Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - Q16644 (MAPK3_HUMAN)

Entry version 170 (13 Feb 2019)
Sequence version 1 (01 Nov 1996)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
Protein

MAP kinase-activated protein kinase 3

Gene

MAPKAPK3

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 cytokines production, endocytosis, cell migration, chromatin remodeling 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. MAPKAPK2 and MAPKAPK3, share the same function and substrate specificity, but MAPKAPK3 kinase activity and level in protein expression are lower compared to MAPKAPK2. Phosphorylates HSP27/HSPB1, KRT18, KRT20, RCSD1, RPS6KA3, TAB3 and TTP/ZFP36. Mediates phosphorylation of HSP27/HSPB1 in response to stress, leading to dissociate HSP27/HSPB1 from large small heat-shock protein (sHsps) oligomers and impair 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, such as TTP/ZFP36, leading to regulate 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 transcript. Involved in toll-like receptor signaling pathway (TLR) in dendritic cells: required for acute TLR-induced macropinocytosis by phosphorylating and activating RPS6KA3. Also acts as a modulator of Polycomb-mediated repression.6 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 by ligand 5B (2'-[2-(1,3-benzodioxol-5-yl)pyrimidin-4-yl]-5',6'-dihydrospiro[piperidine-4,7'-pyrrolo[3,2-c]pyridin]- 4'(1'h)-one) and ligand P4O (2-[2-(2-fluorophenyl)pyridin-4-yl]-1,5,6,7-tetrahydro- 4h-pyrrolo[3,2-c]pyridin-4-one), 2 ATP-competitive 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 sitei73ATPPROSITE-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 sitei166Proton 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 bindingi50 – 58ATPPROSITE-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 binding Source: GO_Central
  • calmodulin-dependent protein kinase activity Source: GO_Central
  • MAP kinase kinase activity Source: ProtInc
  • mitogen-activated protein kinase binding Source: GO_Central
  • protein serine/threonine kinase activity Source: UniProtKB
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
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-171007 p38MAPK events
R-HSA-2559580 Oxidative Stress Induced Senescence
R-HSA-4420097 VEGFA-VEGFR2 Pathway
R-HSA-450302 activated TAK1 mediates p38 MAPK activation

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

More...SignaLinki		Q16644

SIGNOR Signaling Network Open Resource

More...SIGNORi		Q16644

<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 3 (EC:2.7.11.1)
Short name:
MAPK-activated protein kinase 3
Short name:
MAPKAP kinase 3
Short name:
MAPKAP-K3
Short name:
MAPKAPK-3
Short name:
MK-3
Alternative name(s):
Chromosome 3p kinase
Short name:
3pK
<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:MAPKAPK3
<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 3

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000114738.10

Human Gene Nomenclature Database

More...HGNCi		HGNC:6888 MAPKAPK3

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		602130 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q16644

<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

<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

Macular dystrophy, patterned, 3 (MDPT3)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of retinal patterned dystrophy, characterized by retinal pigment epithelium and Bruch's membrane changes resembling a 'dry desert land'. It begins around the age of 30 and progresses to retinitis pigmentosa. MDPT3 inheritance is autosomal dominant.
See also OMIM:617111
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_077085173L → P in MDPT3; decreased localization to the nucleus. 1 PublicationCorresponds to variant dbSNP:rs886037913EnsemblClinVar.1

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>Mutagenesisi73K → M: Higher affinity toward PCH2. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...DisGeNETi		7867

MalaCards human disease database

More...MalaCardsi		MAPKAPK3
MIMi617111 phenotype

Open Targets

More...OpenTargetsi		ENSG00000114738

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

More...Orphaneti		466718 Martinique crinkled retinal pigment epitheliopathy

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA30632

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL4670

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		2095

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		MAPKAPK3

Domain mapping of disease mutations (DMDM)

More...DMDMi		74762148

<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_00000862931 – 382MAP kinase-activated protein kinase 3Add BLAST382

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
Modified residuei201Phosphothreonine; by MAPK14By similarity1
Modified residuei251Phosphoserine; by MAPK14By similarity1
Modified residuei307Phosphoserine; by autocatalysisBy similarity1
Modified residuei313Phosphothreonine; by MAPK14By similarity1

<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 and activated by MAPK1/ERK2 and MAPK3/ERK1. Phosphorylated and activated by MAP kinase p38-alpha/MAPK14 at Thr-201, Ser-251 and Thr-313 (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q16644

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q16644

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q16644

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

More...PaxDbi		Q16644

PeptideAtlas

More...PeptideAtlasi		Q16644

PRoteomics IDEntifications database

More...PRIDEi		Q16644

ProteomicsDB human proteome resource

More...ProteomicsDBi		60998

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q16644

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

More...PhosphoSitePlusi		Q16644

<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

Widely expressed, with a higher expression level observed in heart and skeletal muscle. No expression in brain. Expressed in the retinal pigment epithelium (PubMed:26744326).3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000114738 Expressed in 232 organ(s), highest expression level in cardiac ventricle

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q16644 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q16644 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		HPA058275

<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. The heterodimer with p38-alpha/MAPK14 forms a stable complex: molecules are positioned 'face to face' so that the ATP-binding sites of both kinases are at the heterodimer interface (By similarity). Interacts with TCF3 and with polycomb proteins, such as PCH2 and BMI1/PCGF4.By similarity4 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		113617, 30 interactors

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		Q16644

Protein interaction database and analysis system

More...IntActi		Q16644, 27 interactors

Molecular INTeraction database

More...MINTi		Q16644

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000350639

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q16644

<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

1382
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
3FHRX-ray1.90A33-349[»]
3FXWX-ray2.00A33-349[»]
3R1NX-ray2.09A33-349[»]
3SHEX-ray2.25A33-349[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		Q16644

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

More...SMRi		Q16644

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q16644

<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>Domaini44 – 304Protein 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>Regioni307 – 343Autoinhibitory helixBy similarityAdd BLAST37
Regioni345 – 369p38 MAPK-binding siteBy similarityAdd 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>Motifi335 – 344Nuclear export signal (NES)By similarity10
Motifi350 – 353Bipartite nuclear localization signal 1By similarity4
Motifi364 – 368Bipartite nuclear localization signal 2By similarity5

<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. CAMK Ser/Thr protein kinase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0604 Eukaryota
ENOG410XP8F LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000154089

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000233031

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG106948

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q16644

KEGG Orthology (KO)

More...KOi		K04444

Identification of Orthologs from Complete Genome Data

More...OMAi		RMGQYGF

Database of Orthologous Groups

More...OrthoDBi		843707at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q16644

TreeFam database of animal gene trees

More...TreeFami		TF312891

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		4.10.1170.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...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

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>Sequence (1+)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 has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

Q16644-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDGETAEEQG GPVPPPVAPG GPGLGGAPGG RREPKKYAVT DDYQLSKQVL 
        60         70         80         90        100
GLGVNGKVLE CFHRRTGQKC ALKLLYDSPK ARQEVDHHWQ ASGGPHIVCI 
       110        120        130        140        150
LDVYENMHHG KRCLLIIMEC MEGGELFSRI QERGDQAFTE REAAEIMRDI 
       160        170        180        190        200
GTAIQFLHSH NIAHRDVKPE NLLYTSKEKD AVLKLTDFGF AKETTQNALQ 
       210        220        230        240        250
TPCYTPYYVA PEVLGPEKYD KSCDMWSLGV IMYILLCGFP PFYSNTGQAI 
       260        270        280        290        300
SPGMKRRIRL GQYGFPNPEW SEVSEDAKQL IRLLLKTDPT ERLTITQFMN 
       310        320        330        340        350
HPWINQSMVV PQTPLHTARV LQEDKDHWDE VKEEMTSALA TMRVDYDQVK 
       360        370        380 
IKDLKTSNNR LLNKRRKKQA GSSSASQGCN NQ
Length:382
Mass (Da):42,987
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:i405F958B7F54E6F3
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 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H7C0G6H7C0G6_HUMAN
MAP kinase-activated protein kinase...
MAPKAPK3
97Annotation 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>
C9J8E1C9J8E1_HUMAN
MAP kinase-activated protein kinase...
MAPKAPK3
332Annotation 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>
C9JPW3C9JPW3_HUMAN
MAP kinase-activated protein kinase...
MAPKAPK3
119Annotation 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_04075528P → S in a glioblastoma multiforme sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs375412266Ensembl.1
Natural variantiVAR_040756105E → A in an ovarian endometrioid sample; somatic mutation. 1 Publication1
Natural variantiVAR_077085173L → P in MDPT3; decreased localization to the nucleus. 1 PublicationCorresponds to variant dbSNP:rs886037913EnsemblClinVar.1
Natural variantiVAR_040757276D → Y1 PublicationCorresponds to variant dbSNP:rs56107897Ensembl.1

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
U43784 mRNA Translation: AAC50428.1
U09578 mRNA Translation: AAD09136.1
AB451303 mRNA Translation: BAG70117.1
CH471055 Genomic DNA Translation: EAW65131.1
BC001662 mRNA Translation: AAH01662.1
BC007591 mRNA Translation: AAH07591.1
BC010407 mRNA Translation: AAH10407.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS2832.1

Protein sequence database of the Protein Information Resource

More...PIRi		JC6094

NCBI Reference Sequences

More...RefSeqi		NP_001230854.1, NM_001243925.1
NP_001230855.1, NM_001243926.1
NP_004626.1, NM_004635.4

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.234521
Hs.735013

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000357955; ENSP00000350639; ENSG00000114738
ENST00000446044; ENSP00000396467; ENSG00000114738
ENST00000621469; ENSP00000478922; ENSG00000114738

Database of genes from NCBI RefSeq genomes

More...GeneIDi		7867

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:7867

UCSC genome browser

More...UCSCi		uc003day.3 human

Keywords - Coding sequence diversityi

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
U43784 mRNA Translation: AAC50428.1
U09578 mRNA Translation: AAD09136.1
AB451303 mRNA Translation: BAG70117.1
CH471055 Genomic DNA Translation: EAW65131.1
BC001662 mRNA Translation: AAH01662.1
BC007591 mRNA Translation: AAH07591.1
BC010407 mRNA Translation: AAH10407.1
CCDSiCCDS2832.1
PIRiJC6094
RefSeqiNP_001230854.1, NM_001243925.1
NP_001230855.1, NM_001243926.1
NP_004626.1, NM_004635.4
UniGeneiHs.234521
Hs.735013

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3FHRX-ray1.90A33-349[»]
3FXWX-ray2.00A33-349[»]
3R1NX-ray2.09A33-349[»]
3SHEX-ray2.25A33-349[»]
ProteinModelPortaliQ16644
SMRiQ16644
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113617, 30 interactors
ELMiQ16644
IntActiQ16644, 27 interactors
MINTiQ16644
STRINGi9606.ENSP00000350639

Chemistry databases

BindingDBiQ16644
ChEMBLiCHEMBL4670
GuidetoPHARMACOLOGYi2095

PTM databases

iPTMnetiQ16644
PhosphoSitePlusiQ16644

Polymorphism and mutation databases

BioMutaiMAPKAPK3
DMDMi74762148

Proteomic databases

EPDiQ16644
jPOSTiQ16644
MaxQBiQ16644
PaxDbiQ16644
PeptideAtlasiQ16644
PRIDEiQ16644
ProteomicsDBi60998

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		7867
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000357955; ENSP00000350639; ENSG00000114738
ENST00000446044; ENSP00000396467; ENSG00000114738
ENST00000621469; ENSP00000478922; ENSG00000114738
GeneIDi7867
KEGGihsa:7867
UCSCiuc003day.3 human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		7867
DisGeNETi7867
EuPathDBiHostDB:ENSG00000114738.10

GeneCards: human genes, protein and diseases

More...GeneCardsi		MAPKAPK3
HGNCiHGNC:6888 MAPKAPK3
HPAiHPA058275
MalaCardsiMAPKAPK3
MIMi602130 gene
617111 phenotype
neXtProtiNX_Q16644
OpenTargetsiENSG00000114738
Orphaneti466718 Martinique crinkled retinal pigment epitheliopathy
PharmGKBiPA30632

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0604 Eukaryota
ENOG410XP8F LUCA
GeneTreeiENSGT00940000154089
HOGENOMiHOG000233031
HOVERGENiHBG106948
InParanoidiQ16644
KOiK04444
OMAiRMGQYGF
OrthoDBi843707at2759
PhylomeDBiQ16644
TreeFamiTF312891

Enzyme and pathway databases

ReactomeiR-HSA-171007 p38MAPK events
R-HSA-2559580 Oxidative Stress Induced Senescence
R-HSA-4420097 VEGFA-VEGFR2 Pathway
R-HSA-450302 activated TAK1 mediates p38 MAPK activation
SignaLinkiQ16644
SIGNORiQ16644

Miscellaneous databases

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

More...ChiTaRSi		MAPKAPK3 human
EvolutionaryTraceiQ16644

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		MAPKAPK3

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

More...GenomeRNAii		7867

Protein Ontology

More...PROi		PR:Q16644

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000114738 Expressed in 232 organ(s), highest expression level in cardiac ventricle
ExpressionAtlasiQ16644 baseline and differential
GenevisibleiQ16644 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 nameiMAPK3_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: Q16644
Secondary accession number(s): B5BU67
<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: December 6, 2005
Last sequence update: November 1, 1996
Last modified: February 13, 2019
This is version 170 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again