ID  Q69Z98;
PN  Serine/threonine-protein kinase BRSK2;
GN  Brsk2;
OS  10090;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Note=Detected at centrosomes during mitosis. Localizes to the endoplasmic reticulum in response to stress caused by tunicamycin (By similarity). {ECO:0000250}.
DR  UNIPROT: Q69Z98;
DR  UNIPROT: Q699J3;
DR  UNIPROT: Q699J4;
DR  UNIPROT: Q6DMN7;
DR  UNIPROT: Q6PHM0;
DR  PDB: 4YNZ;
DR  PDB: 4YOM;
DR  Pfam: PF00069;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  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-504' and 'Ser-554'. 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. 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- 175 can inhibit insulin secretion (PubMed:22798068), BRSK2 phosphorylated at Thr-261 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:15705853, ECO:0000269|PubMed:17482548, ECO:0000269|PubMed:20026642, ECO:0000269|PubMed:22669945, ECO:0000269|PubMed:22798068}.
DE  Reference Proteome: Yes;
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0150034;
GO  GO:0005783;
GO  GO:0048471;
GO  GO:0005524;
GO  GO:0051117;
GO  GO:0000287;
GO  GO:0019901;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0050321;
GO  GO:0031532;
GO  GO:0007409;
GO  GO:0051301;
GO  GO:0042149;
GO  GO:0036503;
GO  GO:0030010;
GO  GO:0006887;
GO  GO:0000086;
GO  GO:0035556;
GO  GO:0070059;
GO  GO:0090176;
GO  GO:0030182;
GO  GO:0048812;
GO  GO:0018105;
GO  GO:0006468;
GO  GO:0050770;
GO  GO:0061178;
GO  GO:0010975;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MTSTGKDGGGAQHAQYVGPYRLEKTLGKGQTGLVKLGIHCVTCQKVAIKIVNREKLSESVLMKVEREIAILKLIEHPHVL
SQ  KLHDVYENKKYLYLVLEHVSGGELFDYLVKKGRLTPKEARKFFRQIISALDFCHSHSICHRDLKPENLLLDERNNIRIAD
SQ  FGMASLQVGDSLLETSCGSPHYACPEVIRGEKYDGRKADVWSCGVILFALLVGALPFDDDNLRQLLEKVKRGVFHMPHFI
SQ  PPDCQSLLRGMIEVDAARRLTLEHIQKHIWYIGGKNEPEPEQPIPRKVQIRSLPSLEDIDPDVLDSMHSLGCFRDRNKLL
SQ  QDLLSEEENQEKMIYFLLLDRKERYPSHEDEDLPPRNEIDPPRKRVDSPMLNRHGKRRPERKSMEVLSVTDGGSPVPARR
SQ  AIEMAQHGQRSRSISGASSGLSTSPLSSPRVTPHPSPRGSPLPTPKGTPVHTPKESPAGTPNPTPPSSPSVGGVPWRTRL
SQ  NSIKNSFLGSPRFHRRKLQVPTPEEMSNLTPESSPELAKKSWFGNFINLEKEEQIFVVIKDKPLSSIKADIVHAFLSIPS
SQ  LSHSVISQTSFRAEYKATGGPAVFQKPVKFQVDITYTEGGEAQKENGIYSVTFTLLSGPSRRFKRVVETIQAQLLSTHDQ
SQ  PSAQHLSDTTNCMEVMTGRLSKCGTPLSNFFDVIKQLFSDEKNGQAAQAPSTPAKRSAHGPLGDSAAAGPGGDTEYPMGK
SQ  DMAKMGPPAARREQP
//