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Search results 701 to 750 out of 750 for Sik1

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Type Details Score
Protein
Q60670
Organism: Mus musculus/domesticus
Length: 779  
Fragment?: false
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UniProt Feature
UniProt Feature
Begin: 1
Description: Serine/threonine-protein kinase SIK1
Type: chain
End: 779
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UniProt Feature
UniProt Feature
Begin: 332
Description: Phosphoserine; by SIK1
Type: modified residue
End: 332
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UniProt Feature
UniProt Feature
Begin: 395
Description: Phosphoserine; by SIK1
Type: modified residue
End: 395
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UniProt Feature
UniProt Feature
Begin: 331
Description: Phosphoserine; by SIK1
Type: modified residue
End: 331
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Publication
24698975 | J:213421
First Author: Ferrandi M
Year: 2014
Journal: Hum Mol Genet
Title: SIK1 localizes with nephrin in glomerular podocytes and its polymorphism predicts kidney injury.
Volume: 23
Issue: 16
Pages: 4371-82
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UniProt Feature
UniProt Feature
Begin: 465
Description: Phosphoserine; by CaMK4 and SIK1
Type: modified residue
End: 465
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UniProt Feature
UniProt Feature
Begin: 245
Description: Phosphoserine; by CaMK4 and SIK1
Type: modified residue
End: 245
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HT Sample
Sik1 knockout liver bioreplicate 1
 
Organism Name: mouse, laboratory
Sex: Male
Age: postnatal week 16
Stage: 28
Structure . Name: liver
Curation Status: Curated
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HT Sample
Sik1 knockout liver bioreplicate 3
 
Organism Name: mouse, laboratory
Sex: Male
Age: postnatal week 16
Stage: 28
Structure . Name: liver
Curation Status: Curated
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HT Sample
Sik1 knockout liver bioreplicate 2
 
Organism Name: mouse, laboratory
Sex: Male
Age: postnatal week 16
Stage: 28
Structure . Name: liver
Curation Status: Curated
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UniProt Feature
UniProt Feature
Begin: 171
Description: Phosphoserine; by AMPK, MARK2, SIK1 and SIK2
Type: modified residue
End: 171
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UniProt Feature
UniProt Feature
Begin: 488
Description: Phosphoserine; by AMPK, CaMK1, SIK1 and PKD/PRKD1
Type: modified residue
End: 488
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UniProt Feature
UniProt Feature
Begin: 250
Description: Phosphoserine; by AMPK, CaMK1, SIK1 and PKD/PRKD1
Type: modified residue
End: 250
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HT Sample
Sik1 knockout abdominal muscle bioreplicate 1
 
Organism Name: mouse, laboratory
Sex: Male
Age: postnatal week 16
Stage: 28
Structure . Name: abdomen musculature
Curation Status: Curated
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HT Sample
Sik1 knockout abdominal muscle bioreplicate 2
 
Organism Name: mouse, laboratory
Sex: Male
Age: postnatal week 16
Stage: 28
Structure . Name: abdomen musculature
Curation Status: Curated
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HT Sample
Sik1 knockout abdominal muscle bioreplicate 3
 
Organism Name: mouse, laboratory
Sex: Male
Age: postnatal week 16
Stage: 28
Structure . Name: abdomen musculature
Curation Status: Curated
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HT Sample
Sik1 knockout gonadal adipose bioreplicate 1
 
Organism Name: mouse, laboratory
Sex: Male
Age: postnatal week 16
Stage: 28
Structure . Name: gonadal fat pad
Curation Status: Curated
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HT Sample
Sik1 knockout gonadal adipose bioreplicate 2
 
Organism Name: mouse, laboratory
Sex: Male
Age: postnatal week 16
Stage: 28
Structure . Name: gonadal fat pad
Curation Status: Curated
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HT Sample
Sik1 knockout gonadal adipose bioreplicate 3
 
Organism Name: mouse, laboratory
Sex: Male
Age: postnatal week 16
Stage: 28
Structure . Name: gonadal fat pad
Curation Status: Curated
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Allele
Sik1<em1Smoc> | MGI:7292324
Name: salt inducible kinase 1; endonuclease-mediated mutation 1, Shanghai Model Organisms Center
Allele Type: Endonuclease-mediated
Attribute String: Null/knockout
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Publication
20347966 | -
First Author: Jaitovich A
Year: 2010
Journal: Biochim Biophys Acta
Title: Intracellular sodium sensing: SIK1 network, hormone action and high blood pressure.
Volume: 1802
Issue: 12
Pages: 1140-9
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Strain
MGI:6476275 | C57BL/6-Sik1<em1Smoc>/Smoc
Attribute String: coisogenic, endonuclease-mediated mutation, mutant strain
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Publication
17939993 | -
First Author: Sjöström M
Year: 2007
Journal: Proc Natl Acad Sci U S A
Title: SIK1 is part of a cell sodium-sensing network that regulates active sodium transport through a calcium-dependent process.
Volume: 104
Issue: 43
Pages: 16922-7
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DO Term
DOID:0080465 | developmental and epileptic encephalopathy 30
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HT Experiment
E-MTAB-4035 | RNAseq of coding RNA in the liver, spleen, kidney, abdominal muscle and gonadal adipose tissue of knock out mice and wild type controls
 
Experiment Type: RNA-Seq
Study Type: WT vs. Mutant
Source: ArrayExpress
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Publication
12943728 | -
First Author: Takemori H
Year: 2003
Journal: J Steroid Biochem Mol Biol
Title: Salt-inducible kinase-mediated regulation of steroidogenesis at the early stage of ACTH-stimulation.
Volume: 85
Issue: 2-5
Pages: 397-400
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Publication
22662228 | J:183827
First Author: Uebi T
Year: 2012
Journal: PLoS One
Title: Involvement of SIK3 in glucose and lipid homeostasis in mice.
Volume: 7
Issue: 5
Pages: e37803
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Publication
20708153 | -
First Author: Ahmed AA
Year: 2010
Journal: Cancer Cell
Title: SIK2 is a centrosome kinase required for bipolar mitotic spindle formation that provides a potential target for therapy in ovarian cancer.
Volume: 18
Issue: 2
Pages: 109-21
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Publication
15134808 | -
First Author: Katoh Y
Year: 2004
Journal: Mol Cell Endocrinol
Title: Salt-inducible kinase (SIK) isoforms: their involvement in steroidogenesis and adipogenesis.
Volume: 217
Issue: 1-2
Pages: 109-12
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Publication
18460324 | -
First Author: Hietakangas V
Year: 2008
Journal: Cell Metab
Title: TORCing up metabolic control in the brain.
Volume: 7
Issue: 5
Pages: 357-8
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Protein Domain
IPR034672 | SIK
Type: Domain
Description: SIKs are serine/threonine kinasse that are part of a complex network that regulates Na,K-ATPase to maintain sodium homeostasis and blood pressure []. Vertebrates contain three forms of SIKs (SIK1-3) from three distinct genes, which display tissue-specific effects. SIK1, also called SNF1LK, controls steroidogenic enzyme production in adrenocortical cells []. In the brain, both SIK1 and SIK2 regulate energy metabolism []. SIK2, also called QIK or SNF1LK2, is involved in the regulation of gluconeogenesis in the liver and lipogenesis in adipose tissues, where it phosphorylates the insulin receptor substrate-1 []. In the liver, SIK3 (also called QSK) regulates cholesterol and bile acid metabolism []. In addition, SIK2 plays an important role in the initiation of mitosis and regulates the localization of C-Nap1, a centrosome linker protein [].
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Publication
29211348 | -
First Author: Sonntag T
Year: 2018
Journal: FEBS J
Title: 14-3-3 proteins mediate inhibitory effects of cAMP on salt-inducible kinases (SIKs).
Volume: 285
Issue: 3
Pages: 467-480
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Protein Domain
IPR017090 | Ser/Thr_kinase_SIK1/2
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 entry represents the salt-inducible protein kinases, SIK1 and SIK2, which are serine/threonine-protein kinases primarily activated by the master kinase LKB1 (STK11). SIK1 is involved in a variety of processes, such as cell cycle regulation, gluconeogenesis and lipogenesis regulation and muscle growth [, , , ]. SIK2 phosphorylates insulin receptor substrate-1 (IRS1) in insulin-stimulated adipocytes, potentially modulating the efficiency of insulin signal transduction, and may have a role in the development of insulin resistance in diabetes [. SIK1/2 inhibit CREB activity by phosphorylating and inhibiting activity of TORCs, the CREB-specific coactivators, like CRTC2/TORC2 and CRTC3/TORC3 in response to cAMP signalling [].
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Publication
19651776 | J:156035
First Author: Nedumaran B
Year: 2009
Journal: J Biol Chem
Title: DAX-1 acts as a novel corepressor of orphan nuclear receptor HNF4alpha and negatively regulates gluconeogenic enzyme gene expression.
Volume: 284
Issue: 40
Pages: 27511-23
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Publication
33148508 | J:301206
 
First Author: Nishimori S
Year: 2021
Journal: Bone
Title: PTHrP targets salt-inducible kinases, HDAC4 and HDAC5, to repress chondrocyte hypertrophy in the growth plate.
Volume: 142
Pages: 115709
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Publication
36309093 | J:334306
First Author: van Gijsel-Bonnello M
Year: 2022
Journal: J Biol Chem
Title: Salt-inducible kinase 2 regulates fibrosis during bleomycin-induced lung injury.
Volume: 298
Issue: 12
Pages: 102644
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Publication
28973003 | J:250565
First Author: Lombardi MS
Year: 2017
Journal: PLoS One
Title: Salt-inducible kinases (SIK) inhibition reduces RANKL-induced osteoclastogenesis.
Volume: 12
Issue: 10
Pages: e0185426
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Protein
Q8CFH6
Organism: Mus musculus/domesticus
Length: 931  
Fragment?: false
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Protein
H3BKG1
Organism: Mus musculus/domesticus
Length: 929  
Fragment?: false
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Protein
F8VPT7
Organism: Mus musculus/domesticus
Length: 931  
Fragment?: false
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Protein
H3BJC9
Organism: Mus musculus/domesticus
Length: 927  
Fragment?: false
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Protein
Q6P4S6
Organism: Mus musculus/domesticus
Length: 1369  
Fragment?: false
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Protein
F6S7W6
Organism: Mus musculus/domesticus
Length: 1319  
Fragment?: true
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Protein
F6U6U5
Organism: Mus musculus/domesticus
Length: 1214  
Fragment?: true
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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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