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Serine/threonine-protein kinase BRSK2 (EC 2.7.11.1) (Brain-selective kinase 2) (EC 2.7.11.26) (Brain-specific serine/threonine-protein kinase 2) (BR serine/threonine-protein kinase 2) (Serine/threonine-protein kinase 29) (Serine/threonine-protein kinase SAD-A)

 BRSK2_HUMAN             Reviewed;         736 AA.
Q8IWQ3; B3KVE9; E9PLM7; O60843; O95099; Q5J5B4; Q6ZMQ4; Q8TB60;
29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 3.
22-NOV-2017, entry version 158.
RecName: Full=Serine/threonine-protein kinase BRSK2;
EC=2.7.11.1;
AltName: Full=Brain-selective kinase 2;
EC=2.7.11.26;
AltName: Full=Brain-specific serine/threonine-protein kinase 2;
Short=BR serine/threonine-protein kinase 2;
AltName: Full=Serine/threonine-protein kinase 29;
AltName: Full=Serine/threonine-protein kinase SAD-A;
Name=BRSK2; Synonyms=C11orf7, PEN11B, SADA, STK29; ORFNames=HUSSY-12;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
PubMed=16630837; DOI=10.1016/j.neuron.2006.03.018;
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.;
"SAD: a presynaptic kinase associated with synaptic vesicles and the
active zone cytomatrix that regulates neurotransmitter release.";
Neuron 50:261-275(2006).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
TISSUE=Brain;
Guo J.H., Yu L.;
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORS 5 AND 6).
TISSUE=Amygdala;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
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., 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.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 72-736 (ISOFORM 2).
TISSUE=Brain;
PubMed=11124703;
DOI=10.1002/1097-0061(200101)18:1<69::AID-YEA647>3.0.CO;2-H;
Stanchi F., Bertocco E., Toppo S., Dioguardi R., Simionati B.,
Cannata N., Zimbello R., Lanfranchi G., Valle G.;
"Characterization of 16 novel human genes showing high similarity to
yeast sequences.";
Yeast 18:69-80(2001).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 454-736 (ISOFORM 2).
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 463-736 (ISOFORM 3).
PubMed=9929968; DOI=10.1007/s100380050096;
Miura K., Miyoshi O., Yun K., Inazawa J., Miyamoto T., Hayashi H.,
Masuzaki H., Yoshimura S., Niikawa N., Jinno Y., Ishimaru T.;
"Repeat-directed isolation of a novel gene preferentially expressed
from the maternal allele in human placenta.";
J. Hum. Genet. 44:1-9(1999).
[8]
FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT THR-174, AND
MUTAGENESIS OF THR-174.
PubMed=14976552; DOI=10.1038/sj.emboj.7600110;
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.;
"LKB1 is a master kinase that activates 13 kinases of the AMPK
subfamily, including MARK/PAR-1.";
EMBO J. 23:833-843(2004).
[9]
PHOSPHORYLATION AT THR-260, AND MUTAGENESIS OF THR-260.
PubMed=16870137; DOI=10.1016/j.bbrc.2006.06.178;
Guo Z., Tang W., Yuan J., Chen X., Wan B., Gu X., Luo K., Wang Y.,
Yu L.;
"BRSK2 is activated by cyclic AMP-dependent protein kinase A through
phosphorylation at Thr260.";
Biochem. Biophys. Res. Commun. 347:867-871(2006).
[10]
PHOSPHORYLATION AT THR-174, AND MUTAGENESIS OF THR-174 AND GLY-310.
PubMed=18339622; DOI=10.1074/jbc.M710381200;
Bright N.J., Carling D., Thornton C.;
"Investigating the regulation of brain-specific kinases 1 and 2 by
phosphorylation.";
J. Biol. Chem. 283:14946-14954(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367; SER-382 AND
SER-393, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416 (ISOFORM
4), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-382; SER-393; SER-412
AND THR-509, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[14]
PHOSPHORYLATION.
PubMed=19958286; DOI=10.1042/BJ20091372;
Fogarty S., Hawley S.A., Green K.A., Saner N., Mustard K.J.,
Hardie D.G.;
"Calmodulin-dependent protein kinase kinase-beta activates AMPK
without forming a stable complex: synergistic effects of Ca2+ and
AMP.";
Biochem. J. 426:109-118(2010).
[15]
FUNCTION.
PubMed=20026642; DOI=10.1242/jcs.058230;
Muller M., Lutter D., Puschel A.W.;
"Persistence of the cell-cycle checkpoint kinase Wee1 in SadA- and
SadB-deficient neurons disrupts neuronal polarity.";
J. Cell Sci. 123:286-294(2010).
[16]
INTERACTION WITH COPS5, SUBCELLULAR LOCATION, AND UBIQUITINATION.
PubMed=22609399; DOI=10.1016/j.bbrc.2012.05.045;
Zhou J., Wan B., Li R., Gu X., Zhong Z., Wang Y., Yu L.;
"Jab1 interacts with brain-specific kinase 2 (BRSK2) and promotes its
degradation in the ubiquitin-proteasome pathway.";
Biochem. Biophys. Res. Commun. 422:647-652(2012).
[17]
SUBCELLULAR LOCATION.
PubMed=22713462; DOI=10.1016/j.bbrc.2012.06.046;
Wang Y., Wan B., Li D., Zhou J., Li R., Bai M., Chen F., Yu L.;
"BRSK2 is regulated by ER stress in protein level and involved in ER
stress-induced apoptosis.";
Biochem. Biophys. Res. Commun. 423:813-818(2012).
[18]
FUNCTION, INTERACTION WITH PAK1, AND MUTAGENESIS OF LYS-48; THR-260
AND THR-443.
PubMed=22669945; DOI=10.1074/jbc.M112.378372;
Nie J., Sun C., Faruque O., Ye G., Li J., Liang Q., Chang Z., Yang W.,
Han X., Shi Y.;
"Synapses of amphids defective (SAD-A) kinase promotes glucose-
stimulated insulin secretion through activation of p21-activated
kinase (PAK1) in pancreatic beta-Cells.";
J. Biol. Chem. 287:26435-26444(2012).
[19]
FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND MUTAGENESIS OF
LYS-48 AND THR-174.
PubMed=22798068; DOI=10.1074/jbc.M112.375618;
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.;
"Brain-selective kinase 2 (BRSK2) phosphorylation on PCTAIRE1
negatively regulates glucose-stimulated insulin secretion in
pancreatic beta-cells.";
J. Biol. Chem. 287:30368-30375(2012).
[20]
CATALYTIC ACTIVITY, AND FUNCTION IN MAPT PHOSPHORYLATION.
PubMed=21985311; DOI=10.1111/j.1471-4159.2011.07523.x;
Yoshida H., Goedert M.;
"Phosphorylation of microtubule-associated protein tau by AMPK-related
kinases.";
J. Neurochem. 120:165-176(2012).
[21]
FUNCTION, SUBCELLULAR LOCATION, UBIQUITINATION, INTERACTION WITH FZR1,
AND DOMAIN KEN BOX MOTIF.
PubMed=23029325; DOI=10.1371/journal.pone.0045932;
Li R., Wan B., Zhou J., Wang Y., Luo T., Gu X., Chen F., Yu L.;
"APC/C(Cdh1) targets brain-specific kinase 2 (BRSK2) for degradation
via the ubiquitin-proteasome pathway.";
PLoS ONE 7:E45932-E45932(2012).
-!- 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 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 endoplasmic reticulum (ER) stress.
{ECO:0000269|PubMed:14976552, ECO:0000269|PubMed:20026642,
ECO:0000269|PubMed:21985311, ECO:0000269|PubMed:22669945,
ECO:0000269|PubMed:22798068, ECO:0000269|PubMed:23029325}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- CATALYTIC ACTIVITY: ATP + [tau protein] = ADP + [tau protein]
phosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- ENZYME REGULATION: Activated by phosphorylation on Thr-174 by
STK11/LKB1. {ECO:0000269|PubMed:14976552}.
-!- SUBUNIT: Interacts with FZR1, a regulatory subunit of the APC
ubiquitin ligase complex. Interacts with COPS5. Interacts with
PAK1. {ECO:0000269|PubMed:22609399, ECO:0000269|PubMed:22669945,
ECO:0000269|PubMed:23029325}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome. Cytoplasm, perinuclear region.
Endoplasmic reticulum. Note=Detected at centrosomes during
mitosis. Localizes to the endoplasmic reticulum in response to
stress caused by tunicamycin.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1;
IsoId=Q8IWQ3-1; Sequence=Displayed;
Name=2;
IsoId=Q8IWQ3-2; Sequence=VSP_008154, VSP_008155;
Name=3;
IsoId=Q8IWQ3-3; Sequence=VSP_008156, VSP_008157;
Name=4;
IsoId=Q8IWQ3-4; Sequence=VSP_013945, VSP_008154, VSP_008155;
Note=Contains a phosphoserine at position 416.
{ECO:0000244|PubMed:19369195};
Name=5;
IsoId=Q8IWQ3-5; Sequence=VSP_022603, VSP_022604;
Note=No experimental confirmation available.;
Name=6;
IsoId=Q8IWQ3-6; Sequence=VSP_055679, VSP_008154, VSP_008155;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Detected in pancreas islets (at protein
level). {ECO:0000269|PubMed:22798068}.
-!- DOMAIN: The KEN box motif is required for interaction with
FZR1/CDH1 and essential for APC(CDH1)-mediated ubiquitination.
{ECO:0000269|PubMed:23029325}.
-!- PTM: 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).
{ECO:0000269|PubMed:14976552, ECO:0000269|PubMed:16870137,
ECO:0000269|PubMed:18339622, ECO:0000269|PubMed:19958286,
ECO:0000269|PubMed:22669945}.
-!- PTM: 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.
{ECO:0000269|PubMed:22609399, ECO:0000269|PubMed:23029325}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. SNF1 subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD09654.1; Type=Erroneous termination; Positions=663; Note=Translated as Gly.; Evidence={ECO:0000305};
Sequence=AAD09654.1; Type=Frameshift; Positions=640; Evidence={ECO:0000305};
Sequence=AAH24291.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AY505125; AAS86443.1; -; mRNA.
EMBL; AF533876; AAP97723.1; -; mRNA.
EMBL; AF533877; AAP97724.1; -; mRNA.
EMBL; AF533878; AAP97725.1; -; mRNA.
EMBL; AF533879; AAP97726.1; -; mRNA.
EMBL; AF533880; AAP97727.1; -; mRNA.
EMBL; AY166857; AAN87839.1; -; mRNA.
EMBL; AK122851; BAG53761.1; -; mRNA.
EMBL; AK131534; BAD18671.1; -; mRNA.
EMBL; AC091196; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC136297; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AJ006701; CAA07196.1; -; mRNA.
EMBL; BC024291; AAH24291.1; ALT_INIT; mRNA.
EMBL; AF020089; AAD09654.1; ALT_SEQ; mRNA.
CCDS; CCDS41590.1; -. [Q8IWQ3-3]
CCDS; CCDS58106.1; -. [Q8IWQ3-2]
CCDS; CCDS58107.1; -. [Q8IWQ3-1]
CCDS; CCDS58108.1; -. [Q8IWQ3-5]
CCDS; CCDS60696.1; -. [Q8IWQ3-6]
RefSeq; NP_001243556.1; NM_001256627.1. [Q8IWQ3-1]
RefSeq; NP_001243558.1; NM_001256629.1. [Q8IWQ3-2]
RefSeq; NP_001243559.1; NM_001256630.1. [Q8IWQ3-5]
RefSeq; NP_001269147.1; NM_001282218.1. [Q8IWQ3-6]
RefSeq; NP_003948.2; NM_003957.3. [Q8IWQ3-3]
UniGene; Hs.170819; -.
ProteinModelPortal; Q8IWQ3; -.
SMR; Q8IWQ3; -.
BioGrid; 114491; 9.
IntAct; Q8IWQ3; 3.
STRING; 9606.ENSP00000310697; -.
BindingDB; Q8IWQ3; -.
ChEMBL; CHEMBL4574; -.
GuidetoPHARMACOLOGY; 1947; -.
iPTMnet; Q8IWQ3; -.
PhosphoSitePlus; Q8IWQ3; -.
BioMuta; BRSK2; -.
DMDM; 116241272; -.
EPD; Q8IWQ3; -.
MaxQB; Q8IWQ3; -.
PaxDb; Q8IWQ3; -.
PeptideAtlas; Q8IWQ3; -.
PRIDE; Q8IWQ3; -.
DNASU; 9024; -.
Ensembl; ENST00000308219; ENSP00000310697; ENSG00000174672. [Q8IWQ3-3]
Ensembl; ENST00000382179; ENSP00000371614; ENSG00000174672. [Q8IWQ3-5]
Ensembl; ENST00000526678; ENSP00000433370; ENSG00000174672. [Q8IWQ3-4]
Ensembl; ENST00000528710; ENSP00000433235; ENSG00000174672. [Q8IWQ3-6]
Ensembl; ENST00000528841; ENSP00000432000; ENSG00000174672. [Q8IWQ3-1]
Ensembl; ENST00000529433; ENSP00000433684; ENSG00000174672. [Q8IWQ3-2]
Ensembl; ENST00000531197; ENSP00000431152; ENSG00000174672. [Q8IWQ3-2]
GeneID; 9024; -.
KEGG; hsa:9024; -.
UCSC; uc001lti.5; human. [Q8IWQ3-1]
CTD; 9024; -.
DisGeNET; 9024; -.
EuPathDB; HostDB:ENSG00000174672.15; -.
GeneCards; BRSK2; -.
H-InvDB; HIX0009361; -.
HGNC; HGNC:11405; BRSK2.
HPA; HPA073690; -.
MIM; 609236; gene.
neXtProt; NX_Q8IWQ3; -.
OpenTargets; ENSG00000174672; -.
PharmGKB; PA36212; -.
eggNOG; KOG0588; Eukaryota.
eggNOG; ENOG410XNQ0; LUCA.
GeneTree; ENSGT00900000140977; -.
HOGENOM; HOG000246447; -.
HOVERGEN; HBG007240; -.
InParanoid; Q8IWQ3; -.
KO; K08796; -.
OMA; HRRKMSN; -.
OrthoDB; EOG091G02CG; -.
PhylomeDB; Q8IWQ3; -.
TreeFam; TF313967; -.
SignaLink; Q8IWQ3; -.
SIGNOR; Q8IWQ3; -.
GeneWiki; BRSK2; -.
GenomeRNAi; 9024; -.
PRO; PR:Q8IWQ3; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000174672; -.
CleanEx; HS_BRSK2; -.
ExpressionAtlas; Q8IWQ3; baseline and differential.
Genevisible; Q8IWQ3; HS.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0051117; F:ATPase binding; IDA:ParkinsonsUK-UCL.
GO; GO:0060590; F:ATPase regulator activity; NAS:ParkinsonsUK-UCL.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0050321; F:tau-protein kinase activity; IDA:UniProtKB.
GO; GO:0031532; P:actin cytoskeleton reorganization; IMP:UniProtKB.
GO; GO:0007409; P:axonogenesis; ISS:UniProtKB.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0036503; P:ERAD pathway; IMP:ParkinsonsUK-UCL.
GO; GO:0030010; P:establishment of cell polarity; ISS:UniProtKB.
GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IMP:UniProtKB.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IMP:UniProtKB.
GO; GO:0030182; P:neuron differentiation; ISS:UniProtKB.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0043462; P:regulation of ATPase activity; NAS:ParkinsonsUK-UCL.
GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:UniProtKB.
GO; GO:1904152; P:regulation of retrograde protein transport, ER to cytosol; NAS:ParkinsonsUK-UCL.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 2.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Alternative splicing; Apoptosis; ATP-binding; Cell cycle;
Cell division; Complete proteome; Cytoplasm; Cytoskeleton;
Endoplasmic reticulum; Exocytosis; Kinase; Magnesium; Metal-binding;
Mitosis; Neurogenesis; Nucleotide-binding; Phosphoprotein;
Reference proteome; Serine/threonine-protein kinase; Transferase;
Ubl conjugation.
CHAIN 1 736 Serine/threonine-protein kinase BRSK2.
/FTId=PRO_0000085670.
DOMAIN 19 270 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 297 339 UBA.
NP_BIND 25 33 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 603 605 KEN box.
COMPBIAS 424 468 Pro-rich.
ACT_SITE 141 141 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 48 48 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 174 174 Phosphothreonine; by LKB1.
{ECO:0000269|PubMed:14976552,
ECO:0000269|PubMed:18339622}.
MOD_RES 260 260 Phosphothreonine; by PKA.
{ECO:0000269|PubMed:16870137}.
MOD_RES 294 294 Phosphoserine.
{ECO:0000250|UniProtKB:D3ZML2}.
MOD_RES 367 367 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 382 382 Phosphoserine.
{ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332}.
MOD_RES 393 393 Phosphoserine.
{ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332}.
MOD_RES 412 412 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 422 422 Phosphothreonine.
{ECO:0000269|PubMed:19958286}.
MOD_RES 423 423 Phosphoserine.
{ECO:0000250|UniProtKB:Q69Z98}.
MOD_RES 427 427 Phosphoserine.
{ECO:0000250|UniProtKB:Q69Z98}.
MOD_RES 455 455 Phosphoserine.
{ECO:0000250|UniProtKB:Q69Z98}.
MOD_RES 459 459 Phosphothreonine.
{ECO:0000250|UniProtKB:Q69Z98}.
MOD_RES 463 463 Phosphothreonine.
{ECO:0000250|UniProtKB:Q69Z98}.
MOD_RES 509 509 Phosphothreonine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 512 512 Phosphoserine.
{ECO:0000250|UniProtKB:Q69Z98}.
MOD_RES 513 513 Phosphoserine.
{ECO:0000250|UniProtKB:Q69Z98}.
MOD_RES 520 520 Phosphoserine.
{ECO:0000250|UniProtKB:Q69Z98}.
VAR_SEQ 1 60 Missing (in isoform 6). {ECO:0000305}.
/FTId=VSP_055679.
VAR_SEQ 1 30 MTSTGKDGGAQHAQYVGPYRLEKTLGKGQT -> MSPEGHP
SRWARPRRPCICPSSLCSPREPRSGPAVGRGGAAHHRVPAG
HTPGPQLLQPHLHLPQGQTWLCLQPSPA (in isoform
5). {ECO:0000305}.
/FTId=VSP_022603.
VAR_SEQ 408 408 Q -> QSKAMFSKSLDIAEAHPQFSKED (in isoform
4). {ECO:0000303|PubMed:16630837}.
/FTId=VSP_013945.
VAR_SEQ 647 674 DTTNCMEMMTGRLSKCGSPLSNFFDVIK -> EPPPPAPGL
SWGAGLKGQKVATSYESSL (in isoform 2,
isoform 4 and isoform 6).
{ECO:0000303|PubMed:11124703,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16630837,
ECO:0000303|Ref.2}.
/FTId=VSP_008154.
VAR_SEQ 663 678 Missing (in isoform 5). {ECO:0000305}.
/FTId=VSP_022604.
VAR_SEQ 664 668 SPLSN -> IIPKS (in isoform 3).
{ECO:0000303|PubMed:9929968,
ECO:0000303|Ref.2}.
/FTId=VSP_008156.
VAR_SEQ 669 736 Missing (in isoform 3).
{ECO:0000303|PubMed:9929968,
ECO:0000303|Ref.2}.
/FTId=VSP_008157.
VAR_SEQ 675 736 Missing (in isoform 2, isoform 4 and
isoform 6). {ECO:0000303|PubMed:11124703,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16630837,
ECO:0000303|Ref.2}.
/FTId=VSP_008155.
MUTAGEN 48 48 K->M: Loss of catalytic activity. Causes
disintegration of actin stress fibers.
{ECO:0000269|PubMed:22669945,
ECO:0000269|PubMed:22798068}.
MUTAGEN 174 174 T->A: Prevents phosphorylation and
activation by STK11/LKB1 complex.
{ECO:0000269|PubMed:14976552,
ECO:0000269|PubMed:18339622,
ECO:0000269|PubMed:22798068}.
MUTAGEN 174 174 T->E: Constitutively activated.
{ECO:0000269|PubMed:14976552,
ECO:0000269|PubMed:18339622,
ECO:0000269|PubMed:22798068}.
MUTAGEN 260 260 T->A: Decreased phosphorylation. Nearly
abolishes stimulation of insulin
secretion. {ECO:0000269|PubMed:16870137,
ECO:0000269|PubMed:22669945}.
MUTAGEN 310 310 G->A: Decreased activation of kinase
activity. {ECO:0000269|PubMed:18339622}.
MUTAGEN 443 443 T->A: Constitutively activated. Promotes
formation of actin stress fibers.
{ECO:0000269|PubMed:22669945}.
CONFLICT 251 251 I -> S (in Ref. 2; AAP97723/AAP97724/
AAP97725/AAP97726/AAP97727/AAN87839 and
5; CAA07196). {ECO:0000305}.
CONFLICT 409 409 R -> G (in Ref. 3; BAG53761).
{ECO:0000305}.
SEQUENCE 736 AA; 81633 MW; D9EBA511149449E6 CRC64;
MTSTGKDGGA QHAQYVGPYR LEKTLGKGQT GLVKLGVHCV TCQKVAIKIV NREKLSESVL
MKVEREIAIL KLIEHPHVLK LHDVYENKKY LYLVLEHVSG GELFDYLVKK GRLTPKEARK
FFRQIISALD FCHSHSICHR DLKPENLLLD EKNNIRIADF GMASLQVGDS LLETSCGSPH
YACPEVIRGE KYDGRKADVW SCGVILFALL VGALPFDDDN LRQLLEKVKR GVFHMPHFIP
PDCQSLLRGM IEVDAARRLT LEHIQKHIWY IGGKNEPEPE QPIPRKVQIR SLPSLEDIDP
DVLDSMHSLG CFRDRNKLLQ DLLSEEENQE KMIYFLLLDR KERYPSQEDE DLPPRNEIDP
PRKRVDSPML NRHGKRRPER KSMEVLSVTD GGSPVPARRA IEMAQHGQRS RSISGASSGL
STSPLSSPRV TPHPSPRGSP LPTPKGTPVH TPKESPAGTP NPTPPSSPSV GGVPWRARLN
SIKNSFLGSP RFHRRKLQVP TPEEMSNLTP ESSPELAKKS WFGNFISLEK EEQIFVVIKD
KPLSSIKADI VHAFLSIPSL SHSVISQTSF RAEYKATGGP AVFQKPVKFQ VDITYTEGGE
AQKENGIYSV TFTLLSGPSR RFKRVVETIQ AQLLSTHDPP AAQHLSDTTN CMEMMTGRLS
KCGSPLSNFF DVIKQLFSDE KNGQAAQAPS TPAKRSAHGP LGDSAAAGPG PGGDAEYPTG
KDTAKMGPPT ARREQP


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