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Q9WTK7 (STK11_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase STK11

EC=2.7.11.1
Alternative name(s):
Liver kinase B1 homolog
Short name=LKB1
Short name=mLKB1
Gene names
Name:Stk11
Synonyms:Lkb1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length436 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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, leading to promote 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 and possibly p53/TP53. Acts as a key upstream regulator of AMPK by mediating phosphorylation and activation of AMPK catalytic subunits PRKAA1 and PRKAA2: it thereby regulates 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, 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 neurons 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. Also acts as a mediator p53/TP53-dependent apoptosis via interaction with p53/TP53: translocates to mitochondrion during apoptosis and regulates p53/TP53-dependent apoptosis pathways. Ref.16 Ref.17 Ref.18 Ref.22

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. UniProtKB Q15831

Cofactor

Magnesium or Manganese By similarity. UniProtKB Q15831

Enzyme regulation

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.

Subunit structure

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. Ref.17

Subcellular location

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). Ref.2 Ref.3 Ref.7 Ref.9 Ref.10 Ref.17

Tissue specificity

Widely expressed. Isoform 2 is predominantly expressed in testis (at protein level). Ref.3 Ref.19 Ref.21

Developmental stage

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. Ref.1 Ref.4

Post-translational modification

Phosphorylated by ATM at Thr-366 following ionizing radiations (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. Ref.3 Ref.7 Ref.9 Ref.10 Ref.17 Ref.18 Ref.22

Disruption phenotype

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 (Ref.19). 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 (Ref.16). 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 (Ref.17). 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. Ref.4 Ref.8 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.17 Ref.19

Sequence similarities

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. LKB1 subfamily.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processApoptosis
Autophagy
Cell cycle
DNA damage
   Cellular componentCytoplasm
Membrane
Mitochondrion
Nucleus
   Coding sequence diversityAlternative splicing
   DiseaseTumor suppressor
   LigandATP-binding
Magnesium
Manganese
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMLipoprotein
Methylation
Palmitate
Phosphoprotein
Prenylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGolgi localization

Inferred from mutant phenotype PubMed 21111240. Source: MGI

T cell receptor signaling pathway

Inferred from mutant phenotype PubMed 21487392. Source: MGI

TCR signalosome assembly

Inferred from mutant phenotype PubMed 21487392. Source: MGI

activation of protein kinase activity

Inferred from direct assay Ref.21. Source: MGI

anoikis

Inferred from electronic annotation. Source: Ensembl

autophagy

Inferred from electronic annotation. Source: UniProtKB-KW

axonogenesis

Inferred from mutant phenotype Ref.17. Source: UniProtKB

canonical Wnt signaling pathway

Inferred from mutant phenotype PubMed 18381428. Source: MGI

cell cycle arrest

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to DNA damage stimulus

Inferred from electronic annotation. Source: UniProtKB-KW

establishment of cell polarity

Inferred from mutant phenotype Ref.17. Source: UniProtKB

glucose homeostasis

Inferred from mutant phenotype Ref.16. Source: UniProtKB

intrinsic apoptotic signaling pathway by p53 class mediator

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell growth

Inferred from direct assay Ref.7. Source: UniProtKB

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of epithelial cell proliferation involved in prostate gland development

Inferred from mutant phenotype PubMed 18381428. Source: MGI

positive regulation of axonogenesis

Inferred from genetic interaction PubMed 21111240. Source: MGI

positive regulation of gluconeogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from mutant phenotype PubMed 21487392. Source: MGI

positive regulation of transforming growth factor beta receptor signaling pathway

Inferred from mutant phenotype PubMed 18311138. Source: BHF-UCL

positive thymic T cell selection

Inferred from mutant phenotype PubMed 21487392. Source: MGI

protein autophosphorylation

Inferred from direct assay Ref.9. Source: UniProtKB

protein heterooligomerization

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of Wnt signaling pathway

Inferred from mutant phenotype PubMed 18381428. Source: MGI

regulation of cell growth

Inferred from direct assay Ref.9. Source: UniProtKB

regulation of protein kinase B signaling

Inferred from mutant phenotype PubMed 18381428. Source: MGI

response to glucagon

Inferred from electronic annotation. Source: Ensembl

response to ionizing radiation

Inferred from direct assay Ref.10. Source: UniProtKB

response to lipid

Inferred from electronic annotation. Source: Ensembl

spermatid development

Inferred from mutant phenotype Ref.19. Source: UniProtKB

tissue homeostasis

Inferred from mutant phenotype PubMed 18381428. Source: MGI

vasculature development

Inferred from mutant phenotype Ref.8. Source: UniProtKB

   Cellular_componentTCR signalosome

Inferred from direct assay PubMed 21487392. Source: MGI

cytoplasm

Inferred from direct assay Ref.21PubMed 20142099. Source: MGI

cytosol

Inferred from direct assay Ref.7. Source: UniProtKB

membrane

Inferred from direct assay Ref.21. Source: MGI

mitochondrion

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from direct assay Ref.2Ref.7PubMed 11741830Ref.9Ref.10Ref.17. Source: UniProtKB

protein complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from sequence or structural similarity. Source: UniProtKB

LRR domain binding

Inferred from physical interaction PubMed 11741830. Source: UniProtKB

magnesium ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

p53 binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein kinase activator activity

Inferred from direct assay Ref.17. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from direct assay Ref.9Ref.17. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 (identifier: Q9WTK7-1)

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.
Isoform 2 Ref.5 (identifier: Q9WTK7-2)

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.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 433433Serine/threonine-protein kinase STK11
PRO_0000260032
Propeptide434 – 4363Removed in mature form
PRO_0000422301

Regions

Domain49 – 309261Protein kinase
Nucleotide binding55 – 639ATP By similarity UniProtKB P28523

Sites

Active site1761Proton acceptor By similarity UniProtKB P28523
Binding site781ATP Probable UniProtKB P28523

Amino acid modifications

Modified residue311Phosphoserine Ref.9
Modified residue1891Phosphothreonine; by autocatalysis By similarity
Modified residue3251Phosphoserine Ref.9
Modified residue3361Phosphothreonine; by autocatalysis Ref.9 UniProtKB Q15831
Modified residue3661Phosphothreonine; by ATM and autocatalysis Ref.9 Ref.10 Ref.22 UniProtKB Q15831
Modified residue4311Phosphoserine; by PKA and RPS6KA1 Ref.3 Ref.7 Ref.17 Ref.18 UniProtKB Q15831
Modified residue4331Cysteine methyl ester Ref.9
Lipidation4221S-palmitoyl cysteine Ref.3
Lipidation4331S-farnesyl cysteine Ref.3 Ref.7 Ref.9

Natural variations

Alternative sequence374 – 41542QVLEE…RPGTA → VEEAAEAGLSEDACDTCMWK SQGAGLPGEEPEEGFGALV in isoform 2. Ref.5
VSP_052222
Alternative sequence416 – 43621Missing in isoform 2. Ref.5
VSP_052223

Experimental info

Mutagenesis311S → A: No change in kinase activity; when associated with A-325; A-336 and A-366. Ref.9
Mutagenesis781K → I: Loss of kinase activity.
Mutagenesis1941D → A: Loss of kinase activity and descreased phosphorylation. Ref.9
Mutagenesis3251S → A: No change in kinase activity; when associated with A-31; A-336 and A-366. Ref.9
Mutagenesis3361T → 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. Ref.9
Mutagenesis3661T → A: Decreased phosphorylation; when associated with A-336. No change in kinase activity; when associated with A-31; A-325 and A-336. Ref.9 Ref.10 Ref.22
Mutagenesis4311S → A: Does not prevent S-farnesylation. Defects in neuron polarization. Ref.3 Ref.7 Ref.17 Ref.18
Mutagenesis4331C → A: Does not affect nuclear localization. Does not prevent phosphorylation at S-431. Ref.3 Ref.7 Ref.9
Sequence conflict951V → L in BAE42728. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (LKB1(L)) [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: CCD9BCF94CF5CC9C

FASTA43649,267
        10         20         30         40         50         60 
MDVADPEPLG LFSEGELMSV GMDTFIHRID STEVIYQPRR KRAKLIGKYL MGDLLGEGSY 

        70         80         90        100        110        120 
GKVKEVLDSE TLCRRAVKIL KKKKLRRIPN GEANVKKEIQ LLRRLRHRNV IQLVDVLYNE 

       130        140        150        160        170        180 
EKQKMYMVME YCVCGMQEML DSVPEKRFPV CQAHGYFRQL IDGLEYLHSQ GIVHKDIKPG 

       190        200        210        220        230        240 
NLLLTTNGTL KISDLGVAEA LHPFAVDDTC RTSQGSPAFQ PPEIANGLDT FSGFKVDIWS 

       250        260        270        280        290        300 
AGVTLYNITT GLYPFEGDNI YKLFENIGRG DFTIPCDCGP PLSDLLRGML EYEPAKRFSI 

       310        320        330        340        350        360 
RQIRQHSWFR KKHPLAEALV PIPPSPDTKD RWRSMTVVPY LEDLHGRAEE EEEEDLFDIE 

       370        380        390        400        410        420 
DGIIYTQDFT VPGQVLEEEV GQNGQSHSLP KAVCVNGTEP QLSSKVKPEG RPGTANPARK 

       430 
VCSSNKIRRL SACKQQ 

« Hide

Isoform 2 (LKB1(S)) [UniParc].

Checksum: 7598D55E069EFA19
Show »

FASTA41246,494

References

« Hide 'large scale' references
[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: 129.
[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]"Role of Lkb1, the causative gene of Peutz-Jegher's syndrome, in embryogenesis and polyposis."
Jishage K., Nezu J., Kawase Y., Iwata T., Watanabe M., Miyoshi A., Ose A., Habu K., Kake T., Kamada N., Ueda O., Kinoshita M., Jenne D.E., Shimane M., Suzuki H.
Proc. Natl. Acad. Sci. U.S.A. 99:8903-8908(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
Strain: Swiss Webster / NIH.
Tissue: Embryo.
[5]"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. expand/collapse author list , 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: NOD.
Tissue: Spleen.
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6.
Tissue: Brain.
[7]"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.
[8]"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.
[9]"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.
[10]"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.
[11]"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.
[12]"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.
[13]"Induction of cyclooxygenase-2 in a mouse model of Peutz-Jeghers polyposis."
Rossi D.J., Ylikorkala A., Korsisaari N., Salovaara R., Luukko K., Launonen V., Henkemeyer M., Ristimaki A., Aaltonen L.A., Makela T.P.
Proc. Natl. Acad. Sci. U.S.A. 99:12327-12332(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[14]"Suppression of Peutz-Jeghers polyposis by inhibition of cyclooxygenase-2."
Udd L., Katajisto P., Rossi D.J., Lepisto A., Lahesmaa A.M., Ylikorkala A., Jarvinen H.J., Ristimaki A.P., Makela T.P.
Gastroenterology 127:1030-1037(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[15]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic brain.
[16]"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.
[17]"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.
[18]"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.
[19]"A novel short splice variant of the tumour suppressor LKB1 is required for spermiogenesis."
Towler M.C., Fogarty S., Hawley S.A., Pan D.A., Martin D.M., Morrice N.A., McCarthy A., Galardo M.N., Meroni S.B., Cigorraga S.B., Ashworth A., Sakamoto K., Hardie D.G.
Biochem. J. 416:1-14(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
[20]"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].
[21]"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.
[22]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF129870 mRNA. Translation: AAD22100.1.
AF145287 mRNA. Translation: AAD31044.1.
AF145296 expand/collapse EMBL AC list , 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.
RefSeqNP_035622.1. NM_011492.3.
UniGeneMm.44231.

3D structure databases

ProteinModelPortalQ9WTK7.
SMRQ9WTK7. Positions 45-342.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid203541. 5 interactions.
IntActQ9WTK7. 3 interactions.

PTM databases

PhosphoSiteQ9WTK7.

Proteomic databases

PaxDbQ9WTK7.
PRIDEQ9WTK7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000003152; ENSMUSP00000003152; ENSMUSG00000003068. [Q9WTK7-1]
ENSMUST00000144883; ENSMUSP00000114195; ENSMUSG00000003068. [Q9WTK7-2]
GeneID20869.
KEGGmmu:20869.
UCSCuc007gbu.1. mouse. [Q9WTK7-1]

Organism-specific databases

CTD6794.
MGIMGI:1341870. Stk11.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00530000063214.
HOGENOMHOG000007002.
HOVERGENHBG054467.
InParanoidQ9WTK7.
KOK07298.
OMAKKHPPSE.
OrthoDBEOG7F7W92.
PhylomeDBQ9WTK7.
TreeFamTF105322.

Gene expression databases

ArrayExpressQ9WTK7.
BgeeQ9WTK7.
CleanExMM_STK11.
GenevestigatorQ9WTK7.

Family and domain databases

InterProIPR020636. 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_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERPTHR24347. PTHR24347. 1 hit.
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio299701.
PROQ9WTK7.
SOURCESearch...

Entry information

Entry nameSTK11_MOUSE
AccessionPrimary (citable) accession number: Q9WTK7
Secondary accession number(s): Q3TAE0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 1, 1999
Last modified: April 16, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot