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Q8IWQ3 (BRSK2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:BRSK2
Synonyms:C11orf7, PEN11B, SADA, STK29
ORF Names:HUSSY-12
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length736 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 post-mitotic 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 (Ref.19), BRSK2 phosphorylated at Thr-260 can promote insulin secretion (Ref.18). Regulates reorganization of the actin cytoskeleton. May play a role in the apoptotic response triggered by endoplasmatic reticulum (ER) stress. Ref.8 Ref.15 Ref.18 Ref.19 Ref.20 Ref.21

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.19 Ref.20

ATP + [tau protein] = ADP + [tau protein] phosphate. Ref.19 Ref.20

Cofactor

Magnesium By similarity.

Enzyme regulation

Activated by phosphorylation on Thr-174 by STK11/LKB1. Ref.8

Subunit structure

Interacts with FZR1, a regulatory subunit of the APC ubiquitin ligase complex. Interacts with COPS5. Interacts with PAK1. Ref.16 Ref.18 Ref.21

Subcellular location

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. Ref.16 Ref.17 Ref.21

Tissue specificity

Detected in pancreas islets (at protein level). Ref.19

Domain

The KEN box motif is required for interaction with FZR1/CDH1 and essential for APC(CDH1)-mediated ubiquitination. Ref.21

Post-translational modification

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 (Ref.10), but this may reflect differences in the experimental approach. Phosphorylation at Thr-260 seems to play a role in the regulation of insulin secretion (Ref.18). Ref.8 Ref.9 Ref.10 Ref.14

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.

Sequence similarities

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily.

Contains 1 protein kinase domain.

Contains 1 UBA domain.

Sequence caution

The sequence AAD09654.1 differs from that shown. Reason: Erroneous termination at position 663. Translated as Gly.

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.

Ontologies

Keywords
   Biological processApoptosis
Cell cycle
Cell division
Exocytosis
Mitosis
Neurogenesis
   Cellular componentCytoplasm
Cytoskeleton
Endoplasmic reticulum
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Inferred from mutant phenotype Ref.21. Source: UniProtKB

actin cytoskeleton reorganization

Inferred from mutant phenotype Ref.18. Source: UniProtKB

axonogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

establishment of cell polarity

Inferred from sequence or structural similarity. Source: UniProtKB

exocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress

Inferred from mutant phenotype Ref.17. Source: UniProtKB

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

peptidyl-serine phosphorylation

Inferred from electronic annotation. Source: Ensembl

regulation of insulin secretion involved in cellular response to glucose stimulus

Inferred from mutant phenotype Ref.18. Source: UniProtKB

   Cellular_componentcentrosome

Inferred from direct assay Ref.21. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.17. Source: UniProtKB

endoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from direct assay Ref.8. Source: UniProtKB

magnesium ion binding

Inferred from direct assay Ref.8. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from direct assay Ref.8. Source: UniProtKB

tau-protein kinase activity

Inferred from direct assay Ref.20. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8IWQ3-1)

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.
Isoform 2 (identifier: Q8IWQ3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     647-674: DTTNCMEMMTGRLSKCGSPLSNFFDVIK → EPPPPAPGLSWGAGLKGQKVATSYESSL
     675-736: Missing.
Isoform 3 (identifier: Q8IWQ3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     664-668: SPLSN → IIPKS
     669-736: Missing.
Isoform 4 (identifier: Q8IWQ3-4)

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.
Isoform 5 (identifier: Q8IWQ3-5)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 736736Serine/threonine-protein kinase BRSK2
PRO_0000085670

Regions

Domain19 – 270252Protein kinase
Domain297 – 33943UBA
Nucleotide binding25 – 339ATP By similarity
Motif603 – 6053KEN box
Compositional bias424 – 46845Pro-rich

Sites

Active site1411Proton acceptor By similarity
Binding site481ATP By similarity

Amino acid modifications

Modified residue1741Phosphothreonine; by LKB1 Ref.8 Ref.10
Modified residue2601Phosphothreonine; by PKA Ref.9
Modified residue3671Phosphoserine Ref.12
Modified residue3821Phosphoserine Ref.12 Ref.13
Modified residue3931Phosphoserine Ref.12 Ref.13
Modified residue4121Phosphoserine Ref.13
Modified residue4221Phosphothreonine
Modified residue5091Phosphothreonine Ref.13

Natural variations

Alternative sequence1 – 3030MTSTG…GKGQT → MSPEGHPSRWARPRRPCICP SSLCSPREPRSGPAVGRGGA AHHRVPAGHTPGPQLLQPHL HLPQGQTWLCLQPSPA in isoform 5.
VSP_022603
Alternative sequence4081Q → QSKAMFSKSLDIAEAHPQFS KED in isoform 4.
VSP_013945
Alternative sequence647 – 67428DTTNC…FDVIK → EPPPPAPGLSWGAGLKGQKV ATSYESSL in isoform 2 and isoform 4.
VSP_008154
Alternative sequence663 – 67816Missing in isoform 5.
VSP_022604
Alternative sequence664 – 6685SPLSN → IIPKS in isoform 3.
VSP_008156
Alternative sequence669 – 73668Missing in isoform 3.
VSP_008157
Alternative sequence675 – 73662Missing in isoform 2 and isoform 4.
VSP_008155

Experimental info

Mutagenesis481K → M: Loss of catalytic activity. Causes disintegration of actin stress fibers. Ref.18 Ref.19
Mutagenesis1741T → A: Prevents phosphorylation and activation by STK11/LKB1 complex. Ref.8 Ref.10 Ref.19
Mutagenesis1741T → E: Constitutively activated. Ref.8 Ref.10 Ref.19
Mutagenesis2601T → A: Decreased phosphorylation. Nearly abolishes stimulation of insulin secretion. Ref.9 Ref.18
Mutagenesis3101G → A: Decreased activation of kinase activity. Ref.10
Mutagenesis4431T → A: Constitutively activated. Promotes formation of actin stress fibers. Ref.18
Sequence conflict2511I → S in AAP97723. Ref.2
Sequence conflict2511I → S in AAP97724. Ref.2
Sequence conflict2511I → S in AAP97725. Ref.2
Sequence conflict2511I → S in AAP97726. Ref.2
Sequence conflict2511I → S in AAP97727. Ref.2
Sequence conflict2511I → S in AAN87839. Ref.2
Sequence conflict2511I → S in CAA07196. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 17, 2006. Version 3.
Checksum: D9EBA511149449E6

FASTA73681,633
        10         20         30         40         50         60 
MTSTGKDGGA QHAQYVGPYR LEKTLGKGQT GLVKLGVHCV TCQKVAIKIV NREKLSESVL 

        70         80         90        100        110        120 
MKVEREIAIL KLIEHPHVLK LHDVYENKKY LYLVLEHVSG GELFDYLVKK GRLTPKEARK 

       130        140        150        160        170        180 
FFRQIISALD FCHSHSICHR DLKPENLLLD EKNNIRIADF GMASLQVGDS LLETSCGSPH 

       190        200        210        220        230        240 
YACPEVIRGE KYDGRKADVW SCGVILFALL VGALPFDDDN LRQLLEKVKR GVFHMPHFIP 

       250        260        270        280        290        300 
PDCQSLLRGM IEVDAARRLT LEHIQKHIWY IGGKNEPEPE QPIPRKVQIR SLPSLEDIDP 

       310        320        330        340        350        360 
DVLDSMHSLG CFRDRNKLLQ DLLSEEENQE KMIYFLLLDR KERYPSQEDE DLPPRNEIDP 

       370        380        390        400        410        420 
PRKRVDSPML NRHGKRRPER KSMEVLSVTD GGSPVPARRA IEMAQHGQRS RSISGASSGL 

       430        440        450        460        470        480 
STSPLSSPRV TPHPSPRGSP LPTPKGTPVH TPKESPAGTP NPTPPSSPSV GGVPWRARLN 

       490        500        510        520        530        540 
SIKNSFLGSP RFHRRKLQVP TPEEMSNLTP ESSPELAKKS WFGNFISLEK EEQIFVVIKD 

       550        560        570        580        590        600 
KPLSSIKADI VHAFLSIPSL SHSVISQTSF RAEYKATGGP AVFQKPVKFQ VDITYTEGGE 

       610        620        630        640        650        660 
AQKENGIYSV TFTLLSGPSR RFKRVVETIQ AQLLSTHDPP AAQHLSDTTN CMEMMTGRLS 

       670        680        690        700        710        720 
KCGSPLSNFF DVIKQLFSDE KNGQAAQAPS TPAKRSAHGP LGDSAAAGPG PGGDAEYPTG 

       730 
KDTAKMGPPT ARREQP 

« Hide

Isoform 2 [UniParc].

Checksum: E7E6704028A00876
Show »

FASTA67475,149
Isoform 3 [UniParc].

Checksum: 2E3BE2942B8BD79B
Show »

FASTA66874,741
Isoform 4 [UniParc].

Checksum: 857FBFE1ED9B3672
Show »

FASTA69677,598
Isoform 5 [UniParc].

Checksum: B0E5187AF729E947
Show »

FASTA76684,832

References

« Hide 'large scale' references
[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. expand/collapse author list , 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] (ISOFORM 5).
Tissue: Amygdala.
[4]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
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]"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) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
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.
RefSeqNP_001243556.1. NM_001256627.1.
NP_001243558.1. NM_001256629.1.
NP_001243559.1. NM_001256630.1.
NP_003948.2. NM_003957.3.
UniGeneHs.170819.

3D structure databases

ProteinModelPortalQ8IWQ3.
SMRQ8IWQ3. Positions 15-338.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114491. 8 interactions.
IntActQ8IWQ3. 1 interaction.
STRING9606.ENSP00000310697.

Chemistry

BindingDBQ8IWQ3.
ChEMBLCHEMBL4574.
GuidetoPHARMACOLOGY1947.

PTM databases

PhosphoSiteQ8IWQ3.

Polymorphism databases

DMDM116241272.

Proteomic databases

PaxDbQ8IWQ3.
PRIDEQ8IWQ3.

Protocols and materials databases

DNASU9024.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000308219; ENSP00000310697; ENSG00000174672. [Q8IWQ3-3]
ENST00000308230; ENSP00000310805; ENSG00000174672. [Q8IWQ3-4]
ENST00000382179; ENSP00000371614; ENSG00000174672. [Q8IWQ3-5]
ENST00000526678; ENSP00000433370; ENSG00000174672. [Q8IWQ3-4]
ENST00000528841; ENSP00000432000; ENSG00000174672. [Q8IWQ3-1]
ENST00000529433; ENSP00000433684; ENSG00000174672. [Q8IWQ3-2]
ENST00000531197; ENSP00000431152; ENSG00000174672. [Q8IWQ3-2]
GeneID9024.
KEGGhsa:9024.
UCSCuc001lth.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

CTD9024.
GeneCardsGC11P001368.
H-InvDBHIX0009361.
HGNCHGNC:11405. BRSK2.
MIM609236. gene.
neXtProtNX_Q8IWQ3.
PharmGKBPA36212.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000246447.
HOVERGENHBG007240.
InParanoidQ8IWQ3.
KOK08796.
OMALELPMSQ.
OrthoDBEOG7XSTDH.
PhylomeDBQ8IWQ3.
TreeFamTF313967.

Enzyme and pathway databases

SignaLinkQ8IWQ3.

Gene expression databases

ArrayExpressQ8IWQ3.
BgeeQ8IWQ3.
CleanExHS_BRSK2.
GenevestigatorQ8IWQ3.

Family and domain databases

InterProIPR011009. 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]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 2 hits.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiBRSK2.
GenomeRNAi9024.
NextBio33809.
PROQ8IWQ3.
SOURCESearch...

Entry information

Entry nameBRSK2_HUMAN
AccessionPrimary (citable) accession number: Q8IWQ3
Secondary accession number(s): O60843 expand/collapse secondary AC list , O95099, Q5J5B4, Q6ZMQ4, Q8TB60
Entry history
Integrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: October 17, 2006
Last modified: March 19, 2014
This is version 120 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM