BRSK2
entrez
9024
canonical
uniprot
Q8IWQ3
canonical
ensembl
ENSG00000174672
resolver
ensembl
ENSG00000291428
resolver
ensp
ENSP00000310697
resolver
ensp
ENSP00000371614
resolver
ensp
ENSP00000431152
resolver
ensp
ENSP00000432000
resolver
ensp
ENSP00000433235
resolver
ensp
ENSP00000608514
resolver
ensp
ENSP00000619510
resolver
ensp
ENSP00000716750
resolver
ensp
ENSP00000749402
resolver
ensp
ENSP00000791953
resolver
genesymbol
BRSK2
resolver
genesymbol_syn
C11orf7
resolver
genesymbol_syn
PEN11B
resolver
genesymbol_syn
SADA
resolver
genesymbol_syn
STK29
resolver
hgnc
HGNC:11405
resolver
uniprot
A0A140VJF6
resolver
uniprot
B3KVE9
resolver
uniprot
B4DLY3
resolver
uniprot
E9PLM7
resolver
uniprot
O60843
resolver
uniprot
O95099
resolver
uniprot
Q5J5B4
resolver
uniprot
Q6ZMQ4
resolver
uniprot
Q8TB60
resolver
uniprot_entry
A0A140VJF6_HUMAN
resolver
uniprot_entry
B4DLY3_HUMAN
resolver
uniprot_entry
BRSK2_HUMAN
resolver
uniprot_sec
B3KVE9
resolver
uniprot_sec
E9PLM7
resolver
uniprot_sec
O60843
resolver
uniprot_sec
O95099
resolver
uniprot_sec
Q5J5B4
resolver
uniprot_sec
Q6ZMQ4
resolver
uniprot_sec
Q8TB60
resolver
activity_regulation
ACTIVITY REGULATION: Activated by phosphorylation on Thr-174 by STK11/LKB1. {ECO:0000269|PubMed:14976552}.
uniprot
proteins
amino_acid_sequence
MTSTGKDGGAQHAQYVGPYRLEKTLGKGQTGLVKLGVHCVTCQKVAIKIVNREKLSESVLMKVEREIAILKLIEHPHVLKLHDVYENKKYLYLVLEHVSGGELFDYLVKKGRLTPKEARKFFRQIISALDFCHSHSICHRDLKPENLLLDEKNNIRIADFGMASLQVGDSLLETSCGSPHYACPEVIRGEKYDGRKADVWSCGVILFALLVGALPFDDDNLRQLLEKVKRGVFHMPHFIPPDCQSLLRGMIEVDAARRLTLEHIQKHIWYIGGKNEPEPEQPIPRKVQIRSLPSLEDIDPDVLDSMHSLGCFRDRNKLLQDLLSEEENQEKMIYFLLLDRKERYPSQEDEDLPPRNEIDPPRKRVDSPMLNRHGKRRPERKSMEVLSVTDGGSPVPARRAIEMAQHGQRSRSISGASSGLSTSPLSSPRVTPHPSPRGSPLPTPKGTPVHTPKESPAGTPNPTPPSSPSVGGVPWRARLNSIKNSFLGSPRFHRRKLQVPTPEEMSNLTPESSPELAKKSWFGNFISLEKEEQIFVVIKDKPLSSIKADIVHAFLSIPSLSHSVISQTSFRAEYKATGGPAVFQKPVKFQVDITYTEGGEAQKENGIYSVTFTLLSGPSRRFKRVVETIQAQLLSTHDPPAAQHLSDTTNCMEMMTGRLSKCGSPLSNFFDVIKQLFSDEKNGQAAQAPSTPAKRSAHGPLGDSAAAGPGPGGDAEYPTGKDTAKMGPPTARREQP
uniprot
proteins
ec_number
2.7.11.1
uniprot
proteins
ec_number
2.7.11.26
uniprot
proteins
function
FUNCTION: 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 endoplasmic reticulum (ER) stress. {ECO:0000269|PubMed:14976552, ECO:0000269|PubMed:20026642, ECO:0000269|PubMed:21985311, ECO:0000269|PubMed:22669945, ECO:0000269|PubMed:22798068, ECO:0000269|PubMed:23029325}.
uniprot
proteins
mass_dalton
81633
uniprot
proteins
mutagenesis
MUTAGEN 48; /note="K->M: Loss of catalytic activity. Causes disintegration of actin stress fibers."; /evidence="ECO:0000269|PubMed:22669945, ECO:0000269|PubMed:22798068"; MUTAGEN 174; /note="T->A: Prevents phosphorylation and activation by STK11/LKB1 complex."; /evidence="ECO:0000269|PubMed:14976552, ECO:0000269|PubMed:18339622, ECO:0000269|PubMed:22798068"; MUTAGEN 174; /note="T->E: Constitutively activated."; /evidence="ECO:0000269|PubMed:14976552, ECO:0000269|PubMed:18339622, ECO:0000269|PubMed:22798068"; MUTAGEN 260; /note="T->A: Decreased phosphorylation. Nearly abolishes stimulation of insulin secretion."; /evidence="ECO:0000269|PubMed:16870137, ECO:0000269|PubMed:22669945"; MUTAGEN 310; /note="G->A: Decreased activation of kinase activity."; /evidence="ECO:0000269|PubMed:18339622"; MUTAGEN 443; /note="T->A: Constitutively activated. Promotes formation of actin stress fibers."; /evidence="ECO:0000269|PubMed:22669945
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at Thr-174 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Not phosphorylated at Thr-174 by CaMKK2. In contrast, it is phosphorylated and activated by CaMKK1. May be inactivated via dephosphorylation of Thr-174 by PP2C. Phosphorylated at Thr-260 by PKA. Phosphorylation at Thr-260 by PKA was not observed in another study (PubMed:18339622), but this may reflect differences in the experimental approach. Phosphorylation at Thr-260 seems to play a role in the regulation of insulin secretion (PubMed:22669945). {ECO:0000269|PubMed:14976552, ECO:0000269|PubMed:16870137, ECO:0000269|PubMed:18339622, ECO:0000269|PubMed:19958286, ECO:0000269|PubMed:22669945}.; PTM: Polyubiquitinated by the APC complex in conjunction with FZR1, leading to its proteasomal degradation. Targeted for proteasomal degradation by interaction with COPS5. BRSK2 levels change during the cell cycle. BRSK2 levels are low at the G1/S boundary and gradually increase as cells progress into G2 phase. BRSK2 levels decrease rapidly at the end of mitosis. {ECO:0000269|PubMed:22609399, ECO:0000269|PubMed:23029325}.
uniprot
proteins
protein_family
CAMK Ser/Thr protein kinase family
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
SNF1 subfamily
uniprot
proteins
pubmed
11124703
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14976552
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16554811
uniprot
proteins
pubmed
16630837
uniprot
proteins
pubmed
16870137
uniprot
proteins
pubmed
18339622
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19958286
uniprot
proteins
pubmed
20026642
uniprot
proteins
pubmed
21985311
uniprot
proteins
pubmed
22609399
uniprot
proteins
pubmed
22669945
uniprot
proteins
pubmed
22713462
uniprot
proteins
pubmed
22798068
uniprot
proteins
pubmed
23029325
uniprot
proteins
pubmed
9929968
uniprot
proteins
sequence_length
736
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, perinuclear region. Endoplasmic reticulum. Note=Detected at centrosomes during mitosis. Localizes to the endoplasmic reticulum in response to stress caused by tunicamycin.
uniprot
proteins