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Search results 201 to 249 out of 249 for Ulk2

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Type Details Score
Allele
Ulk2<em1Smoc> | MGI:7293072
Name: unc-51 like kinase 2; endonuclease-mediated mutation 1, Shanghai Model Organisms Center
Allele Type: Endonuclease-mediated
Attribute String: Null/knockout
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Strain
MGI:6429761 | C57BL/6JSmoc-Ulk2<em1Smoc>/Smoc
Attribute String: coisogenic, mutant strain, endonuclease-mediated mutation
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Publication
16887332 | -
First Author: Avery AW
Year: 2007
Journal: Cell Signal
Title: UNC-51-like kinase regulation of fibroblast growth factor receptor substrate 2/3.
Volume: 19
Issue: 1
Pages: 177-84
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Publication
21258367 | J:175316
First Author: Kim J
Year: 2011
Journal: Nat Cell Biol
Title: AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1.
Volume: 13
Issue: 2
Pages: 132-41
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GO Term
GO:1990316 | Atg1/ULK1 kinase complex
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Publication
21460634 | -
First Author: Löffler AS
Year: 2011
Journal: Autophagy
Title: Ulk1-mediated phosphorylation of AMPK constitutes a negative regulatory feedback loop.
Volume: 7
Issue: 7
Pages: 696-706
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Publication
21795849 | J:314079
First Author: Jung CH
Year: 2011
Journal: Autophagy
Title: ULK1 inhibits the kinase activity of mTORC1 and cell proliferation.
Volume: 7
Issue: 10
Pages: 1212-21
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Protein Domain
IPR016237 | Ser/Thr_kin_STPK_Ulk-1/2
Type: Family
Description: Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity []:Serine/threonine-protein kinasesTyrosine-protein kinasesDual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins)Protein kinase function is evolutionarily conserved from Escherichia coli to human []. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation []. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins. The catalytic subunits of protein kinases are highly conserved, and several structures have been solved [], leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases [].This represents serine/threonine-protein kinases (), such as Ulk1 and Ulk2 (Unc-51-Like Kinase). Ulk1 and Ulk2 regulate filopodia extension and branching of sensory axons. They are important for axon growth, playing an essential role in neurite extension of cerebellar granule cells [, ].
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Publication
19225151 | J:314078
First Author: Jung CH
Year: 2009
Journal: Mol Biol Cell
Title: ULK-Atg13-FIP200 complexes mediate mTOR signaling to the autophagy machinery.
Volume: 20
Issue: 7
Pages: 1992-2003
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Publication
32203415 | J:291404
First Author: Tsang T
Year: 2020
Journal: Nat Cell Biol
Title: Copper is an essential regulator of the autophagic kinases ULK1/2 to drive lung adenocarcinoma.
Volume: 22
Issue: 4
Pages: 412-424
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Publication
7389358 | -
   
Year: 1980
Journal: Contrib Nephrol
Title: Disturbances of water and electrolyte metabolism.
Volume: 21
Pages: 1-152
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Protein Coding Gene
MGI:2445123 | Wdr41
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1915368 | Atg101
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
Q8K0Q7
Organism: Mus musculus/domesticus
Length: 327  
Fragment?: true
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Publication
16887826 | -
First Author: Ogura K
Year: 2006
Journal: Development
Title: The autophagy-related kinase UNC-51 and its binding partner UNC-14 regulate the subcellular localization of the Netrin receptor UNC-5 in Caenorhabditis elegans.
Volume: 133
Issue: 17
Pages: 3441-50
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Publication
17890369 | -
First Author: Aladzsity I
Year: 2007
Journal: Genetics
Title: Autophagy genes unc-51 and bec-1 are required for normal cell size in Caenorhabditis elegans.
Volume: 177
Issue: 1
Pages: 655-60
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Publication
19377305 | -
First Author: Tian E
Year: 2009
Journal: Autophagy
Title: epg-1 functions in autophagy-regulated processes and may encode a highly divergent Atg13 homolog in C. elegans.
Volume: 5
Issue: 5
Pages: 608-15
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Protein
A0A0G2JFU2
Organism: Mus musculus/domesticus
Length: 86  
Fragment?: true
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Protein
A0A0G2JG09
Organism: Mus musculus/domesticus
Length: 84  
Fragment?: true
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Publication
24793651 | -
First Author: Fujioka Y
Year: 2014
Journal: Nat Struct Mol Biol
Title: Structural basis of starvation-induced assembly of the autophagy initiation complex.
Volume: 21
Issue: 6
Pages: 513-21
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Publication
21984698 | -
First Author: Suttangkakul A
Year: 2011
Journal: Plant Cell
Title: The ATG1/ATG13 protein kinase complex is both a regulator and a target of autophagic recycling in Arabidopsis.
Volume: 23
Issue: 10
Pages: 3761-79
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Protein Domain
IPR045269 | Atg1-like
Type: Family
Description: This entry represents a group of Serine/threonine-protein kinases, including Atg1 from yeasts, Unc-51 from C. elegans, Ulk1-3 from humans and ATG1a/b/c/t from Arabidopsis.Atg1 is required for vesicle formation in autophagy and the cytoplasm-to-vacuole targeting (Cvt) pathway [].Ulk1-3 are involved in autophagy in response to starvation [, ]. Ulk1 and Ulk2 regulate filopodia extension and branching of sensory axons. They are important for axon growth, playing an essential role in neurite extension of cerebellar granule cells [, ]. Unc-51 is important for axonal elongation and axonal guidance []. It is required for either the maintenance of axons (membrane turnover) or for an unknown neuronal function. C elegans worms lacking Unc-51 exhibit various abnormalities in axonal elongation and axonal structures. Unc-51 could also help control cell size along with Bec-1, as mutations in their corresponding genes results in a reduction in small body size without affecting cell number []. Unc-51 is also a component of the Unc-51/Atg-13 complex that is probably recruited by lgg-1 to preautophagosomes and is required for autophagosome formation [].In plants, the ATG1/13 complex is both a regulator and a target of autophagy [].
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Protein Domain
IPR022708 | Atg1-like_tMIT
Type: Domain
Description: This the Atg13-binding region of Atg1 which comprises two tandem MIT (microtubule interacting and transport) domains, named tMIT [].Members of this entry are Serine/threonine-protein kinases, including Atg1 from yeasts, Unc-51 from C. elegans and Ulk1-2 from humans.Atg1 is required for vesicle formation in autophagy and the cytoplasm-to-vacuole targeting (Cvt) pathway [, ].Ulk1-2 are involved in autophagy in response to starvation [, ]. Ulk1 and Ulk2 regulate filopodia extension and branching of sensory axons. They are important for axon growth, playing an essential role in neurite extension of cerebellar granule cells [, ]. Unc-51 is important for axonal elongation and axonal guidance []. It is required for either the maintenance of axons (membrane turnover) or for an unknown neuronal function. C elegans worms lacking Unc-51 exhibit various abnormalities in axonal elongation and axonal structures. Unc-51 could also help control cell size along with Bec-1, as mutations in their corresponding genes results in a reduction in small body size without affecting cell number []. Unc-51 is also a component of the Unc-51/Atg-13 complex that is probably recruited by lgg-1 to preautophagosomes and is required for autophagosome formation [].
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Publication
17204848 | -
First Author: Meijer WH
Year: 2007
Journal: Autophagy
Title: ATG genes involved in non-selective autophagy are conserved from yeast to man, but the selective Cvt and pexophagy pathways also require organism-specific genes.
Volume: 3
Issue: 2
Pages: 106-16
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Protein Coding Gene
MGI:1196429 | Atg13
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
O70405
Organism: Mus musculus/domesticus
Length: 1051  
Fragment?: false
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Protein
Q3UFT4
Organism: Mus musculus/domesticus
Length: 1057  
Fragment?: false
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Protein
Q6PB82
Organism: Mus musculus/domesticus
Length: 1057  
Fragment?: false
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Protein
A0A0R4J0B3
Organism: Mus musculus/domesticus
Length: 1051  
Fragment?: false
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Protein
Q3UG39
Organism: Mus musculus/domesticus
Length: 1037  
Fragment?: false
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Protein
Q80TT3
Organism: Mus musculus/domesticus
Length: 1004  
Fragment?: true
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Protein
Q3U0V5
Organism: Mus musculus/domesticus
Length: 1051  
Fragment?: false
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Protein
Q3U350
Organism: Mus musculus/domesticus
Length: 1051  
Fragment?: false
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Protein
Q3UIJ5
Organism: Mus musculus/domesticus
Length: 1037  
Fragment?: false
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Protein Coding Gene
MGI:2444720 | Smcr8
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1919488 | Tbc1d5
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1341850 | Rb1cc1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1920455 | C9orf72
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:2651874 | Sesn2
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
Q3TM51
Organism: Mus musculus/domesticus
Length: 261  
Fragment?: true
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Protein
Q3U3Q1
Organism: Mus musculus/domesticus
Length: 472  
Fragment?: false
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Protein Coding Gene
MGI:1270126 | Ulk1
Type: protein_coding_gene
Organism: mouse, laboratory
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Publication
3291115 | J:31015
First Author: Hanks SK
Year: 1988
Journal: Science
Title: The protein kinase family: conserved features and deduced phylogeny of the catalytic domains.
Volume: 241
Issue: 4861
Pages: 42-52
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Publication
12368087 | -
First Author: Manning G
Year: 2002
Journal: Trends Biochem Sci
Title: Evolution of protein kinase signaling from yeast to man.
Volume: 27
Issue: 10
Pages: 514-20
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Publication
12471243 | -
First Author: Manning G
Year: 2002
Journal: Science
Title: The protein kinase complement of the human genome.
Volume: 298
Issue: 5600
Pages: 1912-34
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Publication
15078142 | -
First Author: Stout TJ
Year: 2004
Journal: Curr Pharm Des
Title: High-throughput structural biology in drug discovery: protein kinases.
Volume: 10
Issue: 10
Pages: 1069-82
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Publication
15320712 | -
First Author: Li B
Year: 2004
Journal: Comb Chem High Throughput Screen
Title: Creating chemical diversity to target protein kinases.
Volume: 7
Issue: 5
Pages: 453-72
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Publication
15489334 | -
First Author: Gerhard DS
Year: 2004
Journal: Genome Res
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Volume: 14
Issue: 10B
Pages: 2121-7
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Publication
21183079 | J:292518
First Author: Huttlin EL
Year: 2010
Journal: Cell
Title: A tissue-specific atlas of mouse protein phosphorylation and expression.
Volume: 143
Issue: 7
Pages: 1174-89
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