SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

B2DD29

- BRSK1_RAT

UniProt

B2DD29 - BRSK1_RAT

(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)

Protein

Serine/threonine-protein kinase BRSK1

Gene
Brsk1, Sadb
Organism
Rattus norvegicus (Rat)
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 centrosome duplication. Phosphorylates CDC25B, CDC25C, MAPT/TAU, RIMS1, TUBG1, TUBG2 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-523' and 'Ser-573'. 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. Also acts as a positive regulator of centrosome duplication by mediating phosphorylation of gamma-tubulin (TUBG1 and TUBG2) at 'Ser-131', leading to translocation of gamma-tubulin and its associated proteins to the centrosome. Involved in the UV-induced DNA damage checkpoint response, probably by inhibiting CDK1 activity through phosphorylation and activation of WEE1, and inhibition of CDC25B and CDC25C By similarity. In neurons, localizes to synaptic vesicles and plays a role in neurotransmitter release, possibly by phosphorylating RIMS1.1 Publication

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-189 by STK11/LKB1.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei63 – 631ATP By similarity
Active sitei156 – 1561Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi40 – 489ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. gamma-tubulin binding Source: UniProtKB
  3. magnesium ion binding Source: Ensembl
  4. protein binding Source: UniProtKB
  5. protein serine/threonine kinase activity Source: UniProtKB
  6. tau-protein kinase activity Source: UniProtKB

GO - Biological processi

  1. axonogenesis Source: UniProtKB
  2. centrosome duplication Source: UniProtKB
  3. establishment of cell polarity Source: UniProtKB
  4. G2 DNA damage checkpoint Source: Ensembl
  5. neurotransmitter secretion Source: UniProtKB
  6. protein autophosphorylation Source: UniProtKB
  7. response to UV Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, DNA damage, Neurogenesis

Keywords - Ligandi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase BRSK1 (EC:2.7.11.1, EC:2.7.11.26)
Alternative name(s):
Brain-specific serine/threonine-protein kinase 1
Short name:
BR serine/threonine-protein kinase 1
Serine/threonine-protein kinase SAD-B
Gene namesi
Name:Brsk1
Synonyms:Sadb
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 1

Organism-specific databases

RGDi1563268. Brsk1.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Cell junctionsynapse
Note: Nuclear in the absence of DNA damage. Translocated to the nucleus in response to UV- or MMS-induced DNA damage By similarity. Localizes to synaptic vesicles in neurons.1 Publication

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. centrosome Source: UniProtKB
  3. nucleus Source: UniProtKB-SubCell
  4. plasma membrane Source: Ensembl
  5. synaptic vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoskeleton, Nucleus, Synapse

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi63 – 631K → R: Abolishes kinase activity. 1 Publication
Mutagenesisi189 – 1891T → A: Decreased autophosphorylation; when associated with A-193. 1 Publication
Mutagenesisi193 – 1931S → A: Decreased autophosphorylation; when associated with A-189. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 778778Serine/threonine-protein kinase BRSK1PRO_0000412649Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei189 – 1891Phosphothreonine; by LKB11 Publication
Modified residuei193 – 1931Phosphoserine Inferred
Modified residuei447 – 4471Phosphoserine By similarity
Modified residuei508 – 5081Phosphoserine By similarity
Modified residuei563 – 5631Phosphoserine By similarity

Post-translational modificationi

Phosphorylated at Thr-189 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Not phosphorylated at Thr-189 by CaMKK2. In contrast, it is phosphorylated and activated by CaMKK1. May be inactivated via dephosphorylation of Thr-189 by PP2C. May be autophosphorylated.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiB2DD29.

Expressioni

Tissue specificityi

Mainly present in brain. Present in presynaptic nerve terminals (at protein level).1 Publication

Gene expression databases

GenevestigatoriB2DD29.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000033679.

Structurei

3D structure databases

ProteinModelPortaliB2DD29.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 285252Protein kinaseAdd
BLAST
Domaini314 – 35643UBAAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi492 – 54049Pro-richAdd
BLAST

Sequence similaritiesi

Contains 1 UBA domain.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00750000117372.
HOGENOMiHOG000246447.
HOVERGENiHBG007240.
KOiK08796.
OMAiGRHAQYV.
OrthoDBiEOG7XSTDH.
PhylomeDBiB2DD29.

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.
IPR015940. UBA/transl_elong_EF1B_N_euk.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50030. UBA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B2DD29-1 [UniParc]FASTAAdd to Basket

« Hide

MSSGSKEGGG GSPAYHLPHP HPHPPQHAQY VGPYRLEKTL GKGQTGLVKL    50
GVHCITGQKV AVKIVNREKL SESVLMKVER EIAILKLIEH PHVLKLHDVY 100
ENKKYLYLVL EHVSGGELFD YLVKKGRLTP KEARKFFRQI VSALDFCHSY 150
SICHRDLKPE NLLLDEKNNI RIADFGMASL QVGDSLLETS CGSPHYACPE 200
VIKGEKYDGR RADMWSCGVI LFALLVGALP FDDDNLRQLL EKVKRGVFHM 250
PHFIPPDCQS LLRGMIEVEP EKRLSLEQIQ KHPWYLGGKH EPDPCLEPAP 300
GRRVAMRSLP SNGELDPDVL ESMASLGCFR DRERLHRELR SEEENQEKMI 350
YYLLLDRKER YPSCEDQDLP PRNDVDPPRK RVDSPMLSRH GKRRPERKSM 400
EVLSITDAGS GGSPVPTRRA LEMAQHSQRS RSVSGASTGL SSSPLSSPRS 450
PVFSFSPEPG VGDEARGGGS PTSKTQTLPS RGPRGGGAGE QPPPPSARST 500
PLPGPPGSPR SSGGTPLHSP LHTPRASPTG TPGTTPPPSP GGGVGGAAWR 550
SRLNSIRNSF LGSPRFHRRK MQVPTAEEMS SLTPESSPEL AKRSWFGNFI 600
SLDKEEQIFL VLKDKPLSSI KADIVHAFLS IPSLSHSVLS QTSFRAEYKA 650
SGGPSVFQKP VRFQVDISSS EGPEPSPRRD GSSGGGIYSV TFTLISGPSR 700
RFKRVVETIQ AQLLSTHDQP SVQALADEKN GAQTRPAGTP PRSLQPPPGR 750
PDPDLSSSPR RGPSKDKKLL ATNGTPLP 778
Length:778
Mass (Da):85,183
Last modified:June 10, 2008 - v1
Checksum:iA4F1E7E107359BDD
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB365521 mRNA. Translation: BAG28183.1.
RefSeqiNP_001120809.1. NM_001127337.1.
UniGeneiRn.112844.

Genome annotation databases

EnsembliENSRNOT00000031172; ENSRNOP00000033679; ENSRNOG00000017673.
GeneIDi499073.
KEGGirno:499073.
UCSCiRGD:1563268. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB365521 mRNA. Translation: BAG28183.1 .
RefSeqi NP_001120809.1. NM_001127337.1.
UniGenei Rn.112844.

3D structure databases

ProteinModelPortali B2DD29.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000033679.

Proteomic databases

PaxDbi B2DD29.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000031172 ; ENSRNOP00000033679 ; ENSRNOG00000017673 .
GeneIDi 499073.
KEGGi rno:499073.
UCSCi RGD:1563268. rat.

Organism-specific databases

CTDi 84446.
RGDi 1563268. Brsk1.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00750000117372.
HOGENOMi HOG000246447.
HOVERGENi HBG007240.
KOi K08796.
OMAi GRHAQYV.
OrthoDBi EOG7XSTDH.
PhylomeDBi B2DD29.

Miscellaneous databases

NextBioi 701750.

Gene expression databases

Genevestigatori B2DD29.

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.
IPR015940. UBA/transl_elong_EF1B_N_euk.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50030. UBA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION AT THR-189.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  2. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  3. "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: FUNCTION, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-63; THR-189 AND SER-193.
  4. "Tuberous sclerosis complex proteins control axon formation."
    Choi Y.J., Di Nardo A., Kramvis I., Meikle L., Kwiatkowski D.J., Sahin M., He X.
    Genes Dev. 22:2485-2495(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: REGULATION OF TRANSLATION.

Entry informationi

Entry nameiBRSK1_RAT
AccessioniPrimary (citable) accession number: B2DD29
Secondary accession number(s): F1M6Y8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: June 10, 2008
Last modified: June 11, 2014
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Protein synthesis is inhibited by the TSC1-TSC2 complex acting through TORC1 in neurons, leading to regulate neuron polarization (1 Publication).

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi