BRSK2_MOUSE - dbPTM
BRSK2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BRSK2_MOUSE
UniProt AC Q69Z98
Protein Name Serine/threonine-protein kinase BRSK2
Gene Name Brsk2
Organism Mus musculus (Mouse).
Sequence Length 735
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, perinuclear region. Endoplasmic reticulum. Detected at centrosomes during mitosis. Localizes to the endoplasmic reticulum in response to stress caused by tunicamycin (By s
Protein 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-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]
Protein Sequence MTSTGKDGGGAQHAQYVGPYRLEKTLGKGQTGLVKLGIHCVTCQKVAIKIVNREKLSESVLMKVEREIAILKLIEHPHVLKLHDVYENKKYLYLVLEHVSGGELFDYLVKKGRLTPKEARKFFRQIISALDFCHSHSICHRDLKPENLLLDERNNIRIADFGMASLQVGDSLLETSCGSPHYACPEVIRGEKYDGRKADVWSCGVILFALLVGALPFDDDNLRQLLEKVKRGVFHMPHFIPPDCQSLLRGMIEVDAARRLTLEHIQKHIWYIGGKNEPEPEQPIPRKVQIRSLPSLEDIDPDVLDSMHSLGCFRDRNKLLQDLLSEEENQEKMIYFLLLDRKERYPSHEDEDLPPRNEIDPPRKRVDSPMLNRHGKRRPERKSMEVLSVTDGGSPVPARRAIEMAQHGQRSRSISGASSGLSTSPLSSPRVTPHPSPRGSPLPTPKGTPVHTPKESPAGTPNPTPPSSPSVGGVPWRTRLNSIKNSFLGSPRFHRRKLQVPTPEEMSNLTPESSPELAKKSWFGNFINLEKEEQIFVVIKDKPLSSIKADIVHAFLSIPSLSHSVISQTSFRAEYKATGGPAVFQKPVKFQVDITYTEGGEAQKENGIYSVTFTLLSGPSRRFKRVVETIQAQLLSTHDQPSAQHLSDTTNCMEVMTGRLSKCGTPLSNFFDVIKQLFSDEKNGQAAQAPSTPAKRSAHGPLGDSAAAGPGGDTEYPMGKDMAKMGPPAARREQP
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
28UbiquitinationRLEKTLGKGQTGLVK
EEEEECCCCCCCEEE		51.46-
175PhosphorylationVGDSLLETSCGSPHY
CCCHHHHCCCCCCCC		29.3222322096
176PhosphorylationGDSLLETSCGSPHYA
CCHHHHCCCCCCCCC		13.7022322096
179PhosphorylationLLETSCGSPHYACPE
HHHCCCCCCCCCCCH		16.9022322096
261PhosphorylationVDAARRLTLEHIQKH
HHHHHHCCHHHHHHH		28.43-
292PhosphorylationPRKVQIRSLPSLEDI
CCCEEEECCCCHHHC		46.3818388127
295PhosphorylationVQIRSLPSLEDIDPD
EEEECCCCHHHCCHH		50.0818388127
368PhosphorylationPPRKRVDSPMLNRHG
CCCCCCCCHHHCCCC		14.8925521595
383PhosphorylationKRRPERKSMEVLSVT
CCCCCCCCEEEEEEC		26.7925521595
388PhosphorylationRKSMEVLSVTDGGSP
CCCEEEEEECCCCCC		28.3124759943
390PhosphorylationSMEVLSVTDGGSPVP
CEEEEEECCCCCCCC		26.0822324799
394PhosphorylationLSVTDGGSPVPARRA
EEECCCCCCCCHHHH		28.4025521595
411PhosphorylationMAQHGQRSRSISGAS
HHHHCCCCCCCCCCC		23.6119060867
413PhosphorylationQHGQRSRSISGASSG
HHCCCCCCCCCCCCC		23.5025521595
415PhosphorylationGQRSRSISGASSGLS
CCCCCCCCCCCCCCC		29.5625521595
418PhosphorylationSRSISGASSGLSTSP
CCCCCCCCCCCCCCC		28.5924925903
419PhosphorylationRSISGASSGLSTSPL
CCCCCCCCCCCCCCC		43.1318388127
422PhosphorylationSGASSGLSTSPLSSP
CCCCCCCCCCCCCCC		30.2918388127
423PhosphorylationGASSGLSTSPLSSPR
CCCCCCCCCCCCCCC		39.1325521595
424PhosphorylationASSGLSTSPLSSPRV
CCCCCCCCCCCCCCC		22.0725521595
427PhosphorylationGLSTSPLSSPRVTPH
CCCCCCCCCCCCCCC		41.5024925903
428PhosphorylationLSTSPLSSPRVTPHP
CCCCCCCCCCCCCCC		25.1425521595
432PhosphorylationPLSSPRVTPHPSPRG
CCCCCCCCCCCCCCC		19.7025159016
436PhosphorylationPRVTPHPSPRGSPLP
CCCCCCCCCCCCCCC		24.9725159016
440PhosphorylationPHPSPRGSPLPTPKG
CCCCCCCCCCCCCCC		25.2519060867
444PhosphorylationPRGSPLPTPKGTPVH
CCCCCCCCCCCCCCC		45.3621183079
448PhosphorylationPLPTPKGTPVHTPKE
CCCCCCCCCCCCCCC		28.4121183079
452PhosphorylationPKGTPVHTPKESPAG
CCCCCCCCCCCCCCC		35.9719060867
456PhosphorylationPVHTPKESPAGTPNP
CCCCCCCCCCCCCCC		26.6125521595
460PhosphorylationPKESPAGTPNPTPPS
CCCCCCCCCCCCCCC		23.2319060867
464PhosphorylationPAGTPNPTPPSSPSV
CCCCCCCCCCCCCCC		55.2425521595
467PhosphorylationTPNPTPPSSPSVGGV
CCCCCCCCCCCCCCC		56.9619060867
468PhosphorylationPNPTPPSSPSVGGVP
CCCCCCCCCCCCCCC		27.2830372032
470PhosphorylationPTPPSSPSVGGVPWR
CCCCCCCCCCCCCCH		35.0325521595
482PhosphorylationPWRTRLNSIKNSFLG
CCHHHHHHHHHHCCC		39.2619060867
486PhosphorylationRLNSIKNSFLGSPRF
HHHHHHHHCCCCCCH		19.4920415495
490PhosphorylationIKNSFLGSPRFHRRK
HHHHCCCCCCHHCCC		18.3018388127
502PhosphorylationRRKLQVPTPEEMSNL
CCCCCCCCHHHHHCC		44.4624925903
507PhosphorylationVPTPEEMSNLTPESS
CCCHHHHHCCCCCCC		31.7824925903
510PhosphorylationPEEMSNLTPESSPEL
HHHHHCCCCCCCHHH		29.3018388127
513PhosphorylationMSNLTPESSPELAKK
HHCCCCCCCHHHHHH		53.0125521595
514PhosphorylationSNLTPESSPELAKKS
HCCCCCCCHHHHHHH		22.2625521595
521PhosphorylationSPELAKKSWFGNFIN
CHHHHHHHHCCCCCC		27.2522324799
670 (in isoform 2)Phosphorylation-5.0629899451
671 (in isoform 2)Phosphorylation-9.5529899451
674 (in isoform 2)Phosphorylation-2.2429899451
692PhosphorylationQAAQAPSTPAKRSAH
CCCCCCCCCCCCCCC		26.6329899451
697PhosphorylationPSTPAKRSAHGPLGD
CCCCCCCCCCCCCCC		24.7429899451
705PhosphorylationAHGPLGDSAAAGPGG
CCCCCCCCCCCCCCC		20.2929899451
716PhosphorylationGPGGDTEYPMGKDMA
CCCCCCCCCCCHHHH		10.70-
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
175TPhosphorylationKinaseSTK11Q9WTK7
GPS
261TPhosphorylationKinasePKA-Uniprot
424SPhosphorylationKinaseCDK5Q00535
PSP
428SPhosphorylationKinaseCDK5Q00535
PSP
432TPhosphorylationKinaseCDK5Q00535
PSP
436SPhosphorylationKinaseCDK5Q00535
PSP
440SPhosphorylationKinaseCDK5Q00535
PSP
444TPhosphorylationKinaseCDK5Q00535
PSP
448TPhosphorylationKinaseCDK5Q00535
PSP
452TPhosphorylationKinaseCDK5Q00535
PSP
456SPhosphorylationKinaseCDK5Q00535
PSP
460TPhosphorylationKinaseCDK5Q00535
PSP
464TPhosphorylationKinaseCDK5Q00535
PSP
467SPhosphorylationKinaseCDK5Q00535
PSP
468SPhosphorylationKinaseCDK5Q00535
PSP
490SPhosphorylationKinaseCDK5Q00535
PSP
502TPhosphorylationKinaseCDK5Q00535
PSP
510TPhosphorylationKinaseCDK5Q00535
PSP
513SPhosphorylationKinaseCDK5Q00535
PSP
514SPhosphorylationKinaseCDK5Q00535
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
175TPhosphorylation

17482548
175TPhosphorylation

17482548
175TPhosphorylation

17482548
261TPhosphorylation

17482548
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of BRSK2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of BRSK2_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BRSK2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"LKB1 and SAD kinases define a pathway required for the polarizationof cortical neurons.";
Barnes A.P., Lilley B.N., Pan Y.A., Plummer L.J., Powell A.W.,Raines A.N., Sanes J.R., Polleux F.;
Cell 129:549-563(2007).
Cited for: FUNCTION, PHOSPHORYLATION AT THR-175, AND MUTAGENESIS OF THR-175.
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-423, AND MASSSPECTROMETRY.

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