Q15831 (STK11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	STK11
Synonyms:	LKB1, PJS

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	433 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Ref.31
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. Ref.9 Ref.12 Ref.13 Ref.18 Ref.19
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
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.35 Ref.37 Ref.39 Ref.44 Ref.47 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.32 Ref.40 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 process	Apoptosis Autophagy Cell cycle DNA damage
Cellular component	Cytoplasm Membrane Mitochondrion Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Tumor suppressor
Ligand	ATP-binding Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Lipoprotein Methylation Palmitate Phosphoprotein Prenylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Golgi localization Inferred from electronic annotation. Source: Compara anoikis Inferred from mutant phenotype PubMed 19622832. Source: BHF-UCL autophagy Inferred from electronic annotation. Source: UniProtKB-KW axonogenesis Inferred from electronic annotation. Source: Compara canonical Wnt receptor signaling pathway Inferred from electronic annotation. Source: Compara cell cycle arrest Inferred from direct assay Ref.12Ref.19. Source: UniProtKB 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: Compara positive regulation of axonogenesis Inferred from electronic annotation. Source: Compara positive regulation of gluconeogenesis Inferred from electronic annotation. Source: Compara positive regulation of transforming growth factor beta receptor signaling pathway Inferred from mutant phenotype PubMed 18311138. Source: BHF-UCL protein autophosphorylation Inferred from direct assay Ref.10. Source: UniProtKB protein heterooligomerization Inferred from electronic annotation. Source: Compara regulation of Wnt receptor signaling pathway Inferred from electronic annotation. Source: Compara regulation of fatty acid biosynthetic process Traceable author statement. Source: Reactome regulation of fatty acid oxidation Traceable author statement. Source: Reactome regulation of protein kinase B signaling cascade Inferred from electronic annotation. Source: Compara response to DNA damage stimulus Inferred from electronic annotation. Source: UniProtKB-KW response to glucagon stimulus Inferred from electronic annotation. Source: Compara response to ionizing radiation Inferred from sequence or structural similarity. Source: UniProtKB response to lipid Inferred from electronic annotation. Source: Compara small molecule metabolic process Traceable author statement. Source: Reactome spermatid development Inferred from electronic annotation. Source: Compara tissue homeostasis Inferred from electronic annotation. Source: Compara vasculature development Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytoplasm Inferred from direct assay Ref.24. Source: UniProtKB cytosol Inferred from sequence or structural similarity. Source: UniProtKB membrane Inferred from sequence or structural similarity. Source: UniProtKB mitochondrion Inferred from direct assay Ref.10. Source: UniProtKB nucleus Inferred from direct assay Ref.12Ref.24. Source: UniProtKB protein complex Inferred from electronic annotation. Source: Compara
Molecular_function	ATP 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 kinase activator activity Inferred from direct assay Ref.31. Source: UniProtKB protein serine/threonine kinase activity Inferred from direct assay Ref.10Ref.12Ref.31. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		4	EBI-306838,EBI-306838
CAB39	Q9Y376	4	EBI-306838,EBI-306905
HSP90AB1	P08238	3	EBI-306838,EBI-352572
MARK4	Q96L34	2	EBI-306838,EBI-302319
STRADA	Q7RTN6	9	EBI-306838,EBI-1109114
STRADB	Q9C0K7	6	EBI-306838,EBI-306893
TNIP2	Q8NFZ5	5	EBI-306838,EBI-359372
WDR6	Q9NNW5	3	EBI-306838,EBI-1568315

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 430

430

Serine/threonine-protein kinase STK11

PRO_0000086699

Propeptide

431 – 433

3

Removed in mature form By similarity

PRO_0000422300

Regions

Domain

49 – 309

261

Protein kinase

Nucleotide binding

55 – 63

9

ATP By similarity

Sites

Active site

176

1

Proton acceptor

Binding site

78

1

ATP Probable

Amino acid modifications

Modified residue

31

1

Phosphoserine By similarity

Modified residue

189

1

Phosphothreonine; by autocatalysis Ref.10

Modified residue

325

1

Phosphoserine By similarity

Modified residue

336

1

Phosphothreonine; by autocatalysis Ref.12

Modified residue

363

1

Phosphothreonine; by ATM and autocatalysis Ref.12

Modified residue

428

1

Phosphoserine; by PKA and RPS6KA1 Ref.24

Modified residue

430

1

Cysteine methyl ester By similarity

Lipidation

418

1

S-palmitoyl cysteine By similarity

Lipidation

430

1

S-farnesyl cysteine By similarity

Natural variations

Alternative sequence

371 – 433

63

QVPEE…ACKQQ → GEEASEAGLRAERGLQKSEG SDLSGEEASRPAPQ in isoform 2.

VSP_041746

Natural variant

14

1

E → K in cervical cancer; somatic mutation. Ref.45

VAR_065627

Natural variant

16

1

E → G in PJS. Ref.47

VAR_065628

Natural variant

49

1

Y → D in melanoma; sporadic malignant; somatic mutation. Ref.42

VAR_033138

Natural variant

66

1

V → M in cervical carcinoma; somatic mutation. Ref.31 Ref.45

VAR_065629

Natural variant

67

1

L → P in PJS. Ref.37

VAR_006202

Natural variant

86

1

R → G in sporadic cancer; somatic mutation; no effect on kinase activity nor in heterotrimeric complex assembly with STRADA and CAB39.

VAR_065630

Natural variant

87

1

R → K in a metastatic melanoma sample; somatic mutation. Ref.46

VAR_041139

Natural variant

123

1

Q → R in sporadic cancer; somatic mutation; no effect on kinase activity nor in heterotrimeric complex assembly with STRADA and CAB39.

VAR_065631

Natural variant

135

1

G → R in melanoma; sporadic malignant; somatic mutation. Ref.42

VAR_033139

Natural variant

157

1

F → S in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39.

VAR_065632

Natural variant

160

1

L → P in cervical cancer; somatic mutation. Ref.45

VAR_065633

Natural variant

162 – 164

3

DGL → NDM in PJS.

VAR_007920

Natural variant

163

1

G → 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.31 Ref.32 Ref.40

VAR_033140

Natural variant

170

1

Q → P in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39.

VAR_065634

Natural variant

171

1

G → S in colorectal cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39. Ref.31 Ref.33

VAR_065635

Natural variant

174

1

H → R in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39.

VAR_065636

Natural variant

176

1

D → Y in sporadic cancer; somatic mutation; Loss of kinase activity.

VAR_065637

Natural variant

177

1

I → N in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39.

VAR_065638

Natural variant

181

1

N → E in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39; requires 2 nucleotide substitutions.

VAR_065639

Natural variant

194

1

D → N in PJS. Ref.39

VAR_007921

Natural variant

194

1

D → V in lung cancer; somatic mutation. Ref.38

VAR_065640

Natural variant

194

1

D → Y in melanoma; sporadic malignant; somatic mutation. Ref.43

VAR_033141

Natural variant

199

1

E → K in colorectal cancer; somatic mutation; impaired kinase activity. Ref.33

VAR_065641

Natural variant

199

1

E → Q in sporadic cancer; somatic mutation; does not affect kinase activity.

VAR_065642

Natural variant

205

1

A → T in sporadic cancer; somatic mutation; no effect heterotrimeric complex assembly with STRADA and CAB39.

VAR_065643

Natural variant

208

1

D → N in colorectal cancer; somatic mutation; no effect heterotrimeric complex assembly with STRADA and CAB39. Ref.33

VAR_065644

Natural variant

215

1

G → D in colorectal cancer; somatic mutation. Ref.33

VAR_065645

Natural variant

216

1

S → F in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39.

VAR_065646

Natural variant

223

1

E → V in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39.

VAR_065647

Natural variant

230

1

T → P in sporadic cancer; somatic mutation; no effect heterotrimeric complex assembly with STRADA and CAB39.

VAR_065648

Natural variant

231

1

F → L in cervical cancer; somatic mutation. Ref.45

VAR_065649

Natural variant

232

1

S → P in sporadic cancer; somatic mutation; no effect heterotrimeric complex assembly with STRADA and CAB39.

VAR_065650

Natural variant

239

1

W → C in PJS; late onset suggests reduced penetrance. Ref.44

VAR_033142

Natural variant

245

1

L → R in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39.

VAR_065651

Natural variant

247

1

Missing in PJS. Ref.35

VAR_006203

Natural variant

250

1

T → P in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39.

VAR_065652

Natural variant

272

1

Y → H in sporadic cancer; somatic mutation; no effect on kinase activity nor in heterotrimeric complex assembly with STRADA and CAB39.

VAR_065653

Natural variant

277

1

D → Y in sporadic cancer; somatic mutation; no effect on kinase activity nor in heterotrimeric complex assembly with STRADA and CAB39.

VAR_065654

Natural variant

281

1

P → L in ovarian carcinoma; somatic mutation. Ref.41

VAR_065655

Natural variant

285

1

L → Q in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39.

VAR_065656

Natural variant

297

1

R → K in PJS. Ref.39

VAR_007922

Natural variant

303 – 306

4

IRQH → N in PJS.

VAR_033143

Natural variant

314

1

P → H in colorectal cancer; no effect heterotrimeric complex assembly with STRADA and CAB39. Ref.34

VAR_065657

Natural variant

315

1

P → S in PJS; pathogenicity uncertain; no effect heterotrimeric complex assembly with STRADA and CAB39. Ref.31 Ref.44

VAR_033144

Natural variant

324

1

P → L in gastric carcinoma; no effect heterotrimeric complex assembly with STRADA and CAB39. Ref.36

VAR_065658

Natural variant

354

1

F → L in colorectal cancer; somatic mutation. Ref.33

VAR_065659

Natural variant

367

1

T → M in colorectal cancer; somatic mutation. Ref.33

VAR_065660

Experimental info

Mutagenesis

74

1

R → A: Impaired formation of a heterotrimeric complex with STRADA and CAB39; when associated with A-204. Ref.31

Mutagenesis

78

1

K → M: Loss of kinase activity, leading to reduced autophosphorylation and acting as a dominant-negative mutant. Ref.10

Mutagenesis

189

1

T → A: Reduced phosphorylation. Ref.10

Mutagenesis

194

1

D → A: Loss of kinase activity. Ref.13 Ref.15 Ref.31

Mutagenesis

204

1

F → A: No effect. Impaired formation of a heterotrimeric complex with STRADA and CAB39; when associated with A-74. Ref.31

Mutagenesis

428

1

S → A or E: No effect on kinase activity. Ref.24

Secondary structure

1

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433

Helix Strand Turn

Details...

Beta strand

54 – 57

4

Beta strand

62 – 68

7

Turn

69 – 71

3

Beta strand

74 – 80

7

Helix

82 – 87

6

Helix

91 – 102

12

Beta strand

113 – 118

6

Beta strand

125 – 130

6

Beta strand

133 – 135

3

Helix

136 – 142

7

Helix

150 – 169

20

Helix

179 – 181

3

Beta strand

182 – 184

3

Beta strand

190 – 192

3

Helix

217 – 219

3

Helix

222 – 225

4

Beta strand

231 – 233

3

Helix

234 – 250

17

Helix

260 – 269

10

Beta strand

276 – 278

3

Helix

280 – 289

10

Turn

294 – 296

3

Helix

300 – 305

6

Helix

307 – 310

4

Helix

339 – 341

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (LKB1(L)) [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 6DF4C37AB7A89569	FASTA	433	48,636
	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
	Isoform 2 (LKB1(S)) [UniParc]. Checksum: 6E4F3920F8F873DD	FASTA	404	45,387
	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 IYTQDFTVPG GEEASEAGLR AERGLQKSEG SDLSGEEASR PAPQ

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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. , 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]	"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.
[32]	"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.
[33]	"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.
[34]	"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.
[35]	"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.
[36]	"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.
[37]	"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. , 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.
[38]	"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.
[39]	"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.
[40]	"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.
[41]	"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.
[42]	"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.
[43]	"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.
[44]	"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.
[45]	"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.
[46]	"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.
[47]	"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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

Wikipedia

PJS entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI01024704.
IPI01024909.

RefSeq

NP_000446.1. NM_000455.4.

UniGene

Hs.515005.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2WTK	X-ray	2.65	C/F	43-347	[»]

ProteinModelPortal

Q15831.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31317N.

IntAct

Q15831. 31 interactions.

MINT

MINT-204048.

STRING

9606.ENSP00000324856.

PTM databases

PhosphoSite

Q15831.

Polymorphism databases

DMDM

3024670.

Proteomic databases

PaxDb

Q15831.

PRIDE

Q15831.

Protocols and materials databases

DNASU

6794.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000326873; ENSP00000324856; ENSG00000118046.

GeneID

6794.

KEGG

hsa:6794.

UCSC

uc002lrl.1. human.

Organism-specific databases

CTD

6794.

GeneCards

GC19P001205.

HGNC

HGNC:11389. STK11.

HPA

CAB016231.
CAB022105.
HPA017254.

MIM

175200. phenotype.
273300. phenotype.
602216. gene.

neXtProt

NX_Q15831.

Orphanet

2869. Peutz-Jeghers syndrome.

PharmGKB

PA36198.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000007002.

HOVERGEN

HBG054467.

InParanoid

Q15831.

KO

K07298.

OMA

FRKKHPL.

OrthoDB

EOG49CQ7R.

Enzyme and pathway databases

BRENDA

2.7.11.1. 2681.

Reactome

REACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_11163. Activated AMPK stimulates fatty-acid oxidation in muscle.

Gene expression databases

ArrayExpress

Q15831.

Bgee

Q15831.

CleanEx

HS_STK11.

Genevestigator

Q15831.

GermOnline

ENSG00000118046. Homo sapiens.

Family and domain databases

InterPro

IPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]

PANTHER

PTHR24347. PTHR24347. 1 hit.

Pfam

PF00069. Pkinase. 1 hit.
[Graphical view]

SMART

SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

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Other

BindingDB

Q15831.

ChEMBL

CHEMBL5606.

ChiTaRS

STK11. human.

EvolutionaryTrace

Q15831.

GenomeRNAi

6794.

NextBio

26541.

SOURCE

Search...

Entry information

Entry name

STK11_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 148 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.