating membrane trafficking events []. Additionally, DENN domains are often associated with other domains such as RUN , PLAT , which may further enhance their functional versatility in cellular signalling pathways [].Some proteins known to contain a tripartite DENN domain include:Human mitogen-activated protein kinase activating protein containing death domain (MADD) , orthologous to Rab3GEPHuman SET domain-binding factor 1 (SBF1) Human DENN domain-containing protein 2B Human C-myc promoter-binding protein In Arabidopsis, SCD1 is a unique gene encoding for the only protein containing a complete DENN domain. SCD1 is part of a protein complex that interacts with the exocyst complex and the RabE1 family of GTPases. It is also involved in activating innate immune responses against bacteria [, ].Recent findings highlight the broader target spectrum of DENN domains than previously appreciated. For example, DENND2B interacts with Rab35 as both an effector and a GEF at intercellular bridges during cytokinesis. These discoveries underscore the importance of DENN domain proteins in regulating diverse cellular processes such as vesicle trafficking, signal transduction, ciliogenesis, and cancer progression [].
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Protein Domain
IPR037516 | Tripartite_DENN
Type: Domain
Description: This entry represents the full tripartite DENN domain.The tripartite DENN (Differentially Expressed in Normal and Neoplastic Cells) domain is an evolutionarily conserved protein module found in several proteins involved in Rab-mediated processes and, in some cases, regulation of MAPK (Mitogen-Activated Protein Kinase) signalling pathways and related proteins in eukaryotic organisms. The DENN domain consists of three subdomains: uDENN (upstream DENN) , the core DENN domain , and dDENN (downstream DENN) , which are structurally distinct but functionally interconnected due to their roles in Rab GTPase activation. Recent studies have confirmed the DENN domain's function as a guanine nucleotide exchange factor (GEF) for Rab GTPases, facilitating the exchange of GDP for GTP to activate Rabs. This activity has been demonstrated for various DENN proteins, such as DENND1A and DENND1B, which specifically activate Rab35, and DENND2B, which serves as a GEF for Rab10 and Rab13, influencing processes like primary ciliogenesis and epithelial cancer development [, , ].The tripartite structure of the DENN domain, comprising uDENN, DENN itself, and dDENN, features distinct patterns of sequence conservation and variable interdomain lengths that suggest functional specialisation. Structural studies have revealed conserved residues critical for Rab binding and catalytic activity, emphasising the role of DENN domains in spatially and temporally regulating membrane trafficking events []. Additionally, DENN domains are often associated with other domains such as RUN , PLAT , which may further enhance their functional versatility in cellular signalling pathways [].Some proteins known to contain a tripartite DENN domain include:Human mitogen-activated protein kinase activating protein containing death domain (MADD) , orthologous to Rab3GEPHuman SET domain-binding factor 1 (SBF1) Human DENN domain-containing protein 2B Human C-myc promoter-binding protein In Arabidopsis, SCD1 is a unique gene encoding for the only protein containing a complete DENN domain. SCD1 is part of a protein complex that interacts with the exocyst complex and the RabE1 family of GTPases. It is also involved in activating innate immune responses against bacteria [, ].Recent findings highlight the broader target spectrum of DENN domains than previously appreciated. For example, DENND2B interacts with Rab35 as both an effector and a GEF at intercellular bridges during cytokinesis. These discoveries underscore the importance of DENN domain proteins in regulating diverse cellular processes such as vesicle trafficking, signal transduction, ciliogenesis, and cancer progression [].
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Protein Domain
IPR005113 | uDENN_dom
Type: Domain
Description: The tripartite DENN (Differentially Expressed in Normal and Neoplastic Cells) domain is an evolutionarily conserved protein module found in several proteins involved in Rab-mediated processes and, in some cases, regulation of MAPK (Mitogen-Activated Protein Kinase) signalling pathways and related proteins in eukaryotic organisms. The DENN domain consists of three subdomains: uDENN (upstream DENN) , the core DENN domain , and dDENN (downstream DENN) , which are structurally distinct but functionally interconnected due to their roles in Rab GTPase activation. Recent studies have confirmed the DENN domain's function as a guanine nucleotide exchange factor (GEF) for Rab GTPases, facilitating the exchange of GDP for GTP to activate Rabs. This activity has been demonstrated for various DENN proteins, such as DENND1A and DENND1B, which specifically activate Rab35, and DENND2B, which serves as a GEF for Rab10 and Rab13, influencing processes like primary ciliogenesis and epithelial cancer development [, , ].The tripartite structure of the DENN domain, comprising uDENN, DENN itself, and dDENN, features distinct patterns of sequence conservation and variable interdomain lengths that suggest functional specialisation. Structural studies have revealed conserved residues critical for Rab binding and catalytic activity, emphasising the role of DENN domains in spatially and temporally regulating membrane trafficking events []. Additionally, DENN domains are often associated with other domains such as RUN , PLAT , which may further enhance their functional versatility in cellular signalling pathways [].Some proteins known to contain a tripartite DENN domain include:Human mitogen-activated protein kinase activating protein containing death domain (MADD) , orthologous to Rab3GEPHuman SET domain-binding factor 1 (SBF1) Human DENN domain-containing protein 2B Human C-myc promoter-binding protein In Arabidopsis, SCD1 is a unique gene encoding for the only protein containing a complete DENN domain. SCD1 is part of a protein complex that interacts with the exocyst complex and the RabE1 family of GTPases. It is also involved in activating innate immune responses against bacteria [, ].Recent findings highlight the broader target spectrum of DENN domains than previously appreciated. For example, DENND2B interacts with Rab35 as both an effector and a GEF at intercellular bridges during cytokinesis. These discoveries underscore the importance of DENN domain proteins in regulating diverse cellular processes such as vesicle trafficking, signal transduction, ciliogenesis, and cancer progression [].This entry represents the uDENN domain.
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Protein Domain
IPR001194 | cDENN_dom
Type: Domain
Description: This entry represents the core or cDENN domain.The tripartite DENN (Differentially Expressed in Normal and Neoplastic Cells) domain is an evolutionarily conserved protein module found in several proteins involved in Rab-mediated processes and, in some cases, regulation of MAPK (Mitogen-Activated Protein Kinase) signalling pathways and related proteins in eukaryotic organisms. The DENN domain consists of three subdomains: uDENN (upstream DENN) , the core DENN domain , and dDENN (downstream DENN) , which are structurally distinct but functionally interconnected due to their roles in Rab GTPase activation. Recent studies have confirmed the DENN domain's function as a guanine nucleotide exchange factor (GEF) for Rab GTPases, facilitating the exchange of GDP for GTP to activate Rabs. This activity has been demonstrated for various DENN proteins, such as DENND1A and DENND1B, which specifically activate Rab35, and DENND2B, which serves as a GEF for Rab10 and Rab13, influencing processes like primary ciliogenesis and epithelial cancer development [, , ].The tripartite structure of the DENN domain, comprising uDENN, DENN itself, and dDENN, features distinct patterns of sequence conservation and variable interdomain lengths that suggest functional specialisation. Structural studies have revealed conserved residues critical for Rab binding and catalytic activity, emphasising the role of DENN domains in spatially and temporally regulating membrane trafficking events []. Additionally, DENN domains are often associated with other domains such as RUN , PLAT , which may further enhance their functional versatility in cellular signalling pathways [].Some proteins known to contain a tripartite DENN domain include:Human mitogen-activated protein kinase activating protein containing death domain (MADD) , orthologous to Rab3GEPHuman SET domain-binding factor 1 (SBF1) Human DENN domain-containing protein 2B Human C-myc promoter-binding protein In Arabidopsis, SCD1 is a unique gene encoding for the only protein containing a complete DENN domain. SCD1 is part of a protein complex that interacts with the exocyst complex and the RabE1 family of GTPases. It is also involved in activating innate immune responses against bacteria [, ].Recent findings highlight the broader target spectrum of DENN domains than previously appreciated. For example, DENND2B interacts with Rab35 as both an effector and a GEF at intercellular bridges during cytokinesis. These discoveries underscore the importance of DENN domain proteins in regulating diverse cellular processes such as vesicle trafficking, signal transduction, ciliogenesis, and cancer progression [].
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Protein Domain
IPR043153 | DENN_C
Type: Homologous_superfamily
Description: This entry represents the C-terminal lobe of the DENN domain, which consists of a 5-stranded �� sheet surrounded by helices []. It includes DENN domain found in MAP kinases, myotubularin, and DENN-containing proteins from eukaryotic organisms. It also includes the elicitor of plant defence protein 1 found in fungi.The tripartite DENN (Differentially Expressed in Normal and Neoplastic Cells) domain is an evolutionarily conserved protein module found in several proteins involved in Rab-mediated processes and, in some cases, regulation of MAPK (Mitogen-Activated Protein Kinase) signalling pathways and related proteins in eukaryotic organisms. The DENN domain consists of three subdomains: uDENN (upstream DENN) , the core DENN domain , and dDENN (downstream DENN) , which are structurally distinct but functionally interconnected due to their roles in Rab GTPase activation. Recent studies have confirmed the DENN domain's function as a guanine nucleotide exchange factor (GEF) for Rab GTPases, facilitating the exchange of GDP for GTP to activate Rabs. This activity has been demonstrated for various DENN proteins, such as DENND1A and DENND1B, which specifically activate Rab35, and DENND2B, which serves as a GEF for Rab10 and Rab13, influencing processes like primary ciliogenesis and epithelial cancer development [, , ].The tripartite structure of the DENN domain, comprising uDENN, DENN itself, and dDENN, features distinct patterns of sequence conservation and variable interdomain lengths that suggest functional specialisation. Structural studies have revealed conserved residues critical for Rab binding and catalytic activity, emphasising the role of DENN domains in spatially and temporally regulating membrane trafficking events []. Additionally, DENN domains are often associated with other domains such as RUN , PLAT , which may further enhance their functional versatility in cellular signalling pathways [].Some proteins known to contain a tripartite DENN domain include:Human mitogen-activated protein kinase activating protein containing death domain (MADD) , orthologous to Rab3GEPHuman SET domain-binding factor 1 (SBF1) Human DENN domain-containing protein 2B Human C-myc promoter-binding protein In Arabidopsis, SCD1 is a unique gene encoding for the only protein containing a complete DENN domain. SCD1 is part of a protein complex that interacts with the exocyst complex and the RabE1 family of GTPases. It is also involved in activating innate immune responses against bacteria [, ].Recent findings highlight the broader target spectrum of DENN domains than previously appreciated. For example, DENND2B interacts with Rab35 as both an effector and a GEF at intercellular bridges during cytokinesis. These discoveries underscore the importance of DENN domain proteins in regulating diverse cellular processes such as vesicle trafficking, signal transduction, ciliogenesis, and cancer progression [].
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Protein
Q9D9V7
Organism: Mus musculus/domesticus
Length: 585  
Fragment?: false
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Protein
A6PWP7
Organism: Mus musculus/domesticus
Length: 263  
Fragment?: true
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Protein
B8JKU3
Organism: Mus musculus/domesticus
Length: 146  
Fragment?: true
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Protein
E9Q0R9
Organism: Mus musculus/domesticus
Length: 54  
Fragment?: true
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Protein
Q3TYX0
Organism: Mus musculus/domesticus
Length: 855  
Fragment?: false
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Protein
Q99LH6
Organism: Mus musculus/domesticus
Length: 232  
Fragment?: false
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Protein
Q80U28
Organism: Mus musculus/domesticus
Length: 1577  
Fragment?: false
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Protein
Q924W7
Organism: Mus musculus/domesticus
Length: 1134  
Fragment?: false
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Protein
Q6P9P8
Organism: Mus musculus/domesticus
Length: 914  
Fragment?: false
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Protein
Q8C4S8
Organism: Mus musculus/domesticus
Length: 1000  
Fragment?: false
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Protein
Q91VV4
Organism: Mus musculus/domesticus
Length: 469  
Fragment?: false
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Protein
A0A0R4J1F4
Organism: Mus musculus/domesticus
Length: 1558  
Fragment?: false
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Protein
A2AGQ2
Organism: Mus musculus/domesticus
Length: 1554  
Fragment?: false
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Protein
A2AGQ3
Organism: Mus musculus/domesticus
Length: 1541  
Fragment?: false
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Protein
A2AGQ4
Organism: Mus musculus/domesticus
Length: 1632  
Fragment?: false
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Protein
A2AGQ5
Organism: Mus musculus/domesticus
Length: 1593  
Fragment?: false
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Protein
A2AGQ6
Organism: Mus musculus/domesticus
Length: 1602  
Fragment?: false
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Protein
A2AGQ7
Organism: Mus musculus/domesticus
Length: 1573  
Fragment?: false
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Protein
A2AGQ8
Organism: Mus musculus/domesticus
Length: 1562  
Fragment?: false
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Protein
A2AGQ9
Organism: Mus musculus/domesticus
Length: 1574  
Fragment?: false
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Protein
A2AGR0
Organism: Mus musculus/domesticus
Length: 1577  
Fragment?: false
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Protein
A2AGR1
Organism: Mus musculus/domesticus
Length: 1475  
Fragment?: false
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Protein
A6PWP8
Organism: Mus musculus/domesticus
Length: 1115  
Fragment?: false
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Protein
E9QN47
Organism: Mus musculus/domesticus
Length: 1627  
Fragment?: false
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Protein
B7ZP28
Organism: Mus musculus/domesticus
Length: 999  
Fragment?: false
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Protein
E9Q4E4
Organism: Mus musculus/domesticus
Length: 920  
Fragment?: false
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Protein
G3UYA7
Organism: Mus musculus/domesticus
Length: 863  
Fragment?: false
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Protein
Q69ZA9
Organism: Mus musculus/domesticus
Length: 618  
Fragment?: true
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Protein
Q6NX80
Organism: Mus musculus/domesticus
Length: 668  
Fragment?: false
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Protein
S4R219
Organism: Mus musculus/domesticus
Length: 476  
Fragment?: false
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Publication
12906859 | -
First Author: Semova N
Year: 2003
Journal: Genomics
Title: Molecular cloning, structural analysis, and expression of a human IRLB, MYC promoter-binding protein: new DENN domain-containing protein family emerges.
Volume: 82
Issue: 3
Pages: 343-54
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Publication
35196081 | -
First Author: Kumar R
Year: 2022
Journal: Sci Adv
Title: A cell-based GEF assay reveals new substrates for DENN domains and a role for DENND2B in primary ciliogenesis.
Volume: 8
Issue: 8
Pages: eabk3088
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Publication
37454296 | -
First Author: Kumar R
Year: 2023
Journal: Cell Rep
Title: DENND2B activates Rab35 at the intercellular bridge, regulating cytokinetic abscission and tetraploidy.
Volume: 42
Issue: 7
Pages: 112795
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Publication
38296963 | -
First Author: Kumar R
Year: 2024
Journal: Nat Commun
Title: DENND6A links Arl8b to a Rab34/RILP/dynein complex, regulating lysosomal positioning and autophagy.
Volume: 15
Issue: 1
Pages: 919
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Publication
20472560 | -
First Author: Korasick DA
Year: 2010
Journal: J Biol Chem
Title: Novel functions of Stomatal Cytokinesis-Defective 1 (SCD1) in innate immune responses against bacteria.
Volume: 285
Issue: 30
Pages: 23342-50
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Publication
28970336 | -
First Author: Mayers JR
Year: 2017
Journal: Plant Cell
Title: SCD1 and SCD2 Form a Complex That Functions with the Exocyst and RabE1 in Exocytosis and Cytokinesis.
Volume: 29
Issue: 10
Pages: 2610-2625
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Protein
Q3TYW8
Organism: Mus musculus/domesticus
Length: 417  
Fragment?: false
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Protein
Q3TZ11
Organism: Mus musculus/domesticus
Length: 392  
Fragment?: true
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Protein
A2RT67
Organism: Mus musculus/domesticus
Length: 1274  
Fragment?: false
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Protein
Q3UHG7
Organism: Mus musculus/domesticus
Length: 455  
Fragment?: false
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Protein
Q80U56
Organism: Mus musculus/domesticus
Length: 649  
Fragment?: false
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Protein
Q8BH65
Organism: Mus musculus/domesticus
Length: 605  
Fragment?: false
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Protein
G3UYA1
Organism: Mus musculus/domesticus
Length: 1139  
Fragment?: false
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Protein
A0A0N4SUI4
Organism: Mus musculus/domesticus
Length: 222  
Fragment?: false
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Protein
A0A286YDD5
Organism: Mus musculus/domesticus
Length: 255  
Fragment?: false
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Protein
A6H8H2
Organism: Mus musculus/domesticus
Length: 1906  
Fragment?: false
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Protein
E9PXF8
Organism: Mus musculus/domesticus
Length: 1872  
Fragment?: false
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Protein
Q6ZPE2
Organism: Mus musculus/domesticus
Length: 1867  
Fragment?: false
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Protein
Q3U1Y4
Organism: Mus musculus/domesticus
Length: 1499  
Fragment?: false
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Protein
Q6PAL8
Organism: Mus musculus/domesticus
Length: 1287  
Fragment?: false
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Protein
A2RSQ0
Organism: Mus musculus/domesticus
Length: 1274  
Fragment?: false
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Protein
E9Q8V6
Organism: Mus musculus/domesticus
Length: 1869  
Fragment?: false
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Protein
A0A0R4J172
Organism: Mus musculus/domesticus
Length: 1510  
Fragment?: false
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Protein
A0A0R4J1B6
Organism: Mus musculus/domesticus
Length: 1263  
Fragment?: false
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Protein
B9EKY0
Organism: Mus musculus/domesticus
Length: 1354  
Fragment?: false
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Protein
E9Q449
Organism: Mus musculus/domesticus
Length: 1615  
Fragment?: false
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Publication
11563850 | -
First Author: Levivier E
Year: 2001
Journal: Biochem Biophys Res Commun
Title: uDENN, DENN, and dDENN: indissociable domains in Rab and MAP kinases signaling pathways.
Volume: 287
Issue: 3
Pages: 688-95
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Publication
22065758 | -
First Author: Wu X
Year: 2011
Journal: Proc Natl Acad Sci U S A
Title: Insights regarding guanine nucleotide exchange from the structure of a DENN-domain protein complexed with its Rab GTPase substrate.
Volume: 108
Issue: 46
Pages: 18672-7
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Protein
E9Q0D4
Organism: Mus musculus/domesticus
Length: 1826  
Fragment?: false
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Publication
22977732 | -
First Author: Nookala RK
Year: 2012
Journal: Open Biol
Title: Crystal structure of folliculin reveals a hidDENN function in genetically inherited renal cancer.
Volume: 2
Issue: 8
Pages: 120071
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Publication
23248642 | -
 
First Author: Zhang D
Year: 2012
Journal: Front Genet
Title: Discovery of Novel DENN Proteins: Implications for the Evolution of Eukaryotic Intracellular Membrane Structures and Human Disease.
Volume: 3
Pages: 283
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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