KANPHOS_Str

Search Results (26 substrates found)

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Gene name
Organism
Protein name
BRSK1
Human
Serine/threonine-protein kinase BRSK1
Substrate Information
Organism
Human (Homo sapiens)
Uniprot ID
BRSK1_HUMAN
Accession #
Q8TDC3
Protein names
  • Serine/threonine-protein kinase BRSK1
  • EC 2.7.11.1
  • Brain-selective kinase 1
  • EC 2.7.11.26
  • Brain-specific serine/threonine-protein kinase 1
  • BR serine/threonine-protein kinase 1
  • Serine/threonine-protein kinase SAD-B
  • Synapses of Amphids Defective homolog 1
  • SAD1 homolog
  • hSAD1
Gene names
  • BRSK1
  • KIAA1811
  • SAD1
  • SADB
Description
Serine/threonine-protein kinase that plays a key role in polarization of neurons and centrosome duplication. Phosphorylates CDC25B, CDC25C, MAPT/TAU, RIMS1, TUBG1, TUBG2 and WEE1. Following phosphorylation and activation by STK11/LKB1, acts as a key regulator of polarization of cortical neurons, probably by mediating phosphorylation of microtubule-associated proteins such as MAPT/TAU at 'Thr-529' and 'Ser-579'. Also regulates neuron polarization by mediating phosphorylation of WEE1 at 'Ser-642' in post-mitotic neurons, leading to down-regulate WEE1 activity in polarized neurons. In neurons, localizes to synaptic vesicles and plays a role in neurotransmitter release, possibly by phosphorylating RIMS1. Also acts as a positive regulator of centrosome duplication by mediating phosphorylation of gamma-tubulin (TUBG1 and TUBG2) at 'Ser-131', leading to translocation of gamma-tubulin and its associated proteins to the centrosome. Involved in the UV-induced DNA damage checkpoint response, probably by inhibiting CDK1 activity through phosphorylation and activation of WEE1, and inhibition of CDC25B and CDC25C.
Links

Search Kinases of BRSK1 (Human)
KEGG Pathways (0)
N/A
Phosphorylation Site Information
BRSK2
Human
Serine/threonine-protein kinase BRSK2
Substrate Information
Organism
Human (Homo sapiens)
Uniprot ID
BRSK2_HUMAN
Accession #
Q8IWQ3
Protein names
  • Serine/threonine-protein kinase BRSK2
  • EC 2.7.11.1
  • Brain-selective kinase 2
  • EC 2.7.11.26
  • Brain-specific serine/threonine-protein kinase 2
  • BR serine/threonine-protein kinase 2
  • Serine/threonine-protein kinase 29
  • Serine/threonine-protein kinase SAD-A
Gene names
  • BRSK2
  • C11orf7
  • PEN11B
  • SADA
  • STK29
  • HUSSY-12
Description
Serine/threonine-protein kinase that plays a key role in polarization of neurons and axonogenesis, cell cycle progress and insulin secretion. Phosphorylates CDK16, CDC25C, MAPT/TAU, PAK1 and WEE1. Following phosphorylation and activation by STK11/LKB1, acts as a key regulator of polarization of cortical neurons, probably by mediating phosphorylation of microtubule-associated proteins such as MAPT/TAU at 'Thr-529' and 'Ser-579'. Also regulates neuron polarization by mediating phosphorylation of WEE1 at 'Ser-642' in postmitotic neurons, leading to down-regulate WEE1 activity in polarized neurons. Plays a role in the regulation of the mitotic cell cycle progress and the onset of mitosis. Plays a role in the regulation of insulin secretion in response to elevated glucose levels, probably via phosphorylation of CDK16 and PAK1. While BRSK2 phosphorylated at Thr-174 can inhibit insulin secretion (PubMed:22798068), BRSK2 phosphorylated at Thr-260 can promote insulin secretion (PubMed:22669945). Regulates reorganization of the actin cytoskeleton. May play a role in the apoptotic response triggered by endoplasmatic reticulum (ER) stress.
Links

Search Kinases of BRSK2 (Human)
KEGG Pathways (0)
N/A
Phosphorylation Site Information
MARK1
Human
Serine/threonine-protein kinase MARK1
Substrate Information
Organism
Human (Homo sapiens)
Uniprot ID
MARK1_HUMAN
Accession #
Q9P0L2
Protein names
  • Serine/threonine-protein kinase MARK1
  • EC 2.7.11.1
  • EC 2.7.11.26
  • MAP/microtubule affinity-regulating kinase 1
  • PAR1 homolog c
  • Par-1c
  • Par1c
Gene names
  • MARK1
  • KIAA1477
  • MARK
Description
Serine/threonine-protein kinase involved in cell polarity and microtubule dynamics regulation. Phosphorylates DCX, MAP2, MAP4 and MAPT/TAU. Involved in cell polarity by phosphorylating the microtubule-associated proteins MAP2, MAP4 and MAPT/TAU at KXGS motifs, causing detachment from microtubules, and their disassembly. Involved in the regulation of neuronal migration through its dual activities in regulating cellular polarity and microtubule dynamics, possibly by phosphorylating and regulating DCX. Also acts as a positive regulator of the Wnt signaling pathway, probably by mediating phosphorylation of dishevelled proteins (DVL1, DVL2 and/or DVL3).
Links

Search Kinases of MARK1 (Human)
KEGG Pathways (0)
N/A
Phosphorylation Site Information
MARK2
Human
Serine/threonine-protein kinase MARK2
Substrate Information
Organism
Human (Homo sapiens)
Uniprot ID
MARK2_HUMAN
Accession #
Q7KZI7
Protein names
  • Serine/threonine-protein kinase MARK2
  • EC 2.7.11.1
  • EC 2.7.11.26
  • ELKL motif kinase 1
  • EMK-1
  • MAP/microtubule affinity-regulating kinase 2
  • PAR1 homolog
  • PAR1 homolog b
  • Par-1b
  • Par1b
Gene names
  • MARK2
  • EMK1
Description
Serine/threonine-protein kinase involved in cell polarity and microtubule dynamics regulation. Phosphorylates CRTC2/TORC2, DCX, HDAC7, KIF13B, MAP2, MAP4, MAPT/TAU, and RAB11FIP2. Plays a key role in cell polarity by phosphorylating the microtubule-associated proteins MAP2, MAP4 and MAPT/TAU at KXGS motifs, causing detachment from microtubules, and their disassembly. Regulates epithelial cell polarity by phosphorylating RAB11FIP2. Involved in the regulation of neuronal migration through its dual activities in regulating cellular polarity and microtubule dynamics, possibly by phosphorylating and regulating DCX. Regulates axogenesis by phosphorylating KIF13B, promoting interaction between KIF13B and 14-3-3 and inhibiting microtubule-dependent accumulation of KIF13B. Also required for neurite outgrowth and establishment of neuronal polarity. Regulates localization and activity of some histone deacetylases by mediating phosphorylation of HDAC7, promoting subsequent interaction between HDAC7 and 14-3-3 and export from the nucleus. Also acts as a positive regulator of the Wnt signaling pathway, probably by mediating phosphorylation of dishevelled proteins (DVL1, DVL2 and/or DVL3). Modulates the developmental decision to build a columnar versus a hepatic epithelial cell apparently by promoting a switch from a direct to a transcytotic mode of apical protein delivery. Essential for the asymmetric development of membrane domains of polarized epithelial cells.
Links

Search Kinases of MARK2 (Human)
KEGG Pathways (0)
N/A
Phosphorylation Site Information
MARK3
Human
MAP/microtubule affinity-regulating kinase 3
Substrate Information
Organism
Human (Homo sapiens)
Uniprot ID
MARK3_HUMAN
Accession #
P27448
Protein names
  • MAP/microtubule affinity-regulating kinase 3
  • EC 2.7.11.1
  • C-TAK1
  • cTAK1
  • Cdc25C-associated protein kinase 1
  • ELKL motif kinase 2
  • EMK-2
  • Protein kinase STK10
  • Ser/Thr protein kinase PAR-1
  • Par-1a
  • Serine/threonine-protein kinase p78
Gene names
  • MARK3
  • CTAK1
  • EMK2
Description
Involved in the specific phosphorylation of microtubule-associated proteins for tau, MAP2 and MAP4. Phosphorylates CDC25C on 'Ser-216'. Regulates localization and activity of some histone deacetylases by mediating phosphorylation of HDAC7, promoting subsequent interaction between HDAC7 and 14-3-3 and export from the nucleus.
Links

Search Kinases of MARK3 (Human)
KEGG Pathways (0)
N/A
Phosphorylation Site Information
MARK4
Human
MAP/microtubule affinity-regulating kinase 4
MELK
Human
Maternal embryonic leucine zipper kinase
Substrate Information
Organism
Human (Homo sapiens)
Uniprot ID
MELK_HUMAN
Accession #
Q14680
Protein names
  • Maternal embryonic leucine zipper kinase
  • hMELK
  • EC 2.7.11.1
  • Protein kinase Eg3
  • pEg3 kinase
  • Protein kinase PK38
  • hPK38
  • Tyrosine-protein kinase MELK
  • EC 2.7.10.2
Gene names
  • MELK
  • KIAA0175
Description
Serine/threonine-protein kinase involved in various processes such as cell cycle regulation, self-renewal of stem cells, apoptosis and splicing regulation. Has a broad substrate specificity; phosphorylates BCL2L14, CDC25B, MAP3K5/ASK1 and ZNF622. Acts as an activator of apoptosis by phosphorylating and activating MAP3K5/ASK1. Acts as a regulator of cell cycle, notably by mediating phosphorylation of CDC25B, promoting localization of CDC25B to the centrosome and the spindle poles during mitosis. Plays a key role in cell proliferation and carcinogenesis. Required for proliferation of embryonic and postnatal multipotent neural progenitors. Phosphorylates and inhibits BCL2L14, possibly leading to affect mammary carcinogenesis by mediating inhibition of the pro-apoptotic function of BCL2L14. Also involved in the inhibition of spliceosome assembly during mitosis by phosphorylating ZNF622, thereby contributing to its redirection to the nucleus. May also play a role in primitive hematopoiesis.
Links

Search Kinases of MELK (Human)
KEGG Pathways (0)
N/A
Phosphorylation Site Information
NUAK1
Human
NUAK family SNF1-like kinase 1
Substrate Information
Organism
Human (Homo sapiens)
Uniprot ID
NUAK1_HUMAN
Accession #
O60285
Protein names
  • NUAK family SNF1-like kinase 1
  • EC 2.7.11.1
  • AMPK-related protein kinase 5
  • ARK5
  • Omphalocele kinase 1
Gene names
  • NUAK1
  • ARK5
  • KIAA0537
  • OMPHK1
Description
Serine/threonine-protein kinase involved in various processes such as cell adhesion, regulation of cell ploidy and senescence, cell proliferation and tumor progression. Phosphorylates ATM, CASP6, LATS1, PPP1R12A and p53/TP53. Acts as a regulator of cellular senescence and cellular ploidy by mediating phosphorylation of 'Ser-464' of LATS1, thereby controlling its stability. Controls cell adhesion by regulating activity of the myosin protein phosphatase 1 (PP1) complex. Acts by mediating phosphorylation of PPP1R12A subunit of myosin PP1: phosphorylated PPP1R12A then interacts with 14-3-3, leading to reduced dephosphorylation of myosin MLC2 by myosin PP1. May be involved in DNA damage response: phosphorylates p53/TP53 at 'Ser-15' and 'Ser-392' and is recruited to the CDKN1A/WAF1 promoter to participate to transcription activation by p53/TP53. May also act as a tumor malignancy-associated factor by promoting tumor invasion and metastasis under regulation and phosphorylation by AKT1. Suppresses Fas-induced apoptosis by mediating phosphorylation of CASP6, thereby suppressing the activation of the caspase and the subsequent cleavage of CFLAR.
Links

Search Kinases of NUAK1 (Human)
KEGG Pathways (0)
N/A
Phosphorylation Site Information
NUAK2
Human
NUAK family SNF1-like kinase 2
Substrate Information
Organism
Human (Homo sapiens)
Uniprot ID
NUAK2_HUMAN
Accession #
Q9H093
Protein names
  • NUAK family SNF1-like kinase 2
  • EC 2.7.11.1
  • Omphalocele kinase 2
  • SNF1/AMP kinase-related kinase
  • SNARK
Gene names
  • NUAK2
  • OMPHK2
  • SNARK
Description
Stress-activated kinase involved in tolerance to glucose starvation. Induces cell-cell detachment by increasing F-actin conversion to G-actin. Expression is induced by CD95 or TNF-alpha, via NF-kappa-B. Protects cells from CD95-mediated apoptosis and is required for the increased motility and invasiveness of CD95-activated tumor cells. Able to phosphorylate 'Ser-464' of LATS1.
Links

Search Kinases of NUAK2 (Human)
KEGG Pathways (0)
N/A
Phosphorylation Site Information
PAK1
Human
Serine/threonine-protein kinase PAK 1
Substrate Information
Organism
Human (Homo sapiens)
Uniprot ID
PAK1_HUMAN
Accession #
Q13153
Protein names
  • Serine/threonine-protein kinase PAK 1
  • EC 2.7.11.1
  • Alpha-PAK
  • p21-activated kinase 1
  • PAK-1
  • p65-PAK
Gene names
  • PAK1
Description
Protein kinase involved in intracellular signaling pathways downstream of integrins and receptor-type kinases that plays an important role in cytoskeleton dynamics, in cell adhesion, migration, proliferation, apoptosis, mitosis, and in vesicle-mediated transport processes. Can directly phosphorylate BAD and protects cells against apoptosis. Activated by interaction with CDC42 and RAC1. Functions as GTPase effector that links the Rho-related GTPases CDC42 and RAC1 to the JNK MAP kinase pathway. Phosphorylates and activates MAP2K1, and thereby mediates activation of downstream MAP kinases. Involved in the reorganization of the actin cytoskeleton, actin stress fibers and of focal adhesion complexes. Phosphorylates the tubulin chaperone TBCB and thereby plays a role in the regulation of microtubule biogenesis and organization of the tubulin cytoskeleton. Plays a role in the regulation of insulin secretion in response to elevated glucose levels. Part of a ternary complex that contains PAK1, DVL1 and MUSK that is important for MUSK-dependent regulation of AChR clustering during the formation of the neuromuscular junction (NMJ). Activity is inhibited in cells undergoing apoptosis, potentially due to binding of CDC2L1 and CDC2L2. Phosphorylates MYL9/MLC2. Phosphorylates RAF1 at 'Ser-338' and 'Ser-339' resulting in: activation of RAF1, stimulation of RAF1 translocation to mitochondria, phosphorylation of BAD by RAF1, and RAF1 binding to BCL2. Phosphorylates SNAI1 at 'Ser-246' promoting its transcriptional repressor activity by increasing its accumulation in the nucleus. In podocytes, promotes NR3C2 nuclear localization. Required for atypical chemokine receptor ACKR2-induced phosphorylation of LIMK1 and cofilin (CFL1) and for the up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. In synapses, seems to mediate the regulation of F-actin cluster formation performed by SHANK3, maybe through CFL1 phosphorylation and inactivation.
Links

Search Kinases of PAK1 (Human)
Phosphorylation Site Information
Pak1
Mouse
Serine/threonine-protein kinase PAK 1
Substrate Information
Organism
Mouse (Mus musculus)
Uniprot ID
PAK1_MOUSE
Accession #
O88643
Protein names
  • Serine/threonine-protein kinase PAK 1
  • EC 2.7.11.1
  • Alpha-PAK
  • CDC42/RAC effector kinase PAK-A
  • p21-activated kinase 1
  • PAK-1
  • p65-PAK
Gene names
  • Pak1
  • Paka
Description
Protein kinase involved in intracellular signaling pathways downstream of integrins and receptor-type kinases that plays an important role in cytoskeleton dynamics, in cell adhesion, migration, proliferation, apoptosis, mitosis, and in vesicle-mediated transport processes. Can directly phosphorylate BAD and protects cells against apoptosis. Activated by interaction with CDC42 and RAC1. Functions as GTPase effector that links the Rho-related GTPases CDC42 and RAC1 to the JNK MAP kinase pathway. Phosphorylates and activates MAP2K1, and thereby mediates activation of downstream MAP kinases. Involved in the reorganization of the actin cytoskeleton, actin stress fibers and of focal adhesion complexes. Phosphorylates the tubulin chaperone TBCB and thereby plays a role in the regulation of microtubule biogenesis and organization of the tubulin cytoskeleton. Plays a role in the regulation of insulin secretion in response to elevated glucose levels. Part of a ternary complex that contains PAK1, DVL1 and MUSK that is important for MUSK-dependent regulation of AChR clustering during the formation of the neuromuscular junction (NMJ). Activity is inhibited in cells undergoing apoptosis, potentially due to binding of CDC2L1 and CDC2L2. Phosphorylates MYL9/MLC2. Phosphorylates RAF1 at 'Ser-338' and 'Ser-339' resulting in: activation of RAF1, stimulation of RAF1 translocation to mitochondria, phosphorylation of BAD by RAF1, and RAF1 binding to BCL2. Phosphorylates SNAI1 at 'Ser-246' promoting its transcriptional repressor activity by increasing its accumulation in the nucleus. In podocytes, promotes NR3C2 nuclear localization. Required for atypical chemokine receptor ACKR2-induced phosphorylation of LIMK1 and cofilin (CFL1) and for the up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. In synapses, seems to mediate the regulation of F-actin cluster formation performed by SHANK3, maybe through CFL1 phosphorylation and inactivation.
Links

Search Kinases of Pak1 (Mouse)
KEGG Pathways (0)
N/A
Phosphorylation Site Information
PRKAA1
Human
5'-AMP-activated protein kinase catalytic subunit alpha-1
Substrate Information
Organism
Human (Homo sapiens)
Uniprot ID
AAPK1_HUMAN
Accession #
Q13131
Protein names
  • 5'-AMP-activated protein kinase catalytic subunit alpha-1
  • AMPK subunit alpha-1
  • EC 2.7.11.1
  • Acetyl-CoA carboxylase kinase
  • ACACA kinase
  • EC 2.7.11.27
  • Hydroxymethylglutaryl-CoA reductase kinase
  • HMGCR kinase
  • EC 2.7.11.31
  • Tau-protein kinase PRKAA1
  • EC 2.7.11.26
Gene names
  • PRKAA1
  • AMPK1
Description
Catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Regulates lipid synthesis by phosphorylating and inactivating lipid metabolic enzymes such as ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and cholesterol synthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, respectively. Regulates insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3. AMPK stimulates glucose uptake in muscle by increasing the translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly by mediating phosphorylation of TBC1D4/AS160. Regulates transcription and chromatin structure by phosphorylating transcription regulators involved in energy metabolism such as CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A. Acts as a key regulator of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm. In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription. Acts as a key regulator of cell growth and proliferation by phosphorylating TSC2, RPTOR and ATG1/ULK1: in response to nutrient limitation, negatively regulates the mTORC1 complex by phosphorylating RPTOR component of the mTORC1 complex and by phosphorylating and activating TSC2. In response to nutrient limitation, promotes autophagy by phosphorylating and activating ATG1/ULK1. AMPK also acts as a regulator of circadian rhythm by mediating phosphorylation of CRY1, leading to destabilize it. May regulate the Wnt signaling pathway by phosphorylating CTNNB1, leading to stabilize it. Also has tau-protein kinase activity: in response to amyloid beta A4 protein (APP) exposure, activated by CAMKK2, leading to phosphorylation of MAPT/TAU; however the relevance of such data remains unclear in vivo. Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1.
Links

Search Kinases of PRKAA1 (Human)
Gene Ontology Terms (58)
Phosphorylation Site Information
Prkaa1
Rat
5'-AMP-activated protein kinase catalytic subunit alpha-1
Substrate Information
Organism
Rat (Rattus norvegicus)
Uniprot ID
AAPK1_RAT
Accession #
P54645
Protein names
  • 5'-AMP-activated protein kinase catalytic subunit alpha-1
  • AMPK subunit alpha-1
  • EC 2.7.11.1
  • Acetyl-CoA carboxylase kinase
  • ACACA kinase
  • EC 2.7.11.27
  • Hydroxymethylglutaryl-CoA reductase kinase
  • HMGCR kinase
  • EC 2.7.11.31
  • Tau-protein kinase PRKAA1
  • EC 2.7.11.26
Gene names
  • Prkaa1
  • Ampk1
Description
Catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Regulates lipid synthesis by phosphorylating and inactivating lipid metabolic enzymes such as ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and cholesterol synthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, respectively. Regulates insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3. AMPK stimulates glucose uptake in muscle by increasing the translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly by mediating phosphorylation of TBC1D4/AS160. Regulates transcription and chromatin structure by phosphorylating transcription regulators involved in energy metabolism such as CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A. Acts as a key regulator of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm. In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription. Acts as a key regulator of cell growth and proliferation by phosphorylating TSC2, RPTOR and ATG1/ULK1: in response to nutrient limitation, negatively regulates the mTORC1 complex by phosphorylating RPTOR component of the mTORC1 complex and by phosphorylating and activating TSC2. In response to nutrient limitation, promotes autophagy by phosphorylating and activating ATG1/ULK1. AMPK also acts as a regulator of circadian rhythm by mediating phosphorylation of CRY1, leading to destabilize it. May regulate the Wnt signaling pathway by phosphorylating CTNNB1, leading to stabilize it. Also has tau-protein kinase activity: in response to amyloid beta A4 protein (APP) exposure, activated by CAMKK2, leading to phosphorylation of MAPT/TAU; however the relevance of such data remains unclear in vivo. Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1.
Links

Search Kinases of Prkaa1 (Rat)
Gene Ontology Terms (58)
Phosphorylation Site Information
Prkaa1
Mouse
5'-AMP-activated protein kinase catalytic subunit alpha-1
Substrate Information
Organism
Mouse (Mus musculus)
Uniprot ID
AAPK1_MOUSE
Accession #
Q5EG47
Protein names
  • 5'-AMP-activated protein kinase catalytic subunit alpha-1
  • AMPK subunit alpha-1
  • EC 2.7.11.1
  • Acetyl-CoA carboxylase kinase
  • ACACA kinase
  • EC 2.7.11.27
  • Hydroxymethylglutaryl-CoA reductase kinase
  • HMGCR kinase
  • EC 2.7.11.31
  • Tau-protein kinase PRKAA1
  • EC 2.7.11.26
Gene names
  • Prkaa1
Description
Catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Regulates lipid synthesis by phosphorylating and inactivating lipid metabolic enzymes such as ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and cholesterol synthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, respectively. Regulates insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3. AMPK stimulates glucose uptake in muscle by increasing the translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly by mediating phosphorylation of TBC1D4/AS160. Regulates transcription and chromatin structure by phosphorylating transcription regulators involved in energy metabolism such as CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A. Acts as a key regulator of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm. In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription. Acts as a key regulator of cell growth and proliferation by phosphorylating TSC2, RPTOR and ATG1/ULK1: in response to nutrient limitation, negatively regulates the mTORC1 complex by phosphorylating RPTOR component of the mTORC1 complex and by phosphorylating and activating TSC2. In response to nutrient limitation, promotes autophagy by phosphorylating and activating ATG1/ULK1. AMPK also acts as a regulator of circadian rhythm by mediating phosphorylation of CRY1, leading to destabilize it. May regulate the Wnt signaling pathway by phosphorylating CTNNB1, leading to stabilize it. Also has tau-protein kinase activity: in response to amyloid beta A4 protein (APP) exposure, activated by CAMKK2, leading to phosphorylation of MAPT/TAU; however the relevance of such data remains unclear in vivo. Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1.
Links

Search Kinases of Prkaa1 (Mouse)
Gene Ontology Terms (52)
Phosphorylation Site Information
Prkaa2
Rat
5'-AMP-activated protein kinase catalytic subunit alpha-2
Substrate Information
Organism
Rat (Rattus norvegicus)
Uniprot ID
AAPK2_RAT
Accession #
Q09137
Protein names
  • 5'-AMP-activated protein kinase catalytic subunit alpha-2
  • AMPK subunit alpha-2
  • EC 2.7.11.1
  • Acetyl-CoA carboxylase kinase
  • ACACA kinase
  • EC 2.7.11.27
  • Hydroxymethylglutaryl-CoA reductase kinase
  • HMGCR kinase
  • EC 2.7.11.31
Gene names
  • Prkaa2
  • Ampk
  • Ampk2
Description
Catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Regulates lipid synthesis by phosphorylating and inactivating lipid metabolic enzymes such as ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and cholesterol synthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, respectively. Regulates insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3. AMPK stimulates glucose uptake in muscle by increasing the translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly by mediating phosphorylation of TBC1D4/AS160. Regulates transcription and chromatin structure by phosphorylating transcription regulators involved in energy metabolism such as CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A. Acts as a key regulator of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm. In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription. Acts as a key regulator of cell growth and proliferation by phosphorylating TSC2, RPTOR and ATG1/ULK1: in response to nutrient limitation, negatively regulates the mTORC1 complex by phosphorylating RPTOR component of the mTORC1 complex and by phosphorylating and activating TSC2. In response to nutrient limitation, promotes autophagy by phosphorylating and activating ATG1/ULK1. AMPK also acts as a regulator of circadian rhythm by mediating phosphorylation of CRY1, leading to destabilize it. May regulate the Wnt signaling pathway by phosphorylating CTNNB1, leading to stabilize it. Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1.
Links

Search Kinases of Prkaa2 (Rat)
Phosphorylation Site Information
PTEN
Human
Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
Substrate Information
Organism
Human (Homo sapiens)
Uniprot ID
PTEN_HUMAN
Accession #
P60484
Protein names
  • Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
  • EC 3.1.3.16
  • EC 3.1.3.48
  • EC 3.1.3.67
  • Mutated in multiple advanced cancers 1
  • Phosphatase and tensin homolog
Gene names
  • PTEN
  • MMAC1
  • TEP1
Description
Tumor suppressor. Acts as a dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine-phosphorylated proteins. Also acts as a lipid phosphatase, removing the phosphate in the D3 position of the inositol ring from phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-diphosphate, phosphatidylinositol 3-phosphate and inositol 1,3,4,5-tetrakisphosphate with order of substrate preference in vitro PtdIns(3,4,5)P3 > PtdIns(3,4)P2 > PtdIns3P > Ins(1,3,4,5)P4. The lipid phosphatase activity is critical for its tumor suppressor function. Antagonizes the PI3K-AKT/PKB signaling pathway by dephosphorylating phosphoinositides and thereby modulating cell cycle progression and cell survival. The unphosphorylated form cooperates with AIP1 to suppress AKT1 activation. Dephosphorylates tyrosine-phosphorylated focal adhesion kinase and inhibits cell migration and integrin-mediated cell spreading and focal adhesion formation. Plays a role as a key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. May be a negative regulator of insulin signaling and glucose metabolism in adipose tissue. The nuclear monoubiquitinated form possesses greater apoptotic potential, whereas the cytoplasmic nonubiquitinated form induces less tumor suppressive ability. In motile cells, suppresses the formation of lateral pseudopods and thereby promotes cell polarization and directed movement.Isoform alpha: Functional kinase, like isoform 1 it antagonizes the PI3K-AKT/PKB signaling pathway. Plays a role in mitochondrial energetic metabolism by promoting COX activity and ATP production, via collaboration with isoform 1 in increasing protein levels of PINK1.
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Search Kinases of PTEN (Human)
Gene Ontology Terms (120)
Phosphorylation Site Information
Sik1
Rat
Serine/threonine-protein kinase SIK1
Substrate Information
Organism
Rat (Rattus norvegicus)
Uniprot ID
SIK1_RAT
Accession #
Q9R1U5
Protein names
  • Serine/threonine-protein kinase SIK1
  • EC 2.7.11.1
  • Protein kinase KID2
  • Salt-inducible kinase 1
  • SIK-1
  • Serine/threonine-protein kinase SNF1-like kinase 1
  • Serine/threonine-protein kinase SNF1LK
Gene names
  • Sik1
  • Kid2
  • Sik
  • Snf1lk
Description
Serine/threonine-protein kinase involved in various processes such as cell cycle regulation, gluconeogenesis and lipogenesis regulation, muscle growth and differentiation and tumor suppression. Phosphorylates HDAC4, HDAC5, PPME1, SREBF1, TORC1/CRTC1 and TORC2/CRTC2. Acts as a tumor suppressor and plays a key role in p53/TP53-dependent anoikis, a type of apoptosis triggered by cell detachment: required for phosphorylation of p53/TP53 in response to loss of adhesion and is able to suppress metastasis. Part of a sodium-sensing signaling network, probably by mediating phosphorylation of PPME1: following increases in intracellular sodium, SIK1 is activated by CaMK1 and phosphorylates PPME1 subunit of protein phosphatase 2A (PP2A), leading to dephosphorylation of sodium/potassium-transporting ATPase ATP1A1 and subsequent increase activity of ATP1A1. Acts as a regulator of muscle cells by phosphorylating and inhibiting class II histone deacetylases HDAC4 and HDAC5, leading to promote expression of MEF2 target genes in myocytes. Also required during cardiomyogenesis by regulating the exit of cardiomyoblasts from the cell cycle via down-regulation of CDKN1C/p57Kip2. Acts as a regulator of hepatic gluconeogenesis by phosphorylating and repressing the CREB-specific coactivators TORC1/CRTC1 and TORC2/CRTC2, leading to inhibit CREB activity. Also regulates hepatic lipogenesis by phosphorylating and inhibiting SREBF1.
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Search Kinases of Sik1 (Rat)
KEGG Pathways (0)
N/A
Phosphorylation Site Information
SIK1
Human
Serine/threonine-protein kinase SIK1
Substrate Information
Organism
Human (Homo sapiens)
Uniprot ID
SIK1_HUMAN
Accession #
P57059
Protein names
  • Serine/threonine-protein kinase SIK1
  • EC 2.7.11.1
  • Salt-inducible kinase 1
  • SIK-1
  • Serine/threonine-protein kinase SNF1-like kinase 1
  • Serine/threonine-protein kinase SNF1LK
Gene names
  • SIK1
  • SIK
  • SNF1LK
Description
Serine/threonine-protein kinase involved in various processes such as cell cycle regulation, gluconeogenesis and lipogenesis regulation, muscle growth and differentiation and tumor suppression. Phosphorylates HDAC4, HDAC5, PPME1, SREBF1, TORC1/CRTC1 and TORC2/CRTC2. Acts as a tumor suppressor and plays a key role in p53/TP53-dependent anoikis, a type of apoptosis triggered by cell detachment: required for phosphorylation of p53/TP53 in response to loss of adhesion and is able to suppress metastasis. Part of a sodium-sensing signaling network, probably by mediating phosphorylation of PPME1: following increases in intracellular sodium, SIK1 is activated by CaMK1 and phosphorylates PPME1 subunit of protein phosphatase 2A (PP2A), leading to dephosphorylation of sodium/potassium-transporting ATPase ATP1A1 and subsequent increase activity of ATP1A1. Acts as a regulator of muscle cells by phosphorylating and inhibiting class II histone deacetylases HDAC4 and HDAC5, leading to promote expression of MEF2 target genes in myocytes. Also required during cardiomyogenesis by regulating the exit of cardiomyoblasts from the cell cycle via down-regulation of CDKN1C/p57Kip2. Acts as a regulator of hepatic gluconeogenesis by phosphorylating and repressing the CREB-specific coactivators TORC1/CRTC1 and TORC2/CRTC2, leading to inhibit CREB activity. Also regulates hepatic lipogenesis by phosphorylating and inhibiting SREBF1.
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Search Kinases of SIK1 (Human)
KEGG Pathways (0)
N/A
Phosphorylation Site Information
SIK2
Human
Serine/threonine-protein kinase SIK2
Substrate Information
Organism
Human (Homo sapiens)
Uniprot ID
SIK2_HUMAN
Accession #
Q9H0K1
Protein names
  • Serine/threonine-protein kinase SIK2
  • EC 2.7.11.1
  • Qin-induced kinase
  • Salt-inducible kinase 2
  • SIK-2
  • Serine/threonine-protein kinase SNF1-like kinase 2
Gene names
  • SIK2
  • KIAA0781
  • QIK
  • SNF1LK2
Description
Phosphorylates 'Ser-794' of IRS1 in insulin-stimulated adipocytes, potentially modulating the efficiency of insulin signal transduction. Inhibits CREB activity by phosphorylating and repressing TORCs, the CREB-specific coactivators.
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Search Kinases of SIK2 (Human)
KEGG Pathways (0)
N/A
Phosphorylation Site Information
SIK3
Human
Serine/threonine-protein kinase SIK3
Substrate Information
Organism
Human (Homo sapiens)
Uniprot ID
J3KPC8_HUMAN
Accession #
J3KPC8
Protein names
  • Serine/threonine-protein kinase SIK3
Gene names
  • SIK3
Description
N/A
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Search Kinases of SIK3 (Human)
KEGG Pathways (0)
N/A
Phosphorylation Site Information
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