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Q8IWQ3

- BRSK2_HUMAN

UniProt

Q8IWQ3 - BRSK2_HUMAN

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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

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

Mg2+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
Complete GO annotation...

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-KW
Complete GO annotation...

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 LKB12 Publications
Modified residuei260 – 2601Phosphothreonine; by PKA1 Publication
Modified residuei367 – 3671Phosphoserine1 Publication
Modified residuei382 – 3821Phosphoserine2 Publications
Modified residuei393 – 3931Phosphoserine2 Publications
Modified residuei412 – 4121Phosphoserine1 Publication
Modified residuei422 – 4221Phosphothreonine1 Publication
Modified residuei509 – 5091Phosphothreonine1 Publication

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

BgeeiQ8IWQ3.
CleanExiHS_BRSK2.
ExpressionAtlasiQ8IWQ3. baseline and differential.
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.
GeneTreeiENSGT00760000119244.
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.
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

        10         20         30         40         50
MTSTGKDGGA QHAQYVGPYR LEKTLGKGQT GLVKLGVHCV TCQKVAIKIV
60 70 80 90 100
NREKLSESVL MKVEREIAIL KLIEHPHVLK LHDVYENKKY LYLVLEHVSG
110 120 130 140 150
GELFDYLVKK GRLTPKEARK FFRQIISALD FCHSHSICHR DLKPENLLLD
160 170 180 190 200
EKNNIRIADF GMASLQVGDS LLETSCGSPH YACPEVIRGE KYDGRKADVW
210 220 230 240 250
SCGVILFALL VGALPFDDDN LRQLLEKVKR GVFHMPHFIP PDCQSLLRGM
260 270 280 290 300
IEVDAARRLT LEHIQKHIWY IGGKNEPEPE QPIPRKVQIR SLPSLEDIDP
310 320 330 340 350
DVLDSMHSLG CFRDRNKLLQ DLLSEEENQE KMIYFLLLDR KERYPSQEDE
360 370 380 390 400
DLPPRNEIDP PRKRVDSPML NRHGKRRPER KSMEVLSVTD GGSPVPARRA
410 420 430 440 450
IEMAQHGQRS RSISGASSGL STSPLSSPRV TPHPSPRGSP LPTPKGTPVH
460 470 480 490 500
TPKESPAGTP NPTPPSSPSV GGVPWRARLN SIKNSFLGSP RFHRRKLQVP
510 520 530 540 550
TPEEMSNLTP ESSPELAKKS WFGNFISLEK EEQIFVVIKD KPLSSIKADI
560 570 580 590 600
VHAFLSIPSL SHSVISQTSF RAEYKATGGP AVFQKPVKFQ VDITYTEGGE
610 620 630 640 650
AQKENGIYSV TFTLLSGPSR RFKRVVETIQ AQLLSTHDPP AAQHLSDTTN
660 670 680 690 700
CMEMMTGRLS KCGSPLSNFF DVIKQLFSDE KNGQAAQAPS TPAKRSAHGP
710 720 730
LGDSAAAGPG PGGDAEYPTG KDTAKMGPPT ARREQP
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. Curated
The sequence AAD09654.1 differs from that shown. Reason: Erroneous termination at position 663. Translated as Gly.Curated
The sequence AAH24291.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

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:
EMBLi
GenBanki
DDBJi
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]
CCDS60696.1. [Q8IWQ3-6]
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_001269147.1. NM_001282218.1. [Q8IWQ3-6]
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]
ENST00000544817; ENSP00000445168; ENSG00000174672.
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:
EMBLi
GenBanki
DDBJi
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 ]
CCDS60696.1. [Q8IWQ3-6 ]
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_001269147.1. NM_001282218.1. [Q8IWQ3-6 ]
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 ]
ENST00000544817 ; ENSP00000445168 ; ENSG00000174672 .
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.
GeneTreei ENSGT00760000119244.
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

Bgeei Q8IWQ3.
CleanExi HS_BRSK2.
ExpressionAtlasi Q8IWQ3. baseline and differential.
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.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 128 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