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Q9WTK7

- STK11_MOUSE

UniProt

Q9WTK7 - STK11_MOUSE

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Protein

Serine/threonine-protein kinase STK11

Gene

Stk11

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Tumor suppressor serine/threonine-protein kinase that controls the activity of AMP-activated protein kinase (AMPK) family members, thereby playing a role in various processes such as cell metabolism, cell polarity, apoptosis and DNA damage response. Acts by phosphorylating the T-loop of AMPK family proteins, thus promoting their activity: phosphorylates PRKAA1, PRKAA2, BRSK1, BRSK2, MARK1, MARK2, MARK3, MARK4, NUAK1, NUAK2, SIK1, SIK2, SIK3 and SNRK but not MELK. Also phosphorylates non-AMPK family proteins such as STRADA, PTEN and possibly p53/TP53. Acts as a key upstream regulator of AMPK by mediating phosphorylation and activation of AMPK catalytic subunits PRKAA1 and PRKAA2 and thereby regulates processes including: inhibition of signaling pathways that promote cell growth and proliferation when energy levels are low, glucose homeostasis in liver, activation of autophagy when cells undergo nutrient deprivation, and B-cell differentiation in the germinal center in response to DNA damage. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton. Required for cortical neuron polarization by mediating phosphorylation and activation of BRSK1 and BRSK2, leading to axon initiation and specification. Involved in DNA damage response: interacts with p53/TP53 and recruited to the CDKN1A/WAF1 promoter to participate in transcription activation. Able to phosphorylate p53/TP53; the relevance of such result in vivo is however unclear and phosphorylation may be indirect and mediated by downstream STK11/LKB1 kinase NUAK1. Also acts as a mediator of p53/TP53-dependent apoptosis via interaction with p53/TP53: translocates to the mitochondrion during apoptosis and regulates p53/TP53-dependent apoptosis pathways. In vein endothelial cells, inhibits PI3K/Akt signaling activity and thus induces apoptosis in response to the oxidant peroxynitrite.
Isoform 2: Has a role in spermiogenesis.

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.By similarity

Cofactori

Magnesium or Manganese.By similarity

Enzyme regulationi

Activated by forming a complex with STRAD (STRADA or STRADB) and CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta): STRADA (or STRADB)-binding promotes a conformational change of STK11/LKB1 in an active conformation, which is stabilized by CAB39/MO25alpha (or CAB39L/MO25beta) interacting with the STK11/LKB1 activation loop. Sequestration in the nucleus by NR4A1 prevents it from phosphorylating and activating cytoplasmic AMPK (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei78 – 781ATPCurated
Active sitei176 – 1761Proton acceptorBy similarityPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi55 – 639ATPBy similarityPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. LRR domain binding Source: UniProtKB
  3. magnesium ion binding Source: UniProtKB
  4. p53 binding Source: UniProtKB
  5. protein kinase activator activity Source: UniProtKB
  6. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. activation of protein kinase activity Source: MGI
  2. anoikis Source: Ensembl
  3. autophagy Source: UniProtKB-KW
  4. axonogenesis Source: UniProtKB
  5. canonical Wnt signaling pathway Source: MGI
  6. cell cycle arrest Source: UniProtKB
  7. cellular response to DNA damage stimulus Source: UniProtKB-KW
  8. establishment of cell polarity Source: UniProtKB
  9. glucose homeostasis Source: UniProtKB
  10. Golgi localization Source: MGI
  11. intrinsic apoptotic signaling pathway by p53 class mediator Source: UniProtKB
  12. negative regulation of cell growth Source: UniProtKB
  13. negative regulation of epithelial cell proliferation involved in prostate gland development Source: MGI
  14. positive regulation of axonogenesis Source: MGI
  15. positive regulation of gluconeogenesis Source: Ensembl
  16. positive regulation of peptidyl-tyrosine phosphorylation Source: MGI
  17. positive regulation of transforming growth factor beta receptor signaling pathway Source: BHF-UCL
  18. positive thymic T cell selection Source: MGI
  19. protein autophosphorylation Source: UniProtKB
  20. protein heterooligomerization Source: Ensembl
  21. protein phosphorylation Source: UniProtKB
  22. regulation of cell growth Source: UniProtKB
  23. regulation of protein kinase B signaling Source: MGI
  24. regulation of Wnt signaling pathway Source: MGI
  25. response to glucagon Source: Ensembl
  26. response to ionizing radiation Source: UniProtKB
  27. response to lipid Source: Ensembl
  28. spermatid development Source: UniProtKB
  29. spermatogenesis Source: UniProtKB-KW
  30. T cell receptor signaling pathway Source: MGI
  31. TCR signalosome assembly Source: MGI
  32. tissue homeostasis Source: MGI
  33. vasculature development Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Autophagy, Cell cycle, Differentiation, DNA damage, Spermatogenesis

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiREACT_220701. Regulation of AMPK activity via LKB1.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase STK11 (EC:2.7.11.1)
Alternative name(s):
Liver kinase B1 homolog
Short name:
LKB1
Short name:
mLKB1
Gene namesi
Name:Stk11Imported
Synonyms:Lkb1Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 10

Organism-specific databases

MGIiMGI:1341870. Stk11.

Subcellular locationi

Nucleus. Cytoplasm. Membrane. Mitochondrion By similarity
Note: Translocates to mitochondrion during apoptosis (By similarity). A small fraction localizes at membranes. Relocates to the cytoplasm when bound to STRAD (STRADA or STRADB) and CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta). PTEN promotes cytoplasmic localization (By similarity).By similarity
Isoform 2 : Nucleus By similarity. Cytoplasm By similarity
Note: Relocates to the cytoplasm when bound to STRAD (STRADA or STRADB) and CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta).By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: UniProtKB
  3. extracellular vesicular exosome Source: Ensembl
  4. membrane Source: UniProtKB
  5. mitochondrion Source: UniProtKB
  6. nucleus Source: UniProtKB
  7. TCR signalosome Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion, Nucleus

Pathology & Biotechi

Disruption phenotypei

Mice die in utero 8.5 to 9.5 dpc due to severe defects in their vasculature: embryos show neural tube defects, mesenchymal cell death, and vascular abnormalities. Extraembryonic development is also severely affected; the mutant placentas exhibit defective labyrinth layer development and the fetal vessels fail to invade the placenta. Male mice specifically lacking isoform 2 are sterile (PubMed:18774945). A specifically deletion in liver results in hyperglycemia with increased gluconeogenic and lipogenic gene expression due to loss of AMPK phosphorylation and subsequent dephosphorylation of CRTC2/TORC2 (PubMed:16308421). Use of a conditional allele, leads to defects in defects in axon formation with a thinner cortical wall and larger lateral ventricles in the brain cortex (PubMed:17482548). Heterozygous mice develop multiple gastric adenomatous polyps, with polyps remarkably similar to hamartomas of PJS patients both macroscopically and histologically. Polyps in the heterozygous mice are detected at 5 months, and cause premature lethality progressively from 8 months onwards. Polyps are most frequently observed in the stomach where they typically concentrate close to the pylorus. Polyps in the small and large intestine are significantly less frequent. The histology of the polyps in the heterozygous mice is remarkably similar to PJS polyps including the relative contribution of well-differentiated epithelium, and a prominent smooth muscle component. Ptgs2/Cox2 is highly up-regulated in heterozygous mice polyps concomitantly with activation of the extracellular signal-regulated kinases Mapk1/Erk2 and Mapk3/Erk1: treatment with celecoxib Ptgs2/Cox2 inhibitor significantly reduces the total polyp burden.9 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi31 – 311S → A: No change in kinase activity; when associated with A-325; A-336 and A-366. 1 Publication
Mutagenesisi78 – 781K → I: Loss of kinase activity.
Mutagenesisi194 – 1941D → A: Loss of kinase activity and descreased phosphorylation. 1 Publication
Mutagenesisi325 – 3251S → A: No change in kinase activity; when associated with A-31; A-336 and A-366. 1 Publication
Mutagenesisi336 – 3361T → A: Abolishes ability to suppress cell growth. Decreased phosphorylation; when associated with A-366. No change in kinase activity; when associated with A-31; A-325 and A-366. 1 Publication
Mutagenesisi366 – 3661T → A: Decreased phosphorylation; when associated with A-336. No change in kinase activity; when associated with A-31; A-325 and A-336. 3 Publications
Mutagenesisi431 – 4311S → A: Does not prevent S-farnesylation. Defects in neuron polarization. 4 Publications
Mutagenesisi433 – 4331C → A: Does not affect nuclear localization. Does not prevent phosphorylation at S-431. 3 Publications

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 433433Serine/threonine-protein kinase STK11PRO_0000260032Add
BLAST
Propeptidei434 – 4363Removed in mature formPRO_0000422301

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei31 – 311Phosphoserine1 Publication
Modified residuei44 – 441N6-acetyllysineBy similarity
Modified residuei48 – 481N6-acetyllysineBy similarity
Modified residuei96 – 961N6-acetyllysineBy similarity
Modified residuei97 – 971N6-acetyllysineBy similarity
Modified residuei189 – 1891Phosphothreonine; by autocatalysisBy similarity
Modified residuei296 – 2961N6-acetyllysineBy similarity
Modified residuei311 – 3111N6-acetyllysineBy similarity
Modified residuei325 – 3251Phosphoserine1 Publication
Modified residuei336 – 3361Phosphothreonine; by autocatalysis1 Publication
Modified residuei366 – 3661Phosphothreonine; by ATM and autocatalysis3 Publications
Modified residuei420 – 4201N6-acetyllysineBy similarity
Lipidationi422 – 4221S-palmitoyl cysteine1 Publication
Modified residuei426 – 4261N6-acetyllysineBy similarity
Modified residuei431 – 4311Phosphoserine; by autocatalysis, PKA, PKC/PRKCZ and RPS6KA14 Publications
Modified residuei433 – 4331Cysteine methyl ester1 Publication
Lipidationi433 – 4331S-farnesyl cysteine3 Publications
Modified residuei434 – 4341N6-acetyllysineBy similarity

Post-translational modificationi

Phosphorylated by ATM at Thr-366 following ionizing radiation (IR). Phosphorylation at Ser-431 by RPS6KA1 and/or some PKA is required to inhibit cell growth. Phosphorylation at Ser-431 is also required during neuronal polarization to mediate phosphorylation of BRSK1 and BRSK2. Phosphorylation by PKC/PRKCZ at Ser-428 promotes peroxynitrite-induced nuclear export of STK11, leading to PTEN activation and subsequent inhibition of AKT signaling. Phosphorylation by PKC/PRKCZ at Ser-399 in isoform 2 promotes metformin (or peroxynitrite)-induced nuclear export of STK11 and activation of AMPK.7 Publications
Acetylated. Deacetylation at Lys-48 enhances cytoplasmic localization and kinase activity in vitro.1 Publication

Keywords - PTMi

Acetylation, Lipoprotein, Methylation, Palmitate, Phosphoprotein, Prenylation

Proteomic databases

MaxQBiQ9WTK7.
PaxDbiQ9WTK7.
PRIDEiQ9WTK7.

PTM databases

PhosphoSiteiQ9WTK7.

Expressioni

Tissue specificityi

Widely expressed. Isoform 2 is predominantly expressed in testis (at protein level).3 Publications

Developmental stagei

Ubiquitously expressed 7-11 dpc. Present in nucleated embryonic blood cells from 9 dpc. Restricted to gastrointestinal tract, testis and lung from days 15-19 dpc.2 Publications

Gene expression databases

BgeeiQ9WTK7.
CleanExiMM_STK11.
ExpressionAtlasiQ9WTK7. baseline and differential.
GenevestigatoriQ9WTK7.

Interactioni

Subunit structurei

Catalytic component of a trimeric complex composed of STK11/LKB1, STRAD (STRADA or STRADB) and CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta): the complex tethers STK11/LKB1 in the cytoplasm and stimulates its catalytic activity. Found in a ternary complex composed of SMAD4, STK11/LKB1 and STK11IP. Interacts with p53/TP53, SMAD4, STK11IP and WDR6. Interacts with NR4A1 (By similarity). Interacts with NISCH; this interaction may increase STK11 activity (By similarity). Interacts with PTEN, leading to PTEN phosphorylation (By similarity). Interacts with SIRT1; the interaction deacetylates STK11 (By similarity).By similarity

Protein-protein interaction databases

BioGridi203541. 5 interactions.
DIPiDIP-60722N.
IntActiQ9WTK7. 3 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ9WTK7.
SMRiQ9WTK7. Positions 45-342.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini49 – 309261Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni45 – 9046Sufficient for interaction with SIRT1By similarityAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00530000063214.
HOGENOMiHOG000007002.
HOVERGENiHBG054467.
InParanoidiQ9WTK7.
KOiK07298.
OMAiPQQLGMF.
OrthoDBiEOG7F7W92.
PhylomeDBiQ9WTK7.
TreeFamiTF105322.

Family and domain databases

InterProiIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
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]
PANTHERiPTHR24347. PTHR24347. 1 hit.
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.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 16 Publications (identifier: Q9WTK7-1) [UniParc]FASTAAdd to Basket

Also known as: LKB1(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
MDVADPEPLG LFSEGELMSV GMDTFIHRID STEVIYQPRR KRAKLIGKYL
60 70 80 90 100
MGDLLGEGSY GKVKEVLDSE TLCRRAVKIL KKKKLRRIPN GEANVKKEIQ
110 120 130 140 150
LLRRLRHRNV IQLVDVLYNE EKQKMYMVME YCVCGMQEML DSVPEKRFPV
160 170 180 190 200
CQAHGYFRQL IDGLEYLHSQ GIVHKDIKPG NLLLTTNGTL KISDLGVAEA
210 220 230 240 250
LHPFAVDDTC RTSQGSPAFQ PPEIANGLDT FSGFKVDIWS AGVTLYNITT
260 270 280 290 300
GLYPFEGDNI YKLFENIGRG DFTIPCDCGP PLSDLLRGML EYEPAKRFSI
310 320 330 340 350
RQIRQHSWFR KKHPLAEALV PIPPSPDTKD RWRSMTVVPY LEDLHGRAEE
360 370 380 390 400
EEEEDLFDIE DGIIYTQDFT VPGQVLEEEV GQNGQSHSLP KAVCVNGTEP
410 420 430
QLSSKVKPEG RPGTANPARK VCSSNKIRRL SACKQQ
Length:436
Mass (Da):49,267
Last modified:November 1, 1999 - v1
Checksum:iCCD9BCF94CF5CC9C
GO
Isoform 21 Publication (identifier: Q9WTK7-2) [UniParc]FASTAAdd to Basket

Also known as: LKB1(S)

The sequence of this isoform differs from the canonical sequence as follows:
     374-415: QVLEEEVGQN...VKPEGRPGTA → VEEAAEAGLS...EPEEGFGALV
     416-436: Missing.

Show »
Length:412
Mass (Da):46,494
Checksum:i7598D55E069EFA19
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti95 – 951V → L in BAE42728. (PubMed:10400995)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei374 – 41542QVLEE…RPGTA → VEEAAEAGLSEDACDTCMWK SQGAGLPGEEPEEGFGALV in isoform 2. 2 PublicationsVSP_052222Add
BLAST
Alternative sequencei416 – 43621Missing in isoform 2. 2 PublicationsVSP_052223Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF129870 mRNA. Translation: AAD22100.1.
AF145287 mRNA. Translation: AAD31044.1.
EU730638 mRNA. Translation: ACE73833.1.
AF145296
, AF145288, AF145289, AF145290, AF145291, AF145292, AF145293, AF145294, AF145295 Genomic DNA. Translation: AAD55368.1.
AF151711 mRNA. Translation: AAF21370.1.
AB015801 mRNA. Translation: BAA76749.1.
AK171909 mRNA. Translation: BAE42728.1.
AK172528 mRNA. Translation: BAE43050.1.
AK172385 mRNA. Translation: BAE42977.1.
BC052379 mRNA. Translation: AAH52379.1.
CCDSiCCDS35974.1. [Q9WTK7-1]
RefSeqiNP_035622.1. NM_011492.3. [Q9WTK7-1]
UniGeneiMm.44231.

Genome annotation databases

EnsembliENSMUST00000003152; ENSMUSP00000003152; ENSMUSG00000003068. [Q9WTK7-1]
ENSMUST00000144883; ENSMUSP00000114195; ENSMUSG00000003068. [Q9WTK7-2]
GeneIDi20869.
KEGGimmu:20869.
UCSCiuc007gbu.1. mouse. [Q9WTK7-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF129870 mRNA. Translation: AAD22100.1 .
AF145287 mRNA. Translation: AAD31044.1 .
EU730638 mRNA. Translation: ACE73833.1 .
AF145296
, AF145288 , AF145289 , AF145290 , AF145291 , AF145292 , AF145293 , AF145294 , AF145295 Genomic DNA. Translation: AAD55368.1 .
AF151711 mRNA. Translation: AAF21370.1 .
AB015801 mRNA. Translation: BAA76749.1 .
AK171909 mRNA. Translation: BAE42728.1 .
AK172528 mRNA. Translation: BAE43050.1 .
AK172385 mRNA. Translation: BAE42977.1 .
BC052379 mRNA. Translation: AAH52379.1 .
CCDSi CCDS35974.1. [Q9WTK7-1 ]
RefSeqi NP_035622.1. NM_011492.3. [Q9WTK7-1 ]
UniGenei Mm.44231.

3D structure databases

ProteinModelPortali Q9WTK7.
SMRi Q9WTK7. Positions 45-342.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 203541. 5 interactions.
DIPi DIP-60722N.
IntActi Q9WTK7. 3 interactions.

PTM databases

PhosphoSitei Q9WTK7.

Proteomic databases

MaxQBi Q9WTK7.
PaxDbi Q9WTK7.
PRIDEi Q9WTK7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000003152 ; ENSMUSP00000003152 ; ENSMUSG00000003068 . [Q9WTK7-1 ]
ENSMUST00000144883 ; ENSMUSP00000114195 ; ENSMUSG00000003068 . [Q9WTK7-2 ]
GeneIDi 20869.
KEGGi mmu:20869.
UCSCi uc007gbu.1. mouse. [Q9WTK7-1 ]

Organism-specific databases

CTDi 6794.
MGIi MGI:1341870. Stk11.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00530000063214.
HOGENOMi HOG000007002.
HOVERGENi HBG054467.
InParanoidi Q9WTK7.
KOi K07298.
OMAi PQQLGMF.
OrthoDBi EOG7F7W92.
PhylomeDBi Q9WTK7.
TreeFami TF105322.

Enzyme and pathway databases

Reactomei REACT_220701. Regulation of AMPK activity via LKB1.

Miscellaneous databases

NextBioi 299701.
PROi Q9WTK7.
SOURCEi Search...

Gene expression databases

Bgeei Q9WTK7.
CleanExi MM_STK11.
ExpressionAtlasi Q9WTK7. baseline and differential.
Genevestigatori Q9WTK7.

Family and domain databases

InterProi IPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
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 ]
PANTHERi PTHR24347. PTHR24347. 1 hit.
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.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Expression of LKB1 and PTEN tumor suppressor genes during mouse embryonic development."
    Luukko K., Ylikorkala A., Tiainen M., Makela T.P.
    Mech. Dev. 83:187-190(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DEVELOPMENTAL STAGE.
  2. "The mouse Peutz-Jeghers syndrome gene Lkb1 encodes a nuclear protein kinase."
    Smith D.P., Spicer J., Smith A., Swift S., Ashworth A.
    Hum. Mol. Genet. 8:1479-1485(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
    Strain: 129Imported.
  3. "LKB1, a novel serine/threonine protein kinase and potential tumour suppressor, is phosphorylated by cAMP-dependent protein kinase (PKA) and prenylated in vivo."
    Collins S.P., Reoma J.L., Gamm D.M., Uhler M.D.
    Biochem. J. 345:673-680(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PALMITOYLATION AT CYS-422, PHOSPHORYLATION AT SER-431, ISOPRENYLATION AT CYS-433, MUTAGENESIS OF SER-431 AND CYS-433.
  4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
    Strain: Swiss Webster / NIHImported.
    Tissue: EmbryoImported.
  5. Ido Y., Lan F.
    Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  6. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: NODImported.
    Tissue: SpleenImported.
  7. "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] (ISOFORM 1).
    Strain: C57BL/6Imported.
    Tissue: BrainImported.
  8. "Phosphorylation of the protein kinase mutated in Peutz-Jeghers cancer syndrome, LKB1/STK11, at Ser431 by p90(RSK) and cAMP-dependent protein kinase, but not its farnesylation at Cys(433), is essential for LKB1 to suppress cell vrowth."
    Sapkota G.P., Kieloch A., Lizcano J.M., Lain S., Arthur J.S., Williams M.R., Morrice N., Deak M., Alessi D.R.
    J. Biol. Chem. 276:19469-19482(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-431, ISOPRENYLATION AT CYS-433, MUTAGENESIS OF SER-431 AND CYS-433.
  9. "Vascular abnormalities and deregulation of VEGF in Lkb1-deficient mice."
    Ylikorkala A., Rossi D.J., Korsisaari N., Luukko K., Alitalo K., Henkemeyer M., Makela T.P.
    Science 293:1323-1326(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  10. "Identification and characterization of four novel phosphorylation sites (Ser31, Ser325, Thr336 and Thr366) on LKB1/STK11, the protein kinase mutated in Peutz-Jeghers cancer syndrome."
    Sapkota G.P., Boudeau J., Deak M., Kieloch A., Morrice N., Alessi D.R.
    Biochem. J. 362:481-490(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT SER-31; SER-325; THR-336 AND THR-366, ISOPRENYLATION AT CYS-433, METHYLATION AT CYS-433, MUTAGENESIS OF SER-31; ARP-194; SER-325; THR-336; THR-366 AND CYS-433.
  11. "Ionizing radiation induces ataxia telangiectasia mutated kinase (ATM)-mediated phosphorylation of LKB1/STK11 at Thr-366."
    Sapkota G.P., Deak M., Kieloch A., Morrice N., Goodarzi A.A., Smythe C., Shiloh Y., Lees-Miller S.P., Alessi D.R.
    Biochem. J. 368:507-516(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-366, MUTAGENESIS OF THR-366.
  12. "Gastrointestinal hamartomatous polyposis in Lkb1 heterozygous knockout mice."
    Miyoshi H., Nakau M., Ishikawa T.O., Seldin M.F., Oshima M., Taketo M.M.
    Cancer Res. 62:2261-2266(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  13. "Loss of the Lkb1 tumour suppressor provokes intestinal polyposis but resistance to transformation."
    Bardeesy N., Sinha M., Hezel A.F., Signoretti S., Hathaway N.A., Sharpless N.E., Loda M., Carrasco D.R., DePinho R.A.
    Nature 419:162-167(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  14. Cited for: DISRUPTION PHENOTYPE.
  15. Cited for: DISRUPTION PHENOTYPE.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  17. "The kinase LKB1 mediates glucose homeostasis in liver and therapeutic effects of metformin."
    Shaw R.J., Lamia K.A., Vasquez D., Koo S.-H., Bardeesy N., Depinho R.A., Montminy M., Cantley L.C.
    Science 310:1642-1646(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  18. "LKB1 and SAD kinases define a pathway required for the polarization of cortical neurons."
    Barnes A.P., Lilley B.N., Pan Y.A., Plummer L.J., Powell A.W., Raines A.N., Sanes J.R., Polleux F.
    Cell 129:549-563(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT SER-431, MUTAGENESIS OF SER-431, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, INTERACTION WITH STRADA.
  19. "LKB1/STRAD promotes axon initiation during neuronal polarization."
    Shelly M., Cancedda L., Heilshorn S., Sumbre G., Poo M.M.
    Cell 129:565-577(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT SER-431, MUTAGENESIS OF SER-431.
  20. Cited for: ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  21. "SIRT1 modulation of the acetylation status, cytosolic localization, and activity of LKB1. Possible role in AMP-activated protein kinase activation."
    Lan F., Cacicedo J.M., Ruderman N., Ido Y.
    J. Biol. Chem. 283:27628-27635(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION.
  22. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Characterization of an alternative splice variant of LKB1."
    Denison F.C., Hiscock N.J., Carling D., Woods A.
    J. Biol. Chem. 284:67-76(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
  24. "AID-induced genotoxic stress promotes B cell differentiation in the germinal center via ATM and LKB1 signaling."
    Sherman M.H., Kuraishy A.I., Deshpande C., Hong J.S., Cacalano N.A., Gatti R.A., Manis J.P., Damore M.A., Pellegrini M., Teitell M.A.
    Mol. Cell 39:873-885(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT THR-366, MUTAGENESIS OF THR-366.

Entry informationi

Entry nameiSTK11_MOUSE
AccessioniPrimary (citable) accession number: Q9WTK7
Secondary accession number(s): B3VBP0, Q3TAE0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 1, 1999
Last modified: October 29, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3