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Protein

MAP kinase-activated protein kinase 2

Gene

MAPKAPK2

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 serine/threonine-protein kinase involved in cytokine production, endocytosis, reorganization of the cytoskeleton, cell migration, cell cycle control, chromatin remodeling, DNA damage response and transcriptional regulation. Following stress, it is phosphorylated and activated by MAP kinase p38-alpha/MAPK14, leading to phosphorylation of substrates. Phosphorylates serine in the peptide sequence, Hyd-X-R-X2-S, where Hyd is a large hydrophobic residue. Phosphorylates ALOX5, CDC25B, CDC25C, CEP131, ELAVL1, HNRNPA0, HSP27/HSPB1, KRT18, KRT20, LIMK1, LSP1, PABPC1, PARN, PDE4A, RCSD1, RPS6KA3, TAB3 and TTP/ZFP36. Phosphorylates HSF1; leading to the interaction with HSP90 proteins and inhibiting HSF1 homotrimerization, DNA-binding and transactivation activities (PubMed:16278218). Mediates phosphorylation of HSP27/HSPB1 in response to stress, leading to the dissociation of HSP27/HSPB1 from large small heat-shock protein (sHsps) oligomers and impairment of their chaperone activities and ability to protect against oxidative stress effectively. Involved in inflammatory response by regulating tumor necrosis factor (TNF) and IL6 production post-transcriptionally: acts by phosphorylating AU-rich elements (AREs)-binding proteins ELAVL1, HNRNPA0, PABPC1 and TTP/ZFP36, leading to the regulation of the stability and translation of TNF and IL6 mRNAs. Phosphorylation of TTP/ZFP36, a major post-transcriptional regulator of TNF, promotes its binding to 14-3-3 proteins and reduces its ARE mRNA affinity, leading to inhibition of dependent degradation of ARE-containing transcripts. Phosphorylates CEP131 in response to cellular stress induced by ultraviolet irradiation which promotes binding of CEP131 to 14-3-3 proteins and inhibits formation of novel centriolar satellites (PubMed:26616734). Also involved in late G2/M checkpoint following DNA damage through a process of post-transcriptional mRNA stabilization: following DNA damage, relocalizes from nucleus to cytoplasm and phosphorylates HNRNPA0 and PARN, leading to stabilization of GADD45A mRNA. Involved in toll-like receptor signaling pathway (TLR) in dendritic cells: required for acute TLR-induced macropinocytosis by phosphorylating and activating RPS6KA3.17 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 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 following phosphorylation by p38-alpha/MAPK14 following various stresses. Inhibited following sumoylation. Specifically inhibited by pyrrolopyridine inhibitors.

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 sitei93ATPPROSITE-ProRule annotation1
<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 sitei186Proton 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 bindingi70 – 78ATPPROSITE-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

  • ATP binding Source: UniProtKB-KW
  • calcium-dependent protein serine/threonine kinase activity Source: GO_Central
  • calmodulin-dependent protein kinase activity Source: GO_Central
  • mitogen-activated protein kinase binding Source: GO_Central
  • protein kinase activity Source: ProtInc
  • protein serine/threonine kinase activity Source: UniProtKB

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 processDNA damage
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
MetaCyc:HS08751-MONOMER

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-171007 p38MAPK events
R-HSA-199920 CREB phosphorylation
R-HSA-2142691 Synthesis of Leukotrienes (LT) and Eoxins (EX)
R-HSA-2559580 Oxidative Stress Induced Senescence
R-HSA-3371453 Regulation of HSF1-mediated heat shock response
R-HSA-4420097 VEGFA-VEGFR2 Pathway
R-HSA-450302 activated TAK1 mediates p38 MAPK activation
R-HSA-450385 Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA
R-HSA-450513 Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA

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

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SignaLinki
P49137

SIGNOR Signaling Network Open Resource

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SIGNORi
P49137

<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:
MAP kinase-activated protein kinase 2 (EC:2.7.11.1)
Short name:
MAPK-activated protein kinase 2
Short name:
MAPKAP kinase 2
Short name:
MAPKAP-K2
Short name:
MAPKAPK-2
Short name:
MK-2
Short name:
MK2
<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
<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 1

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000162889.10

Human Gene Nomenclature Database

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HGNCi
HGNC:6887 MAPKAPK2

Online Mendelian Inheritance in Man (OMIM)

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MIMi
602006 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P49137

<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; 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>Mutagenesisi93K → R: Kinase defective mutant, abolishes activity. 1 Publication1
Mutagenesisi207D → A: Kinase defective mutant, abolishes activity. 1 Publication1
Mutagenesisi222T → A: Strong decrease in kinase activity. 3 Publications1
Mutagenesisi222T → D: Mimicks phosphorylation state, leading to slight increase of basal kinase activity. 3 Publications1
Mutagenesisi222T → E: Mimicks phosphorylation state and constitutive protein kinase activity; when associated with E-334. 3 Publications1
Mutagenesisi272S → A: Strong decrease in kinase activity. 1 Publication1
Mutagenesisi272S → D: Mimicks phosphorylation state, leading to slight increase of basal kinase activity. 1 Publication1
Mutagenesisi334T → A: Slight decrease in kinase activity. 3 Publications1
Mutagenesisi334T → D or E: Mimicks phosphorylation state, leading to elevated basal kinase activity. 3 Publications1
Mutagenesisi334T → E: Mimicks phosphorylation state and constitutive protein kinase activity; when associated with E-222. 3 Publications1
Mutagenesisi353K → R: Induces decreased sumoylation and increase in protein kinase activity. 1 Publication1

Organism-specific databases

DisGeNET

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DisGeNETi
9261

Open Targets

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OpenTargetsi
ENSG00000162889

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA30631

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL2208

Drug and drug target database

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DrugBanki
DB02010 Staurosporine

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
2094

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
MAPKAPK2

Domain mapping of disease mutations (DMDM)

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DMDMi
1346538

<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_00000862881 – 400MAP kinase-activated protein kinase 2Add BLAST400

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 residuei9Phosphoserine1 Publication1
Modified residuei25Phosphothreonine1 Publication1
Modified residuei222Phosphothreonine; by MAPK141 Publication1
Modified residuei272Phosphoserine; by MAPK141 Publication1
Modified residuei328Phosphoserine; by autocatalysisBy similarity1
Modified residuei334Phosphothreonine; by MAPK14Combined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki353Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication

<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

Sumoylation inhibits the protein kinase activity.1 Publication
Phosphorylated and activated by MAP kinase p38-alpha/MAPK14 at Thr-222, Ser-272 and Thr-334.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P49137

MaxQB - The MaxQuant DataBase

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MaxQBi
P49137

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

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PaxDbi
P49137

PeptideAtlas

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PeptideAtlasi
P49137

PRoteomics IDEntifications database

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PRIDEi
P49137

ProteomicsDB human proteome resource

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ProteomicsDBi
55964
55965 [P49137-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P49137

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

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PhosphoSitePlusi
P49137

<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 in all tissues examined.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000162889 Expressed in 233 organ(s), highest expression level in apex of heart

CleanEx database of gene expression profiles

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CleanExi
HS_MAPKAPK2

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P49137 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB010297
HPA045556
HPA063708
HPA064435

<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

Heterodimer with p38-alpha/MAPK14; this heterodimer forms a stable complex: molecules are positioned 'face to face' so that the ATP-binding sites of both kinases are at the heterodimer interface (PubMed:12171911, PubMed:17576063, PubMed:17255097, PubMed:17480064, PubMed:17449059, PubMed:17395714). Interacts with PHC2 (PubMed:15094067). Interacts with HSF1 (PubMed:16278218).8 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
114683, 63 interactors

Database of interacting proteins

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DIPi
DIP-35671N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
P49137

Protein interaction database and analysis system

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IntActi
P49137, 15 interactors

Molecular INTeraction database

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MINTi
P49137

STRING: functional protein association networks

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STRINGi
9606.ENSP00000356070

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P49137

<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

1400
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P49137

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

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SMRi
P49137

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
P49137

<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>Domaini64 – 325Protein kinasePROSITE-ProRule annotationAdd BLAST262

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>Regioni139 – 141Staurosporine binding3
Regioni328 – 364Autoinhibitory helixBy similarityAdd BLAST37
Regioni366 – 390p38 MAPK-binding siteAdd BLAST25

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi356 – 365Nuclear export signal (NES)10
Motifi371 – 374Bipartite nuclear localization signal 14
Motifi385 – 389Bipartite nuclear localization signal 25

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 biasi10 – 40Pro-richAdd BLAST31
Compositional biasi35 – 40Poly-Pro6

<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
KOG0604 Eukaryota
ENOG410XP8F LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000157261

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000233031

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG106948

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P49137

KEGG Orthology (KO)

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KOi
K04443

Identification of Orthologs from Complete Genome Data

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OMAi
GMKSRIR

Database of Orthologous Groups

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OrthoDBi
EOG091G14PL

Database for complete collections of gene phylogenies

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PhylomeDBi
P49137

TreeFam database of animal gene trees

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TreeFami
TF312891

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
4.10.1170.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR027442 MAPKAPK_C
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS

Pfam protein domain database

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Pfami
View protein in Pfam
PF00069 Pkinase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00220 S_TKc, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

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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.

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
Isoform 1 (identifier: P49137-1) [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.

« Hide
        10         20         30         40         50
MLSNSQGQSP PVPFPAPAPP PQPPTPALPH PPAQPPPPPP QQFPQFHVKS
60 70 80 90 100
GLQIKKNAII DDYKVTSQVL GLGINGKVLQ IFNKRTQEKF ALKMLQDCPK
110 120 130 140 150
ARREVELHWR ASQCPHIVRI VDVYENLYAG RKCLLIVMEC LDGGELFSRI
160 170 180 190 200
QDRGDQAFTE REASEIMKSI GEAIQYLHSI NIAHRDVKPE NLLYTSKRPN
210 220 230 240 250
AILKLTDFGF AKETTSHNSL TTPCYTPYYV APEVLGPEKY DKSCDMWSLG
260 270 280 290 300
VIMYILLCGY PPFYSNHGLA ISPGMKTRIR MGQYEFPNPE WSEVSEEVKM
310 320 330 340 350
LIRNLLKTEP TQRMTITEFM NHPWIMQSTK VPQTPLHTSR VLKEDKERWE
360 370 380 390 400
DVKEEMTSAL ATMRVDYEQI KIKKIEDASN PLLLKRRKKA RALEAAALAH
Note: Has a nuclear localization signal.
Length:400
Mass (Da):45,568
Last modified:February 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:iE4EFFF11CCF288DC
GO
Isoform 2 (identifier: P49137-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     354-400: EEMTSALATMRVDYEQIKIKKIEDASNPLLLKRRKKARALEAAALAH → GCLHDKNSDQATWLTRL

Show »
Length:370
Mass (Da):42,203
Checksum:iFF09AD93D4F73BDB
GO

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 conflicti116H → D in CAA53094 (PubMed:8280084).Curated1
Sequence conflicti247 – 248WS → LV in CAA53094 (PubMed:8280084).Curated2

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_040753173A → G1 PublicationCorresponds to variant dbSNP:rs35671930Ensembl.1
Natural variantiVAR_040754361A → S1 PublicationCorresponds to variant dbSNP:rs55894011Ensembl.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. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_004910354 – 400EEMTS…AALAH → GCLHDKNSDQATWLTRL in isoform 2. 1 PublicationAdd BLAST47

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
U12779 mRNA Translation: AAA20851.1
AL591846 Genomic DNA No translation available.
CH471100 Genomic DNA Translation: EAW93526.1
CH471100 Genomic DNA Translation: EAW93529.1
BC036060 mRNA Translation: AAH36060.2
BC052584 mRNA Translation: AAH52584.1
X75346 mRNA Translation: CAA53094.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS1466.1 [P49137-2]
CCDS31001.1 [P49137-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
JC2204
S39793

NCBI Reference Sequences

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RefSeqi
NP_004750.1, NM_004759.4 [P49137-2]
NP_116584.2, NM_032960.3 [P49137-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.643566
Hs.713747

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000294981; ENSP00000294981; ENSG00000162889 [P49137-2]
ENST00000367103; ENSP00000356070; ENSG00000162889 [P49137-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
9261

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:9261

UCSC genome browser

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UCSCi
uc001hel.3 human [P49137-1]

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12779 mRNA Translation: AAA20851.1
AL591846 Genomic DNA No translation available.
CH471100 Genomic DNA Translation: EAW93526.1
CH471100 Genomic DNA Translation: EAW93529.1
BC036060 mRNA Translation: AAH36060.2
BC052584 mRNA Translation: AAH52584.1
X75346 mRNA Translation: CAA53094.1
CCDSiCCDS1466.1 [P49137-2]
CCDS31001.1 [P49137-1]
PIRiJC2204
S39793
RefSeqiNP_004750.1, NM_004759.4 [P49137-2]
NP_116584.2, NM_032960.3 [P49137-1]
UniGeneiHs.643566
Hs.713747

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
1KWPX-ray2.80A/B1-400[»]
1NXKX-ray2.70A/B/C/D1-400[»]
1NY3X-ray3.00A1-400[»]
2JBOX-ray3.10A41-364[»]
2JBPX-ray3.31A/B/C/D/E/F/G/H/I/J/K/L41-364[»]
2OKRX-ray2.00C/F370-393[»]
2ONLX-ray4.00C/D1-400[»]
2OZAX-ray2.70A47-400[»]
2P3GX-ray3.80X45-371[»]
2PZYX-ray2.90A/B/C/D41-364[»]
3A2CX-ray2.90A/B/C/D/E/F/G/H/I/J/K/L41-364[»]
3FPMX-ray3.30A41-364[»]
3FYJX-ray3.80X45-371[»]
3FYKX-ray3.50X45-371[»]
3GOKX-ray3.20A/B/C/D/E/F/G/H/I/J/K/L41-364[»]
3KA0X-ray2.90A47-366[»]
3KC3X-ray2.90A/B/C/D/E/F/G/H/I/J/K/L41-364[»]
3KGAX-ray2.55A47-364[»]
3M2WX-ray2.41A47-364[»]
3M42X-ray2.68A47-364[»]
3R2BX-ray2.90A/B/C/D/E/F/G/H/I/J/K/L47-364[»]
3R2YX-ray3.00A46-364[»]
3R30X-ray3.20A46-364[»]
3WI6X-ray2.99A/B/C/D/E/F41-364[»]
4TYHX-ray3.00A51-400[»]
ProteinModelPortaliP49137
SMRiP49137
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114683, 63 interactors
DIPiDIP-35671N
ELMiP49137
IntActiP49137, 15 interactors
MINTiP49137
STRINGi9606.ENSP00000356070

Chemistry databases

BindingDBiP49137
ChEMBLiCHEMBL2208
DrugBankiDB02010 Staurosporine
GuidetoPHARMACOLOGYi2094

PTM databases

iPTMnetiP49137
PhosphoSitePlusiP49137

Polymorphism and mutation databases

BioMutaiMAPKAPK2
DMDMi1346538

Proteomic databases

EPDiP49137
MaxQBiP49137
PaxDbiP49137
PeptideAtlasiP49137
PRIDEiP49137
ProteomicsDBi55964
55965 [P49137-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
9261
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000294981; ENSP00000294981; ENSG00000162889 [P49137-2]
ENST00000367103; ENSP00000356070; ENSG00000162889 [P49137-1]
GeneIDi9261
KEGGihsa:9261
UCSCiuc001hel.3 human [P49137-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
9261
DisGeNETi9261
EuPathDBiHostDB:ENSG00000162889.10

GeneCards: human genes, protein and diseases

More...
GeneCardsi
MAPKAPK2
HGNCiHGNC:6887 MAPKAPK2
HPAiCAB010297
HPA045556
HPA063708
HPA064435
MIMi602006 gene
neXtProtiNX_P49137
OpenTargetsiENSG00000162889
PharmGKBiPA30631

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0604 Eukaryota
ENOG410XP8F LUCA
GeneTreeiENSGT00940000157261
HOGENOMiHOG000233031
HOVERGENiHBG106948
InParanoidiP49137
KOiK04443
OMAiGMKSRIR
OrthoDBiEOG091G14PL
PhylomeDBiP49137
TreeFamiTF312891

Enzyme and pathway databases

BioCyciMetaCyc:HS08751-MONOMER
BRENDAi2.7.11.1 2681
ReactomeiR-HSA-171007 p38MAPK events
R-HSA-199920 CREB phosphorylation
R-HSA-2142691 Synthesis of Leukotrienes (LT) and Eoxins (EX)
R-HSA-2559580 Oxidative Stress Induced Senescence
R-HSA-3371453 Regulation of HSF1-mediated heat shock response
R-HSA-4420097 VEGFA-VEGFR2 Pathway
R-HSA-450302 activated TAK1 mediates p38 MAPK activation
R-HSA-450385 Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA
R-HSA-450513 Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA
SignaLinkiP49137
SIGNORiP49137

Miscellaneous databases

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

More...
ChiTaRSi
MAPKAPK2 human
EvolutionaryTraceiP49137

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
MAPKAPK2

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

More...
GenomeRNAii
9261

Protein Ontology

More...
PROi
PR:P49137

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000162889 Expressed in 233 organ(s), highest expression level in apex of heart
CleanExiHS_MAPKAPK2
GenevisibleiP49137 HS

Family and domain databases

Gene3Di4.10.1170.10, 1 hit
InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR027442 MAPKAPK_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 nameiMAPK2_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: P49137
Secondary accession number(s): Q5SY30, Q5SY41, Q8IYD6
<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 1, 1996
Last sequence update: February 1, 1996
Last modified: December 5, 2018
This is version 195 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.

<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, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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 and mouse protein kinases
    Human and mouse protein kinases: classification and index
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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