BRSK1_HUMAN
ID BRSK1_HUMAN Reviewed; 778 AA.
AC Q8TDC3; F1DG44; Q5J5B5; Q8NDD0; Q8NDR4; Q8TDC2; Q96AV4; Q96JL4;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Serine/threonine-protein kinase BRSK1;
DE EC=2.7.11.1;
DE AltName: Full=Brain-selective kinase 1;
DE EC=2.7.11.26;
DE AltName: Full=Brain-specific serine/threonine-protein kinase 1;
DE Short=BR serine/threonine-protein kinase 1;
DE AltName: Full=Serine/threonine-protein kinase SAD-B;
DE AltName: Full=Synapses of Amphids Defective homolog 1;
DE Short=SAD1 homolog;
DE Short=hSAD1;
GN Name=BRSK1; Synonyms=KIAA1811, SAD1, SADB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, ACTIVITY REGULATION,
RP PHOSPHORYLATION AT THR-189, AND MUTAGENESIS OF THR-189.
RX PubMed=14976552; DOI=10.1038/sj.emboj.7600110;
RA Lizcano J.M., Goeransson O., Toth R., Deak M., Morrice N.A., Boudeau J.,
RA Hawley S.A., Udd L., Maekelae T.P., Hardie D.G., Alessi D.R.;
RT "LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily,
RT including MARK/PAR-1.";
RL EMBO J. 23:833-843(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND MUTAGENESIS OF LYS-59.
RC TISSUE=Testis;
RX PubMed=15150265; DOI=10.1074/jbc.m404728200;
RA Lu R., Niida H., Nakanishi M.;
RT "Human SAD1 kinase is involved in UV-induced DNA damage checkpoint
RT function.";
RL J. Biol. Chem. 279:31164-31170(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=16630837; DOI=10.1016/j.neuron.2006.03.018;
RA Inoue E., Mochida S., Takagi H., Higa S., Deguchi-Tawarada M.,
RA Takao-Rikitsu E., Inoue M., Yao I., Takeuchi K., Kitajima I., Setou M.,
RA Ohtsuka T., Takai Y.;
RT "SAD: a presynaptic kinase associated with synaptic vesicles and the active
RT zone cytomatrix that regulates neurotransmitter release.";
RL Neuron 50:261-275(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX PubMed=19648910; DOI=10.1038/ncb1921;
RA Alvarado-Kristensson M., Rodriguez M.J., Silio V., Valpuesta J.M.,
RA Carrera A.C.;
RT "SADB phosphorylation of gamma-tubulin regulates centrosome duplication.";
RL Nat. Cell Biol. 11:1081-1092(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RA She X.Y., Yu L., Guo J.H.;
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 35-778.
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 64-778.
RC TISSUE=Brain;
RX PubMed=11347906; DOI=10.1093/dnares/8.2.85;
RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 8:85-95(2001).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 287-778.
RC TISSUE=Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP PHOSPHORYLATION AT THR-189, AND MUTAGENESIS OF GLY-327.
RX PubMed=18339622; DOI=10.1074/jbc.m710381200;
RA Bright N.J., Carling D., Thornton C.;
RT "Investigating the regulation of brain-specific kinases 1 and 2 by
RT phosphorylation.";
RL J. Biol. Chem. 283:14946-14954(2008).
RN [11]
RP PHOSPHORYLATION.
RX PubMed=19958286; DOI=10.1042/bj20091372;
RA Fogarty S., Hawley S.A., Green K.A., Saner N., Mustard K.J., Hardie D.G.;
RT "Calmodulin-dependent protein kinase kinase-beta activates AMPK without
RT forming a stable complex: synergistic effects of Ca2+ and AMP.";
RL Biochem. J. 426:109-118(2010).
RN [12]
RP FUNCTION.
RX PubMed=20026642; DOI=10.1242/jcs.058230;
RA Muller M., Lutter D., Puschel A.W.;
RT "Persistence of the cell-cycle checkpoint kinase Wee1 in SadA- and SadB-
RT deficient neurons disrupts neuronal polarity.";
RL J. Cell Sci. 123:286-294(2010).
RN [13]
RP CATALYTIC ACTIVITY, AND FUNCTION IN MAPT PHOSPHORYLATION.
RX PubMed=21985311; DOI=10.1111/j.1471-4159.2011.07523.x;
RA Yoshida H., Goedert M.;
RT "Phosphorylation of microtubule-associated protein tau by AMPK-related
RT kinases.";
RL J. Neurochem. 120:165-176(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-508, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP VARIANTS [LARGE SCALE ANALYSIS] TRP-303; ILE-319; GLU-391; ASN-531; SER-749
RP AND ALA-764.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Serine/threonine-protein kinase that plays a key role in
CC polarization of neurons and centrosome duplication. Phosphorylates
CC CDC25B, CDC25C, MAPT/TAU, RIMS1, TUBG1, TUBG2 and WEE1. Following
CC phosphorylation and activation by STK11/LKB1, acts as a key regulator
CC of polarization of cortical neurons, probably by mediating
CC phosphorylation of microtubule-associated proteins such as MAPT/TAU at
CC 'Thr-529' and 'Ser-579'. Also regulates neuron polarization by
CC mediating phosphorylation of WEE1 at 'Ser-642' in postmitotic neurons,
CC leading to down-regulate WEE1 activity in polarized neurons. In
CC neurons, localizes to synaptic vesicles and plays a role in
CC neurotransmitter release, possibly by phosphorylating RIMS1. Also acts
CC as a positive regulator of centrosome duplication by mediating
CC phosphorylation of gamma-tubulin (TUBG1 and TUBG2) at 'Ser-131',
CC leading to translocation of gamma-tubulin and its associated proteins
CC to the centrosome. Involved in the UV-induced DNA damage checkpoint
CC response, probably by inhibiting CDK1 activity through phosphorylation
CC and activation of WEE1, and inhibition of CDC25B and CDC25C.
CC {ECO:0000269|PubMed:14976552, ECO:0000269|PubMed:15150265,
CC ECO:0000269|PubMed:20026642, ECO:0000269|PubMed:21985311}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:21985311};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:21985311};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[tau protein] = ADP + H(+) + O-phospho-L-seryl-
CC [tau protein]; Xref=Rhea:RHEA:12801, Rhea:RHEA-COMP:13701, Rhea:RHEA-
CC COMP:13702, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.26;
CC Evidence={ECO:0000269|PubMed:21985311};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[tau protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[tau protein]; Xref=Rhea:RHEA:53904, Rhea:RHEA-COMP:13703,
CC Rhea:RHEA-COMP:13704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.26; Evidence={ECO:0000269|PubMed:21985311};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by phosphorylation on Thr-189 by
CC STK11/LKB1. {ECO:0000269|PubMed:14976552}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15150265}. Nucleus
CC {ECO:0000269|PubMed:15150265}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250}. Synapse
CC {ECO:0000250|UniProtKB:B2DD29}. Presynaptic active zone
CC {ECO:0000250|UniProtKB:B2DD29}. Cytoplasmic vesicle, secretory vesicle,
CC synaptic vesicle {ECO:0000250|UniProtKB:B2DD29}. Note=Nuclear in the
CC absence of DNA damage. Translocated to the nucleus in response to
CC UV- or MMS-induced DNA damage (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=SADB-Long, L;
CC IsoId=Q8TDC3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TDC3-2; Sequence=VSP_008158;
CC Name=3; Synonyms=SADB-short, S;
CC IsoId=Q8TDC3-3; Sequence=VSP_041742;
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in brain and
CC testis. Protein levels remain constant throughout the cell cycle.
CC {ECO:0000269|PubMed:15150265}.
CC -!- PTM: Phosphorylated at Thr-189 by STK11/LKB1 in complex with STE20-
CC related adapter-alpha (STRADA) pseudo kinase and CAB39. Not
CC phosphorylated at Thr-189 by CaMKK2. In contrast, it is phosphorylated
CC and activated by CaMKK1. May be inactivated via dephosphorylation of
CC Thr-189 by PP2C. {ECO:0000269|PubMed:14976552,
CC ECO:0000269|PubMed:18339622, ECO:0000269|PubMed:19958286}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. SNF1 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH16681.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY458602; AAS10354.1; -; mRNA.
DR EMBL; AY505124; AAS86442.1; -; mRNA.
DR EMBL; HQ830199; ADX95745.1; -; mRNA.
DR EMBL; AF479826; AAL87697.1; -; mRNA.
DR EMBL; AF479827; AAL87698.1; -; mRNA.
DR EMBL; AC008974; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC020922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL831945; CAD38595.1; -; mRNA.
DR EMBL; AL834275; CAD38950.2; -; mRNA.
DR EMBL; AB058714; BAB47440.1; -; mRNA.
DR EMBL; BC016681; AAH16681.1; ALT_INIT; mRNA.
DR CCDS; CCDS12921.1; -. [Q8TDC3-1]
DR RefSeq; NP_115806.1; NM_032430.1. [Q8TDC3-1]
DR AlphaFoldDB; Q8TDC3; -.
DR SMR; Q8TDC3; -.
DR BioGRID; 124084; 9.
DR IntAct; Q8TDC3; 24.
DR MINT; Q8TDC3; -.
DR STRING; 9606.ENSP00000310649; -.
DR BindingDB; Q8TDC3; -.
DR ChEMBL; CHEMBL5650; -.
DR DrugCentral; Q8TDC3; -.
DR GlyGen; Q8TDC3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8TDC3; -.
DR PhosphoSitePlus; Q8TDC3; -.
DR BioMuta; BRSK1; -.
DR DMDM; 347595639; -.
DR jPOST; Q8TDC3; -.
DR MassIVE; Q8TDC3; -.
DR PaxDb; Q8TDC3; -.
DR PeptideAtlas; Q8TDC3; -.
DR PRIDE; Q8TDC3; -.
DR ProteomicsDB; 74264; -. [Q8TDC3-1]
DR ProteomicsDB; 74265; -. [Q8TDC3-2]
DR ProteomicsDB; 74266; -. [Q8TDC3-3]
DR Antibodypedia; 19545; 476 antibodies from 36 providers.
DR DNASU; 84446; -.
DR Ensembl; ENST00000309383.6; ENSP00000310649.1; ENSG00000160469.17. [Q8TDC3-1]
DR Ensembl; ENST00000585418.1; ENSP00000467357.1; ENSG00000160469.17. [Q8TDC3-3]
DR Ensembl; ENST00000590333.5; ENSP00000468190.1; ENSG00000160469.17. [Q8TDC3-2]
DR GeneID; 84446; -.
DR KEGG; hsa:84446; -.
DR MANE-Select; ENST00000309383.6; ENSP00000310649.1; NM_032430.2; NP_115806.1.
DR UCSC; uc002qkf.4; human. [Q8TDC3-1]
DR CTD; 84446; -.
DR DisGeNET; 84446; -.
DR GeneCards; BRSK1; -.
DR HGNC; HGNC:18994; BRSK1.
DR HPA; ENSG00000160469; Group enriched (brain, pituitary gland).
DR MIM; 609235; gene.
DR neXtProt; NX_Q8TDC3; -.
DR OpenTargets; ENSG00000160469; -.
DR PharmGKB; PA134888976; -.
DR VEuPathDB; HostDB:ENSG00000160469; -.
DR eggNOG; KOG0588; Eukaryota.
DR GeneTree; ENSGT00940000161254; -.
DR HOGENOM; CLU_000288_156_2_1; -.
DR InParanoid; Q8TDC3; -.
DR OMA; LFALLVX; -.
DR OrthoDB; 1127668at2759; -.
DR PhylomeDB; Q8TDC3; -.
DR TreeFam; TF313967; -.
DR PathwayCommons; Q8TDC3; -.
DR SignaLink; Q8TDC3; -.
DR SIGNOR; Q8TDC3; -.
DR BioGRID-ORCS; 84446; 8 hits in 1109 CRISPR screens.
DR ChiTaRS; BRSK1; human.
DR GeneWiki; BRSK1; -.
DR GenomeRNAi; 84446; -.
DR Pharos; Q8TDC3; Tchem.
DR PRO; PR:Q8TDC3; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q8TDC3; protein.
DR Bgee; ENSG00000160469; Expressed in right frontal lobe and 120 other tissues.
DR ExpressionAtlas; Q8TDC3; baseline and differential.
DR Genevisible; Q8TDC3; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0150034; C:distal axon; ISS:ARUK-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048786; C:presynaptic active zone; TAS:ARUK-UCL.
DR GO; GO:0008021; C:synaptic vesicle; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IC:UniProtKB.
DR GO; GO:0043015; F:gamma-tubulin binding; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0048156; F:tau protein binding; NAS:ARUK-UCL.
DR GO; GO:0050321; F:tau-protein kinase activity; IDA:UniProtKB.
DR GO; GO:0008306; P:associative learning; ISS:ARUK-UCL.
DR GO; GO:0007409; P:axonogenesis; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0042149; P:cellular response to glucose starvation; IBA:GO_Central.
DR GO; GO:0051298; P:centrosome duplication; ISS:UniProtKB.
DR GO; GO:0030010; P:establishment of cell polarity; ISS:UniProtKB.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IDA:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0090176; P:microtubule cytoskeleton organization involved in establishment of planar polarity; ISS:ARUK-UCL.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IDA:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; ISS:UniProtKB.
DR GO; GO:0007269; P:neurotransmitter secretion; ISS:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0050770; P:regulation of axonogenesis; ISS:ARUK-UCL.
DR GO; GO:0010975; P:regulation of neuron projection development; ISS:ARUK-UCL.
DR GO; GO:0048167; P:regulation of synaptic plasticity; ISS:ARUK-UCL.
DR GO; GO:2000807; P:regulation of synaptic vesicle clustering; TAS:ARUK-UCL.
DR GO; GO:0009411; P:response to UV; IDA:UniProtKB.
DR GO; GO:0099504; P:synaptic vesicle cycle; ISS:ARUK-UCL.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR015940; UBA.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50030; UBA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell cycle; Cell projection; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; DNA damage; Kinase; Magnesium;
KW Metal-binding; Methylation; Neurogenesis; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Synapse; Transferase.
FT CHAIN 1..778
FT /note="Serine/threonine-protein kinase BRSK1"
FT /id="PRO_0000085669"
FT DOMAIN 34..285
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 314..356
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..510
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..758
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 156
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 40..48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 189
FT /note="Phosphothreonine; by LKB1"
FT /evidence="ECO:0000269|PubMed:14976552,
FT ECO:0000269|PubMed:18339622"
FT MOD_RES 399
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5RJI5"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5RJI5"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5RJI5"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5RJI5"
FT MOD_RES 466
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q5RJI5"
FT MOD_RES 481
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q5RJI5"
FT MOD_RES 484
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q5RJI5"
FT MOD_RES 498
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q5RJI5"
FT MOD_RES 508
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 525
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q5RJI5"
FT MOD_RES 529
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5RJI5"
FT MOD_RES 535
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5RJI5"
FT MOD_RES 550
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q5RJI5"
FT MOD_RES 583
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5RJI5"
FT MOD_RES 586
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2DD29"
FT MOD_RES 587
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2DD29"
FT MOD_RES 601
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2DD29"
FT VAR_SEQ 1..26
FT /note="MSSGAKEGGGGSPAYHLPHPHPHPPQ -> MVAGLTLGKGPESPDGDVSVPE
FT RKDEVAGGGGEEEEAEERGR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14976552, ECO:0000303|Ref.5"
FT /id="VSP_008158"
FT VAR_SEQ 344..778
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:19648910"
FT /id="VSP_041742"
FT VARIANT 303
FT /note="R -> W (in a gastric adenocarcinoma sample; somatic
FT mutation; dbSNP:rs144130246)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040394"
FT VARIANT 319
FT /note="V -> I (in a lung large cell carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040395"
FT VARIANT 391
FT /note="G -> E (in a metastatic melanoma sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040396"
FT VARIANT 531
FT /note="T -> N (in dbSNP:rs55892637)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040397"
FT VARIANT 749
FT /note="G -> S (in dbSNP:rs12978445)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040398"
FT VARIANT 764
FT /note="P -> A (in dbSNP:rs55796422)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040399"
FT MUTAGEN 59
FT /note="K->A: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:15150265"
FT MUTAGEN 189
FT /note="T->A: Prevents phosphorylation and activation by
FT STK11/LKB1 complex."
FT /evidence="ECO:0000269|PubMed:14976552"
FT MUTAGEN 327
FT /note="G->A: Abolishes activation of kinase activity."
FT /evidence="ECO:0000269|PubMed:18339622"
FT CONFLICT 762
FT /note="G -> A (in Ref. 9; AAH16681)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 778 AA; 85087 MW; 8D1818D4E54398BB CRC64;
MSSGAKEGGG GSPAYHLPHP HPHPPQHAQY VGPYRLEKTL GKGQTGLVKL GVHCITGQKV
AIKIVNREKL SESVLMKVER EIAILKLIEH PHVLKLHDVY ENKKYLYLVL EHVSGGELFD
YLVKKGRLTP KEARKFFRQI VSALDFCHSY SICHRDLKPE NLLLDEKNNI RIADFGMASL
QVGDSLLETS CGSPHYACPE VIKGEKYDGR RADMWSCGVI LFALLVGALP FDDDNLRQLL
EKVKRGVFHM PHFIPPDCQS LLRGMIEVEP EKRLSLEQIQ KHPWYLGGKH EPDPCLEPAP
GRRVAMRSLP SNGELDPDVL ESMASLGCFR DRERLHRELR SEEENQEKMI YYLLLDRKER
YPSCEDQDLP PRNDVDPPRK RVDSPMLSRH GKRRPERKSM EVLSITDAGG GGSPVPTRRA
LEMAQHSQRS RSVSGASTGL SSSPLSSPRS PVFSFSPEPG AGDEARGGGS PTSKTQTLPS
RGPRGGGAGE QPPPPSARST PLPGPPGSPR SSGGTPLHSP LHTPRASPTG TPGTTPPPSP
GGGVGGAAWR SRLNSIRNSF LGSPRFHRRK MQVPTAEEMS SLTPESSPEL AKRSWFGNFI
SLDKEEQIFL VLKDKPLSSI KADIVHAFLS IPSLSHSVLS QTSFRAEYKA SGGPSVFQKP
VRFQVDISSS EGPEPSPRRD GSGGGGIYSV TFTLISGPSR RFKRVVETIQ AQLLSTHDQP
SVQALADEKN GAQTRPAGAP PRSLQPPPGR PDPELSSSPR RGPPKDKKLL ATNGTPLP
