BRSK1_RAT - dbPTM
BRSK1_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BRSK1_RAT
UniProt AC B2DD29
Protein Name Serine/threonine-protein kinase BRSK1
Gene Name Brsk1
Organism Rattus norvegicus (Rat).
Sequence Length 778
Subcellular Localization Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cell junction, synapse . Nuclear in the absence of DNA damage. Translocated to the nucleus in response to UV- or MMS-induced DNA damage (By similarity). Localizes
Protein 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-523' and 'Ser-573'. 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. 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 (By similarity). In neurons, localizes to synaptic vesicles and plays a role in neurotransmitter release, possibly by phosphorylating RIMS1..
Protein Sequence MSSGSKEGGGGSPAYHLPHPHPHPPQHAQYVGPYRLEKTLGKGQTGLVKLGVHCITGQKVAVKIVNREKLSESVLMKVEREIAILKLIEHPHVLKLHDVYENKKYLYLVLEHVSGGELFDYLVKKGRLTPKEARKFFRQIVSALDFCHSYSICHRDLKPENLLLDEKNNIRIADFGMASLQVGDSLLETSCGSPHYACPEVIKGEKYDGRRADMWSCGVILFALLVGALPFDDDNLRQLLEKVKRGVFHMPHFIPPDCQSLLRGMIEVEPEKRLSLEQIQKHPWYLGGKHEPDPCLEPAPGRRVAMRSLPSNGELDPDVLESMASLGCFRDRERLHRELRSEEENQEKMIYYLLLDRKERYPSCEDQDLPPRNDVDPPRKRVDSPMLSRHGKRRPERKSMEVLSITDAGSGGSPVPTRRALEMAQHSQRSRSVSGASTGLSSSPLSSPRSPVFSFSPEPGVGDEARGGGSPTSKTQTLPSRGPRGGGAGEQPPPPSARSTPLPGPPGSPRSSGGTPLHSPLHTPRASPTGTPGTTPPPSPGGGVGGAAWRSRLNSIRNSFLGSPRFHRRKMQVPTAEEMSSLTPESSPELAKRSWFGNFISLDKEEQIFLVLKDKPLSSIKADIVHAFLSIPSLSHSVLSQTSFRAEYKASGGPSVFQKPVRFQVDISSSEGPEPSPRRDGSSGGGIYSVTFTLISGPSRRFKRVVETIQAQLLSTHDQPSVQALADEKNGAQTRPAGTPPRSLQPPPGRPDPDLSSSPRRGPSKDKKLLATNGTPLP
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
34PhosphorylationHAQYVGPYRLEKTLG
CCCEECCEEEEEECC		23.15-
189PhosphorylationVGDSLLETSCGSPHY
CCCHHHHCCCCCCCC		29.3218324781
193PhosphorylationLLETSCGSPHYACPE
HHHCCCCCCCCCCCH		16.90-
308PhosphorylationGRRVAMRSLPSNGEL
CCCEEEEECCCCCCC		31.3922673903
311PhosphorylationVAMRSLPSNGELDPD
EEEEECCCCCCCCHH		63.8622673903
351PhosphorylationENQEKMIYYLLLDRK
HHHHHHHHHHHCCCH		5.64-
384PhosphorylationPPRKRVDSPMLSRHG
CCCCCCCCHHHHHCC		14.8928432305
399PhosphorylationKRRPERKSMEVLSIT
CCCCCCCCEEEEEEC		26.7927097102
406PhosphorylationSMEVLSITDAGSGGS
CEEEEEECCCCCCCC		19.2028432305
410PhosphorylationLSITDAGSGGSPVPT
EEECCCCCCCCCCCH		41.5228432305
413PhosphorylationTDAGSGGSPVPTRRA
CCCCCCCCCCCHHHH		26.6728432305
417PhosphorylationSGGSPVPTRRALEMA
CCCCCCCHHHHHHHH		32.7822673903
430PhosphorylationMAQHSQRSRSVSGAS
HHHHHHHHHCCCCCC		22.6728432305
432PhosphorylationQHSQRSRSVSGASTG
HHHHHHHCCCCCCCC		23.1428432305
434PhosphorylationSQRSRSVSGASTGLS
HHHHHCCCCCCCCCC		29.8628432305
437PhosphorylationSRSVSGASTGLSSSP
HHCCCCCCCCCCCCC		26.9128432305
438PhosphorylationRSVSGASTGLSSSPL
HCCCCCCCCCCCCCC		41.4228432305
441PhosphorylationSGASTGLSSSPLSSP
CCCCCCCCCCCCCCC		30.0728432305
442PhosphorylationGASTGLSSSPLSSPR
CCCCCCCCCCCCCCC		40.8028432305
443PhosphorylationASTGLSSSPLSSPRS
CCCCCCCCCCCCCCC		26.8727097102
446PhosphorylationGLSSSPLSSPRSPVF
CCCCCCCCCCCCCCE		41.5028432305
447PhosphorylationLSSSPLSSPRSPVFS
CCCCCCCCCCCCCEE		31.8327097102
450PhosphorylationSPLSSPRSPVFSFSP
CCCCCCCCCCEEECC		28.8827097102
454PhosphorylationSPRSPVFSFSPEPGV
CCCCCCEEECCCCCC		25.6728432305
456PhosphorylationRSPVFSFSPEPGVGD
CCCCEEECCCCCCCC		27.4428432305
466MethylationPGVGDEARGGGSPTS
CCCCCCCCCCCCCCC		42.09-
470PhosphorylationDEARGGGSPTSKTQT
CCCCCCCCCCCCCCC		28.4225403869
472PhosphorylationARGGGSPTSKTQTLP
CCCCCCCCCCCCCCC		44.5525403869
481MethylationKTQTLPSRGPRGGGA
CCCCCCCCCCCCCCC		58.14-
484MethylationTLPSRGPRGGGAGEQ
CCCCCCCCCCCCCCC		60.25-
498MethylationQPPPPSARSTPLPGP
CCCCCCCCCCCCCCC		45.46-
499PhosphorylationPPPPSARSTPLPGPP
CCCCCCCCCCCCCCC		33.8128432305
500PhosphorylationPPPSARSTPLPGPPG
CCCCCCCCCCCCCCC		24.2428432305
508PhosphorylationPLPGPPGSPRSSGGT
CCCCCCCCCCCCCCC		23.9427097102
511PhosphorylationGPPGSPRSSGGTPLH
CCCCCCCCCCCCCCC		36.4028432305
512PhosphorylationPPGSPRSSGGTPLHS
CCCCCCCCCCCCCCC		42.3928432305
515PhosphorylationSPRSSGGTPLHSPLH
CCCCCCCCCCCCCCC		26.6328432305
519PhosphorylationSGGTPLHSPLHTPRA
CCCCCCCCCCCCCCC		36.5228432305
523PhosphorylationPLHSPLHTPRASPTG
CCCCCCCCCCCCCCC		23.3528432305
525MethylationHSPLHTPRASPTGTP
CCCCCCCCCCCCCCC		49.18-
527PhosphorylationPLHTPRASPTGTPGT
CCCCCCCCCCCCCCC		25.0327097102
529PhosphorylationHTPRASPTGTPGTTP
CCCCCCCCCCCCCCC		51.7127097102
531PhosphorylationPRASPTGTPGTTPPP
CCCCCCCCCCCCCCC		22.4827097102
534PhosphorylationSPTGTPGTTPPPSPG
CCCCCCCCCCCCCCC		37.0127097102
535PhosphorylationPTGTPGTTPPPSPGG
CCCCCCCCCCCCCCC		39.4527097102
539PhosphorylationPGTTPPPSPGGGVGG
CCCCCCCCCCCCCCH		41.7828551015
550MethylationGVGGAAWRSRLNSIR
CCCHHHHHHHHHHHH		13.74-
551PhosphorylationVGGAAWRSRLNSIRN
CCHHHHHHHHHHHHH		30.3422276854
555PhosphorylationAWRSRLNSIRNSFLG
HHHHHHHHHHHHHCC		27.7622276854
563PhosphorylationIRNSFLGSPRFHRRK
HHHHHCCCHHHHCCC		18.3027097102
575PhosphorylationRRKMQVPTAEEMSSL
CCCCCCCCHHHHHHC		48.0928432305
580PhosphorylationVPTAEEMSSLTPESS
CCCHHHHHHCCCCCC		26.0228432305
581PhosphorylationPTAEEMSSLTPESSP
CCHHHHHHCCCCCCH		34.6528432305
583PhosphorylationAEEMSSLTPESSPEL
HHHHHHCCCCCCHHH		27.2727097102
586PhosphorylationMSSLTPESSPELAKR
HHHCCCCCCHHHHHH		53.0127097102
587PhosphorylationSSLTPESSPELAKRS
HHCCCCCCHHHHHHC		22.2627097102
601PhosphorylationSWFGNFISLDKEEQI
CCCCCEECCCHHHEE		26.7816630837
659UbiquitinationGGPSVFQKPVRFQVD
CCCCCCCCCEEEEEE		33.73-
668PhosphorylationVRFQVDISSSEGPEP
EEEEEECCCCCCCCC		24.2928432305
669PhosphorylationRFQVDISSSEGPEPS
EEEEECCCCCCCCCC		32.5128432305
670PhosphorylationFQVDISSSEGPEPSP
EEEECCCCCCCCCCC		39.5228432305
676PhosphorylationSSEGPEPSPRRDGSS
CCCCCCCCCCCCCCC		29.4028432305
756PhosphorylationGRPDPDLSSSPRRGP
CCCCCCCCCCCCCCC		35.8328432305
757PhosphorylationRPDPDLSSSPRRGPS
CCCCCCCCCCCCCCC		52.2228432305
758PhosphorylationPDPDLSSSPRRGPSK
CCCCCCCCCCCCCCC		21.0328432305
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
189TPhosphorylationKinaseCAMK2AQ9UQM7
PSP
189TPhosphorylationKinaseSTK11D4AE59
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
189TPhosphorylation

18324781
189TPhosphorylation

18324781
189TPhosphorylation

18324781
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 BRSK1_RAT !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of BRSK1_RAT !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BRSK1_RAT

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Activation of SAD kinase by Ca2+/calmodulin-dependent protein kinasekinase.";
Fujimoto T., Yurimoto S., Hatano N., Nozaki N., Sueyoshi N.,Kameshita I., Mizutani A., Mikoshiba K., Kobayashi R., Tokumitsu H.;
Biochemistry 47:4151-4159(2008).
Cited for: NUCLEOTIDE SEQUENCE [MRNA], AND PHOSPHORYLATION AT THR-189.

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