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Q15831

- STK11_HUMAN

UniProt

Q15831 - STK11_HUMAN

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Protein

Serine/threonine-protein kinase STK11

Gene

STK11

Organism
Homo sapiens (Human)
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 (in vitro).10 Publications
Isoform 2: Has a role in spermiogenesis.By similarity

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Cofactori

Magnesium or Manganese.

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.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei78 – 781ATPCurated
Active sitei176 – 1761Proton acceptor

Regions

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

GO - Molecular functioni

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

GO - Biological processi

  1. activation of protein kinase activity Source: MGI
  2. anoikis Source: BHF-UCL
  3. autophagy Source: UniProtKB-KW
  4. axonogenesis Source: Ensembl
  5. canonical Wnt signaling pathway Source: Ensembl
  6. cell cycle arrest Source: UniProtKB
  7. cellular response to DNA damage stimulus Source: UniProtKB-KW
  8. energy reserve metabolic process Source: Reactome
  9. establishment of cell polarity Source: UniProtKB
  10. glucose homeostasis Source: UniProtKB
  11. Golgi localization Source: Ensembl
  12. insulin receptor signaling pathway Source: Reactome
  13. intrinsic apoptotic signaling pathway by p53 class mediator Source: UniProtKB
  14. negative regulation of cell growth Source: UniProtKB
  15. negative regulation of cell proliferation Source: UniProtKB
  16. negative regulation of epithelial cell proliferation involved in prostate gland development Source: Ensembl
  17. positive regulation of axonogenesis Source: Ensembl
  18. positive regulation of gluconeogenesis Source: Ensembl
  19. positive regulation of peptidyl-tyrosine phosphorylation Source: Ensembl
  20. positive regulation of transforming growth factor beta receptor signaling pathway Source: BHF-UCL
  21. positive thymic T cell selection Source: Ensembl
  22. protein autophosphorylation Source: UniProtKB
  23. protein heterooligomerization Source: Ensembl
  24. protein phosphorylation Source: UniProtKB
  25. regulation of cell growth Source: UniProtKB
  26. regulation of fatty acid biosynthetic process Source: Reactome
  27. regulation of protein kinase B signaling Source: Ensembl
  28. regulation of Wnt signaling pathway Source: Ensembl
  29. response to glucagon Source: Ensembl
  30. response to ionizing radiation Source: UniProtKB
  31. response to lipid Source: Ensembl
  32. small molecule metabolic process Source: Reactome
  33. spermatid development Source: Ensembl
  34. T cell receptor signaling pathway Source: Ensembl
  35. TCR signalosome assembly Source: Ensembl
  36. tissue homeostasis Source: Ensembl
  37. 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

BRENDAi2.7.11.1. 2681.
ReactomeiREACT_1988. AMPK inhibits chREBP transcriptional activation activity.
REACT_21285. Regulation of AMPK activity via LKB1.
SignaLinkiQ15831.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase STK11 (EC:2.7.11.1)
Alternative name(s):
Liver kinase B1
Short name:
LKB1
Short name:
hLKB1
Renal carcinoma antigen NY-REN-19
Gene namesi
Name:STK11
Synonyms:LKB1, PJS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:11389. STK11.

Subcellular locationi

Nucleus. Cytoplasm. Membrane By similarity. Mitochondrion
Note: A small fraction localizes at membranes By similarity. Relocates to the cytoplasm when bound to STRAD (STRADA or STRADB) and CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta). Translocates to the mitochondrion during apoptosis. Translocates to the cytoplasm in response to metformin or peroxynitrite treatment. PTEN promotes cytoplasmic localization.By similarity
Isoform 2 : Nucleus 1 Publication. Cytoplasm 1 Publication
Note: Predominantly nuclear, but translocates to the cytoplasm in response to metformin or peroxynitrite treatment.

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion, Nucleus

Pathology & Biotechi

Involvement in diseasei

Peutz-Jeghers syndrome (PJS) [MIM:175200]: An autosomal dominant disorder characterized by melanocytic macules of the lips, multiple gastrointestinal hamartomatous polyps and an increased risk for various neoplasms, including gastrointestinal cancer.7 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti16 – 161E → G in PJS. 1 Publication
VAR_065628
Natural varianti50 – 534Missing in PJS. 1 Publication
VAR_071057
Natural varianti67 – 671L → P in PJS; abolishes kinase activity, leading to loss of autophosphorylation. 1 Publication
VAR_006202
Natural varianti162 – 1643DGL → NDM in PJS.
VAR_007920
Natural varianti176 – 1761D → N in PJS; loss of kinase activity, leading to greatly reduced autophosphorylation; fails to phosphorylate PTEN in vitro; no significant effect on nucleocytoplasmic localization. 1 Publication
VAR_071058
Natural varianti194 – 1941D → N in PJS. 1 Publication
VAR_007921
Natural varianti239 – 2391W → C in PJS; late onset suggests reduced penetrance. 1 Publication
VAR_033142
Natural varianti247 – 2471Missing in PJS. 1 Publication
VAR_006203
Natural varianti297 – 2971R → K in PJS. 1 Publication
VAR_007922
Natural varianti303 – 3064IRQH → N in PJS.
VAR_033143
Natural varianti308 – 3081W → C in PJS; abolishes kinase activity, leading to loss of autophosphorylation. 1 Publication
VAR_071059
Natural varianti315 – 3151P → S in PJS; pathogenicity uncertain; no effect heterotrimeric complex assembly with STRADA and CAB39. 1 Publication
VAR_033144
Testicular germ cell tumor (TGCT) [MIM:273300]: A common malignancy in males representing 95% of all testicular neoplasms. TGCTs have various pathologic subtypes including: unclassified intratubular germ cell neoplasia, seminoma (including cases with syncytiotrophoblastic cells), spermatocytic seminoma, embryonal carcinoma, yolk sac tumor, choriocarcinoma, and teratoma.1 Publication
Note: The gene represented in this entry may be involved in disease pathogenesis.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti163 – 1631G → D in TGCT; a tumor with seminoma and teratoma components; associated with severely impaired but detectable kinase activity; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39; predominantly nuclear localization. 1 Publication
VAR_033140
Defects in STK11 are associated with some sporadic cancers, especially lung cancers. Frequently mutated and inactivated in non-small cell lung cancer (NSCLC). Defects promote lung cancerigenesis process, especially lung cancer progression and metastasis. Confers lung adenocarcinoma the ability to trans-differentiate into squamous cell carcinoma. Also able to promotes lung cancer metastasis, via both cancer-cell autonomous and non-cancer-cell autonomous mechanisms.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi44 – 441K → R: No effect on kinase activity. 1 Publication
Mutagenesisi48 – 481K → Q: No effect on basal nucleocytoplasmic localization, but fails to translocate to the cytoplasm when coexpressed with SIRT1. 1 Publication
Mutagenesisi48 – 481K → R: Enhanced phosphorylation at Thr-336 and Ser-428, enhanced cytoplasmic localization and increased kinase activity. 1 Publication
Mutagenesisi74 – 741R → A: Impaired formation of a heterotrimeric complex with STRADA and CAB39; when associated with A-204. 1 Publication
Mutagenesisi78 – 781K → I: Loss of kinase activity, leading to greatly reduced autophosphorylation. 2 Publications
Mutagenesisi78 – 781K → M: Loss of kinase activity, leading to reduced autophosphorylation and acting as a dominant-negative mutant. 2 Publications
Mutagenesisi96 – 961K → R: No effect on kinase activity. 1 Publication
Mutagenesisi97 – 971K → R: No effect on kinase activity. 1 Publication
Mutagenesisi189 – 1891T → A: Reduced phosphorylation. 1 Publication
Mutagenesisi194 – 1941D → A: Loss of kinase activity. 3 Publications
Mutagenesisi204 – 2041F → A: No effect. Impaired formation of a heterotrimeric complex with STRADA and CAB39; when associated with A-74. 1 Publication
Mutagenesisi428 – 4281S → A or E: No effect on kinase activity. 2 Publications
Mutagenesisi428 – 4281S → A: Inhibits peroxynitrite-induced nuclear export of STK11, and consequent PTEN phosphorylation and inhibition of PI3K/Akt signaling. 2 Publications

Keywords - Diseasei

Disease mutation, Tumor suppressor

Organism-specific databases

MIMi175200. phenotype.
273300. phenotype.
Orphaneti2869. Peutz-Jeghers syndrome.
PharmGKBiPA36198.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 430430Serine/threonine-protein kinase STK11PRO_0000086699Add
BLAST
Propeptidei431 – 4333Removed in mature formBy similarityPRO_0000422300

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei31 – 311PhosphoserineBy similarity
Modified residuei44 – 441N6-acetyllysine1 Publication
Modified residuei48 – 481N6-acetyllysine1 Publication
Modified residuei96 – 961N6-acetyllysine1 Publication
Modified residuei97 – 971N6-acetyllysine1 Publication
Modified residuei189 – 1891Phosphothreonine; by autocatalysis1 Publication
Modified residuei296 – 2961N6-acetyllysine1 Publication
Modified residuei311 – 3111N6-acetyllysine1 Publication
Modified residuei325 – 3251PhosphoserineBy similarity
Modified residuei336 – 3361Phosphothreonine; by autocatalysis1 Publication
Modified residuei363 – 3631Phosphothreonine; by ATM and autocatalysis1 Publication
Modified residuei416 – 4161N6-acetyllysine1 Publication
Lipidationi418 – 4181S-palmitoyl cysteineBy similarity
Modified residuei423 – 4231N6-acetyllysine1 Publication
Modified residuei428 – 4281Phosphoserine; by autocatalysis, PKA, PKC/PRKCZ and RPS6KA12 Publications
Modified residuei430 – 4301Cysteine methyl esterBy similarity
Lipidationi430 – 4301S-farnesyl cysteineBy similarity
Modified residuei431 – 4311N6-acetyllysine1 Publication

Post-translational modificationi

Phosphorylated by ATM at Thr-363 following ionizing radiation (IR). Phosphorylation at Ser-428 by RPS6KA1 and/or some PKA is required to inhibit cell growth. Phosphorylation at Ser-428 is also required during neuronal polarization to mediate phosphorylation of BRSK1 and BRSK2 By similarity. 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.By similarity4 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

MaxQBiQ15831.
PaxDbiQ15831.
PRIDEiQ15831.

PTM databases

PhosphoSiteiQ15831.

Expressioni

Tissue specificityi

Ubiquitously expressed. Strongest expression in testis and fetal liver.

Gene expression databases

BgeeiQ15831.
CleanExiHS_STK11.
ExpressionAtlasiQ15831. baseline and differential.
GenevestigatoriQ15831.

Organism-specific databases

HPAiCAB016231.
CAB022105.
HPA017254.

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. Interacts with NISCH; this interaction may increase STK11 activity. Interacts with PTEN; leading to PTEN phosphorylation. Interacts with SIRT1; the interaction deacetylates STK11.10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CAB39Q9Y3765EBI-306838,EBI-306905
CDC37Q165433EBI-306838,EBI-295634
FKBP5Q134513EBI-306838,EBI-306914
HSP90AA1P079002EBI-306838,EBI-296047
HSP90AB1P082383EBI-306838,EBI-352572
MARK4Q96L342EBI-306838,EBI-302319
STRADAQ7RTN610EBI-306838,EBI-1109114
STRADBQ9C0K76EBI-306838,EBI-306893
TNIP2Q8NFZ55EBI-306838,EBI-359372
WDR6Q9NNW53EBI-306838,EBI-1568315
YWHAZP631046EBI-306838,EBI-347088

Protein-protein interaction databases

BioGridi112670. 34 interactions.
DIPiDIP-31317N.
IntActiQ15831. 47 interactions.
MINTiMINT-204048.
STRINGi9606.ENSP00000324856.

Structurei

Secondary structure

1
433
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi54 – 574
Beta strandi62 – 687
Turni69 – 713
Beta strandi74 – 807
Helixi82 – 876
Helixi91 – 10212
Beta strandi113 – 1186
Beta strandi125 – 1306
Beta strandi133 – 1353
Helixi136 – 1427
Helixi150 – 16920
Helixi179 – 1813
Beta strandi182 – 1843
Beta strandi190 – 1923
Helixi217 – 2193
Helixi222 – 2254
Beta strandi231 – 2333
Helixi234 – 25017
Helixi260 – 26910
Beta strandi276 – 2783
Helixi280 – 28910
Turni294 – 2963
Helixi300 – 3056
Helixi307 – 3104
Helixi339 – 3413

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WTKX-ray2.65C/F43-347[»]
ProteinModelPortaliQ15831.
SMRiQ15831. Positions 22-369.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15831.

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 SIRT1Add
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00530000063214.
HOGENOMiHOG000007002.
HOVERGENiHBG054467.
InParanoidiQ15831.
KOiK07298.
OMAiPQQLGMF.
OrthoDBiEOG7F7W92.
PhylomeDBiQ15831.
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 1 (identifier: Q15831-1) [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
MEVVDPQQLG MFTEGELMSV GMDTFIHRID STEVIYQPRR KRAKLIGKYL
60 70 80 90 100
MGDLLGEGSY GKVKEVLDSE TLCRRAVKIL KKKKLRRIPN GEANVKKEIQ
110 120 130 140 150
LLRRLRHKNV IQLVDVLYNE EKQKMYMVME YCVCGMQEML DSVPEKRFPV
160 170 180 190 200
CQAHGYFCQL IDGLEYLHSQ GIVHKDIKPG NLLLTTGGTL KISDLGVAEA
210 220 230 240 250
LHPFAADDTC RTSQGSPAFQ PPEIANGLDT FSGFKVDIWS AGVTLYNITT
260 270 280 290 300
GLYPFEGDNI YKLFENIGKG SYAIPGDCGP PLSDLLKGML EYEPAKRFSI
310 320 330 340 350
RQIRQHSWFR KKHPPAEAPV PIPPSPDTKD RWRSMTVVPY LEDLHGADED
360 370 380 390 400
EDLFDIEDDI IYTQDFTVPG QVPEEEASHN GQRRGLPKAV CMNGTEAAQL
410 420 430
STKSRAEGRA PNPARKACSA SSKIRRLSAC KQQ
Length:433
Mass (Da):48,636
Last modified:November 1, 1996 - v1
Checksum:i6DF4C37AB7A89569
GO
Isoform 2 (identifier: Q15831-2) [UniParc]FASTAAdd to Basket

Also known as: LKB1(S)

The sequence of this isoform differs from the canonical sequence as follows:
     371-433: QVPEEEASHN...IRRLSACKQQ → GEEASEAGLRAERGLQKSEGSDLSGEEASRPAPQ

Note: Phosphorylated by PKC/PRKCZ on Ser-399.

Show »
Length:404
Mass (Da):45,387
Checksum:i6E4F3920F8F873DD
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti14 – 141E → K in cervical cancer; somatic mutation. 1 Publication
VAR_065627
Natural varianti16 – 161E → G in PJS. 1 Publication
VAR_065628
Natural varianti49 – 491Y → D in melanoma; sporadic malignant; somatic mutation. 1 Publication
VAR_033138
Natural varianti50 – 534Missing in PJS. 1 Publication
VAR_071057
Natural varianti66 – 661V → M in cervical carcinoma; somatic mutation. 1 Publication
VAR_065629
Natural varianti67 – 671L → P in PJS; abolishes kinase activity, leading to loss of autophosphorylation. 1 Publication
VAR_006202
Natural varianti86 – 861R → G in sporadic cancer; somatic mutation; no effect on kinase activity nor in heterotrimeric complex assembly with STRADA and CAB39.
VAR_065630
Natural varianti87 – 871R → K in a metastatic melanoma sample; somatic mutation. 1 Publication
VAR_041139
Natural varianti123 – 1231Q → R in sporadic cancer; somatic mutation; no effect on kinase activity nor in heterotrimeric complex assembly with STRADA and CAB39.
VAR_065631
Natural varianti135 – 1351G → R in melanoma; sporadic malignant; somatic mutation. 1 Publication
VAR_033139
Natural varianti157 – 1571F → S in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39.
VAR_065632
Natural varianti160 – 1601L → P in cervical cancer; somatic mutation. 1 Publication
VAR_065633
Natural varianti162 – 1643DGL → NDM in PJS.
VAR_007920
Natural varianti163 – 1631G → D in TGCT; a tumor with seminoma and teratoma components; associated with severely impaired but detectable kinase activity; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39; predominantly nuclear localization. 1 Publication
VAR_033140
Natural varianti170 – 1701Q → P in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39.
VAR_065634
Natural varianti171 – 1711G → S in colorectal cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39. 1 Publication
VAR_065635
Natural varianti174 – 1741H → R in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39.
VAR_065636
Natural varianti176 – 1761D → N in PJS; loss of kinase activity, leading to greatly reduced autophosphorylation; fails to phosphorylate PTEN in vitro; no significant effect on nucleocytoplasmic localization. 1 Publication
VAR_071058
Natural varianti176 – 1761D → Y in sporadic cancer; somatic mutation; Loss of kinase activity.
VAR_065637
Natural varianti177 – 1771I → N in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39.
VAR_065638
Natural varianti181 – 1811N → E in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39; requires 2 nucleotide substitutions.
VAR_065639
Natural varianti194 – 1941D → N in PJS. 1 Publication
VAR_007921
Natural varianti194 – 1941D → V in lung cancer; somatic mutation. 1 Publication
VAR_065640
Natural varianti194 – 1941D → Y in melanoma; sporadic malignant; somatic mutation. 1 Publication
VAR_033141
Natural varianti199 – 1991E → K in colorectal cancer; somatic mutation; impaired kinase activity. 1 Publication
VAR_065641
Natural varianti199 – 1991E → Q in sporadic cancer; somatic mutation; does not affect kinase activity.
VAR_065642
Natural varianti205 – 2051A → T in sporadic cancer; somatic mutation; no effect heterotrimeric complex assembly with STRADA and CAB39.
VAR_065643
Natural varianti208 – 2081D → N in colorectal cancer; somatic mutation; no effect heterotrimeric complex assembly with STRADA and CAB39. 1 Publication
VAR_065644
Natural varianti215 – 2151G → D in colorectal cancer; somatic mutation. 1 Publication
VAR_065645
Natural varianti216 – 2161S → F in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39.
VAR_065646
Natural varianti223 – 2231E → V in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39.
VAR_065647
Natural varianti230 – 2301T → P in sporadic cancer; somatic mutation; no effect heterotrimeric complex assembly with STRADA and CAB39.
VAR_065648
Natural varianti231 – 2311F → L in cervical cancer; somatic mutation. 1 Publication
VAR_065649
Natural varianti232 – 2321S → P in sporadic cancer; somatic mutation; no effect heterotrimeric complex assembly with STRADA and CAB39.
VAR_065650
Natural varianti239 – 2391W → C in PJS; late onset suggests reduced penetrance. 1 Publication
VAR_033142
Natural varianti245 – 2451L → R in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39.
VAR_065651
Natural varianti247 – 2471Missing in PJS. 1 Publication
VAR_006203
Natural varianti250 – 2501T → P in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39.
VAR_065652
Natural varianti272 – 2721Y → H in sporadic cancer; somatic mutation; no effect on kinase activity nor in heterotrimeric complex assembly with STRADA and CAB39.
VAR_065653
Natural varianti277 – 2771D → Y in sporadic cancer; somatic mutation; no effect on kinase activity nor in heterotrimeric complex assembly with STRADA and CAB39.
VAR_065654
Natural varianti281 – 2811P → L in ovarian carcinoma; somatic mutation. 1 Publication
VAR_065655
Natural varianti285 – 2851L → Q in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39.
VAR_065656
Natural varianti297 – 2971R → K in PJS. 1 Publication
VAR_007922
Natural varianti303 – 3064IRQH → N in PJS.
VAR_033143
Natural varianti308 – 3081W → C in PJS; abolishes kinase activity, leading to loss of autophosphorylation. 1 Publication
VAR_071059
Natural varianti314 – 3141P → H in colorectal cancer; no effect heterotrimeric complex assembly with STRADA and CAB39. 1 Publication
VAR_065657
Natural varianti315 – 3151P → S in PJS; pathogenicity uncertain; no effect heterotrimeric complex assembly with STRADA and CAB39. 1 Publication
VAR_033144
Natural varianti324 – 3241P → L in gastric carcinoma; no effect heterotrimeric complex assembly with STRADA and CAB39. 1 Publication
VAR_065658
Natural varianti354 – 3541F → L in colorectal cancer; somatic mutation. 1 Publication
VAR_065659
Natural varianti367 – 3671T → M in colorectal cancer; somatic mutation. 1 Publication
VAR_065660

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei371 – 43363QVPEE…ACKQQ → GEEASEAGLRAERGLQKSEG SDLSGEEASRPAPQ in isoform 2. CuratedVSP_041746Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U63333 mRNA. Translation: AAB05809.1.
AF035625 mRNA. Translation: AAC39527.1.
AF032984 Genomic DNA. Translation: AAB97833.1.
AF055327
, AF055320, AF055321, AF055322, AF055323, AF055324, AF055325, AF055326 Genomic DNA. Translation: AAC15742.1.
AK314858 mRNA. Translation: BAG37374.1.
AC011544 Genomic DNA. No translation available.
AC004221 Genomic DNA. No translation available.
CH471139 Genomic DNA. Translation: EAW69540.1.
BC007981 mRNA. Translation: AAH07981.1.
BC019334 mRNA. Translation: AAH19334.1.
CCDSiCCDS45896.1. [Q15831-1]
RefSeqiNP_000446.1. NM_000455.4. [Q15831-1]
XP_005259675.1. XM_005259618.2. [Q15831-2]
UniGeneiHs.515005.

Genome annotation databases

EnsembliENST00000326873; ENSP00000324856; ENSG00000118046. [Q15831-1]
GeneIDi6794.
KEGGihsa:6794.
UCSCiuc002lrl.1. human. [Q15831-1]

Polymorphism databases

DMDMi3024670.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
Wikipedia

PJS entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U63333 mRNA. Translation: AAB05809.1 .
AF035625 mRNA. Translation: AAC39527.1 .
AF032984 Genomic DNA. Translation: AAB97833.1 .
AF055327
, AF055320 , AF055321 , AF055322 , AF055323 , AF055324 , AF055325 , AF055326 Genomic DNA. Translation: AAC15742.1 .
AK314858 mRNA. Translation: BAG37374.1 .
AC011544 Genomic DNA. No translation available.
AC004221 Genomic DNA. No translation available.
CH471139 Genomic DNA. Translation: EAW69540.1 .
BC007981 mRNA. Translation: AAH07981.1 .
BC019334 mRNA. Translation: AAH19334.1 .
CCDSi CCDS45896.1. [Q15831-1 ]
RefSeqi NP_000446.1. NM_000455.4. [Q15831-1 ]
XP_005259675.1. XM_005259618.2. [Q15831-2 ]
UniGenei Hs.515005.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2WTK X-ray 2.65 C/F 43-347 [» ]
ProteinModelPortali Q15831.
SMRi Q15831. Positions 22-369.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112670. 34 interactions.
DIPi DIP-31317N.
IntActi Q15831. 47 interactions.
MINTi MINT-204048.
STRINGi 9606.ENSP00000324856.

Chemistry

BindingDBi Q15831.
ChEMBLi CHEMBL5606.
GuidetoPHARMACOLOGYi 2212.

PTM databases

PhosphoSitei Q15831.

Polymorphism databases

DMDMi 3024670.

Proteomic databases

MaxQBi Q15831.
PaxDbi Q15831.
PRIDEi Q15831.

Protocols and materials databases

DNASUi 6794.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000326873 ; ENSP00000324856 ; ENSG00000118046 . [Q15831-1 ]
GeneIDi 6794.
KEGGi hsa:6794.
UCSCi uc002lrl.1. human. [Q15831-1 ]

Organism-specific databases

CTDi 6794.
GeneCardsi GC19P001205.
GeneReviewsi STK11.
HGNCi HGNC:11389. STK11.
HPAi CAB016231.
CAB022105.
HPA017254.
MIMi 175200. phenotype.
273300. phenotype.
602216. gene.
neXtProti NX_Q15831.
Orphaneti 2869. Peutz-Jeghers syndrome.
PharmGKBi PA36198.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00530000063214.
HOGENOMi HOG000007002.
HOVERGENi HBG054467.
InParanoidi Q15831.
KOi K07298.
OMAi PQQLGMF.
OrthoDBi EOG7F7W92.
PhylomeDBi Q15831.
TreeFami TF105322.

Enzyme and pathway databases

BRENDAi 2.7.11.1. 2681.
Reactomei REACT_1988. AMPK inhibits chREBP transcriptional activation activity.
REACT_21285. Regulation of AMPK activity via LKB1.
SignaLinki Q15831.

Miscellaneous databases

ChiTaRSi STK11. human.
EvolutionaryTracei Q15831.
GeneWikii STK11.
GenomeRNAii 6794.
NextBioi 26541.
PROi Q15831.
SOURCEi Search...

Gene expression databases

Bgeei Q15831.
CleanExi HS_STK11.
ExpressionAtlasi Q15831. baseline and differential.
Genevestigatori Q15831.

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. "Peutz-Jeghers syndrome is caused by mutations in a novel serine threonine kinase."
    Jenne D.E., Reimann H., Nezu J., Friedl W., Loff S., Jeschke R., Mueller O., Back W., Zimmer M.
    Nat. Genet. 18:38-43(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INVOLVEMENT IN PJS.
    Tissue: Liver.
  2. "Low frequency of somatic mutations in the LKB1/Peutz-Jeghers syndrome gene in sporadic breast cancer."
    Bignell G.R., Barfoot R., Seal S., Collins N., Warren W., Stratton M.R.
    Cancer Res. 58:1384-1386(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  4. "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].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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].
    Tissue: Lung and Uterus.
  7. Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
    Tissue: Renal cell carcinoma.
  8. "Frequent loss of heterozygosity at the 19p13.3 locus without LKB1/STK11 mutations in human carcinoma metastases to the brain."
    Sobottka S.B., Haase M., Fitze G., Hahn M., Schackert H.K., Schackert G.
    J. Neurooncol. 49:187-195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN LUNG CANCER.
  9. "LIP1, a cytoplasmic protein functionally linked to the Peutz-Jeghers syndrome kinase LKB1."
    Smith D.P., Rayter S.I., Niederlander C., Spicer J., Jones C.M., Ashworth A.
    Hum. Mol. Genet. 10:2869-2877(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A TERNARY COMPLEX COMPOSED OF SMAD4 AND STK11IP, INTERACTION WITH SMAD4 AND STK11IP.
  10. "The Peutz-Jegher gene product LKB1 is a mediator of p53-dependent cell death."
    Karuman P., Gozani O., Odze R.D., Zhou X.C., Zhu H., Shaw R., Brien T.P., Bozzuto C.D., Ooi D., Cantley L.C., Yuan J.
    Mol. Cell 7:1307-1319(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, FUNCTION, MUTAGENESIS OF LYS-78 AND THR-189, PHOSPHORYLATION AT THR-189.
  11. "Inactivation of LKB1/STK11 is a common event in adenocarcinomas of the lung."
    Sanchez-Cespedes M., Parrella P., Esteller M., Nomoto S., Trink B., Engles J.M., Westra W.H., Herman J.G., Sidransky D.
    Cancer Res. 62:3659-3662(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN LUNG CANCER.
  12. "Activation of the tumour suppressor kinase LKB1 by the STE20-like pseudokinase STRAD."
    Baas A.F., Boudeau J., Sapkota G.P., Smit L., Medema R., Morrice N.A., Alessi D.R., Clevers H.C.
    EMBO J. 22:3062-3072(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH STRADA, PHOSPHORYLATION AT THR-336 AND THR-363, CHARACTERIZATION OF VARIANT SPORADIC CANCER TYR-176.
  13. "MO25alpha/beta interact with STRADalpha/beta enhancing their ability to bind, activate and localize LKB1 in the cytoplasm."
    Boudeau J., Baas A.F., Deak M., Morrice N.A., Kieloch A., Schutkowski M., Prescott A.R., Clevers H.C., Alessi D.R.
    EMBO J. 22:5102-5114(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-194, IDENTIFICATION IN A COMPLEX WITH STRADA AND CAB39, INTERACTION WITH STRADA; STRADB; CAB39 AND CAB39L.
  14. "Complete polarization of single intestinal epithelial cells upon activation of LKB1 by STRAD."
    Baas A.F., Kuipers J., van der Wel N.N., Batlle E., Koerten H.K., Peters P.J., Clevers H.C.
    Cell 116:457-466(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL POLARITY.
  15. "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: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-194.
  16. "Novel and natural knockout lung cancer cell lines for the LKB1/STK11 tumor suppressor gene."
    Carretero J., Medina P.P., Pio R., Montuenga L.M., Sanchez-Cespedes M.
    Oncogene 23:4037-4040(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN LUNG CANCER.
  17. "Identification of the sucrose non-fermenting related kinase SNRK, as a novel LKB1 substrate."
    Jaleel M., McBride A., Lizcano J.M., Deak M., Toth R., Morrice N.A., Alessi D.R.
    FEBS Lett. 579:1417-1423(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. "LKB1 interacts with and phosphorylates PTEN: a functional link between two proteins involved in cancer predisposing syndromes."
    Mehenni H., Lin-Marq N., Buchet-Poyau K., Reymond A., Collart M.A., Picard D., Antonarakis S.E.
    Hum. Mol. Genet. 14:2209-2219(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PTEN, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT PJS ASN-176.
  19. "LKB1 is recruited to the p21/WAF1 promoter by p53 to mediate transcriptional activation."
    Zeng P.Y., Berger S.L.
    Cancer Res. 66:10701-10708(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TP53.
  20. "Association of LKB1 with a WD-repeat protein WDR6 is implicated in cell growth arrest and p27(Kip1) induction."
    Xie X., Wang Z., Chen Y.
    Mol. Cell. Biochem. 301:115-122(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH WDR6.
  21. Cited for: INVOLVEMENT IN LUNG CANCER.
  22. Cited for: INVOLVEMENT IN LUNG CANCER.
  23. Cited for: INVOLVEMENT IN LUNG CANCER.
  24. "Mutations in the LKB1 tumour suppressor are frequently detected in tumours from Caucasian but not Asian lung cancer patients."
    Koivunen J.P., Kim J., Lee J., Rogers A.M., Park J.O., Zhao X., Naoki K., Okamoto I., Nakagawa K., Yeap B.Y., Meyerson M., Wong K.K., Richards W.G., Sugarbaker D.J., Johnson B.E., Janne P.A.
    Br. J. Cancer 99:245-252(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN LUNG CANCER.
  25. "Protein kinase Czeta-dependent LKB1 serine 428 phosphorylation increases LKB1 nucleus export and apoptosis in endothelial cells."
    Song P., Xie Z., Wu Y., Xu J., Dong Y., Zou M.H.
    J. Biol. Chem. 283:12446-12455(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-428, MUTAGENESIS OF SER-428.
  26. "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: INTERACTION WITH SIRT1, ACETYLATION AT LYS-44; LYS-48; LYS-96; LYS-97; LYS-296; LYS-311; LYS-416; LYS-423 AND LYS-431, MUTAGENESIS OF LYS-44; LYS-48; LYS-96 AND LYS-97.
  27. "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), SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-428, MUTAGENESIS OF SER-428.
  28. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  29. "Spectrum of LKB1, EGFR, and KRAS mutations in Chinese lung adenocarcinomas."
    Gao B., Sun Y., Zhang J., Ren Y., Fang R., Han X., Shen L., Liu X.Y., Pao W., Chen H., Ji H.
    J. Thorac. Oncol. 5:1130-1135(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN LUNG CANCER.
  30. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  31. "A new role of NUAK1: directly phosphorylating p53 and regulating cell proliferation."
    Hou X., Liu J.E., Liu W., Liu C.Y., Liu Z.Y., Sun Z.Y.
    Oncogene 30:2933-2942(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  32. "The role of LKB1 and AMPK in cellular responses to stress and damage."
    Alexander A., Walker C.L.
    FEBS Lett. 585:952-957(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  33. "LKB1 in lung cancerigenesis: a serine/threonine kinase as tumor suppressor."
    Gao Y., Ge G., Ji H.
    Protein Cell 2:99-107(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON INVOLVEMENT IN LUNG CANCER.
  34. Cited for: ENZYME REGULATION, INTERACTION WITH NR4A1, SUBCELLULAR LOCATION.
  35. "Integrin-binding protein nischarin interacts with tumor suppressor liver kinase B1 (LKB1) to regulate cell migration of breast epithelial cells."
    Jain P., Baranwal S., Dong S., Struckhoff A.P., Worthylake R.A., Alahari S.K.
    J. Biol. Chem. 288:15495-15509(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NISCH, SUBCELLULAR LOCATION.
  36. "Phosphorylation of serine 399 in LKB1 protein short form by protein kinase Czeta is required for its nucleocytoplasmic transport and consequent AMP-activated protein kinase (AMPK) activation."
    Zhu H., Moriasi C.M., Zhang M., Zhao Y., Zou M.H.
    J. Biol. Chem. 288:16495-16505(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION (ISOFORM 2), PHOSPHORYLATION (ISOFORM 2).
  37. "Structure of the LKB1-STRAD-MO25 complex reveals an allosteric mechanism of kinase activation."
    Zeqiraj E., Filippi B.M., Deak M., Alessi D.R., van Aalten D.M.
    Science 326:1707-1711(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 43-347 IN COMPLEX WITH STRADA AND CAB39, ENZYME REGULATION, CHARACTERIZATION OF VARIANTS SPORADIC CANCER MET-66; GLY-86; ARG-123; SER-157; ASP-163; PRO-170; SER-171; ARG-174; TYR-176; ASN-177; GLU-181; GLN-199; THR-205; PHE-216; VAL-223; PRO-230; PRO-232; ARG-245; PRO-250; HIS-272; TYR-277; GLN-285 AND SER-315, MUTAGENESIS OF ARG-74; ASP-194 AND PHE-204.
  38. "Loss of LKB1 kinase activity in Peutz-Jeghers syndrome, and evidence for allelic and locus heterogeneity."
    Mehenni H., Gehrig C., Nezu J., Oku A., Shimane M., Rossier C., Guex N., Blouin J.L., Scott H.S., Antonarakis S.E.
    Am. J. Hum. Genet. 63:1641-1650(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PJS 50-LEU--ASP-53 DEL; ASN-176 AND CYS-308, CHARACTERIZATION OF VARIANTS PJS PRO-67; ASN-176 AND CYS-308, MUTAGENESIS OF LYS-78.
  39. "Somatic mutations in LKB1 are rare in sporadic colorectal and testicular tumors."
    Avizienyte E., Roth S., Loukola A., Hemminki A., Lothe R.A., Stenwig A.E., Fossaa S.D., Salovaara R., Aaltonen L.A.
    Cancer Res. 58:2087-2090(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT TGCT ASP-163.
  40. "Frequent somatic mutations in serine/threonine kinase 11/Peutz-Jeghers syndrome gene in left-sided colon cancer."
    Dong S.M., Kim K.M., Kim S.Y., Shin M.S., Na E.Y., Lee S.H., Park W.S., Yoo N.J., Jang J.J., Yoon C.Y., Kim J.W., Kim S.Y., Yang Y.M., Kim S.H., Kim C.S., Lee J.Y.
    Cancer Res. 58:3787-3790(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS COLORECTAL CANCER SER-171; LYS-199; ASN-208; ASP-215; LEU-354 AND MET-367.
  41. "STK11 mutations in Peutz-Jeghers syndrome and sporadic colon cancer."
    Resta N., Simone C., Mareni C., Montera M., Gentile M., Susca F., Gristina R., Pozzi S., Bertario L., Bufo P., Carlomagno N., Ingrosso M., Rossini F.P., Tenconi R., Guanti G.
    Cancer Res. 58:4799-4801(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT COLORECTAL CANCER HIS-314.
  42. "Nine novel germline mutations of STK11 in ten families with Peutz-Jeghers syndrome."
    Nakagawa H., Koyama K., Miyoshi Y., Ando H., Baba S., Watatani M., Yasutomi M., Matsuura N., Monden M., Nakamura Y.
    Hum. Genet. 103:168-172(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PJS ASN-247 DEL.
  43. "Mutations of the STK11 gene in sporadic gastric carcinoma."
    Park W.S., Moon Y.W., Yang Y.M., Kim Y.S., Kim Y.D., Fuller B.G., Vortmeyer A.O., Fogt F., Lubensky I.A., Zhuang Z.
    Int. J. Oncol. 13:601-604(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT GASTRIC CARCINOMA LEU-324.
  44. Cited for: VARIANTS PJS PRO-67 AND 303-ILE--GLN-306 DELINS ASN.
  45. Cited for: VARIANT LUNG CANCER VAL-194.
  46. Cited for: VARIANTS PJS 162-ASN--MET-164; ASN-194 AND LYS-297.
  47. "Mutations and impaired function of LKB1 in familial and non-familial Peutz-Jeghers syndrome and a sporadic testicular cancer."
    Ylikorkala A., Avizienyte E., Tomlinson I.P., Tiainen M., Roth S., Loukola A., Hemminki A., Johansson M., Sistonen P., Markie D., Neale K., Phillips R., Zauber P., Twama T., Sampson J., Jaervinen H., Maekelae T.P., Aaltonen L.A.
    Hum. Mol. Genet. 8:45-51(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANT TGCT ASP-163.
  48. "Mutational analysis of STK11 gene in ovarian carcinomas."
    Nishioka Y., Kobayashi K., Sagae S., Sugimura M., Ishioka S., Nagata M., Terasawa K., Tokino T., Kudo R.
    Jpn. J. Cancer Res. 90:629-632(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT OVARIAN CARCINOMA LEU-281.
  49. "Somatic mutations in the Peutz-Jeghers (LKB1/STKII) gene in sporadic malignant melanomas."
    Rowan A., Bataille V., MacKie R., Healy E., Bicknell D., Bodmer W., Tomlinson I.
    J. Invest. Dermatol. 112:509-511(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MELANOMA ASP-49 AND ARG-135.
  50. "Somatic mutation of the Peutz-Jeghers syndrome gene, LKB1/STK11, in malignant melanoma."
    Guldberg P., thor Straten P., Ahrenkiel V., Seremet T., Kirkin A.F., Zeuthen J.
    Oncogene 18:1777-1780(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MELANOMA TYR-194.
  51. "Mutation analysis of the STK11/LKB1 gene and clinical characteristics of an Australian series of Peutz-Jeghers syndrome patients."
    Scott R.J., Crooks R., Meldrum C.J., Thomas L., Smith C.J.A., Mowat D., McPhillips M., Spigelman A.D.
    Clin. Genet. 62:282-287(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PJS CYS-239 AND SER-315.
  52. "Mutations in the STK11 gene characterize minimal deviation adenocarcinoma of the uterine cervix."
    Kuragaki C., Enomoto T., Ueno Y., Sun H., Fujita M., Nakashima R., Ueda Y., Wada H., Murata Y., Toki T., Konishi I., Fujii S.
    Lab. Invest. 83:35-45(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CERVICAL CANCER LYS-14; PRO-160 AND LEU-231, VARIANT CERVICAL CARCINOMA MET-66.
  53. "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: VARIANT [LARGE SCALE ANALYSIS] LYS-87.
  54. "A novel de novo mutation in LKB1 gene in a Chinese Peutz Jeghers syndrome patient significantly diminished p53 activity."
    Liu L., Du X., Nie J.
    Clin. Res. Hepatol. Gastroenterol. 35:221-226(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PJS GLY-16.

Entry informationi

Entry nameiSTK11_HUMAN
AccessioniPrimary (citable) accession number: Q15831
Secondary accession number(s): B2RBX7, E7EW76
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 164 of the entry and version 1 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

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3