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Entry version 188 (13 Feb 2019)
Sequence version 2 (30 May 2000)
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Protein

Dual specificity mitogen-activated protein kinase kinase 7

Gene

MAP2K7

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

Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. Essential component of the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. With MAP2K4/MKK4, is the one of the only known kinase to directly activate the stress-activated protein kinase/c-Jun N-terminal kinases MAPK8/JNK1, MAPK9/JNK2 and MAPK10/JNK3. MAP2K4/MKK4 and MAP2K7/MKK7 both activate the JNKs by phosphorylation, but they differ in their preference for the phosphorylation site in the Thr-Pro-Tyr motif. MAP2K4/MKK4 shows preference for phosphorylation of the Tyr residue and MAP2K7/MKK7 for the Thr residue. The monophosphorylation of JNKs on the Thr residue is sufficient to increase JNK activity indicating that MAP2K7/MKK7 is important to trigger JNK activity, while the additional phosphorylation of the Tyr residue by MAP2K4/MKK4 ensures optimal JNK activation. Has a specific role in JNK signal transduction pathway activated by proinflammatory cytokines. The MKK/JNK signaling pathway is also involved in mitochondrial death signaling pathway, including the release cytochrome c, leading to apoptosis. Part of a non-canonical MAPK signaling pathway, composed of the upstream MAP3K12 kinase and downstream MAP kinases MAPK1/ERK2 and MAPK3/ERK1, that enhances the AP-1-mediated transcription of APP in response to APOE (PubMed:28111074).5 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

Activated by phosphorylation by specific MAP kinase kinase kinases such as MAP3K1/MEKK1, MAP3K3/MEKK3, MAP3K11/MLK3 and MAP3K12/DLK.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 sitei149ATPPROSITE-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 sitei243Proton 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 bindingi126 – 134ATPPROSITE-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
  • enzyme binding Source: BHF-UCL
  • JUN kinase kinase activity Source: GO_Central
  • magnesium ion binding Source: UniProtKB
  • MAP kinase kinase activity Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • protein phosphatase binding Source: BHF-UCL
  • protein serine/threonine kinase activity Source: GO_Central
  • protein tyrosine kinase activity Source: UniProtKB-KW

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, Tyrosine-protein kinase
Biological processApoptosis, Stress response
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
2.7.12.2 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-2559580 Oxidative Stress Induced Senescence
R-HSA-2871796 FCERI mediated MAPK activation
R-HSA-450321 JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1
R-HSA-5210891 Uptake and function of anthrax toxins

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

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SignaLinki
O14733

SIGNOR Signaling Network Open Resource

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SIGNORi
O14733

<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:
Dual specificity mitogen-activated protein kinase kinase 7 (EC:2.7.12.2)
Short name:
MAP kinase kinase 7
Short name:
MAPKK 7
Alternative name(s):
JNK-activating kinase 2
MAPK/ERK kinase 7
Short name:
MEK 7
Stress-activated protein kinase kinase 4
Short name:
SAPK kinase 4
Short name:
SAPKK-4
Short name:
SAPKK4
c-Jun N-terminal kinase kinase 2
Short name:
JNK kinase 2
Short name:
JNKK 2
<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:MAP2K7
Synonyms:JNKK2, MEK7, MKK7, PRKMK7, SKK4
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 19

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000076984.17

Human Gene Nomenclature Database

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HGNCi
HGNC:6847 MAP2K7

Online Mendelian Inheritance in Man (OMIM)

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MIMi
603014 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_O14733

<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

Organism-specific databases

DisGeNET

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DisGeNETi
5609

Open Targets

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OpenTargetsi
ENSG00000076984

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA284

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL3530

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
2068

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
MAP2K7

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<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_00000863882 – 419Dual specificity mitogen-activated protein kinase kinase 7Add BLAST418

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 residuei2N-acetylalanineCombined sources1
Modified residuei271Phosphoserine; by MAP3KBy similarity1
Modified residuei275Phosphothreonine; by MAP3KBy similarity1
Modified residuei411PhosphoserineCombined 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

Activated by phosphorylation on Ser-271 and Thr-275 by MAP kinase kinase kinases (MAP3Ks).By similarity

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>Sitei44 – 45Cleavage; by anthrax lethal factor2
Sitei76 – 77Cleavage; by anthrax lethal factor2

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
O14733

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
O14733

MaxQB - The MaxQuant DataBase

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MaxQBi
O14733

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

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PaxDbi
O14733

PeptideAtlas

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PeptideAtlasi
O14733

PRoteomics IDEntifications database

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PRIDEi
O14733

ProteomicsDB human proteome resource

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ProteomicsDBi
48192
48193 [O14733-2]
48194 [O14733-3]
48195 [O14733-4]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
O14733

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

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PhosphoSitePlusi
O14733

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
O14733

<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

Ubiquitous; with highest level of expression in skeletal muscle. Isoform 3 is found at low levels in placenta, fetal liver, and skeletal muscle.3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000076984 Expressed in 225 organ(s), highest expression level in buccal mucosa cell

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
O14733 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB004262
HPA001633
HPA064711

<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

Interacts with isoform 1 of VRK2. Interacts (via its D domain) with its substrates MAPK8/JNK1, MAPK9/JNK2 and MAPK10/JNK3 (By similarity). Interacts (via its DVD domain) with MAP3Ks activators like MAP3K5/ASK1 and MAP3K1/MEKK1 (By similarity). Interacts with MAPK8IP1/JIP1, MAPK8IP2/JIP2 and MAPK8IP3/JIP3 scaffold proteins. Interacts with RASSF7, the interaction promotes phosphorylation. Found in a complex with SH3RF1, RAC1, MAP3K11/MLK3, MAPK8IP1/JIP1 and MAPK8/JNK1. Found in a complex with SH3RF1, RAC2, MAP3K7/TAK1, MAPK8IP1/JIP1, MAPK8/JNK1 and MAPK9/JNK2 (By similarity).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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
111595, 63 interactors

Protein interaction database and analysis system

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IntActi
O14733, 26 interactors

Molecular INTeraction database

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MINTi
O14733

STRING: functional protein association networks

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STRINGi
9606.ENSP00000381066

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
O14733

<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

1419
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DYLX-ray2.45A101-405[»]
3WZUX-ray3.01A103-419[»]
4UX9X-ray2.34F/G/H/I37-48[»]
5B2KX-ray2.75A103-419[»]
5B2LX-ray2.10A103-419[»]
5B2MX-ray3.06A103-419[»]
5Y8UX-ray2.92A103-419[»]
5Y90X-ray1.30A103-419[»]
5Z1DX-ray2.28A102-419[»]
5Z1EX-ray2.30A102-419[»]

Database of protein disorder

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DisProti
DP00841

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
O14733

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

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SMRi
O14733

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

More...
EvolutionaryTracei
O14733

<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>Domaini120 – 380Protein 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>Regioni37 – 57D domainBy similarityAdd BLAST21
Regioni377 – 400DVD domainAdd BLAST24

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 coili2 – 30Sequence analysisAdd BLAST29

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The DVD domain (residues 377-400) contains a conserved docking site and is found in the mammalian MAP kinase kinases (MAP2Ks). The DVD sites bind to their specific upstream MAP kinase kinase kinases (MAP3Ks) and are essential for activation.1 Publication
The D domain (residues 37-57) contains a conserved docking site and is required for the binding to MAPK substrates.1 Publication

<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

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0983 Eukaryota
ENOG410XTNQ LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000158914

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG108518

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O14733

KEGG Orthology (KO)

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KOi
K04431

Identification of Orthologs from Complete Genome Data

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OMAi
SSQCYSH

Database of Orthologous Groups

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OrthoDBi
688282at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
O14733

TreeFam database of animal gene trees

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TreeFami
TF350701

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
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

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SUPFAMi
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
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 (4)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 4 <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: O14733-1) [UniParc]FASTAAdd to basket
Also known as: A

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
MAASSLEQKL SRLEAKLKQE NREARRRIDL NLDISPQRPR PTLQLPLAND
60 70 80 90 100
GGSRSPSSES SPQHPTPPAR PRHMLGLPST LFTPRSMESI EIDQKLQEIM
110 120 130 140 150
KQTGYLTIGG QRYQAEINDL ENLGEMGSGT CGQVWKMRFR KTGHVIAVKQ
160 170 180 190 200
MRRSGNKEEN KRILMDLDVV LKSHDCPYIV QCFGTFITNT DVFIAMELMG
210 220 230 240 250
TCAEKLKKRM QGPIPERILG KMTVAIVKAL YYLKEKHGVI HRDVKPSNIL
260 270 280 290 300
LDERGQIKLC DFGISGRLVD SKAKTRSAGC AAYMAPERID PPDPTKPDYD
310 320 330 340 350
IRADVWSLGI SLVELATGQF PYKNCKTDFE VLTKVLQEEP PLLPGHMGFS
360 370 380 390 400
GDFQSFVKDC LTKDHRKRPK YNKLLEHSFI KRYETLEVDV ASWFKDVMAK
410
TESPRTSGVL SQPHLPFFR
Length:419
Mass (Da):47,485
Last modified:May 30, 2000 - 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:iF1B22E050F54299A
GO
Isoform 2 (identifier: O14733-2) [UniParc]FASTAAdd to basket
Also known as: B

The sequence of this isoform differs from the canonical sequence as follows:
     111-111: Q → QVPPSLWRGEGGGPARLDPSWERQWGAGGGGRAPGTLQPSLSSQ

Note: May be due to intron retention.
Show »
Length:462
Mass (Da):51,881
Checksum:iDF3496066961B0C7
GO
Isoform 3 (identifier: O14733-3) [UniParc]FASTAAdd to basket
Also known as: gamma1

The sequence of this isoform differs from the canonical sequence as follows:
     42-42: T → IIVITLSPAPAPSQRAA

Show »
Length:435
Mass (Da):49,071
Checksum:i8812A87DB28F2C22
GO
Isoform 4 (identifier: O14733-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     312-312: L → LPCPSPSQ

Note: No experimental confirmation available.
Show »
Length:426
Mass (Da):48,182
Checksum:i7934E29217D8A137
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAB97813 differs from that shown. Reason: Frameshift at positions 402 and 410.Curated
The sequence AAB97813 differs from that shown. Reason: Erroneous termination at position 420. Translated as stop.Curated

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 conflicti94Q → H in AAB97813 (PubMed:9312068).Curated1
Sequence conflicti106L → P in ABE03013 (PubMed:16442502).Curated1
Sequence conflicti133Q → P in AAB97813 (PubMed:9312068).Curated1
Sequence conflicti142T → N in AAB88048 (PubMed:9372971).Curated1
Sequence conflicti407S → N in AAB97813 (PubMed:9312068).Curated1
Sequence conflicti415L → LG in AAB97813 (PubMed:9312068).Curated1

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_040825118N → S1 PublicationCorresponds to variant dbSNP:rs56316660Ensembl.1
Natural variantiVAR_040826138R → C1 PublicationCorresponds to variant dbSNP:rs56106612Ensembl.1
Natural variantiVAR_040827162R → C in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_040828162R → H in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_040829195A → T1 PublicationCorresponds to variant dbSNP:rs55800262Ensembl.1
Natural variantiVAR_029890259L → F1 PublicationCorresponds to variant dbSNP:rs1053566Ensembl.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_02230942T → IIVITLSPAPAPSQRAA in isoform 3. 1 Publication1
Alternative sequenceiVSP_004883111Q → QVPPSLWRGEGGGPARLDPS WERQWGAGGGGRAPGTLQPS LSSQ in isoform 2. 1 Publication1
Alternative sequenceiVSP_022310312L → LPCPSPSQ in isoform 4. 1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF014401 mRNA Translation: AAB88048.1
AF006689 mRNA Translation: AAB97813.1 Sequence problems.
AF013588 mRNA Translation: AAC16272.1
AF013589 mRNA Translation: AAC16273.1
DQ445915 mRNA Translation: ABE03013.1
AF022805 mRNA Translation: AAC26142.1
AK313899 mRNA Translation: BAG36622.1
CH471139 Genomic DNA Translation: EAW68964.1
CH471139 Genomic DNA Translation: EAW68968.1
BC038295 mRNA Translation: AAH38295.1
AF003199 mRNA Translation: AAB63374.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS42491.1 [O14733-1]
CCDS74277.1 [O14733-3]
CCDS74278.1 [O14733-4]

NCBI Reference Sequences

More...
RefSeqi
NP_001284484.1, NM_001297555.1 [O14733-3]
NP_001284485.1, NM_001297556.1 [O14733-4]
NP_660186.1, NM_145185.3 [O14733-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.531754

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000397979; ENSP00000381066; ENSG00000076984 [O14733-1]
ENST00000397981; ENSP00000381068; ENSG00000076984 [O14733-4]
ENST00000397983; ENSP00000381070; ENSG00000076984 [O14733-3]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
5609

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:5609

UCSC genome browser

More...
UCSCi
uc002mit.4 human [O14733-1]

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
AF014401 mRNA Translation: AAB88048.1
AF006689 mRNA Translation: AAB97813.1 Sequence problems.
AF013588 mRNA Translation: AAC16272.1
AF013589 mRNA Translation: AAC16273.1
DQ445915 mRNA Translation: ABE03013.1
AF022805 mRNA Translation: AAC26142.1
AK313899 mRNA Translation: BAG36622.1
CH471139 Genomic DNA Translation: EAW68964.1
CH471139 Genomic DNA Translation: EAW68968.1
BC038295 mRNA Translation: AAH38295.1
AF003199 mRNA Translation: AAB63374.1
CCDSiCCDS42491.1 [O14733-1]
CCDS74277.1 [O14733-3]
CCDS74278.1 [O14733-4]
RefSeqiNP_001284484.1, NM_001297555.1 [O14733-3]
NP_001284485.1, NM_001297556.1 [O14733-4]
NP_660186.1, NM_145185.3 [O14733-1]
UniGeneiHs.531754

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DYLX-ray2.45A101-405[»]
3WZUX-ray3.01A103-419[»]
4UX9X-ray2.34F/G/H/I37-48[»]
5B2KX-ray2.75A103-419[»]
5B2LX-ray2.10A103-419[»]
5B2MX-ray3.06A103-419[»]
5Y8UX-ray2.92A103-419[»]
5Y90X-ray1.30A103-419[»]
5Z1DX-ray2.28A102-419[»]
5Z1EX-ray2.30A102-419[»]
DisProtiDP00841
ProteinModelPortaliO14733
SMRiO14733
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111595, 63 interactors
IntActiO14733, 26 interactors
MINTiO14733
STRINGi9606.ENSP00000381066

Chemistry databases

BindingDBiO14733
ChEMBLiCHEMBL3530
GuidetoPHARMACOLOGYi2068

PTM databases

iPTMnetiO14733
PhosphoSitePlusiO14733

Polymorphism and mutation databases

BioMutaiMAP2K7

Proteomic databases

EPDiO14733
jPOSTiO14733
MaxQBiO14733
PaxDbiO14733
PeptideAtlasiO14733
PRIDEiO14733
ProteomicsDBi48192
48193 [O14733-2]
48194 [O14733-3]
48195 [O14733-4]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
5609
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000397979; ENSP00000381066; ENSG00000076984 [O14733-1]
ENST00000397981; ENSP00000381068; ENSG00000076984 [O14733-4]
ENST00000397983; ENSP00000381070; ENSG00000076984 [O14733-3]
GeneIDi5609
KEGGihsa:5609
UCSCiuc002mit.4 human [O14733-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5609
DisGeNETi5609
EuPathDBiHostDB:ENSG00000076984.17

GeneCards: human genes, protein and diseases

More...
GeneCardsi
MAP2K7
HGNCiHGNC:6847 MAP2K7
HPAiCAB004262
HPA001633
HPA064711
MIMi603014 gene
neXtProtiNX_O14733
OpenTargetsiENSG00000076984
PharmGKBiPA284

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0983 Eukaryota
ENOG410XTNQ LUCA
GeneTreeiENSGT00940000158914
HOVERGENiHBG108518
InParanoidiO14733
KOiK04431
OMAiSSQCYSH
OrthoDBi688282at2759
PhylomeDBiO14733
TreeFamiTF350701

Enzyme and pathway databases

BRENDAi2.7.12.2 2681
ReactomeiR-HSA-2559580 Oxidative Stress Induced Senescence
R-HSA-2871796 FCERI mediated MAPK activation
R-HSA-450321 JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1
R-HSA-5210891 Uptake and function of anthrax toxins
SignaLinkiO14733
SIGNORiO14733

Miscellaneous databases

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

More...
ChiTaRSi
MAP2K7 human
EvolutionaryTraceiO14733

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
MAP2K7

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

More...
GenomeRNAii
5609
PMAP-CutDBiO14733

Protein Ontology

More...
PROi
PR:O14733

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000076984 Expressed in 225 organ(s), highest expression level in buccal mucosa cell
GenevisibleiO14733 HS

Family and domain databases

InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
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
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 nameiMP2K7_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: O14733
Secondary accession number(s): B2R9S5
, D6W659, O14648, O14816, O60452, O60453, Q1PG43, Q8IY10
<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: May 30, 2000
Last sequence update: May 30, 2000
Last modified: February 13, 2019
This is version 188 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, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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