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UniProtKB - Q13188 (STK3_HUMAN)

Entry version 198 (10 Apr 2019)
Sequence version 2 (26 Apr 2004)
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Protein

Serine/threonine-protein kinase 3

Gene

STK3

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

Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. STK3/MST2 and STK4/MST1 are required to repress proliferation of mature hepatocytes, to prevent activation of facultative adult liver stem cells (oval cells), and to inhibit tumor formation. Phosphorylates NKX2-1 (By similarity). Phosphorylates NEK2 and plays a role in centrosome disjunction by regulating the localization of NEK2 to centrosome, and its ability to phosphorylate CROCC and CEP250. In conjunction with SAV1, activates the transcriptional activity of ESR1 through the modulation of its phosphorylation. Positively regulates RAF1 activation via suppression of the inhibitory phosphorylation of RAF1 on 'Ser-259'. Phosphorylates MOBKL1A and RASSF2. Phosphorylates MOBKL1B on 'Thr-74'. Acts cooperatively with MOBKL1B to activate STK38.By similarity11 Publications

<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+

<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

Inhibited by the C-terminal non-catalytic region. Activated by caspase-cleavage. Full activation also requires homodimerization and autophosphorylation of Thr-180, which are inhibited by the proto-oncogene product RAF1. Activated by RASSF1 which acts by preventing its dephosphorylation.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 sitei56ATP1
<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 sitei146Proton acceptorPROSITE-ProRule annotation1

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 bindingi33 – 41ATPPROSITE-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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<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
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.7.11.1 2681

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-2028269 Signaling by Hippo

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

More...SignaLinki		Q13188

SIGNOR Signaling Network Open Resource

More...SIGNORi		Q13188

<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 3 (EC:2.7.11.1)
Alternative name(s):
Mammalian STE20-like protein kinase 2
Short name:
MST-2
STE20-like kinase MST2
Serine/threonine-protein kinase Krs-1
Cleaved into the following 2 chains:
Serine/threonine-protein kinase 3 36kDa subunit
Short name:
MST2/N
Serine/threonine-protein kinase 3 20kDa subunit
Short name:
MST2/C
<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:STK3
Synonyms:KRS1, MST2
<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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<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 8

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000104375.15

Human Gene Nomenclature Database

More...HGNCi		HGNC:11406 STK3

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		605030 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q13188

<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, 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

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>Mutagenesisi56K → R: Loss of activity. 1 Publication1
Mutagenesisi322D → N: Resistant to proteolytic cleavage. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		6788

Open Targets

More...OpenTargetsi		ENSG00000104375

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA36213

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL4708

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		2219

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		STK3

Domain mapping of disease mutations (DMDM)

More...DMDMi		46577700

<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_00000866891 – 491Serine/threonine-protein kinase 3Add BLAST491
ChainiPRO_00004137131 – 322Serine/threonine-protein kinase 3 36kDa subunitAdd BLAST322
ChainiPRO_0000413714323 – 491Serine/threonine-protein kinase 3 20kDa subunitAdd BLAST169

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 residuei1N-acetylmethionineCombined sources1 Publication1
Modified residuei15PhosphoserineCombined sources1
Modified residuei117Phosphothreonine; by PKB/AKT12 Publications1
Modified residuei180Phosphothreonine; by autocatalysisBy similarityCurated1
Modified residuei316PhosphoserineCombined sources1
Modified residuei336PhosphothreonineCombined sources1
Modified residuei384Phosphothreonine; by PKB/AKT11 Publication1
Modified residuei385PhosphoserineCombined sources1
Modified residuei444PhosphoserineCombined sources1

<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

Phosphorylation at Thr-117 and Thr-384 by PKB/AKT1, leads to inhibition of its: cleavage, kinase activity, autophosphorylation at Thr-180, binding to RASSF1 and nuclear translocation, and increase in its binding to RAF1.3 Publications
Proteolytically cleaved by caspase-3 during apoptosis. Proteolytic cleavage results in kinase activation and nuclear translocation of the truncated form (MST1/N).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei322 – 323Cleavage; by caspase-32

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q13188

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q13188

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q13188

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

More...PaxDbi		Q13188

PeptideAtlas

More...PeptideAtlasi		Q13188

PRoteomics IDEntifications database

More...PRIDEi		Q13188

ProteomicsDB human proteome resource

More...ProteomicsDBi		59211

2D gel databases

USC-OGP 2-DE database

More...OGPi		Q13188

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q13188

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

More...PhosphoSitePlusi		Q13188

Miscellaneous databases

CutDB - Proteolytic event database

More...PMAP-CutDBi		Q13188

<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

Expressed at high levels in adult kidney, skeletal and placenta tissues and at very low levels in adult heart, lung and brain tissues.1 Publication

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Activity increases during mitosis.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000104375 Expressed in 222 organ(s), highest expression level in chorionic villus

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q13188 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q13188 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB025316
HPA007120

<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

Homodimer; mediated via the coiled-coil region. Interacts with NORE1, which inhibits autoactivation (By similarity). Interacts with and stabilizes SAV1 (PubMed:15688006, PubMed:16930133, PubMed:28087714). Interacts with RAF1, which prevents dimerization and phosphorylation. Interacts with RASSF1. Interacts (via SARAH domain) with isoform 1 of NEK2. Interacts with ESR1 only in the presence of SAV1. Interacts with PKB/AKT1. Forms a tripartite complex with MOBKL1B and STK38. Interacts with RASSF2 (via SARAH domain). Interacts with DLG5 (via PDZ domain 3) (PubMed:28087714). Interacts with LATS1; this interaction is inhibited in the presence of DLG5 (PubMed:28087714). Interacts with MARK3 in the presence of DLG5 (PubMed:28087714).By similarity12 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

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		112664, 97 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q13188

Database of interacting proteins

More...DIPi		DIP-36128N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		Q13188

Protein interaction database and analysis system

More...IntActi		Q13188, 82 interactors

Molecular INTeraction database

More...MINTi		Q13188

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000429744

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q13188

<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

1491
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3WWSX-ray2.01A/B/C/D436-484[»]
4HKDX-ray1.50A/B/C/D436-484[»]
4L0NX-ray1.40A/B/C/D/E/F/G/H/I/J436-484[»]
4LG4X-ray2.42A/B/C/D/E/F16-313[»]
4LGDX-ray3.05A/B/C/D9-491[»]
4OH9X-ray1.70A/B436-484[»]
5BRMX-ray2.65G/H/I/J/K/L/M/N/O371-401[»]
5DH3X-ray2.47A/B15-313[»]
6AO5X-ray2.96A16-491[»]
6AR2X-ray1.55C/D373-382[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		Q13188

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

More...SMRi		Q13188

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<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>Domaini27 – 278Protein kinasePROSITE-ProRule annotationAdd BLAST252
Domaini437 – 484SARAHPROSITE-ProRule annotationAdd BLAST48

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili287 – 328Sequence analysisAdd BLAST42
Coiled coili442 – 475Sequence analysisAdd BLAST34

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi308 – 314Poly-Glu7
Compositional biasi370 – 375Poly-Glu6

<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

Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0201 Eukaryota
ENOG410XP9G LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000154984

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000234203

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG108518

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q13188

KEGG Orthology (KO)

More...KOi		K04412

Identification of Orthologs from Complete Genome Data

More...OMAi		DGAQTMI

Database of Orthologous Groups

More...OrthoDBi		1035379at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q13188

TreeFam database of animal gene trees

More...TreeFami		TF354217

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR024205 Mst1_SARAH_domain
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR011524 SARAH_dom

Pfam protein domain database

More...Pfami		View protein in Pfam
PF11629 Mst1_SARAH, 1 hit
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
PS50951 SARAH, 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 4 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q13188-1) [UniParc]FASTAAdd to basket

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.

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MEQPPAPKSK LKKLSEDSLT KQPEEVFDVL EKLGEGSYGS VFKAIHKESG 
        60         70         80         90        100
QVVAIKQVPV ESDLQEIIKE ISIMQQCDSP YVVKYYGSYF KNTDLWIVME 
       110        120        130        140        150
YCGAGSVSDI IRLRNKTLIE DEIATILKST LKGLEYLHFM RKIHRDIKAG 
       160        170        180        190        200
NILLNTEGHA KLADFGVAGQ LTDTMAKRNT VIGTPFWMAP EVIQEIGYNC 
       210        220        230        240        250
VADIWSLGIT SIEMAEGKPP YADIHPMRAI FMIPTNPPPT FRKPELWSDD 
       260        270        280        290        300
FTDFVKKCLV KNPEQRATAT QLLQHPFIKN AKPVSILRDL ITEAMEIKAK 
       310        320        330        340        350
RHEEQQRELE EEEENSDEDE LDSHTMVKTS VESVGTMRAT STMSEGAQTM 
       360        370        380        390        400
IEHNSTMLES DLGTMVINSE DEEEEDGTMK RNATSPQVQR PSFMDYFDKQ 
       410        420        430        440        450
DFKNKSHENC NQNMHEPFPM SKNVFPDNWK VPQDGDFDFL KNLSLEELQM 
       460        470        480        490 
RLKALDPMME REIEELRQRY TAKRQPILDA MDAKKRRQQN F
Length:491
Mass (Da):56,301
Last modified:April 26, 2004 - v2
<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:i84F598ED3617292C
GO
Isoform 2 (identifier: Q13188-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-8: MEQPPAPK → MLQLMDSGITICLRNGAASVFKKKEWSTQGEENKQD

Note: No experimental confirmation available.
Show »
Length:519
Mass (Da):59,462
Checksum:i84CB5FEAA629AE68
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 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A087WZ06A0A087WZ06_HUMAN
Serine/threonine-protein kinase 3
STK3
380Annotation 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>
E5RFQ9E5RFQ9_HUMAN
Serine/threonine-protein kinase 3
STK3
228Annotation 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>
E5RIM6E5RIM6_HUMAN
Serine/threonine-protein kinase 3
STK3
82Annotation 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>
Q8NBU1Q8NBU1_HUMAN
Serine/threonine-protein kinase 3
STK3
168Annotation 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>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti96 – 98WIV → YLY in CAA80909 (PubMed:8274451).Curated3
Sequence conflicti121D → Y in CAA80909 (PubMed:8274451).Curated1
Sequence conflicti203D → G in CAA80909 (PubMed:8274451).Curated1
Sequence conflicti303E → D in AAC50386 (PubMed:8566796).Curated1
Sequence conflicti332 – 334ESV → GEC in AAC50386 (PubMed:8566796).Curated3

Natural variant

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_04112260V → L in an ovarian clear cell carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_051670418F → C. Corresponds to variant dbSNP:rs36047674Ensembl.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_0541671 – 8MEQPPAPK → MLQLMDSGITICLRNGAASV FKKKEWSTQGEENKQD in isoform 2. 1 Publication8

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
U26424 mRNA Translation: AAC50386.1
U60206 mRNA Translation: AAB17261.1
AK131363 mRNA Translation: BAG54769.1
AK291837 mRNA Translation: BAF84526.1
AC016877 Genomic DNA No translation available.
AP002087 Genomic DNA No translation available.
AP003355 Genomic DNA No translation available.
AP003467 Genomic DNA No translation available.
AP003551 Genomic DNA No translation available.
CH471060 Genomic DNA Translation: EAW91781.1
BC010640 mRNA Translation: AAH10640.1
Z25422 mRNA Translation: CAA80909.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS47900.1 [Q13188-1]
CCDS59108.1 [Q13188-2]

Protein sequence database of the Protein Information Resource

More...PIRi		I38212

NCBI Reference Sequences

More...RefSeqi		NP_001243241.1, NM_001256312.1 [Q13188-2]
NP_006272.2, NM_006281.3 [Q13188-1]

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.492333
Hs.738869

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000419617; ENSP00000390500; ENSG00000104375 [Q13188-1]
ENST00000523601; ENSP00000429744; ENSG00000104375 [Q13188-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		6788

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:6788

UCSC genome browser

More...UCSCi		uc003yio.5 human [Q13188-1]

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U26424 mRNA Translation: AAC50386.1
U60206 mRNA Translation: AAB17261.1
AK131363 mRNA Translation: BAG54769.1
AK291837 mRNA Translation: BAF84526.1
AC016877 Genomic DNA No translation available.
AP002087 Genomic DNA No translation available.
AP003355 Genomic DNA No translation available.
AP003467 Genomic DNA No translation available.
AP003551 Genomic DNA No translation available.
CH471060 Genomic DNA Translation: EAW91781.1
BC010640 mRNA Translation: AAH10640.1
Z25422 mRNA Translation: CAA80909.1
CCDSiCCDS47900.1 [Q13188-1]
CCDS59108.1 [Q13188-2]
PIRiI38212
RefSeqiNP_001243241.1, NM_001256312.1 [Q13188-2]
NP_006272.2, NM_006281.3 [Q13188-1]
UniGeneiHs.492333
Hs.738869

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3WWSX-ray2.01A/B/C/D436-484[»]
4HKDX-ray1.50A/B/C/D436-484[»]
4L0NX-ray1.40A/B/C/D/E/F/G/H/I/J436-484[»]
4LG4X-ray2.42A/B/C/D/E/F16-313[»]
4LGDX-ray3.05A/B/C/D9-491[»]
4OH9X-ray1.70A/B436-484[»]
5BRMX-ray2.65G/H/I/J/K/L/M/N/O371-401[»]
5DH3X-ray2.47A/B15-313[»]
6AO5X-ray2.96A16-491[»]
6AR2X-ray1.55C/D373-382[»]
ProteinModelPortaliQ13188
SMRiQ13188
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112664, 97 interactors
CORUMiQ13188
DIPiDIP-36128N
ELMiQ13188
IntActiQ13188, 82 interactors
MINTiQ13188
STRINGi9606.ENSP00000429744

Chemistry databases

BindingDBiQ13188
ChEMBLiCHEMBL4708
GuidetoPHARMACOLOGYi2219

PTM databases

iPTMnetiQ13188
PhosphoSitePlusiQ13188

Polymorphism and mutation databases

BioMutaiSTK3
DMDMi46577700

2D gel databases

OGPiQ13188

Proteomic databases

EPDiQ13188
jPOSTiQ13188
MaxQBiQ13188
PaxDbiQ13188
PeptideAtlasiQ13188
PRIDEiQ13188
ProteomicsDBi59211

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		6788
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000419617; ENSP00000390500; ENSG00000104375 [Q13188-1]
ENST00000523601; ENSP00000429744; ENSG00000104375 [Q13188-2]
GeneIDi6788
KEGGihsa:6788
UCSCiuc003yio.5 human [Q13188-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		6788
DisGeNETi6788
EuPathDBiHostDB:ENSG00000104375.15

GeneCards: human genes, protein and diseases

More...GeneCardsi		STK3
HGNCiHGNC:11406 STK3
HPAiCAB025316
HPA007120
MIMi605030 gene
neXtProtiNX_Q13188
OpenTargetsiENSG00000104375
PharmGKBiPA36213

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0201 Eukaryota
ENOG410XP9G LUCA
GeneTreeiENSGT00940000154984
HOGENOMiHOG000234203
HOVERGENiHBG108518
InParanoidiQ13188
KOiK04412
OMAiDGAQTMI
OrthoDBi1035379at2759
PhylomeDBiQ13188
TreeFamiTF354217

Enzyme and pathway databases

BRENDAi2.7.11.1 2681
ReactomeiR-HSA-2028269 Signaling by Hippo
SignaLinkiQ13188
SIGNORiQ13188

Miscellaneous databases

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

More...ChiTaRSi		STK3 human

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		STK3

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

More...GenomeRNAii		6788
PMAP-CutDBiQ13188

Protein Ontology

More...PROi		PR:Q13188

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000104375 Expressed in 222 organ(s), highest expression level in chorionic villus
ExpressionAtlasiQ13188 baseline and differential
GenevisibleiQ13188 HS

Family and domain databases

InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR024205 Mst1_SARAH_domain
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR011524 SARAH_dom
PfamiView protein in Pfam
PF11629 Mst1_SARAH, 1 hit
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
PS50951 SARAH, 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 nameiSTK3_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: Q13188
Secondary accession number(s): A8K722
, B3KYA7, Q15445, Q15801, Q96FM6
<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: February 21, 2001
Last sequence update: April 26, 2004
Last modified: April 10, 2019
This is version 198 of the entry and version 2 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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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