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Entry version 208 (13 Feb 2019)
Sequence version 1 (01 Nov 1996)
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Protein

Serine/threonine-protein kinase STK11

Gene

STK11

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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). Regulates UV radiation-induced DNA damage response mediated by CDKN1A. In association with NUAK1, phosphorylates CDKN1A in response to UV radiation and contributes to its degradation which is necessary for optimal DNA repair (PubMed:25329316).11 Publications
Isoform 2: Has a role in spermiogenesis.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+, Mn2+

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei78ATPCurated1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei176Proton acceptor1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi55 – 63ATPPROSITE-ProRule annotation9

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processApoptosis, Autophagy, Cell cycle, Differentiation, DNA damage, Spermatogenesis
LigandATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
2.7.11.1 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-163680 AMPK inhibits chREBP transcriptional activation activity
R-HSA-380972 Energy dependent regulation of mTOR by LKB1-AMPK
R-HSA-6804756 Regulation of TP53 Activity through Phosphorylation
R-HSA-9614657 FOXO-mediated transcription of cell death genes

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
Q15831

SIGNOR Signaling Network Open Resource

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SIGNORi
Q15831

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:STK11
Synonyms:LKB1, PJS
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 19

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000118046.14

Human Gene Nomenclature Database

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HGNCi
HGNC:11389 STK11

Online Mendelian Inheritance in Man (OMIM)

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MIMi
602216 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q15831

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Peutz-Jeghers syndrome (PJS)8 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant disorder characterized by melanocytic macules of the lips, multiple gastrointestinal hamartomatous polyps and an increased risk for various neoplasms, including gastrointestinal cancer.
See also OMIM:175200
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_06562816E → G in PJS. 1 Publication1
Natural variantiVAR_07105750 – 53Missing in PJS. 1 Publication4
Natural variantiVAR_00620267L → P in PJS; abolishes kinase activity, leading to loss of autophosphorylation. 2 PublicationsCorresponds to variant dbSNP:rs137853077EnsemblClinVar.1
Natural variantiVAR_007920162 – 164DGL → NDM in PJS. 3
Natural variantiVAR_071058176D → N in PJS; loss of kinase activity, leading to greatly reduced autophosphorylation; fails to phosphorylate PTEN in vitro; no significant effect on nucleocytoplasmic localization. 2 PublicationsCorresponds to variant dbSNP:rs730881979EnsemblClinVar.1
Natural variantiVAR_007921194D → N in PJS. 1 PublicationCorresponds to variant dbSNP:rs121913315EnsemblClinVar.1
Natural variantiVAR_033142239W → C in PJS; late onset suggests reduced penetrance. 1 PublicationCorresponds to variant dbSNP:rs137853082EnsemblClinVar.1
Natural variantiVAR_006203247Missing in PJS. 1 Publication1
Natural variantiVAR_007922297R → K in PJS. 1 Publication1
Natural variantiVAR_033143303 – 306IRQH → N in PJS. 4
Natural variantiVAR_071059308W → C in PJS; abolishes kinase activity, leading to loss of autophosphorylation. 1 PublicationCorresponds to variant dbSNP:rs1057520042Ensembl.1
Natural variantiVAR_033144315P → S in PJS; pathogenicity uncertain; no effect heterotrimeric complex assembly with STRADA and CAB39. 2 PublicationsCorresponds to variant dbSNP:rs786202431EnsemblClinVar.1
Testicular germ cell tumor (TGCT)2 Publications
The gene represented in this entry may be involved in disease pathogenesis.
Disease descriptionA 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.
See also OMIM:273300
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_033140163G → 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. 3 PublicationsCorresponds to variant dbSNP:rs137853078EnsemblClinVar.1
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)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi44K → R: No effect on kinase activity. 1 Publication1
Mutagenesisi48K → Q: No effect on basal nucleocytoplasmic localization, but fails to translocate to the cytoplasm when coexpressed with SIRT1. 1 Publication1
Mutagenesisi48K → R: Enhanced phosphorylation at Thr-336 and Ser-428, enhanced cytoplasmic localization and increased kinase activity. 1 Publication1
Mutagenesisi74R → A: Impaired formation of a heterotrimeric complex with STRADA and CAB39; when associated with A-204. 1 Publication1
Mutagenesisi78K → I: Loss of kinase activity, leading to greatly reduced autophosphorylation. 2 Publications1
Mutagenesisi78K → M: Loss of kinase activity, leading to reduced autophosphorylation and acting as a dominant-negative mutant. 2 Publications1
Mutagenesisi96K → R: No effect on kinase activity. 1 Publication1
Mutagenesisi97K → R: No effect on kinase activity. 1 Publication1
Mutagenesisi189T → A: Reduced phosphorylation. 1 Publication1
Mutagenesisi194D → A: Loss of kinase activity. 3 Publications1
Mutagenesisi204F → A: No effect. Impaired formation of a heterotrimeric complex with STRADA and CAB39; when associated with A-74. 1 Publication1
Mutagenesisi428S → A or E: No effect on kinase activity. 2 Publications1
Mutagenesisi428S → A: Inhibits peroxynitrite-induced nuclear export of STK11, and consequent PTEN phosphorylation and inhibition of PI3K/Akt signaling. 2 Publications1

Keywords - Diseasei

Disease mutation, Tumor suppressor

Organism-specific databases

DisGeNET

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DisGeNETi
6794

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
STK11

MalaCards human disease database

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MalaCardsi
STK11
MIMi175200 phenotype
273300 phenotype

Open Targets

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OpenTargetsi
ENSG00000118046

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
2869 Peutz-Jeghers syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA36198

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL5606

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
STK11

Domain mapping of disease mutations (DMDM)

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DMDMi
3024670

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000866991 – 430Serine/threonine-protein kinase STK11Add BLAST430
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000422300431 – 433Removed in mature formBy similarity3

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei31PhosphoserineCombined sources1
Modified residuei44N6-acetyllysine1 Publication1
Modified residuei48N6-acetyllysine1 Publication1
Modified residuei96N6-acetyllysine1 Publication1
Modified residuei97N6-acetyllysine1 Publication1
Modified residuei189Phosphothreonine; by autocatalysis1 Publication1
Modified residuei296N6-acetyllysine1 Publication1
Modified residuei311N6-acetyllysine1 Publication1
Modified residuei325PhosphoserineBy similarity1
Modified residuei336Phosphothreonine; by autocatalysis1 Publication1
Modified residuei363Phosphothreonine; by ATM and autocatalysis1 Publication1
Modified residuei401PhosphoserineCombined sources1
Modified residuei416N6-acetyllysine1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi418S-palmitoyl cysteineBy similarity1
Modified residuei423N6-acetyllysine1 Publication1
Modified residuei428Phosphoserine; by autocatalysis, PKA, PKC/PRKCZ and RPS6KA12 Publications1
Modified residuei430Cysteine methyl esterBy similarity1
Lipidationi430S-farnesyl cysteineBy similarity1
Modified residuei431N6-acetyllysine1 Publication1
Isoform 2 (identifier: Q15831-2)
Modified residuei399Phosphoserine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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. UV radiation-induced phosphorylation at Thr-363 mediates CDKN1A degradation (By similarity).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

Encyclopedia of Proteome Dynamics

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EPDi
Q15831

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q15831

MaxQB - The MaxQuant DataBase

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MaxQBi
Q15831

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q15831

PeptideAtlas

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PeptideAtlasi
Q15831

PRoteomics IDEntifications database

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PRIDEi
Q15831

ProteomicsDB human proteome resource

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ProteomicsDBi
60780
60781 [Q15831-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q15831

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q15831

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Ubiquitously expressed. Strongest expression in testis and fetal liver.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000118046 Expressed in 189 organ(s), highest expression level in testis

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q15831 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q15831 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB016231
CAB022105
HPA017254
HPA067481

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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. Interacts with CDKN1A.11 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
112670, 143 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q15831

Database of interacting proteins

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DIPi
DIP-31317N

Protein interaction database and analysis system

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IntActi
Q15831, 112 interactors

Molecular INTeraction database

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MINTi
Q15831

STRING: functional protein association networks

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STRINGi
9606.ENSP00000324856

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
Q15831

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1433
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WTKX-ray2.65C/F43-347[»]
4ZDRX-ray2.90A/B333-340[»]
5WXNX-ray2.93C/D331-343[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q15831

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q15831

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q15831

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini49 – 309Protein kinasePROSITE-ProRule annotationAdd BLAST261

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni45 – 90Sufficient for interaction with SIRT11 PublicationAdd BLAST46

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0583 Eukaryota
COG0515 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000158050

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000007002

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG054467

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q15831

KEGG Orthology (KO)

More...
KOi
K07298

Identification of Orthologs from Complete Genome Data

More...
OMAi
KNIKMVG

Database of Orthologous Groups

More...
OrthoDBi
1104340at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q15831

TreeFam database of animal gene trees

More...
TreeFami
TF105322

Family and domain databases

Conserved Domains Database

More...
CDDi
cd14119 STKc_LKB1, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR039154 LKB1_c
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00069 Pkinase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00220 S_TKc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 5 potential isoforms that are computationally mapped.Show allAlign All

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
K7EP59K7EP59_HUMAN
Serine/threonine-protein kinase STK...
STK11
432Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
K7EQN8K7EQN8_HUMAN
Serine/threonine-protein kinase STK...
STK11
153Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
K7EMR0K7EMR0_HUMAN
Serine/threonine-protein kinase STK...
STK11
101Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A087WT72A0A087WT72_HUMAN
Serine/threonine-protein kinase STK...
STK11
21Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A1B0GUW2A0A1B0GUW2_HUMAN
Serine/threonine-protein kinase STK...
STK11
43Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06562714E → K in cervical cancer; somatic mutation. 1 Publication1
Natural variantiVAR_06562816E → G in PJS. 1 Publication1
Natural variantiVAR_03313849Y → D in melanoma; sporadic malignant; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs137853080EnsemblClinVar.1
Natural variantiVAR_07105750 – 53Missing in PJS. 1 Publication4
Natural variantiVAR_06562966V → M in cervical carcinoma; somatic mutation. 2 Publications1
Natural variantiVAR_00620267L → P in PJS; abolishes kinase activity, leading to loss of autophosphorylation. 2 PublicationsCorresponds to variant dbSNP:rs137853077EnsemblClinVar.1
Natural variantiVAR_06563086R → G in sporadic cancer; somatic mutation; no effect on kinase activity nor in heterotrimeric complex assembly with STRADA and CAB39. 1 PublicationCorresponds to variant dbSNP:rs1057520039Ensembl.1
Natural variantiVAR_04113987R → K in a metastatic melanoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_065631123Q → R in sporadic cancer; somatic mutation; no effect on kinase activity nor in heterotrimeric complex assembly with STRADA and CAB39. 1 PublicationCorresponds to variant dbSNP:rs764449808EnsemblClinVar.1
Natural variantiVAR_033139135G → R in melanoma; sporadic malignant; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs137853081EnsemblClinVar.1
Natural variantiVAR_065632157F → S in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39. 1 Publication1
Natural variantiVAR_065633160L → P in cervical cancer; somatic mutation. 1 Publication1
Natural variantiVAR_007920162 – 164DGL → NDM in PJS. 3
Natural variantiVAR_033140163G → 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. 3 PublicationsCorresponds to variant dbSNP:rs137853078EnsemblClinVar.1
Natural variantiVAR_065634170Q → P in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39. 1 Publication1
Natural variantiVAR_065635171G → S in colorectal cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39. 2 Publications1
Natural variantiVAR_065636174H → R in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39. 1 Publication1
Natural variantiVAR_071058176D → N in PJS; loss of kinase activity, leading to greatly reduced autophosphorylation; fails to phosphorylate PTEN in vitro; no significant effect on nucleocytoplasmic localization. 2 PublicationsCorresponds to variant dbSNP:rs730881979EnsemblClinVar.1
Natural variantiVAR_065637176D → Y in sporadic cancer; somatic mutation; Loss of kinase activity. 2 Publications1
Natural variantiVAR_065638177I → N in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39. 1 PublicationCorresponds to variant dbSNP:rs1057520041Ensembl.1
Natural variantiVAR_065639181N → E in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39; requires 2 nucleotide substitutions. 1 Publication1
Natural variantiVAR_007921194D → N in PJS. 1 PublicationCorresponds to variant dbSNP:rs121913315EnsemblClinVar.1
Natural variantiVAR_065640194D → V in lung cancer; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs121913316EnsemblClinVar.1
Natural variantiVAR_033141194D → Y in melanoma; sporadic malignant; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs121913315EnsemblClinVar.1
Natural variantiVAR_065641199E → K in colorectal cancer; somatic mutation; impaired kinase activity. 1 PublicationCorresponds to variant dbSNP:rs121913317EnsemblClinVar.1
Natural variantiVAR_065642199E → Q in sporadic cancer; somatic mutation; does not affect kinase activity. 1 Publication1
Natural variantiVAR_065643205A → T in sporadic cancer; somatic mutation; no effect heterotrimeric complex assembly with STRADA and CAB39. 1 PublicationCorresponds to variant dbSNP:rs730881981EnsemblClinVar.1
Natural variantiVAR_065644208D → N in colorectal cancer; somatic mutation; no effect heterotrimeric complex assembly with STRADA and CAB39. 1 Publication1
Natural variantiVAR_065645215G → D in colorectal cancer; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs1057520038Ensembl.1
Natural variantiVAR_065646216S → F in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39. 1 PublicationCorresponds to variant dbSNP:rs1057520017Ensembl.1
Natural variantiVAR_065647223E → V in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39. 1 Publication1
Natural variantiVAR_065648230T → P in sporadic cancer; somatic mutation; no effect heterotrimeric complex assembly with STRADA and CAB39. 1 Publication1
Natural variantiVAR_065649231F → L in cervical cancer; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs929783669Ensembl.1
Natural variantiVAR_065650232S → P in sporadic cancer; somatic mutation; no effect heterotrimeric complex assembly with STRADA and CAB39. 1 Publication1
Natural variantiVAR_033142239W → C in PJS; late onset suggests reduced penetrance. 1 PublicationCorresponds to variant dbSNP:rs137853082EnsemblClinVar.1
Natural variantiVAR_065651245L → R in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39. 1 Publication1
Natural variantiVAR_006203247Missing in PJS. 1 Publication1
Natural variantiVAR_065652250T → P in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39. 1 Publication1
Natural variantiVAR_065653272Y → H in sporadic cancer; somatic mutation; no effect on kinase activity nor in heterotrimeric complex assembly with STRADA and CAB39. 1 Publication1
Natural variantiVAR_065654277D → Y in sporadic cancer; somatic mutation; no effect on kinase activity nor in heterotrimeric complex assembly with STRADA and CAB39. 1 Publication1
Natural variantiVAR_065655281P → L in ovarian carcinoma; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs121913322EnsemblClinVar.1
Natural variantiVAR_065656285L → Q in sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39. 1 Publication1
Natural variantiVAR_007922297R → K in PJS. 1 Publication1
Natural variantiVAR_033143303 – 306IRQH → N in PJS. 4
Natural variantiVAR_071059308W → C in PJS; abolishes kinase activity, leading to loss of autophosphorylation. 1 PublicationCorresponds to variant dbSNP:rs1057520042Ensembl.1
Natural variantiVAR_065657314P → H in colorectal cancer; no effect heterotrimeric complex assembly with STRADA and CAB39. 1 Publication1
Natural variantiVAR_033144315P → S in PJS; pathogenicity uncertain; no effect heterotrimeric complex assembly with STRADA and CAB39. 2 PublicationsCorresponds to variant dbSNP:rs786202431EnsemblClinVar.1
Natural variantiVAR_065658324P → L in gastric carcinoma; no effect heterotrimeric complex assembly with STRADA and CAB39. 1 PublicationCorresponds to variant dbSNP:rs367807476EnsemblClinVar.1
Natural variantiVAR_065659354F → L in colorectal cancer; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs59912467EnsemblClinVar.1
Natural variantiVAR_065660367T → M in colorectal cancer; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs587782835EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_041746371 – 433QVPEE…ACKQQ → GEEASEAGLRAERGLQKSEG SDLSGEEASRPAPQ in isoform 2. CuratedAdd BLAST63

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
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

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS45896.1 [Q15831-1]

NCBI Reference Sequences

More...
RefSeqi
NP_000446.1, NM_000455.4 [Q15831-1]
XP_005259675.1, XM_005259618.3 [Q15831-2]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.515005

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000326873; ENSP00000324856; ENSG00000118046 [Q15831-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
6794

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:6794

UCSC genome browser

More...
UCSCi
uc002lrl.2 human [Q15831-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
Wikipedia

PJS entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_005259618.3 [Q15831-2]
UniGeneiHs.515005

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WTKX-ray2.65C/F43-347[»]
4ZDRX-ray2.90A/B333-340[»]
5WXNX-ray2.93C/D331-343[»]
ProteinModelPortaliQ15831
SMRiQ15831
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112670, 143 interactors
CORUMiQ15831
DIPiDIP-31317N
IntActiQ15831, 112 interactors
MINTiQ15831
STRINGi9606.ENSP00000324856

Chemistry databases

BindingDBiQ15831
ChEMBLiCHEMBL5606

PTM databases

iPTMnetiQ15831
PhosphoSitePlusiQ15831

Polymorphism and mutation databases

BioMutaiSTK11
DMDMi3024670

Proteomic databases

EPDiQ15831
jPOSTiQ15831
MaxQBiQ15831
PaxDbiQ15831
PeptideAtlasiQ15831
PRIDEiQ15831
ProteomicsDBi60780
60781 [Q15831-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
6794
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000326873; ENSP00000324856; ENSG00000118046 [Q15831-1]
GeneIDi6794
KEGGihsa:6794
UCSCiuc002lrl.2 human [Q15831-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
6794
DisGeNETi6794
EuPathDBiHostDB:ENSG00000118046.14

GeneCards: human genes, protein and diseases

More...
GeneCardsi
STK11
GeneReviewsiSTK11
HGNCiHGNC:11389 STK11
HPAiCAB016231
CAB022105
HPA017254
HPA067481
MalaCardsiSTK11
MIMi175200 phenotype
273300 phenotype
602216 gene
neXtProtiNX_Q15831
OpenTargetsiENSG00000118046
Orphaneti2869 Peutz-Jeghers syndrome
PharmGKBiPA36198

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0583 Eukaryota
COG0515 LUCA
GeneTreeiENSGT00940000158050
HOGENOMiHOG000007002
HOVERGENiHBG054467
InParanoidiQ15831
KOiK07298
OMAiKNIKMVG
OrthoDBi1104340at2759
PhylomeDBiQ15831
TreeFamiTF105322

Enzyme and pathway databases

BRENDAi2.7.11.1 2681
ReactomeiR-HSA-163680 AMPK inhibits chREBP transcriptional activation activity
R-HSA-380972 Energy dependent regulation of mTOR by LKB1-AMPK
R-HSA-6804756 Regulation of TP53 Activity through Phosphorylation
R-HSA-9614657 FOXO-mediated transcription of cell death genes
SignaLinkiQ15831
SIGNORiQ15831

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
STK11 human
EvolutionaryTraceiQ15831

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
STK11

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
6794

Protein Ontology

More...
PROi
PR:Q15831

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000118046 Expressed in 189 organ(s), highest expression level in testis
ExpressionAtlasiQ15831 baseline and differential
GenevisibleiQ15831 HS

Family and domain databases

CDDicd14119 STKc_LKB1, 1 hit
InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR039154 LKB1_c
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF00069 Pkinase, 1 hit
SMARTiView protein in SMART
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSTK11_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q15831
Secondary accession number(s): B2RBX7, E7EW76
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: February 13, 2019
This is version 208 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

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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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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