Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q8IWQ3

- BRSK2_HUMAN

UniProt

Q8IWQ3 - BRSK2_HUMAN

Protein

Serine/threonine-protein kinase BRSK2

Gene

BRSK2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 3 (17 Oct 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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-529' and 'Ser-579'. Also regulates neuron polarization by mediating phosphorylation of WEE1 at 'Ser-642' in postmitotic 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-174 can inhibit insulin secretion (PubMed:22798068), BRSK2 phosphorylated at Thr-260 can promote insulin secretion (PubMed:22669945). Regulates reorganization of the actin cytoskeleton. May play a role in the apoptotic response triggered by endoplasmatic reticulum (ER) stress.6 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.
    ATP + [tau protein] = ADP + [tau protein] phosphate.

    Cofactori

    Magnesium.By similarity

    Enzyme regulationi

    Activated by phosphorylation on Thr-174 by STK11/LKB1.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei48 – 481ATPPROSITE-ProRule annotation
    Active sitei141 – 1411Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi25 – 339ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. magnesium ion binding Source: UniProtKB
    3. protein serine/threonine kinase activity Source: UniProtKB
    4. tau-protein kinase activity Source: UniProtKB

    GO - Biological processi

    1. actin cytoskeleton reorganization Source: UniProtKB
    2. axonogenesis Source: UniProtKB
    3. establishment of cell polarity Source: UniProtKB
    4. exocytosis Source: UniProtKB-KW
    5. G2/M transition of mitotic cell cycle Source: UniProtKB
    6. intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: UniProtKB
    7. mitotic nuclear division Source: UniProtKB-KW
    8. neuron differentiation Source: UniProtKB
    9. peptidyl-serine phosphorylation Source: Ensembl
    10. protein phosphorylation Source: UniProtKB
    11. regulation of insulin secretion involved in cellular response to glucose stimulus Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Apoptosis, Cell cycle, Cell division, Exocytosis, Mitosis, Neurogenesis

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    SignaLinkiQ8IWQ3.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase BRSK2 (EC:2.7.11.1)
    Alternative name(s):
    Brain-selective kinase 2 (EC:2.7.11.26)
    Brain-specific serine/threonine-protein kinase 2
    Short name:
    BR serine/threonine-protein kinase 2
    Serine/threonine-protein kinase 29
    Serine/threonine-protein kinase SAD-A
    Gene namesi
    Name:BRSK2
    Synonyms:C11orf7, PEN11B, SADA, STK29
    ORF Names:HUSSY-12
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:11405. BRSK2.

    Subcellular locationi

    Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmperinuclear region. Endoplasmic reticulum
    Note: Detected at centrosomes during mitosis. Localizes to the endoplasmic reticulum in response to stress caused by tunicamycin.

    GO - Cellular componenti

    1. centrosome Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. endoplasmic reticulum Source: UniProtKB-SubCell
    4. perinuclear region of cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Endoplasmic reticulum

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi48 – 481K → M: Loss of catalytic activity. Causes disintegration of actin stress fibers. 2 Publications
    Mutagenesisi174 – 1741T → A: Prevents phosphorylation and activation by STK11/LKB1 complex. 3 Publications
    Mutagenesisi174 – 1741T → E: Constitutively activated. 3 Publications
    Mutagenesisi260 – 2601T → A: Decreased phosphorylation. Nearly abolishes stimulation of insulin secretion. 2 Publications
    Mutagenesisi310 – 3101G → A: Decreased activation of kinase activity. 1 Publication
    Mutagenesisi443 – 4431T → A: Constitutively activated. Promotes formation of actin stress fibers. 1 Publication

    Organism-specific databases

    PharmGKBiPA36212.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 736736Serine/threonine-protein kinase BRSK2PRO_0000085670Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei174 – 1741Phosphothreonine; by LKB13 Publications
    Modified residuei260 – 2601Phosphothreonine; by PKA2 Publications
    Modified residuei367 – 3671Phosphoserine2 Publications
    Modified residuei382 – 3821Phosphoserine3 Publications
    Modified residuei393 – 3931Phosphoserine3 Publications
    Modified residuei412 – 4121Phosphoserine2 Publications
    Modified residuei422 – 4221Phosphothreonine1 Publication
    Modified residuei509 – 5091Phosphothreonine2 Publications

    Post-translational modificationi

    Phosphorylated at Thr-174 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Not phosphorylated at Thr-174 by CaMKK2. In contrast, it is phosphorylated and activated by CaMKK1. May be inactivated via dephosphorylation of Thr-174 by PP2C. Phosphorylated at Thr-260 by PKA. Phosphorylation at Thr-260 by PKA was not observed in another study (PubMed:18339622), but this may reflect differences in the experimental approach. Phosphorylation at Thr-260 seems to play a role in the regulation of insulin secretion (PubMed:22669945).7 Publications
    Polyubiquitinated by the APC complex in conjunction with FZR1, leading to its proteasomal degradation. Targeted for proteasomal degradation by interaction with COPS5. BRSK2 levels change during the cell cycle. BRSK2 levels are low at the G1/S boundary and gradually increase as cells progress into G2 phase. BRSK2 levels decrease rapidly at the end of mitosis.2 Publications

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ8IWQ3.
    PaxDbiQ8IWQ3.
    PRIDEiQ8IWQ3.

    PTM databases

    PhosphoSiteiQ8IWQ3.

    Expressioni

    Tissue specificityi

    Detected in pancreas islets (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiQ8IWQ3.
    BgeeiQ8IWQ3.
    CleanExiHS_BRSK2.
    GenevestigatoriQ8IWQ3.

    Interactioni

    Subunit structurei

    Interacts with FZR1, a regulatory subunit of the APC ubiquitin ligase complex. Interacts with COPS5. Interacts with PAK1.3 Publications

    Protein-protein interaction databases

    BioGridi114491. 9 interactions.
    IntActiQ8IWQ3. 1 interaction.
    STRINGi9606.ENSP00000310697.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8IWQ3.
    SMRiQ8IWQ3. Positions 15-338.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini19 – 270252Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini297 – 33943UBAAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi603 – 6053KEN box

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi424 – 46845Pro-richAdd
    BLAST

    Domaini

    The KEN box motif is required for interaction with FZR1/CDH1 and essential for APC(CDH1)-mediated ubiquitination.1 Publication

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 1 UBA domain.Curated

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000246447.
    HOVERGENiHBG007240.
    InParanoidiQ8IWQ3.
    KOiK08796.
    OMAiLELPMSQ.
    OrthoDBiEOG7XSTDH.
    PhylomeDBiQ8IWQ3.
    TreeFamiTF313967.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 2 hits.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8IWQ3-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MTSTGKDGGA QHAQYVGPYR LEKTLGKGQT GLVKLGVHCV TCQKVAIKIV    50
    NREKLSESVL MKVEREIAIL KLIEHPHVLK LHDVYENKKY LYLVLEHVSG 100
    GELFDYLVKK GRLTPKEARK FFRQIISALD FCHSHSICHR DLKPENLLLD 150
    EKNNIRIADF GMASLQVGDS LLETSCGSPH YACPEVIRGE KYDGRKADVW 200
    SCGVILFALL VGALPFDDDN LRQLLEKVKR GVFHMPHFIP PDCQSLLRGM 250
    IEVDAARRLT LEHIQKHIWY IGGKNEPEPE QPIPRKVQIR SLPSLEDIDP 300
    DVLDSMHSLG CFRDRNKLLQ DLLSEEENQE KMIYFLLLDR KERYPSQEDE 350
    DLPPRNEIDP PRKRVDSPML NRHGKRRPER KSMEVLSVTD GGSPVPARRA 400
    IEMAQHGQRS RSISGASSGL STSPLSSPRV TPHPSPRGSP LPTPKGTPVH 450
    TPKESPAGTP NPTPPSSPSV GGVPWRARLN SIKNSFLGSP RFHRRKLQVP 500
    TPEEMSNLTP ESSPELAKKS WFGNFISLEK EEQIFVVIKD KPLSSIKADI 550
    VHAFLSIPSL SHSVISQTSF RAEYKATGGP AVFQKPVKFQ VDITYTEGGE 600
    AQKENGIYSV TFTLLSGPSR RFKRVVETIQ AQLLSTHDPP AAQHLSDTTN 650
    CMEMMTGRLS KCGSPLSNFF DVIKQLFSDE KNGQAAQAPS TPAKRSAHGP 700
    LGDSAAAGPG PGGDAEYPTG KDTAKMGPPT ARREQP 736
    Length:736
    Mass (Da):81,633
    Last modified:October 17, 2006 - v3
    Checksum:iD9EBA511149449E6
    GO
    Isoform 2 (identifier: Q8IWQ3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         647-674: DTTNCMEMMTGRLSKCGSPLSNFFDVIK → EPPPPAPGLSWGAGLKGQKVATSYESSL
         675-736: Missing.

    Show »
    Length:674
    Mass (Da):75,149
    Checksum:iE7E6704028A00876
    GO
    Isoform 3 (identifier: Q8IWQ3-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         664-668: SPLSN → IIPKS
         669-736: Missing.

    Show »
    Length:668
    Mass (Da):74,741
    Checksum:i2E3BE2942B8BD79B
    GO
    Isoform 4 (identifier: Q8IWQ3-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         408-408: Q → QSKAMFSKSLDIAEAHPQFSKED
         647-674: DTTNCMEMMTGRLSKCGSPLSNFFDVIK → EPPPPAPGLSWGAGLKGQKVATSYESSL
         675-736: Missing.

    Note: Contains a phosphoserine at position 416.

    Show »
    Length:696
    Mass (Da):77,598
    Checksum:i857FBFE1ED9B3672
    GO
    Isoform 5 (identifier: Q8IWQ3-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-30: MTSTGKDGGAQHAQYVGPYRLEKTLGKGQT → MSPEGHPSRW...TWLCLQPSPA
         663-678: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:766
    Mass (Da):84,832
    Checksum:iB0E5187AF729E947
    GO
    Isoform 6 (identifier: Q8IWQ3-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-60: Missing.
         647-674: DTTNCMEMMTGRLSKCGSPLSNFFDVIK → EPPPPAPGLSWGAGLKGQKVATSYESSL
         675-736: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:614
    Mass (Da):68,740
    Checksum:iA2CBD024EB3321B9
    GO

    Sequence cautioni

    The sequence AAD09654.1 differs from that shown. Reason: Frameshift at position 640.
    The sequence AAH24291.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAD09654.1 differs from that shown. Reason: Erroneous termination at position 663. Translated as Gly.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti251 – 2511I → S in AAP97723. 1 PublicationCurated
    Sequence conflicti251 – 2511I → S in AAP97724. 1 PublicationCurated
    Sequence conflicti251 – 2511I → S in AAP97725. 1 PublicationCurated
    Sequence conflicti251 – 2511I → S in AAP97726. 1 PublicationCurated
    Sequence conflicti251 – 2511I → S in AAP97727. 1 PublicationCurated
    Sequence conflicti251 – 2511I → S in AAN87839. 1 PublicationCurated
    Sequence conflicti251 – 2511I → S in CAA07196. (PubMed:11124703)Curated
    Sequence conflicti409 – 4091R → G in BAG53761. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6060Missing in isoform 6. CuratedVSP_055679Add
    BLAST
    Alternative sequencei1 – 3030MTSTG…GKGQT → MSPEGHPSRWARPRRPCICP SSLCSPREPRSGPAVGRGGA AHHRVPAGHTPGPQLLQPHL HLPQGQTWLCLQPSPA in isoform 5. CuratedVSP_022603Add
    BLAST
    Alternative sequencei408 – 4081Q → QSKAMFSKSLDIAEAHPQFS KED in isoform 4. 1 PublicationVSP_013945
    Alternative sequencei647 – 67428DTTNC…FDVIK → EPPPPAPGLSWGAGLKGQKV ATSYESSL in isoform 2, isoform 4 and isoform 6. 4 PublicationsVSP_008154Add
    BLAST
    Alternative sequencei663 – 67816Missing in isoform 5. CuratedVSP_022604Add
    BLAST
    Alternative sequencei664 – 6685SPLSN → IIPKS in isoform 3. 2 PublicationsVSP_008156
    Alternative sequencei669 – 73668Missing in isoform 3. 2 PublicationsVSP_008157Add
    BLAST
    Alternative sequencei675 – 73662Missing in isoform 2, isoform 4 and isoform 6. 4 PublicationsVSP_008155Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY505125 mRNA. Translation: AAS86443.1.
    AF533876 mRNA. Translation: AAP97723.1.
    AF533877 mRNA. Translation: AAP97724.1.
    AF533878 mRNA. Translation: AAP97725.1.
    AF533879 mRNA. Translation: AAP97726.1.
    AF533880 mRNA. Translation: AAP97727.1.
    AY166857 mRNA. Translation: AAN87839.1.
    AK122851 mRNA. Translation: BAG53761.1.
    AK131534 mRNA. Translation: BAD18671.1.
    AC091196 Genomic DNA. No translation available.
    AC136297 Genomic DNA. No translation available.
    AJ006701 mRNA. Translation: CAA07196.1.
    BC024291 mRNA. Translation: AAH24291.1. Different initiation.
    AF020089 mRNA. Translation: AAD09654.1. Sequence problems.
    CCDSiCCDS41590.1. [Q8IWQ3-3]
    CCDS58106.1. [Q8IWQ3-2]
    CCDS58107.1. [Q8IWQ3-1]
    CCDS58108.1. [Q8IWQ3-5]
    RefSeqiNP_001243556.1. NM_001256627.1. [Q8IWQ3-1]
    NP_001243558.1. NM_001256629.1. [Q8IWQ3-2]
    NP_001243559.1. NM_001256630.1. [Q8IWQ3-5]
    NP_003948.2. NM_003957.3. [Q8IWQ3-3]
    UniGeneiHs.170819.

    Genome annotation databases

    EnsembliENST00000308219; ENSP00000310697; ENSG00000174672. [Q8IWQ3-3]
    ENST00000382179; ENSP00000371614; ENSG00000174672. [Q8IWQ3-5]
    ENST00000526678; ENSP00000433370; ENSG00000174672. [Q8IWQ3-4]
    ENST00000528710; ENSP00000433235; ENSG00000174672. [Q8IWQ3-6]
    ENST00000528841; ENSP00000432000; ENSG00000174672. [Q8IWQ3-1]
    ENST00000529433; ENSP00000433684; ENSG00000174672. [Q8IWQ3-2]
    ENST00000531197; ENSP00000431152; ENSG00000174672. [Q8IWQ3-2]
    GeneIDi9024.
    KEGGihsa:9024.
    UCSCiuc001lth.1. human. [Q8IWQ3-2]
    uc001lti.4. human. [Q8IWQ3-1]
    uc001ltj.4. human. [Q8IWQ3-3]
    uc001ltm.4. human. [Q8IWQ3-5]
    uc009ycv.1. human. [Q8IWQ3-4]

    Polymorphism databases

    DMDMi116241272.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY505125 mRNA. Translation: AAS86443.1 .
    AF533876 mRNA. Translation: AAP97723.1 .
    AF533877 mRNA. Translation: AAP97724.1 .
    AF533878 mRNA. Translation: AAP97725.1 .
    AF533879 mRNA. Translation: AAP97726.1 .
    AF533880 mRNA. Translation: AAP97727.1 .
    AY166857 mRNA. Translation: AAN87839.1 .
    AK122851 mRNA. Translation: BAG53761.1 .
    AK131534 mRNA. Translation: BAD18671.1 .
    AC091196 Genomic DNA. No translation available.
    AC136297 Genomic DNA. No translation available.
    AJ006701 mRNA. Translation: CAA07196.1 .
    BC024291 mRNA. Translation: AAH24291.1 . Different initiation.
    AF020089 mRNA. Translation: AAD09654.1 . Sequence problems.
    CCDSi CCDS41590.1. [Q8IWQ3-3 ]
    CCDS58106.1. [Q8IWQ3-2 ]
    CCDS58107.1. [Q8IWQ3-1 ]
    CCDS58108.1. [Q8IWQ3-5 ]
    RefSeqi NP_001243556.1. NM_001256627.1. [Q8IWQ3-1 ]
    NP_001243558.1. NM_001256629.1. [Q8IWQ3-2 ]
    NP_001243559.1. NM_001256630.1. [Q8IWQ3-5 ]
    NP_003948.2. NM_003957.3. [Q8IWQ3-3 ]
    UniGenei Hs.170819.

    3D structure databases

    ProteinModelPortali Q8IWQ3.
    SMRi Q8IWQ3. Positions 15-338.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114491. 9 interactions.
    IntActi Q8IWQ3. 1 interaction.
    STRINGi 9606.ENSP00000310697.

    Chemistry

    BindingDBi Q8IWQ3.
    ChEMBLi CHEMBL4574.
    GuidetoPHARMACOLOGYi 1947.

    PTM databases

    PhosphoSitei Q8IWQ3.

    Polymorphism databases

    DMDMi 116241272.

    Proteomic databases

    MaxQBi Q8IWQ3.
    PaxDbi Q8IWQ3.
    PRIDEi Q8IWQ3.

    Protocols and materials databases

    DNASUi 9024.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000308219 ; ENSP00000310697 ; ENSG00000174672 . [Q8IWQ3-3 ]
    ENST00000382179 ; ENSP00000371614 ; ENSG00000174672 . [Q8IWQ3-5 ]
    ENST00000526678 ; ENSP00000433370 ; ENSG00000174672 . [Q8IWQ3-4 ]
    ENST00000528710 ; ENSP00000433235 ; ENSG00000174672 . [Q8IWQ3-6 ]
    ENST00000528841 ; ENSP00000432000 ; ENSG00000174672 . [Q8IWQ3-1 ]
    ENST00000529433 ; ENSP00000433684 ; ENSG00000174672 . [Q8IWQ3-2 ]
    ENST00000531197 ; ENSP00000431152 ; ENSG00000174672 . [Q8IWQ3-2 ]
    GeneIDi 9024.
    KEGGi hsa:9024.
    UCSCi uc001lth.1. human. [Q8IWQ3-2 ]
    uc001lti.4. human. [Q8IWQ3-1 ]
    uc001ltj.4. human. [Q8IWQ3-3 ]
    uc001ltm.4. human. [Q8IWQ3-5 ]
    uc009ycv.1. human. [Q8IWQ3-4 ]

    Organism-specific databases

    CTDi 9024.
    GeneCardsi GC11P001368.
    H-InvDB HIX0009361.
    HGNCi HGNC:11405. BRSK2.
    MIMi 609236. gene.
    neXtProti NX_Q8IWQ3.
    PharmGKBi PA36212.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000246447.
    HOVERGENi HBG007240.
    InParanoidi Q8IWQ3.
    KOi K08796.
    OMAi LELPMSQ.
    OrthoDBi EOG7XSTDH.
    PhylomeDBi Q8IWQ3.
    TreeFami TF313967.

    Enzyme and pathway databases

    SignaLinki Q8IWQ3.

    Miscellaneous databases

    GeneWikii BRSK2.
    GenomeRNAii 9024.
    NextBioi 33809.
    PROi Q8IWQ3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8IWQ3.
    Bgeei Q8IWQ3.
    CleanExi HS_BRSK2.
    Genevestigatori Q8IWQ3.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 2 hits.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "SAD: a presynaptic kinase associated with synaptic vesicles and the active zone cytomatrix that regulates neurotransmitter release."
      Inoue E., Mochida S., Takagi H., Higa S., Deguchi-Tawarada M., Takao-Rikitsu E., Inoue M., Yao I., Takeuchi K., Kitajima I., Setou M., Ohtsuka T., Takai Y.
      Neuron 50:261-275(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
    2. Guo J.H., Yu L.
      Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
      Tissue: Brain.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORS 5 AND 6).
      Tissue: Amygdala.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Characterization of 16 novel human genes showing high similarity to yeast sequences."
      Stanchi F., Bertocco E., Toppo S., Dioguardi R., Simionati B., Cannata N., Zimbello R., Lanfranchi G., Valle G.
      Yeast 18:69-80(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 72-736 (ISOFORM 2).
      Tissue: Brain.
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 454-736 (ISOFORM 2).
      Tissue: Eye.
    7. "Repeat-directed isolation of a novel gene preferentially expressed from the maternal allele in human placenta."
      Miura K., Miyoshi O., Yun K., Inazawa J., Miyamoto T., Hayashi H., Masuzaki H., Yoshimura S., Niikawa N., Jinno Y., Ishimaru T.
      J. Hum. Genet. 44:1-9(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 463-736 (ISOFORM 3).
    8. "LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, 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) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT THR-174, MUTAGENESIS OF THR-174.
    9. "BRSK2 is activated by cyclic AMP-dependent protein kinase A through phosphorylation at Thr260."
      Guo Z., Tang W., Yuan J., Chen X., Wan B., Gu X., Luo K., Wang Y., Yu L.
      Biochem. Biophys. Res. Commun. 347:867-871(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-260, MUTAGENESIS OF THR-260.
    10. "Investigating the regulation of brain-specific kinases 1 and 2 by phosphorylation."
      Bright N.J., Carling D., Thornton C.
      J. Biol. Chem. 283:14946-14954(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-174, MUTAGENESIS OF THR-174 AND GLY-310.
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367; SER-382 AND SER-393, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416 (ISOFORM 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-382; SER-393; SER-412 AND THR-509, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "Calmodulin-dependent protein kinase kinase-beta activates AMPK without forming a stable complex: synergistic effects of Ca2+ and AMP."
      Fogarty S., Hawley S.A., Green K.A., Saner N., Mustard K.J., Hardie D.G.
      Biochem. J. 426:109-118(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    15. "Persistence of the cell-cycle checkpoint kinase Wee1 in SadA- and SadB-deficient neurons disrupts neuronal polarity."
      Muller M., Lutter D., Puschel A.W.
      J. Cell Sci. 123:286-294(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. "Jab1 interacts with brain-specific kinase 2 (BRSK2) and promotes its degradation in the ubiquitin-proteasome pathway."
      Zhou J., Wan B., Li R., Gu X., Zhong Z., Wang Y., Yu L.
      Biochem. Biophys. Res. Commun. 422:647-652(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH COPS5, SUBCELLULAR LOCATION, UBIQUITINATION.
    17. "BRSK2 is regulated by ER stress in protein level and involved in ER stress-induced apoptosis."
      Wang Y., Wan B., Li D., Zhou J., Li R., Bai M., Chen F., Yu L.
      Biochem. Biophys. Res. Commun. 423:813-818(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    18. "Synapses of amphids defective (SAD-A) kinase promotes glucose-stimulated insulin secretion through activation of p21-activated kinase (PAK1) in pancreatic beta-Cells."
      Nie J., Sun C., Faruque O., Ye G., Li J., Liang Q., Chang Z., Yang W., Han X., Shi Y.
      J. Biol. Chem. 287:26435-26444(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PAK1, MUTAGENESIS OF LYS-48; THR-260 AND THR-443.
    19. "Brain-selective kinase 2 (BRSK2) phosphorylation on PCTAIRE1 negatively regulates glucose-stimulated insulin secretion in pancreatic beta-cells."
      Chen X.Y., Gu X.T., Saiyin H., Wan B., Zhang Y.J., Li J., Wang Y.L., Gao R., Wang Y.F., Dong W.P., Najjar S.M., Zhang C.Y., Ding H.F., Liu J.O., Yu L.
      J. Biol. Chem. 287:30368-30375(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-48 AND THR-174.
    20. "Phosphorylation of microtubule-associated protein tau by AMPK-related kinases."
      Yoshida H., Goedert M.
      J. Neurochem. 120:165-176(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, FUNCTION IN MAPT PHOSPHORYLATION.
    21. "APC/C(Cdh1) targets brain-specific kinase 2 (BRSK2) for degradation via the ubiquitin-proteasome pathway."
      Li R., Wan B., Zhou J., Wang Y., Luo T., Gu X., Chen F., Yu L.
      PLoS ONE 7:E45932-E45932(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, UBIQUITINATION, INTERACTION WITH FZR1, DOMAIN KEN BOX MOTIF.

    Entry informationi

    Entry nameiBRSK2_HUMAN
    AccessioniPrimary (citable) accession number: Q8IWQ3
    Secondary accession number(s): B3KVE9
    , E9PLM7, O60843, O95099, Q5J5B4, Q6ZMQ4, Q8TB60
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 29, 2003
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 126 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3