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Protein

Mitogen-activated protein kinase kinase kinase 7

Gene

MAP3K7

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

Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. Plays an important role in the cascades of cellular responses evoked by changes in the environment. Mediates signal transduction of TRAF6, various cytokines including interleukin-1 (IL-1), transforming growth factor-beta (TGFB), TGFB-related factors like BMP2 and BMP4, toll-like receptors (TLR), tumor necrosis factor receptor CD40 and B-cell receptor (BCR). Ceramides are also able to activate MAP3K7/TAK1. Once activated, acts as an upstream activator of the MKK/JNK signal transduction cascade and the p38 MAPK signal transduction cascade through the phosphorylation and activation of several MAP kinase kinases like MAP2K1/MEK1, MAP2K3/MKK3, MAP2K6/MKK6 and MAP2K7/MKK7. These MAP2Ks in turn activate p38 MAPKs, c-jun N-terminal kinases (JNKs) and I-kappa-B kinase complex (IKK). Both p38 MAPK and JNK pathways control the transcription factors activator protein-1 (AP-1), while nuclear factor-kappa B is activated by IKK. MAP3K7 activates also IKBKB and MAPK8/JNK1 in response to TRAF6 signaling and mediates BMP2-induced apoptosis. In osmotic stress signaling, plays a major role in the activation of MAPK8/JNK1, but not that of NF-kappa-B. Promotes TRIM5 capsid-specific restriction activity.8 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

<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 proinflammatory cytokines and in response to physical and chemical stresses, including osmotic stress, oxidative stress, arsenic and ultraviolet light irradiation. Activated by 'Lys-63'-linked polyubiquitination and by autophosphorylation. Association with TAB1/MAP3K7IP1 and TAB2/MAP3K7IP2 promotes activation through autophosphorylation, whereas PPM1B/PP2CB, PP2A and PPP6C dephosphorylation leads to inactivation.6 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 sitei63ATP1
<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 sitei156Proton 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 bindingi42 – 50ATPPROSITE-ProRule annotation9

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

GO - Biological processi

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

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processApoptosis, Host-virus interaction, Stress response, Transcription, Transcription regulation
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-1169091 Activation of NF-kappaB in B cells
R-HSA-168638 NOD1/2 Signaling Pathway
R-HSA-202424 Downstream TCR signaling
R-HSA-2871837 FCERI mediated NF-kB activation
R-HSA-4086398 Ca2+ pathway
R-HSA-445989 TAK1 activates NFkB by phosphorylation and activation of IKKs complex
R-HSA-450302 activated TAK1 mediates p38 MAPK activation
R-HSA-450321 JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1
R-HSA-5357956 TNFR1-induced NFkappaB signaling pathway
R-HSA-5607764 CLEC7A (Dectin-1) signaling
R-HSA-5689880 Ub-specific processing proteases
R-HSA-9014325 TICAM1,TRAF6-dependent induction of TAK1 complex
R-HSA-9020702 Interleukin-1 signaling
R-HSA-937042 IRAK2 mediated activation of TAK1 complex
R-HSA-937072 TRAF6-mediated induction of TAK1 complex within TLR4 complex
R-HSA-975163 IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation

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

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SignaLinki
O43318

SIGNOR Signaling Network Open Resource

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SIGNORi
O43318

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

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MoonDBi
O43318 Predicted

<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:
Mitogen-activated protein kinase kinase kinase 7 (EC:2.7.11.253 Publications)
Alternative name(s):
Transforming growth factor-beta-activated kinase 1
Short name:
TGF-beta-activated kinase 1
<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:MAP3K71 PublicationImported
Synonyms:TAK1
<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 6

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000135341.17

Human Gene Nomenclature Database

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HGNCi
HGNC:6859 MAP3K7

Online Mendelian Inheritance in Man (OMIM)

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MIMi
602614 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_O43318

<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

Cell membrane, Cytoplasm, Membrane

<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

Frontometaphyseal dysplasia 2 (FMD2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of frontometaphyseal dysplasia, a progressive sclerosing skeletal dysplasia affecting the long bones and skull. Characteristic features include supraorbital hyperostosis, cranial hyperostosis, undermodeling of the small bones, flared metaphyses, and digital anomalies. Extra-skeletal manifestations include hearing loss, cardiac malformations, and stenosis, particularly of the upper airway and urinary tract. FMD2 inheritance is autosomal dominant.
See also OMIM:617137
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_07734270E → Q in FMD2. 1 PublicationCorresponds to variant dbSNP:rs886039231EnsemblClinVar.1
Natural variantiVAR_077343100V → E in FMD2. 1 PublicationCorresponds to variant dbSNP:rs886039232EnsemblClinVar.1
Natural variantiVAR_077345168G → R in FMD2; increases autophosphorylation; no effect on MAPK signaling; no effect on NF-kappa-B signaling. 1 PublicationCorresponds to variant dbSNP:rs886039233EnsemblClinVar.1
Natural variantiVAR_077347512P → L in FMD2; does not affect interaction with TAB2; does not affect homodimerization; increases autophosphorylation; increases MAPK signaling; increases NF-kappa-B signaling. 1 PublicationCorresponds to variant dbSNP:rs886039230EnsemblClinVar.1
Cardiospondylocarpofacial syndrome (CSCF)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA syndrome characterized by growth retardation, dysmorphic facial features, brachydactyly with carpal-tarsal fusion and extensive posterior cervical vertebral synostosis, cardiac septal defects with valve dysplasia, and deafness with inner ear malformations. CSCF transmission pattern is consistent with autosomal dominant inheritance.
See also OMIM:157800
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07734150Missing in CSCF. 1 Publication1
Natural variantiVAR_077344110G → C in CSCF. 1 PublicationCorresponds to variant dbSNP:rs886039235EnsemblClinVar.1
Natural variantiVAR_077346241W → R in CSCF. 1 PublicationCorresponds to variant dbSNP:rs886039237EnsemblClinVar.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>Mutagenesisi34K → R: No effect on ubiquitination. 1 Publication1
Mutagenesisi63K → W: Loss of kinase activity. 1 Publication1
Mutagenesisi158K → R: Abolishes ubiquitination. 1 Publication1
Mutagenesisi209K → R: Strongly decreases ubiquitination. 1 Publication1
Mutagenesisi512P → R or A: Enhances autophosphorylation; Alters MAPK signaling. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

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DisGeNETi
6885

MalaCards human disease database

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MalaCardsi
MAP3K7
MIMi157800 phenotype
617137 phenotype

Open Targets

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OpenTargetsi
ENSG00000135341

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

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Orphaneti
3238 Cardiospondylocarpofacial syndrome
1826 Frontometaphyseal dysplasia

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA30603

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL5776

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
2082

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
MAP3K7

<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_00000862521 – 606Mitogen-activated protein kinase kinase kinase 7Add BLAST606

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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-linki72Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki158Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
<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 residuei184Phosphothreonine; by autocatalysis1 Publication1
Modified residuei187Phosphothreonine; by autocatalysis4 Publications1
Modified residuei192Phosphoserine; by autocatalysis2 Publications1
Cross-linki209Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei367PhosphoserineCombined sources1
Modified residuei389PhosphoserineCombined sources1
Modified residuei439PhosphoserineCombined sources1
Modified residuei455PhosphoserineCombined 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

Association with TAB1/MAP3K7IP1 promotes autophosphorylation at Ser-192 and subsequent activation. Association with TAB2/MAP3K7IP2, itself associated with free unanchored Lys-63 polyubiquitin chain, promotes autophosphorylation and subsequent activation of MAP3K7. Dephosphorylation at Ser-192 by PPM1B/PP2CB and at Thr-187 by PP2A and PPP6C leads to inactivation.6 Publications
'Lys-48'-linked polyubiquitination at Lys-72 is induced by TNFalpha, and leads to proteasomal degradation. Undergoes 'Lys-48'-linked polyubiquitination catalyzed by ITCH (By similarity). Requires 'Lys-63'-linked polyubiquitination for autophosphorylation and subsequent activation. 'Lys-63'-linked ubiquitination does not lead to proteasomal degradation. Deubiquitinated by CYLD, a protease that selectively cleaves 'Lys-63'-linked ubiquitin chains. Deubiquitinated by Y.enterocolitica YopP.By similarity2 Publications

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
O43318

MaxQB - The MaxQuant DataBase

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MaxQBi
O43318

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

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PaxDbi
O43318

PeptideAtlas

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PeptideAtlasi
O43318

PRoteomics IDEntifications database

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PRIDEi
O43318

ProteomicsDB human proteome resource

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ProteomicsDBi
48898
48899 [O43318-2]
48900 [O43318-3]
48901 [O43318-4]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
O43318

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

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PhosphoSitePlusi
O43318

<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

Isoform 1A is the most abundant in ovary, skeletal muscle, spleen and blood mononuclear cells. Isoform 1B is highly expressed in brain, kidney and small intestine. Isoform 1C is the major form in prostate. Isoform 1D is the less abundant form.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000135341 Expressed in 231 organ(s), highest expression level in tendon

CleanEx database of gene expression profiles

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CleanExi
HS_MAP3K7

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
O43318 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
O43318 HS

Organism-specific databases

Human Protein Atlas

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HPAi
HPA007633

<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

Can form homodimer (PubMed:27426733). Binds both upstream activators and downstream substrates in multimolecular complexes. Interacts with TAB1/MAP3K7IP1, TAB2/MAP3K7IP2 and TAB3/MAP3K7IP3 (PubMed:10838074, PubMed:11460167, PubMed:12242293, PubMed:14670075, PubMed:16289117, PubMed:19675569, PubMed:8638164). Identified in the TRIKA2 complex composed of MAP3K7/TAK1, TAB1/MAP3K7IP1 and TAB2/MAP3K7IP2 (PubMed:11460167). Interacts with PPM1L and PPM1B/PP2CB (PubMed:11104763). Interaction with PP2A and PPP6C leads to its repressed activity (PubMed:17079228). Interacts with TRAF6 and TAB1/MAP3K7IP1; during IL-1 signaling (PubMed:10094049, PubMed:12242293). Interacts with TAOK1 and TAOK2; interaction with TAOK2 interferes with MAP3K7 interaction with IKKA, thus preventing NF-kappa-B activation (PubMed:16893890). Interacts with WDR34 (via WD domains) (PubMed:19521662). Interacts with CYLD and RBCK1 (PubMed:17449468, PubMed:17548520). Interacts with TGFBR1; induces MAP3K7/TAK1 activation by TRAF6 (PubMed:18758450). Interacts with MAPK8IP1 and SMAD6 (By similarity). Interacts with isoform 1 of VRK2 (PubMed:18286207). Interacts with DAB2; the interaction is induced by TGF-beta stimulation and may mediate TGF-beta stimulated JNK activation (PubMed:15894542). Interacts with TRIM5 (PubMed:21512573). Part of a complex containing ITCH, NDFIP1 and MAP3K7 (By similarity). Interacts with IFIT5; the interaction synergizes the recruitment of IKK to MAP3K7 and enhances IKK phosphorylation (PubMed:26334375). Interacts with PLEKHM1 (via N- and C-terminus) (By similarity). Interacts with TRIM8 (PubMed:22084099). Found in a complex with SH3RF1, RAC2, MAP2K7/MKK7, MAPK8IP1/JIP1, MAPK8/JNK1 and MAPK9/JNK2 (By similarity).By similarity25 Publications
(Microbial infection) Interacts with herpes simplex virus 2 protein US2; this interaction induced MAP3K7 phosphorylation and subsequent actviation.1 Publication

<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
112748, 168 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
O43318

Database of interacting proteins

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DIPi
DIP-27523N

Protein interaction database and analysis system

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IntActi
O43318, 56 interactors

Molecular INTeraction database

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MINTi
O43318

STRING: functional protein association networks

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STRINGi
9606.ENSP00000358335

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
O43318

<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

1606
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
O43318

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

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SMRi
O43318

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
O43318

<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>Domaini36 – 291Protein kinasePROSITE-ProRule annotationAdd BLAST256

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>Regioni1 – 300Interaction with MAPK8IP1By similarityAdd BLAST300

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 biasi8 – 14Poly-Ser7

<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
KOG0192 Eukaryota
COG0515 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000157785

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000231735

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG003485

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
O43318

KEGG Orthology (KO)

More...
KOi
K04427

Identification of Orthologs from Complete Genome Data

More...
OMAi
IGTESSQ

Database of Orthologous Groups

More...
OrthoDBi
EOG091G03QO

Database for complete collections of gene phylogenies

More...
PhylomeDBi
O43318

TreeFam database of animal gene trees

More...
TreeFami
TF105116

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR017421 MAPKKK7
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR008271 Ser/Thr_kinase_AS

The PANTHER Classification System

More...
PANTHERi
PTHR26392:SF74 PTHR26392:SF74, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF07714 Pkinase_Tyr, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF038168 MAPKKK7, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00109 TYRKINASE

Simple Modular Architecture Research Tool; a protein domain database

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

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

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

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

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

This entry has 4 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1B (identifier: O43318-1) [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
MSTASAASSS SSSSAGEMIE APSQVLNFEE IDYKEIEVEE VVGRGAFGVV
60 70 80 90 100
CKAKWRAKDV AIKQIESESE RKAFIVELRQ LSRVNHPNIV KLYGACLNPV
110 120 130 140 150
CLVMEYAEGG SLYNVLHGAE PLPYYTAAHA MSWCLQCSQG VAYLHSMQPK
160 170 180 190 200
ALIHRDLKPP NLLLVAGGTV LKICDFGTAC DIQTHMTNNK GSAAWMAPEV
210 220 230 240 250
FEGSNYSEKC DVFSWGIILW EVITRRKPFD EIGGPAFRIM WAVHNGTRPP
260 270 280 290 300
LIKNLPKPIE SLMTRCWSKD PSQRPSMEEI VKIMTHLMRY FPGADEPLQY
310 320 330 340 350
PCQYSDEGQS NSATSTGSFM DIASTNTSNK SDTNMEQVPA TNDTIKRLES
360 370 380 390 400
KLLKNQAKQQ SESGRLSLGA SRGSSVESLP PTSEGKRMSA DMSEIEARIA
410 420 430 440 450
ATTAYSKPKR GHRKTASFGN ILDVPEIVIS GNGQPRRRSI QDLTVTGTEP
460 470 480 490 500
GQVSSRSSSP SVRMITTSGP TSEKPTRSHP WTPDDSTDTN GSDNSIPMAY
510 520 530 540 550
LTLDHQLQPL APCPNSKESM AVFEQHCKMA QEYMKVQTEI ALLLQRKQEL
560 570 580 590 600
VAELDQDEKD QQNTSRLVQE HKKLLDENKS LSTYYQQCKK QLEVIRSQQQ

KRQGTS
Length:606
Mass (Da):67,196
Last modified:June 1, 1998 - 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:i3D8F8147CD174013
GO
Isoform 1A (identifier: O43318-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     404-430: Missing.

Show »
Length:579
Mass (Da):64,230
Checksum:i40EDE237BBB568EE
GO
Isoform 1C (identifier: O43318-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     509-518: PLAPCPNSKE → ARTSCRTGPG
     519-606: Missing.

Show »
Length:518
Mass (Da):56,706
Checksum:iA92C927A8621AF90
GO
Isoform 1D (identifier: O43318-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     404-430: Missing.
     509-518: PLAPCPNSKE → ARTSCRTGPG
     519-606: Missing.

Show »
Length:491
Mass (Da):53,740
Checksum:iB7D8832E286A99C5
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q9UG54Q9UG54_HUMAN
Mitogen-activated protein kinase ki...
MAP3K7 DKFZp586F0420
260Annotation 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_07734150Missing in CSCF. 1 Publication1
Natural variantiVAR_07734270E → Q in FMD2. 1 PublicationCorresponds to variant dbSNP:rs886039231EnsemblClinVar.1
Natural variantiVAR_077343100V → E in FMD2. 1 PublicationCorresponds to variant dbSNP:rs886039232EnsemblClinVar.1
Natural variantiVAR_077344110G → C in CSCF. 1 PublicationCorresponds to variant dbSNP:rs886039235EnsemblClinVar.1
Natural variantiVAR_077345168G → R in FMD2; increases autophosphorylation; no effect on MAPK signaling; no effect on NF-kappa-B signaling. 1 PublicationCorresponds to variant dbSNP:rs886039233EnsemblClinVar.1
Natural variantiVAR_077346241W → R in CSCF. 1 PublicationCorresponds to variant dbSNP:rs886039237EnsemblClinVar.1
Natural variantiVAR_080761410R → Q Found in a consanguineous family with intellectual disability; unknown pathological significance. 1 Publication1
Natural variantiVAR_077347512P → L in FMD2; does not affect interaction with TAB2; does not affect homodimerization; increases autophosphorylation; increases MAPK signaling; increases NF-kappa-B signaling. 1 PublicationCorresponds to variant dbSNP:rs886039230EnsemblClinVar.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_004886404 – 430Missing in isoform 1A and isoform 1D. 4 PublicationsAdd BLAST27
Alternative sequenceiVSP_004887509 – 518PLAPCPNSKE → ARTSCRTGPG in isoform 1C and isoform 1D. 2 Publications10
Alternative sequenceiVSP_004888519 – 606Missing in isoform 1C and isoform 1D. 2 PublicationsAdd BLAST88

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
AB009357 mRNA Translation: BAA25026.1
AB009356 mRNA Translation: BAA25025.1
AB009358 mRNA Translation: BAA25027.2
AF218074 mRNA Translation: AAF27652.1
DQ314875 Genomic DNA Translation: ABC40734.1
AK315774 mRNA Translation: BAG38124.1
AL121964 Genomic DNA No translation available.
AL121837 Genomic DNA No translation available.
CH471051 Genomic DNA Translation: EAW48525.1
CH471051 Genomic DNA Translation: EAW48526.1
CH471051 Genomic DNA Translation: EAW48527.1
CH471051 Genomic DNA Translation: EAW48529.1
BC017715 mRNA Translation: AAH17715.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS5027.1 [O43318-2]
CCDS5028.1 [O43318-1]
CCDS5029.1 [O43318-3]
CCDS5030.1 [O43318-4]

Protein sequence database of the Protein Information Resource

More...
PIRi
JC5955
JC5956

NCBI Reference Sequences

More...
RefSeqi
NP_003179.1, NM_003188.3 [O43318-2]
NP_663304.1, NM_145331.2 [O43318-1]
NP_663305.1, NM_145332.2 [O43318-3]
NP_663306.1, NM_145333.2 [O43318-4]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.594838

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000369325; ENSP00000358331; ENSG00000135341 [O43318-3]
ENST00000369327; ENSP00000358333; ENSG00000135341 [O43318-4]
ENST00000369329; ENSP00000358335; ENSG00000135341 [O43318-1]
ENST00000369332; ENSP00000358338; ENSG00000135341 [O43318-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
6885

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:6885

UCSC genome browser

More...
UCSCi
uc003pnz.3 human [O43318-1]

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
AB009357 mRNA Translation: BAA25026.1
AB009356 mRNA Translation: BAA25025.1
AB009358 mRNA Translation: BAA25027.2
AF218074 mRNA Translation: AAF27652.1
DQ314875 Genomic DNA Translation: ABC40734.1
AK315774 mRNA Translation: BAG38124.1
AL121964 Genomic DNA No translation available.
AL121837 Genomic DNA No translation available.
CH471051 Genomic DNA Translation: EAW48525.1
CH471051 Genomic DNA Translation: EAW48526.1
CH471051 Genomic DNA Translation: EAW48527.1
CH471051 Genomic DNA Translation: EAW48529.1
BC017715 mRNA Translation: AAH17715.1
CCDSiCCDS5027.1 [O43318-2]
CCDS5028.1 [O43318-1]
CCDS5029.1 [O43318-3]
CCDS5030.1 [O43318-4]
PIRiJC5955
JC5956
RefSeqiNP_003179.1, NM_003188.3 [O43318-2]
NP_663304.1, NM_145331.2 [O43318-1]
NP_663305.1, NM_145332.2 [O43318-3]
NP_663306.1, NM_145333.2 [O43318-4]
UniGeneiHs.594838

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
2EVAX-ray2.00A31-412[»]
2YIYX-ray2.49A31-303[»]
4GS6X-ray2.20A31-303[»]
4L3PX-ray2.68A31-303[»]
4L52X-ray2.54A31-303[»]
4L53X-ray2.55A31-303[»]
4O91X-ray2.39A31-303[»]
5E7RX-ray2.11A31-303[»]
5GJDX-ray2.79A31-303[»]
5GJFX-ray2.89A31-303[»]
5GJGX-ray2.61A31-303[»]
5J7SX-ray2.37A31-303[»]
5J8IX-ray2.40A31-303[»]
5J9LX-ray2.75A31-303[»]
5JGAX-ray2.00A31-303[»]
5JGBX-ray2.80A31-303[»]
5JGDX-ray3.10A31-303[»]
5JH6X-ray2.37A31-303[»]
5JK3X-ray2.37A31-303[»]
5V5NX-ray2.01A31-303[»]
ProteinModelPortaliO43318
SMRiO43318
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112748, 168 interactors
CORUMiO43318
DIPiDIP-27523N
IntActiO43318, 56 interactors
MINTiO43318
STRINGi9606.ENSP00000358335

Chemistry databases

BindingDBiO43318
ChEMBLiCHEMBL5776
GuidetoPHARMACOLOGYi2082

Protein family/group databases

MoonDBiO43318 Predicted

PTM databases

iPTMnetiO43318
PhosphoSitePlusiO43318

Polymorphism and mutation databases

BioMutaiMAP3K7

Proteomic databases

EPDiO43318
MaxQBiO43318
PaxDbiO43318
PeptideAtlasiO43318
PRIDEiO43318
ProteomicsDBi48898
48899 [O43318-2]
48900 [O43318-3]
48901 [O43318-4]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
6885
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000369325; ENSP00000358331; ENSG00000135341 [O43318-3]
ENST00000369327; ENSP00000358333; ENSG00000135341 [O43318-4]
ENST00000369329; ENSP00000358335; ENSG00000135341 [O43318-1]
ENST00000369332; ENSP00000358338; ENSG00000135341 [O43318-2]
GeneIDi6885
KEGGihsa:6885
UCSCiuc003pnz.3 human [O43318-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
6885
DisGeNETi6885
EuPathDBiHostDB:ENSG00000135341.17

GeneCards: human genes, protein and diseases

More...
GeneCardsi
MAP3K7
HGNCiHGNC:6859 MAP3K7
HPAiHPA007633
MalaCardsiMAP3K7
MIMi157800 phenotype
602614 gene
617137 phenotype
neXtProtiNX_O43318
OpenTargetsiENSG00000135341
Orphaneti3238 Cardiospondylocarpofacial syndrome
1826 Frontometaphyseal dysplasia
PharmGKBiPA30603

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0192 Eukaryota
COG0515 LUCA
GeneTreeiENSGT00940000157785
HOGENOMiHOG000231735
HOVERGENiHBG003485
InParanoidiO43318
KOiK04427
OMAiIGTESSQ
OrthoDBiEOG091G03QO
PhylomeDBiO43318
TreeFamiTF105116

Enzyme and pathway databases

ReactomeiR-HSA-1169091 Activation of NF-kappaB in B cells
R-HSA-168638 NOD1/2 Signaling Pathway
R-HSA-202424 Downstream TCR signaling
R-HSA-2871837 FCERI mediated NF-kB activation
R-HSA-4086398 Ca2+ pathway
R-HSA-445989 TAK1 activates NFkB by phosphorylation and activation of IKKs complex
R-HSA-450302 activated TAK1 mediates p38 MAPK activation
R-HSA-450321 JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1
R-HSA-5357956 TNFR1-induced NFkappaB signaling pathway
R-HSA-5607764 CLEC7A (Dectin-1) signaling
R-HSA-5689880 Ub-specific processing proteases
R-HSA-9014325 TICAM1,TRAF6-dependent induction of TAK1 complex
R-HSA-9020702 Interleukin-1 signaling
R-HSA-937042 IRAK2 mediated activation of TAK1 complex
R-HSA-937072 TRAF6-mediated induction of TAK1 complex within TLR4 complex
R-HSA-975163 IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation
SignaLinkiO43318
SIGNORiO43318

Miscellaneous databases

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

More...
ChiTaRSi
MAP3K7 human
EvolutionaryTraceiO43318

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
MAP3K7

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

More...
GenomeRNAii
6885

Protein Ontology

More...
PROi
PR:O43318

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000135341 Expressed in 231 organ(s), highest expression level in tendon
CleanExiHS_MAP3K7
ExpressionAtlasiO43318 baseline and differential
GenevisibleiO43318 HS

Family and domain databases

InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR017421 MAPKKK7
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR008271 Ser/Thr_kinase_AS
PANTHERiPTHR26392:SF74 PTHR26392:SF74, 1 hit
PfamiView protein in Pfam
PF07714 Pkinase_Tyr, 1 hit
PIRSFiPIRSF038168 MAPKKK7, 1 hit
PRINTSiPR00109 TYRKINASE
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 nameiM3K7_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: O43318
Secondary accession number(s): B2RE27
, E1P523, O43317, O43319, Q5TDN2, Q5TDN3, Q5TDT7, Q9NTR3, Q9NZ70
<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 1, 2000
Last sequence update: June 1, 1998
Last modified: December 5, 2018
This is version 208 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  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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