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Q8TDC3

- BRSK1_HUMAN

UniProt

Q8TDC3 - BRSK1_HUMAN

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Protein

Serine/threonine-protein kinase BRSK1

Gene

BRSK1

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 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-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. In neurons, localizes to synaptic vesicles and plays a role in neurotransmitter release, possibly by phosphorylating RIMS1. 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.4 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication
ATP + [tau protein] = ADP + [tau protein] phosphate.1 Publication

Cofactori

Magnesium.By similarity

Enzyme regulationi

Activated by phosphorylation on Thr-189 by STK11/LKB1.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei63 – 631ATPPROSITE-ProRule annotation
Active sitei156 – 1561Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi40 – 489ATPPROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. axonogenesis Source: UniProtKB
  2. cellular response to DNA damage stimulus Source: UniProtKB
  3. centrosome duplication Source: UniProtKB
  4. establishment of cell polarity Source: UniProtKB
  5. G2 DNA damage checkpoint Source: UniProtKB
  6. neuron differentiation Source: UniProtKB
  7. neurotransmitter secretion Source: UniProtKB
  8. protein phosphorylation Source: UniProtKB
  9. response to UV Source: UniProtKB
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

Enzyme and pathway databases

SignaLinkiQ8TDC3.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase BRSK1 (EC:2.7.11.1)
Alternative name(s):
Brain-selective kinase 1 (EC:2.7.11.26)
Brain-specific serine/threonine-protein kinase 1
Short name:
BR serine/threonine-protein kinase 1
Serine/threonine-protein kinase SAD-B
Synapses of Amphids Defective homolog 1
Short name:
SAD1 homolog
Short name:
hSAD1
Gene namesi
Name:BRSK1
Synonyms:KIAA1811, SAD1, SADB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:18994. BRSK1.

Subcellular locationi

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

GO - Cellular componenti

  1. cell junction Source: HPA
  2. centrosome Source: UniProtKB
  3. cytoplasm Source: UniProtKB
  4. nucleus Source: UniProtKB
  5. plasma membrane Source: HPA
  6. 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
Mutagenesisi59 – 591K → A: Loss of kinase activity. 1 Publication
Mutagenesisi189 – 1891T → A: Prevents phosphorylation and activation by STK11/LKB1 complex. 1 Publication
Mutagenesisi327 – 3271G → A: Abolishes activation of kinase activity. 1 Publication

Organism-specific databases

PharmGKBiPA134888976.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 778778Serine/threonine-protein kinase BRSK1PRO_0000085669Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei189 – 1891Phosphothreonine; by LKB12 Publications
Modified residuei447 – 4471Phosphoserine1 Publication
Modified residuei508 – 5081Phosphoserine1 Publication
Modified residuei563 – 5631Phosphoserine1 Publication

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.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ8TDC3.
PRIDEiQ8TDC3.

PTM databases

PhosphoSiteiQ8TDC3.

Expressioni

Tissue specificityi

Widely expressed, with highest levels in brain and testis. Protein levels remain constant throughout the cell cycle.1 Publication

Gene expression databases

BgeeiQ8TDC3.
CleanExiHS_BRSK1.
ExpressionAtlasiQ8TDC3. baseline.
GenevestigatoriQ8TDC3.

Organism-specific databases

HPAiHPA021212.

Interactioni

Protein-protein interaction databases

BioGridi124084. 4 interactions.
IntActiQ8TDC3. 2 interactions.
MINTiMINT-1651556.
STRINGi9606.ENSP00000310649.

Structurei

3D structure databases

ProteinModelPortaliQ8TDC3.
SMRiQ8TDC3. Positions 30-355.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 285252Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini314 – 35643UBAPROSITE-ProRule annotationAdd
BLAST

Compositional bias

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

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119244.
HOVERGENiHBG007240.
InParanoidiQ8TDC3.
KOiK08796.
OMAiGRHAQYV.
OrthoDBiEOG7XSTDH.
PhylomeDBiQ8TDC3.
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.
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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8TDC3-1) [UniParc]FASTAAdd to Basket

Also known as: SADB-Long, L

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
MSSGAKEGGG GSPAYHLPHP HPHPPQHAQY VGPYRLEKTL GKGQTGLVKL
60 70 80 90 100
GVHCITGQKV AIKIVNREKL SESVLMKVER EIAILKLIEH PHVLKLHDVY
110 120 130 140 150
ENKKYLYLVL EHVSGGELFD YLVKKGRLTP KEARKFFRQI VSALDFCHSY
160 170 180 190 200
SICHRDLKPE NLLLDEKNNI RIADFGMASL QVGDSLLETS CGSPHYACPE
210 220 230 240 250
VIKGEKYDGR RADMWSCGVI LFALLVGALP FDDDNLRQLL EKVKRGVFHM
260 270 280 290 300
PHFIPPDCQS LLRGMIEVEP EKRLSLEQIQ KHPWYLGGKH EPDPCLEPAP
310 320 330 340 350
GRRVAMRSLP SNGELDPDVL ESMASLGCFR DRERLHRELR SEEENQEKMI
360 370 380 390 400
YYLLLDRKER YPSCEDQDLP PRNDVDPPRK RVDSPMLSRH GKRRPERKSM
410 420 430 440 450
EVLSITDAGG GGSPVPTRRA LEMAQHSQRS RSVSGASTGL SSSPLSSPRS
460 470 480 490 500
PVFSFSPEPG AGDEARGGGS PTSKTQTLPS RGPRGGGAGE QPPPPSARST
510 520 530 540 550
PLPGPPGSPR SSGGTPLHSP LHTPRASPTG TPGTTPPPSP GGGVGGAAWR
560 570 580 590 600
SRLNSIRNSF LGSPRFHRRK MQVPTAEEMS SLTPESSPEL AKRSWFGNFI
610 620 630 640 650
SLDKEEQIFL VLKDKPLSSI KADIVHAFLS IPSLSHSVLS QTSFRAEYKA
660 670 680 690 700
SGGPSVFQKP VRFQVDISSS EGPEPSPRRD GSGGGGIYSV TFTLISGPSR
710 720 730 740 750
RFKRVVETIQ AQLLSTHDQP SVQALADEKN GAQTRPAGAP PRSLQPPPGR
760 770
PDPELSSSPR RGPPKDKKLL ATNGTPLP
Length:778
Mass (Da):85,087
Last modified:September 21, 2011 - v2
Checksum:i8D1818D4E54398BB
GO
Isoform 2 (identifier: Q8TDC3-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: MSSGAKEGGGGSPAYHLPHPHPHPPQ → MVAGLTLGKGPESPDGDVSVPERKDEVAGGGGEEEEAEERGR

Show »
Length:794
Mass (Da):86,753
Checksum:i5DD395B0E61AEF77
GO
Isoform 3 (identifier: Q8TDC3-3) [UniParc]FASTAAdd to Basket

Also known as: SADB-short, S

The sequence of this isoform differs from the canonical sequence as follows:
     344-778: Missing.

Show »
Length:343
Mass (Da):38,782
Checksum:i225C16D92E18BD8C
GO

Sequence cautioni

The sequence AAH16681.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti762 – 7621G → A in AAH16681. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti303 – 3031R → W in a gastric adenocarcinoma sample; somatic mutation. 1 Publication
VAR_040394
Natural varianti319 – 3191V → I in a lung large cell carcinoma sample; somatic mutation. 1 Publication
VAR_040395
Natural varianti391 – 3911G → E in a metastatic melanoma sample; somatic mutation. 1 Publication
VAR_040396
Natural varianti531 – 5311T → N.1 Publication
Corresponds to variant rs55892637 [ dbSNP | Ensembl ].
VAR_040397
Natural varianti749 – 7491G → S.1 Publication
Corresponds to variant rs12978445 [ dbSNP | Ensembl ].
VAR_040398
Natural varianti764 – 7641P → A.1 Publication
Corresponds to variant rs55796422 [ dbSNP | Ensembl ].
VAR_040399

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2626MSSGA…PHPPQ → MVAGLTLGKGPESPDGDVSV PERKDEVAGGGGEEEEAEER GR in isoform 2. 2 PublicationsVSP_008158Add
BLAST
Alternative sequencei344 – 778435Missing in isoform 3. 1 PublicationVSP_041742Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY458602 mRNA. Translation: AAS10354.1.
AY505124 mRNA. Translation: AAS86442.1.
HQ830199 mRNA. Translation: ADX95745.1.
AF479826 mRNA. Translation: AAL87697.1.
AF479827 mRNA. Translation: AAL87698.1.
AC008974 Genomic DNA. No translation available.
AC020922 Genomic DNA. No translation available.
AL831945 mRNA. Translation: CAD38595.1.
AL834275 mRNA. Translation: CAD38950.2.
AB058714 mRNA. Translation: BAB47440.1.
BC016681 mRNA. Translation: AAH16681.1. Different initiation.
CCDSiCCDS12921.1. [Q8TDC3-1]
RefSeqiNP_115806.1. NM_032430.1. [Q8TDC3-1]
UniGeneiHs.182081.

Genome annotation databases

EnsembliENST00000309383; ENSP00000310649; ENSG00000160469. [Q8TDC3-1]
ENST00000585418; ENSP00000467357; ENSG00000160469. [Q8TDC3-3]
ENST00000590333; ENSP00000468190; ENSG00000160469. [Q8TDC3-2]
GeneIDi84446.
KEGGihsa:84446.
UCSCiuc002qkf.3. human. [Q8TDC3-2]
uc002qkg.3. human. [Q8TDC3-1]
uc021vbs.1. human. [Q8TDC3-3]

Polymorphism databases

DMDMi347595639.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY458602 mRNA. Translation: AAS10354.1 .
AY505124 mRNA. Translation: AAS86442.1 .
HQ830199 mRNA. Translation: ADX95745.1 .
AF479826 mRNA. Translation: AAL87697.1 .
AF479827 mRNA. Translation: AAL87698.1 .
AC008974 Genomic DNA. No translation available.
AC020922 Genomic DNA. No translation available.
AL831945 mRNA. Translation: CAD38595.1 .
AL834275 mRNA. Translation: CAD38950.2 .
AB058714 mRNA. Translation: BAB47440.1 .
BC016681 mRNA. Translation: AAH16681.1 . Different initiation.
CCDSi CCDS12921.1. [Q8TDC3-1 ]
RefSeqi NP_115806.1. NM_032430.1. [Q8TDC3-1 ]
UniGenei Hs.182081.

3D structure databases

ProteinModelPortali Q8TDC3.
SMRi Q8TDC3. Positions 30-355.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 124084. 4 interactions.
IntActi Q8TDC3. 2 interactions.
MINTi MINT-1651556.
STRINGi 9606.ENSP00000310649.

Chemistry

BindingDBi Q8TDC3.
ChEMBLi CHEMBL5650.
GuidetoPHARMACOLOGYi 1946.

PTM databases

PhosphoSitei Q8TDC3.

Polymorphism databases

DMDMi 347595639.

Proteomic databases

PaxDbi Q8TDC3.
PRIDEi Q8TDC3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000309383 ; ENSP00000310649 ; ENSG00000160469 . [Q8TDC3-1 ]
ENST00000585418 ; ENSP00000467357 ; ENSG00000160469 . [Q8TDC3-3 ]
ENST00000590333 ; ENSP00000468190 ; ENSG00000160469 . [Q8TDC3-2 ]
GeneIDi 84446.
KEGGi hsa:84446.
UCSCi uc002qkf.3. human. [Q8TDC3-2 ]
uc002qkg.3. human. [Q8TDC3-1 ]
uc021vbs.1. human. [Q8TDC3-3 ]

Organism-specific databases

CTDi 84446.
GeneCardsi GC19P055795.
H-InvDB HIX0015461.
HGNCi HGNC:18994. BRSK1.
HPAi HPA021212.
MIMi 609235. gene.
neXtProti NX_Q8TDC3.
PharmGKBi PA134888976.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000119244.
HOVERGENi HBG007240.
InParanoidi Q8TDC3.
KOi K08796.
OMAi GRHAQYV.
OrthoDBi EOG7XSTDH.
PhylomeDBi Q8TDC3.
TreeFami TF313967.

Enzyme and pathway databases

SignaLinki Q8TDC3.

Miscellaneous databases

ChiTaRSi BRSK1. human.
GeneWikii BRSK1.
GenomeRNAii 84446.
NextBioi 74213.
PROi Q8TDC3.
SOURCEi Search...

Gene expression databases

Bgeei Q8TDC3.
CleanExi HS_BRSK1.
ExpressionAtlasi Q8TDC3. baseline.
Genevestigatori Q8TDC3.

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.
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. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT THR-189, MUTAGENESIS OF THR-189.
  2. "Human SAD1 kinase is involved in UV-induced DNA damage checkpoint function."
    Lu R., Niida H., Nakanishi M.
    J. Biol. Chem. 279:31164-31170(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-59.
    Tissue: Testis.
  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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "SADB phosphorylation of gamma-tubulin regulates centrosome duplication."
    Alvarado-Kristensson M., Rodriguez M.J., Silio V., Valpuesta J.M., Carrera A.C.
    Nat. Cell Biol. 11:1081-1092(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
  5. She X.Y., Yu L., Guo J.H.
    Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Brain.
  6. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 35-778.
    Tissue: Brain.
  8. "Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.
    DNA Res. 8:85-95(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 64-778.
    Tissue: Brain.
  9. "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 287-778.
    Tissue: Lymph.
  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-189, MUTAGENESIS OF GLY-327.
  11. "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.
  12. "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.
  13. "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.
  14. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] TRP-303; ILE-319; GLU-391; ASN-531; SER-749 AND ALA-764.

Entry informationi

Entry nameiBRSK1_HUMAN
AccessioniPrimary (citable) accession number: Q8TDC3
Secondary accession number(s): F1DG44
, Q5J5B5, Q8NDD0, Q8NDR4, Q8TDC2, Q96AV4, Q96JL4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: September 21, 2011
Last modified: October 29, 2014
This is version 124 of the entry and version 2 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 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3