dbPTM

BRSK1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	BRSK1_HUMAN
UniProt AC	Q8TDC3
Protein Name	Serine/threonine-protein kinase BRSK1
Gene Name	BRSK1
Organism	Homo sapiens (Human).
Sequence Length	778
Subcellular Localization	Cytoplasm . Nucleus . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cell junction, synapse. Localizes to synaptic vesicles in neurons (By similarity). Nuclear in the absence of DNA damage. Translocated to the nucleus in response
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-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..
Protein Sequence	MSSGAKEGGGGSPAYHLPHPHPHPPQHAQYVGPYRLEKTLGKGQTGLVKLGVHCITGQKVAIKIVNREKLSESVLMKVEREIAILKLIEHPHVLKLHDVYENKKYLYLVLEHVSGGELFDYLVKKGRLTPKEARKFFRQIVSALDFCHSYSICHRDLKPENLLLDEKNNIRIADFGMASLQVGDSLLETSCGSPHYACPEVIKGEKYDGRRADMWSCGVILFALLVGALPFDDDNLRQLLEKVKRGVFHMPHFIPPDCQSLLRGMIEVEPEKRLSLEQIQKHPWYLGGKHEPDPCLEPAPGRRVAMRSLPSNGELDPDVLESMASLGCFRDRERLHRELRSEEENQEKMIYYLLLDRKERYPSCEDQDLPPRNDVDPPRKRVDSPMLSRHGKRRPERKSMEVLSITDAGGGGSPVPTRRALEMAQHSQRSRSVSGASTGLSSSPLSSPRSPVFSFSPEPGAGDEARGGGSPTSKTQTLPSRGPRGGGAGEQPPPPSARSTPLPGPPGSPRSSGGTPLHSPLHTPRASPTGTPGTTPPPSPGGGVGGAAWRSRLNSIRNSFLGSPRFHRRKMQVPTAEEMSSLTPESSPELAKRSWFGNFISLDKEEQIFLVLKDKPLSSIKADIVHAFLSIPSLSHSVLSQTSFRAEYKASGGPSVFQKPVRFQVDISSSEGPEPSPRRDGSGGGGIYSVTFTLISGPSRRFKRVVETIQAQLLSTHDQPSVQALADEKNGAQTRPAGAPPRSLQPPPGRPDPELSSSPRRGPPKDKKLLATNGTPLP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
38	Sumoylation	VGPYRLEKTLGKGQT ECCEEEEEECCCCCC	54.35	-
42	Ubiquitination	RLEKTLGKGQTGLVK EEEEECCCCCCCEEE	51.46	32142685
86	Ubiquitination	EREIAILKLIEHPHV HHHHHHHHHHHCCCE	41.11	30230243
167	Ubiquitination	ENLLLDEKNNIRIAD HHCCCCCCCCCCCCH	55.77	30230243
189	Phosphorylation	VGDSLLETSCGSPHY CCCHHHHCCCCCCCC	29.32	14976552
193	Phosphorylation	LLETSCGSPHYACPE HHHCCCCCCCCCCCH	16.90	-
205	Phosphorylation	CPEVIKGEKYDGRRA CCHHHCCCCCCCCCC	43.36	14976552
260	Phosphorylation	FIPPDCQSLLRGMIE CCCHHHHHHHCCCCC	35.38	24719451
272	Ubiquitination	MIEVEPEKRLSLEQI CCCCCHHHCCCHHHH	70.16	30230243
275	Phosphorylation	VEPEKRLSLEQIQKH CCHHHCCCHHHHHHC	33.61	-
281	Ubiquitination	LSLEQIQKHPWYLGG CCHHHHHHCCCCCCC	53.95	30230243
308	Phosphorylation	GRRVAMRSLPSNGEL CCCEEEEECCCCCCC	31.39	28348404
311	Phosphorylation	VAMRSLPSNGELDPD EEEEECCCCCCCCHH	63.86	32142685
384	Phosphorylation	PPRKRVDSPMLSRHG CCCCCCCCHHHHHCC	14.89	29255136
388	Phosphorylation	RVDSPMLSRHGKRRP CCCCHHHHHCCCCCC	18.91	28122231
399	Phosphorylation	KRRPERKSMEVLSIT CCCCCCCCEEEEEEC	26.79	22199227
404	Phosphorylation	RKSMEVLSITDAGGG CCCEEEEEECCCCCC	28.72	29255136
406	Phosphorylation	SMEVLSITDAGGGGS CEEEEEECCCCCCCC	19.20	29255136
413	Phosphorylation	TDAGGGGSPVPTRRA CCCCCCCCCCCHHHH	26.46	29255136
417	Phosphorylation	GGGSPVPTRRALEMA CCCCCCCHHHHHHHH	32.78	29255136
427	Phosphorylation	ALEMAQHSQRSRSVS HHHHHHHHHHHHCCC	18.40	-
430	Phosphorylation	MAQHSQRSRSVSGAS HHHHHHHHHCCCCCC	22.67	21130716
431	Methylation	AQHSQRSRSVSGAST HHHHHHHHCCCCCCC	43.18	-
432	Phosphorylation	QHSQRSRSVSGASTG HHHHHHHCCCCCCCC	23.14	23403867
434	Phosphorylation	SQRSRSVSGASTGLS HHHHHCCCCCCCCCC	29.86	27732954
437	Phosphorylation	SRSVSGASTGLSSSP HHCCCCCCCCCCCCC	26.91	27732954
438	Phosphorylation	RSVSGASTGLSSSPL HCCCCCCCCCCCCCC	41.42	27732954
441	Phosphorylation	SGASTGLSSSPLSSP CCCCCCCCCCCCCCC	30.07	27732954
442	Phosphorylation	GASTGLSSSPLSSPR CCCCCCCCCCCCCCC	40.80	25307156
443	Phosphorylation	ASTGLSSSPLSSPRS CCCCCCCCCCCCCCC	26.87	27732954
446	Phosphorylation	GLSSSPLSSPRSPVF CCCCCCCCCCCCCCE	41.50	21130716
447	Phosphorylation	LSSSPLSSPRSPVFS CCCCCCCCCCCCCEE	31.83	19958286
450	Phosphorylation	SPLSSPRSPVFSFSP CCCCCCCCCCEEECC	28.88	25850435
454	Phosphorylation	SPRSPVFSFSPEPGA CCCCCCEEECCCCCC	25.67	27732954
456	Phosphorylation	RSPVFSFSPEPGAGD CCCCEEECCCCCCCC	27.44	27732954
466	Methylation	PGAGDEARGGGSPTS CCCCCCCCCCCCCCC	42.09	-
481	Methylation	KTQTLPSRGPRGGGA CCCCCCCCCCCCCCC	58.14	-
484	Methylation	TLPSRGPRGGGAGEQ CCCCCCCCCCCCCCC	60.25	-
498	Methylation	QPPPPSARSTPLPGP CCCCCCCCCCCCCCC	45.46	-
499	Phosphorylation	PPPPSARSTPLPGPP CCCCCCCCCCCCCCC	33.81	24117733
500	Phosphorylation	PPPSARSTPLPGPPG CCCCCCCCCCCCCCC	24.24	24117733
508	Phosphorylation	PLPGPPGSPRSSGGT CCCCCCCCCCCCCCC	23.94	22617229
510	Methylation	PGPPGSPRSSGGTPL CCCCCCCCCCCCCCC	45.19	-
511	Phosphorylation	GPPGSPRSSGGTPLH CCCCCCCCCCCCCCC	36.40	27732954
512	Phosphorylation	PPGSPRSSGGTPLHS CCCCCCCCCCCCCCC	42.39	27732954
515	Phosphorylation	SPRSSGGTPLHSPLH CCCCCCCCCCCCCCC	26.63	27732954
519	Phosphorylation	SGGTPLHSPLHTPRA CCCCCCCCCCCCCCC	36.52	25332170
523	Phosphorylation	PLHSPLHTPRASPTG CCCCCCCCCCCCCCC	23.35	27732954
525	Methylation	HSPLHTPRASPTGTP CCCCCCCCCCCCCCC	49.18	-
527	Phosphorylation	PLHTPRASPTGTPGT CCCCCCCCCCCCCCC	25.03	27732954
529	Phosphorylation	HTPRASPTGTPGTTP CCCCCCCCCCCCCCC	51.71	27732954
531	Phosphorylation	PRASPTGTPGTTPPP CCCCCCCCCCCCCCC	22.48	27732954
534	Phosphorylation	SPTGTPGTTPPPSPG CCCCCCCCCCCCCCC	37.01	27732954
535	Phosphorylation	PTGTPGTTPPPSPGG CCCCCCCCCCCCCCC	39.45	28985074
539	Phosphorylation	PGTTPPPSPGGGVGG CCCCCCCCCCCCCCH	41.78	27732954
550	Methylation	GVGGAAWRSRLNSIR CCCHHHHHHHHHHHH	13.74	-
555	Phosphorylation	AWRSRLNSIRNSFLG HHHHHHHHHHHHHCC	27.76	24719451
559	Phosphorylation	RLNSIRNSFLGSPRF HHHHHHHHHCCCHHH	16.40	29396449
563	Phosphorylation	IRNSFLGSPRFHRRK HHHHHCCCHHHHCCC	18.30	22167270
575	Phosphorylation	RRKMQVPTAEEMSSL CCCCCCCCHHHHHHC	48.09	27732954
580	Phosphorylation	VPTAEEMSSLTPESS CCCHHHHHHCCCCCC	26.02	22199227
581	Phosphorylation	PTAEEMSSLTPESSP CCHHHHHHCCCCCCH	34.65	22199227
583	Phosphorylation	AEEMSSLTPESSPEL HHHHHHCCCCCCHHH	27.27	22199227
586	Phosphorylation	MSSLTPESSPELAKR HHHCCCCCCHHHHHH	53.01	22199227
587	Phosphorylation	SSLTPESSPELAKRS HHCCCCCCHHHHHHC	22.26	29507054
601	Phosphorylation	SWFGNFISLDKEEQI CCCCCEECCCHHHEE	26.78	-
618	Phosphorylation	VLKDKPLSSIKADIV EECCCCHHHCCHHHH	38.25	24719451
668	Phosphorylation	VRFQVDISSSEGPEP EEEEEECCCCCCCCC	24.29	29083192
669	Phosphorylation	RFQVDISSSEGPEPS EEEEECCCCCCCCCC	32.51	29083192
670	Phosphorylation	FQVDISSSEGPEPSP EEEECCCCCCCCCCC	39.52	29083192
676	Phosphorylation	SSEGPEPSPRRDGSG CCCCCCCCCCCCCCC	29.40	25307156
682	Phosphorylation	PSPRRDGSGGGGIYS CCCCCCCCCCCCEEE	38.26	25332170
688	Phosphorylation	GSGGGGIYSVTFTLI CCCCCCEEEEEEEEE	10.60	24719451
691	Phosphorylation	GGGIYSVTFTLISGP CCCEEEEEEEEEECC	12.64	24719451
693	Phosphorylation	GIYSVTFTLISGPSR CEEEEEEEEEECCCH	17.51	24719451
696	Phosphorylation	SVTFTLISGPSRRFK EEEEEEEECCCHHHH	48.00	22210691
743	Phosphorylation	PAGAPPRSLQPPPGR CCCCCCCCCCCCCCC	36.81	23312004
756	Phosphorylation	GRPDPELSSSPRRGP CCCCCCCCCCCCCCC	27.40	27732954
757	Phosphorylation	RPDPELSSSPRRGPP CCCCCCCCCCCCCCC	57.92	27732954
758	Phosphorylation	PDPELSSSPRRGPPK CCCCCCCCCCCCCCC	21.03	27732954
772	Phosphorylation	KDKKLLATNGTPLP- CCCCHHCCCCCCCC-	33.86	-

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
189	T	Phosphorylation	Kinase	STK11	Q15831	GPS
205	T	Phosphorylation	Kinase	STK11	Q15831	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
189	T	Phosphorylation	14976552
May be inactivated via dephosphorylation of Thr-189 by PP2C.
189	T	Phosphorylation	14976552
Not phosphorylated at Thr-189 by CaMKK2.
189	T	Phosphorylation	14976552
Phosphorylated at Thr-189 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39.

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DHB7_HUMAN	HSD17B7	physical	21988832
BRCA1_HUMAN	BRCA1	physical	25184681
PAK1_HUMAN	PAK1	physical	22669945

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of BRSK1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-447 AND SER-508, ANDMASS SPECTROMETRY.	19369195 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-563, AND MASSSPECTROMETRY.	19413330 [Abstract]
"Investigating the regulation of brain-specific kinases 1 and 2 byphosphorylation."; Bright N.J., Carling D., Thornton C.; J. Biol. Chem. 283:14946-14954(2008). Cited for: PHOSPHORYLATION AT THR-189, AND MUTAGENESIS OF GLY-327.	18339622 [Abstract]
"LKB1 is a master kinase that activates 13 kinases of the AMPKsubfamily, including MARK/PAR-1."; Lizcano J.M., Goeransson O., Toth R., Deak M., Morrice N.A.,Boudeau J., Hawley S.A., Udd L., Maekelae T.P., Hardie D.G.,Alessi D.R.; EMBO J. 23:833-843(2004). Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, ENZYME REGULATION,PHOSPHORYLATION AT THR-189, AND MUTAGENESIS OF THR-189.	14976552 [Abstract]

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