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Q15831 (STK11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 161. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·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
Short name=LKB1
Short name=hLKB1
Renal carcinoma antigen NY-REN-19
Gene names
Name:STK11
Synonyms:LKB1, PJS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length433 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 and phosphorylation may be indirect and mediated by downstream STK11/LKB1 kinase NUAK1 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.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.28

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.15

Cofactor

Magnesium or Manganese.

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. Ref.31 Ref.33

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. Interacts with NISCH; this interaction may increase STK11 activity. Ref.9 Ref.12 Ref.13 Ref.18 Ref.19 Ref.31 Ref.32

Subcellular location

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 mitochondrion during apoptosis. Ref.10 Ref.12 Ref.13 Ref.18 Ref.24 Ref.31 Ref.32

Tissue specificity

Ubiquitously expressed. Strongest expression in testis and fetal liver.

Post-translational modification

Phosphorylated by ATM at Thr-363 following ionizing radiations (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. Ref.10 Ref.12 Ref.24

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.37 Ref.39 Ref.41 Ref.46 Ref.49

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.
Note: The gene represented in this entry may be involved in disease pathogenesis. Ref.34 Ref.42

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.

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
Polymorphism
   DiseaseDisease mutation
Tumor suppressor
   LigandATP-binding
Magnesium
Manganese
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMLipoprotein
Methylation
Palmitate
Phosphoprotein
Prenylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGolgi localization

Inferred from electronic annotation. Source: Ensembl

T cell receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

TCR signalosome assembly

Inferred from electronic annotation. Source: Ensembl

activation of protein kinase activity

Inferred from direct assay Ref.24. Source: MGI

anoikis

Inferred from mutant phenotype PubMed 19622832. Source: BHF-UCL

autophagy

Inferred from electronic annotation. Source: UniProtKB-KW

axonogenesis

Inferred from electronic annotation. Source: Ensembl

canonical Wnt signaling pathway

Inferred from electronic annotation. Source: Ensembl

cell cycle arrest

Inferred from direct assay Ref.12Ref.19. Source: UniProtKB

cellular response to DNA damage stimulus

Inferred from electronic annotation. Source: UniProtKB-KW

energy reserve metabolic process

Traceable author statement. Source: Reactome

establishment of cell polarity

Inferred from sequence or structural similarity. Source: UniProtKB

glucose homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

insulin receptor signaling pathway

Traceable author statement. Source: Reactome

intrinsic apoptotic signaling pathway by p53 class mediator

Inferred from direct assay Ref.10. Source: UniProtKB

negative regulation of cell growth

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell proliferation

Inferred from mutant phenotype Ref.19. Source: UniProtKB

negative regulation of epithelial cell proliferation involved in prostate gland development

Inferred from electronic annotation. Source: Ensembl

positive regulation of axonogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of gluconeogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from electronic annotation. Source: Ensembl

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 electronic annotation. Source: Ensembl

protein autophosphorylation

Inferred from direct assay Ref.10. Source: UniProtKB

protein heterooligomerization

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Inferred from direct assay Ref.12. Source: UniProtKB

regulation of Wnt signaling pathway

Inferred from electronic annotation. Source: Ensembl

regulation of cell growth

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of fatty acid biosynthetic process

Traceable author statement. Source: Reactome

regulation of protein kinase B signaling

Inferred from electronic annotation. Source: Ensembl

response to glucagon

Inferred from electronic annotation. Source: Ensembl

response to ionizing radiation

Inferred from sequence or structural similarity. Source: UniProtKB

response to lipid

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

spermatid development

Inferred from electronic annotation. Source: Ensembl

tissue homeostasis

Inferred from electronic annotation. Source: Ensembl

vasculature development

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentTCR signalosome

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay Ref.24. Source: MGI

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

membrane

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrion

Inferred from direct assay Ref.10. Source: UniProtKB

nucleus

Inferred from direct assay Ref.24. Source: MGI

   Molecular_functionATP binding

Inferred from direct assay Ref.12. Source: UniProtKB

magnesium ion binding

Inferred from direct assay Ref.12. Source: UniProtKB

p53 binding

Inferred from direct assay Ref.10. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.19. Source: UniProtKB

protein kinase activator activity

Inferred from direct assay Ref.33. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from direct assay Ref.10Ref.12Ref.33. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q15831-1)

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 (identifier: Q15831-2)

Also known as: LKB1(S);

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 430430Serine/threonine-protein kinase STK11
PRO_0000086699
Propeptide431 – 4333Removed in mature form By similarity
PRO_0000422300

Regions

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

Sites

Active site1761Proton acceptor
Binding site781ATP Probable

Amino acid modifications

Modified residue311Phosphoserine By similarity
Modified residue1891Phosphothreonine; by autocatalysis Ref.10
Modified residue3251Phosphoserine By similarity
Modified residue3361Phosphothreonine; by autocatalysis Ref.12
Modified residue3631Phosphothreonine; by ATM and autocatalysis Ref.12
Modified residue4281Phosphoserine; by PKA and RPS6KA1 Ref.24
Modified residue4301Cysteine methyl ester By similarity
Lipidation4181S-palmitoyl cysteine By similarity
Lipidation4301S-farnesyl cysteine By similarity

Natural variations

Alternative sequence371 – 43363QVPEE…ACKQQ → GEEASEAGLRAERGLQKSEG SDLSGEEASRPAPQ in isoform 2.
VSP_041746
Natural variant141E → K in cervical cancer; somatic mutation. Ref.47
VAR_065627
Natural variant161E → G in PJS. Ref.49
VAR_065628
Natural variant491Y → D in melanoma; sporadic malignant; somatic mutation. Ref.44
VAR_033138
Natural variant661V → M in cervical carcinoma; somatic mutation. Ref.33 Ref.47
VAR_065629
Natural variant671L → P in PJS. Ref.39
VAR_006202
Natural variant861R → G in sporadic cancer; somatic mutation; no effect on kinase activity nor in heterotrimeric complex assembly with STRADA and CAB39.
VAR_065630
Natural variant871R → K in a metastatic melanoma sample; somatic mutation. Ref.48
VAR_041139
Natural variant1231Q → R in sporadic cancer; somatic mutation; no effect on kinase activity nor in heterotrimeric complex assembly with STRADA and CAB39.
VAR_065631
Natural variant1351G → R in melanoma; sporadic malignant; somatic mutation. Ref.44
VAR_033139
Natural variant1571F → S in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39.
VAR_065632
Natural variant1601L → P in cervical cancer; somatic mutation. Ref.47
VAR_065633
Natural variant162 – 1643DGL → NDM in PJS.
VAR_007920
Natural variant1631G → 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. Ref.33 Ref.34 Ref.42
VAR_033140
Natural variant1701Q → P in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39.
VAR_065634
Natural variant1711G → S in colorectal cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39. Ref.33 Ref.35
VAR_065635
Natural variant1741H → R in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39.
VAR_065636
Natural variant1761D → Y in sporadic cancer; somatic mutation; Loss of kinase activity.
VAR_065637
Natural variant1771I → N in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39.
VAR_065638
Natural variant1811N → E in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39; requires 2 nucleotide substitutions.
VAR_065639
Natural variant1941D → N in PJS. Ref.41
VAR_007921
Natural variant1941D → V in lung cancer; somatic mutation. Ref.40
VAR_065640
Natural variant1941D → Y in melanoma; sporadic malignant; somatic mutation. Ref.45
VAR_033141
Natural variant1991E → K in colorectal cancer; somatic mutation; impaired kinase activity. Ref.35
VAR_065641
Natural variant1991E → Q in sporadic cancer; somatic mutation; does not affect kinase activity.
VAR_065642
Natural variant2051A → T in sporadic cancer; somatic mutation; no effect heterotrimeric complex assembly with STRADA and CAB39.
VAR_065643
Natural variant2081D → N in colorectal cancer; somatic mutation; no effect heterotrimeric complex assembly with STRADA and CAB39. Ref.35
VAR_065644
Natural variant2151G → D in colorectal cancer; somatic mutation. Ref.35
VAR_065645
Natural variant2161S → F in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39.
VAR_065646
Natural variant2231E → V in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39.
VAR_065647
Natural variant2301T → P in sporadic cancer; somatic mutation; no effect heterotrimeric complex assembly with STRADA and CAB39.
VAR_065648
Natural variant2311F → L in cervical cancer; somatic mutation. Ref.47
VAR_065649
Natural variant2321S → P in sporadic cancer; somatic mutation; no effect heterotrimeric complex assembly with STRADA and CAB39.
VAR_065650
Natural variant2391W → C in PJS; late onset suggests reduced penetrance. Ref.46
VAR_033142
Natural variant2451L → R in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39.
VAR_065651
Natural variant2471Missing in PJS. Ref.37
VAR_006203
Natural variant2501T → P in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39.
VAR_065652
Natural variant2721Y → H in sporadic cancer; somatic mutation; no effect on kinase activity nor in heterotrimeric complex assembly with STRADA and CAB39.
VAR_065653
Natural variant2771D → Y in sporadic cancer; somatic mutation; no effect on kinase activity nor in heterotrimeric complex assembly with STRADA and CAB39.
VAR_065654
Natural variant2811P → L in ovarian carcinoma; somatic mutation. Ref.43
VAR_065655
Natural variant2851L → Q in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39.
VAR_065656
Natural variant2971R → K in PJS. Ref.41
VAR_007922
Natural variant303 – 3064IRQH → N in PJS.
VAR_033143
Natural variant3141P → H in colorectal cancer; no effect heterotrimeric complex assembly with STRADA and CAB39. Ref.36
VAR_065657
Natural variant3151P → S in PJS; pathogenicity uncertain; no effect heterotrimeric complex assembly with STRADA and CAB39. Ref.33 Ref.46
VAR_033144
Natural variant3241P → L in gastric carcinoma; no effect heterotrimeric complex assembly with STRADA and CAB39. Ref.38
VAR_065658
Natural variant3541F → L in colorectal cancer; somatic mutation. Ref.35
VAR_065659
Natural variant3671T → M in colorectal cancer; somatic mutation. Ref.35
VAR_065660

Experimental info

Mutagenesis741R → A: Impaired formation of a heterotrimeric complex with STRADA and CAB39; when associated with A-204. Ref.33
Mutagenesis781K → M: Loss of kinase activity, leading to reduced autophosphorylation and acting as a dominant-negative mutant. Ref.10
Mutagenesis1891T → A: Reduced phosphorylation. Ref.10
Mutagenesis1941D → A: Loss of kinase activity. Ref.13 Ref.15 Ref.33
Mutagenesis2041F → A: No effect. Impaired formation of a heterotrimeric complex with STRADA and CAB39; when associated with A-74. Ref.33
Mutagenesis4281S → A or E: No effect on kinase activity. Ref.24

Secondary structure

............................................... 433
Helix Strand Turn

Details...

Sequences

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

Last modified November 1, 1996. Version 1.
Checksum: 6DF4C37AB7A89569

FASTA43348,636
        10         20         30         40         50         60 
MEVVDPQQLG MFTEGELMSV GMDTFIHRID STEVIYQPRR KRAKLIGKYL MGDLLGEGSY 

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

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

       190        200        210        220        230        240 
NLLLTTGGTL KISDLGVAEA LHPFAADDTC RTSQGSPAFQ PPEIANGLDT FSGFKVDIWS 

       250        260        270        280        290        300 
AGVTLYNITT GLYPFEGDNI YKLFENIGKG SYAIPGDCGP PLSDLLKGML EYEPAKRFSI 

       310        320        330        340        350        360 
RQIRQHSWFR KKHPPAEAPV PIPPSPDTKD RWRSMTVVPY LEDLHGADED EDLFDIEDDI 

       370        380        390        400        410        420 
IYTQDFTVPG QVPEEEASHN GQRRGLPKAV CMNGTEAAQL STKSRAEGRA PNPARKACSA 

       430 
SSKIRRLSAC KQQ 

« Hide

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

Checksum: 6E4F3920F8F873DD
Show »

FASTA40445,387

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Antigens recognized by autologous antibody in patients with renal-cell carcinoma."
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., Old L.J.
Int. J. Cancer 83:456-464(1999) [PubMed] [Europe PMC] [Abstract]
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, AUTOPHOSPHORYLATION 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 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.
[19]"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.
[20]"LKB1 gene mutations in Japanese lung cancer patients."
Onozato R., Kosaka T., Achiwa H., Kuwano H., Takahashi T., Yatabe Y., Mitsudomi T.
Cancer Sci. 98:1747-1751(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN LUNG CANCER.
[21]"LKB1 modulates lung cancer differentiation and metastasis."
Ji H., Ramsey M.R., Hayes D.N., Fan C., McNamara K., Kozlowski P., Torrice C., Wu M.C., Shimamura T., Perera S.A., Liang M.C., Cai D., Naumov G.N., Bao L., Contreras C.M., Li D., Chen L., Krishnamurthy J. expand/collapse author list , Koivunen J., Chirieac L.R., Padera R.F., Bronson R.T., Lindeman N.I., Christiani D.C., Lin X., Shapiro G.I., Janne P.A., Johnson B.E., Meyerson M., Kwiatkowski D.J., Castrillon D.H., Bardeesy N., Sharpless N.E., Wong K.K.
Nature 448:807-810(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN LUNG CANCER.
[22]"Prevalence and specificity of LKB1 genetic alterations in lung cancers."
Matsumoto S., Iwakawa R., Takahashi K., Kohno T., Nakanishi Y., Matsuno Y., Suzuki K., Nakamoto M., Shimizu E., Minna J.D., Yokota J.
Oncogene 26:5911-5918(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN LUNG CANCER.
[23]"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.
[24]"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.
[25]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"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.
[27]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"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.
[29]"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.
[30]"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.
[31]"The orphan nuclear receptor Nur77 regulates LKB1 localization and activates AMPK."
Zhan Y.Y., Chen Y., Zhang Q., Zhuang J.J., Tian M., Chen H.Z., Zhang L.R., Zhang H.K., He J.P., Wang W.J., Wu R., Wang Y., Shi C., Yang K., Li A.Z., Xin Y.Z., Li T.Y., Yang J.Y. expand/collapse author list , Zheng Z.H., Yu C.D., Lin S.C., Chang C., Huang P.Q., Lin T., Wu Q.
Nat. Chem. Biol. 8:897-904(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, INTERACTION WITH NR4A1, SUBCELLULAR LOCATION.
[32]"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.
[33]"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.
[34]"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.
[35]"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.
[36]"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.
[37]"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.
[38]"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.
[39]"A serine/threonine kinase gene defective in Peutz-Jeghers syndrome."
Hemminki A., Markie D., Tomlinson I., Avizienyte E., Roth S., Loukola A., Bignell G., Warren W., Aminoff M., Hoeglund P., Jaervinen H., Kristo P., Pelin K., Ridanpaeae M., Salovaara R., Toro T., Bodmer W., Olschwang S. expand/collapse author list , Olsen A.S., Stratton M.R., de la Chapelle A., Aaltonen L.A.
Nature 391:184-187(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PJS PRO-67 AND 303-ILE--GLN-306 DELINS ASN.
[40]"LKB1 somatic mutations in sporadic cancers."
Avizienyte E., Loukola A., Roth S., Hemminki A., Tarkkanen M., Salovaara R., Arola J., Butzow R., Husgafvel-Pursiainen K., Kokkola A., Jarvinen H., Aaltonen L.A.
Am. J. Pathol. 154:677-681(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LUNG CANCER VAL-194.
[41]"Novel mutations in the LKB1/STK11 gene in Dutch Peutz-Jeghers families."
Westerman A.M., Entius M.M., Boor P.P.C., Koole R., de Baar E., Offerhaus G.J.A., Lubinski J., Lindhout D., Halley D.J.J., de Rooij F.W.M., Wilson J.H.P.
Hum. Mutat. 13:476-481(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PJS 162-ASN--MET-164; ASN-194 AND LYS-297.
[42]"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.
[43]"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.
[44]"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.
[45]"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.
[46]"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.
[47]"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.
[48]"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. expand/collapse author list , 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.
[49]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U63333 mRNA. Translation: AAB05809.1.
AF035625 mRNA. Translation: AAC39527.1.
AF032984 Genomic DNA. Translation: AAB97833.1.
AF055327 expand/collapse EMBL AC list , 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.
CCDSCCDS45896.1. [Q15831-1]
RefSeqNP_000446.1. NM_000455.4. [Q15831-1]
XP_005259675.1. XM_005259618.2. [Q15831-2]
UniGeneHs.515005.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2WTKX-ray2.65C/F43-347[»]
ProteinModelPortalQ15831.
SMRQ15831. Positions 22-369.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112670. 34 interactions.
DIPDIP-31317N.
IntActQ15831. 37 interactions.
MINTMINT-204048.
STRING9606.ENSP00000324856.

Chemistry

BindingDBQ15831.
ChEMBLCHEMBL5606.
GuidetoPHARMACOLOGY2212.

PTM databases

PhosphoSiteQ15831.

Polymorphism databases

DMDM3024670.

Proteomic databases

MaxQBQ15831.
PaxDbQ15831.
PRIDEQ15831.

Protocols and materials databases

DNASU6794.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000326873; ENSP00000324856; ENSG00000118046. [Q15831-1]
GeneID6794.
KEGGhsa:6794.
UCSCuc002lrl.1. human. [Q15831-1]

Organism-specific databases

CTD6794.
GeneCardsGC19P001205.
GeneReviewsSTK11.
HGNCHGNC:11389. STK11.
HPACAB016231.
CAB022105.
HPA017254.
MIM175200. phenotype.
273300. phenotype.
602216. gene.
neXtProtNX_Q15831.
Orphanet2869. Peutz-Jeghers syndrome.
PharmGKBPA36198.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000007002.
HOVERGENHBG054467.
InParanoidQ15831.
KOK07298.
OMAPQQLGMF.
OrthoDBEOG7F7W92.
PhylomeDBQ15831.
TreeFamTF105322.

Enzyme and pathway databases

BRENDA2.7.11.1. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
SignaLinkQ15831.

Gene expression databases

ArrayExpressQ15831.
BgeeQ15831.
CleanExHS_STK11.
GenevestigatorQ15831.

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

ChiTaRSSTK11. human.
EvolutionaryTraceQ15831.
GeneWikiSTK11.
GenomeRNAi6794.
NextBio26541.
PROQ15831.
SOURCESearch...

Entry information

Entry nameSTK11_HUMAN
AccessionPrimary (citable) accession number: Q15831
Secondary accession number(s): B2RBX7, E7EW76
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 161 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM