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Protein

TNF receptor-associated factor 6

Gene

Traf6

Organism
Mus musculus (Mouse)
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

E3 ubiquitin ligase that, together with UBE2N and UBE2V1, mediates the synthesis of 'Lys-63'-linked-polyubiquitin chains conjugated to proteins, such as IKBKG, IRAK1, AKT1 and AKT2. Also mediates ubiquitination of free/unanchored polyubiquitin chain that leads to MAP3K7 activation (By similarity). Leads to the activation of NF-kappa-B and JUN. May be essential for the formation of functional osteoclasts. Seems to also play a role in dendritic cells (DCs) maturation and/or activation. Represses c-Myb-mediated transactivation, in B-lymphocytes. Adapter protein that seems to play a role in signal transduction initiated via TNF receptor, IL-1 receptor and IL-17 receptor. Regulates osteoclast differentiation by mediating the activation of adapter protein complex 1 (AP-1) and NF-kappa-B, in response to RANK-L stimulation. Together with MAP3K8, mediates CD40 signals that activate ERK in B-cells and macrophages, and thus may play a role in the regulation of immunoglobulin production.By similarity7 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

  • S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine. EC:2.3.2.27

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri70 – 109RING-typePROSITE-ProRule annotationAdd BLAST40
Zinc fingeri150 – 202TRAF-type 1PROSITE-ProRule annotationAdd BLAST53
Zinc fingeri203 – 259TRAF-type 2PROSITE-ProRule annotationAdd BLAST57

<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 functionTransferase
Biological processDNA damage, Immunity, Osteogenesis, Ubl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-1257604 PIP3 activates AKT signaling
R-MMU-166058 MyD88:MAL(TIRAP) cascade initiated on plasma membrane
R-MMU-168638 NOD1/2 Signaling Pathway
R-MMU-193692 Regulated proteolysis of p75NTR
R-MMU-202424 Downstream TCR signaling
R-MMU-205043 NRIF signals cell death from the nucleus
R-MMU-209543 p75NTR recruits signalling complexes
R-MMU-209560 NF-kB is activated and signals survival
R-MMU-2871837 FCERI mediated NF-kB activation
R-MMU-445989 TAK1 activates NFkB by phosphorylation and activation of IKKs complex
R-MMU-450302 activated TAK1 mediates p38 MAPK activation
R-MMU-450321 JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1
R-MMU-5607764 CLEC7A (Dectin-1) signaling
R-MMU-5689880 Ub-specific processing proteases
R-MMU-5689896 Ovarian tumor domain proteases
R-MMU-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-MMU-9020702 Interleukin-1 signaling
R-MMU-937039 IRAK1 recruits IKK complex
R-MMU-937041 IKK complex recruitment mediated by RIP1
R-MMU-937042 IRAK2 mediated activation of TAK1 complex
R-MMU-937072 TRAF6-mediated induction of TAK1 complex within TLR4 complex
R-MMU-975110 TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling
R-MMU-975138 TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation
R-MMU-975144 IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation
R-MMU-975155 MyD88 dependent cascade initiated on endosome
R-MMU-975163 IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation
R-MMU-975871 MyD88 cascade initiated on plasma membrane

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00143

<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:
TNF receptor-associated factor 6 (EC:2.3.2.27)
Alternative name(s):
E3 ubiquitin-protein ligase TRAF6
RING-type E3 ubiquitin transferase TRAF6Curated
<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:Traf6
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 2

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:108072 Traf6

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Lipid droplet, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Abrogation of IL-1-induced activation of NF-kappa-B, MAPK8/JNK and MAPK14/p38. Animals appears normal at birth but becomes smaller after one week. Show runting, failure of tooth eruption and die after three weeks. Exhibit severe osteopetrosis, thymic atrophy, lymph node deficiency, splenomegaly, and have alopecia and lack sweat glands.7 Publications

<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_00000564081 – 530TNF receptor-associated factor 6Add BLAST530

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-linki124Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki124Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Cross-linki142Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Cross-linki461Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

<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

Sumoylated on Lys-124, Lys-142 and Lys-461 with SUMO1.By similarity
Polyubiquitinated; after cell stimulation with IL-1-beta or TGF-beta. This ligand-induced cell stimulation leads to dimerization/oligomerization of TRAF6 molecules, followed by auto-ubiquitination which involves UBE2N and UBE2V1 and leads to TRAF6 activation. This 'Lys-63' site-specific poly-ubiquitination appears to be associated with the activation of signaling molecules. Endogenous autoubiquitination occurs only for the cytoplasmic form. Deubiquitinated by USP10 in a TANK-dependent manner, leading to the negative regulation of NF-kappaB signaling upon DNA damage.By similarity

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P70196

MaxQB - The MaxQuant DataBase

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MaxQBi
P70196

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

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PaxDbi
P70196

PeptideAtlas

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PeptideAtlasi
P70196

PRoteomics IDEntifications database

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PRIDEi
P70196

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P70196

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

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PhosphoSitePlusi
P70196

<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

Highly expressed in brain, lung, liver, skeletal muscle, and kidney; lower expression in heart, spleen, and testis.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000027164 Expressed in 241 organ(s), highest expression level in lumbar subsegment of spinal cord

CleanEx database of gene expression profiles

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CleanExi
MM_TRAF6

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P70196 MM

<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

Homotrimer (By similarity). Homooligomer (By similarity). N-terminal region is dimeric while C-terminal region is trimeric; maybe providing a mode of oligomerization. Upon IL1B treatment, forms a complex with PELI1, IRAK1, IRAK4 and MYD88; this complex recruits MAP3K7/TAK1, TAB1 and TAB2 to mediate NF-kappa-B activation. Direct binding of SMAD6 to PELI1 prevents the complex formation and hence negatively regulates IL1R-TLR signaling and eventually NF-kappa-B-mediated gene expression. Binds to TNFRSF5/CD40 and TNFRSF11A/RANK (By similarity). Associates with NGFR, TNFRSF17, IRAK2, IRAK3, PELI2, PELI3, RIPK2, MAP3K1, MAP3K5, MAP3K14, CSK, TRAF, TRAF-interacting protein TRIP and TNF receptor associated protein TDP2. Binds UBE2V1. Interacts with MAVS/IPS1. Interacts with TAX1BP1 (By similarity). Interacts with IL17R. Interacts with SQSTM1 bridging NTRK1 and NGFR. Forms a ternary complex with SQSTM1 and PRKCZ. Interacts with IL1RL1. Interacts with AJUBA (By similarity). Interacts with TRAFD1. Interacts with TICAM2. Interacts with ZFAND5. Interacts with ARRB1 and ARRB2 (By similarity). Interacts with MAP3K7 and TAB1/MAP3K7IP1; during IL-1 signaling. Interacts with UBE2N. Interacts with TGFBR1, HDAC1 and RANGAP1. Interacts with AKT1, AKT2 and AKT3. Interacts (via TRAF domains) with NUMBL (via C-terminal) (By similarity). Interacts (via TRAF domains) with WDR34 (via WD domains). Interacts with RBCK1 (By similarity). Interacts with TRAF3IP2 (By similarity). Interacts with LIMD1 (via LIM domains). Interacts with RSAD2/viperin. Interacts with IFIT3 (via N-terminus) (By similarity). Interacts (via C-terminus) with EIF2AK2/PKR (via the kinase catalytic domain). Interacts with CARD14 (By similarity). Interacts with CD40 and MAP3K8; the interaction is required for ERK activation. Interacts with TICAM1 and this interaction is enhanced in the presence of WDFY1 (By similarity). Interacts with TANK; this interaction increases in response to DNA damage (By similarity). Interacts with USP10; this interaction increases in response to DNA damage (By similarity). Interacts with ZC3H12A; this interaction increases in response to DNA damage and is stimulated by TANK (By similarity). Interacts with WDFY3 (PubMed:27330028). Interacts with TRIM13 (By similarity). Interacts with GPS2 (PubMed:22424771).By similarity10 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
204307, 105 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P70196

Database of interacting proteins

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DIPi
DIP-29812N

Protein interaction database and analysis system

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IntActi
P70196, 40 interactors

Molecular INTeraction database

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MINTi
P70196

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000004949

<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

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P70196

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

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SMRi
P70196

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...

<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>Domaini358 – 507MATHPROSITE-ProRule annotationAdd BLAST150

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 – 362Interaction with TAX1BP1By similarityAdd BLAST362
Regioni363 – 530Interaction with TANKBy similarityAdd BLAST168

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 coili299 – 356Sequence analysisAdd BLAST58

<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 coiled coil domain mediates homo- and hetero-oligomerization.
The MATH/TRAF domain binds to receptor cytoplasmic domains.

<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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri70 – 109RING-typePROSITE-ProRule annotationAdd BLAST40
Zinc fingeri150 – 202TRAF-type 1PROSITE-ProRule annotationAdd BLAST53
Zinc fingeri203 – 259TRAF-type 2PROSITE-ProRule annotationAdd BLAST57

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG410ISDW Eukaryota
ENOG410XTXK LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000155426

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000006625

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG060248

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P70196

KEGG Orthology (KO)

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KOi
K03175

Identification of Orthologs from Complete Genome Data

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OMAi
IRQNHEE

Database of Orthologous Groups

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OrthoDBi
918518at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P70196

TreeFam database of animal gene trees

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TreeFami
TF321154

Family and domain databases

Conserved Domains Database

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CDDi
cd03776 MATH_TRAF6, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.60.210.10, 1 hit
3.30.40.10, 3 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR002083 MATH/TRAF_dom
IPR012227 TNF_rcpt--assoc_TRAF
IPR008974 TRAF-like
IPR027139 TRAF6
IPR037309 TRAF6_MATH
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
IPR017907 Znf_RING_CS
IPR001293 Znf_TRAF

The PANTHER Classification System

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PANTHERi
PTHR10131:SF111 PTHR10131:SF111, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF02176 zf-TRAF, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF015614 TRAF, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00061 MATH, 1 hit
SM00184 RING, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF49599 SSF49599, 3 hits

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50144 MATH, 1 hit
PS00518 ZF_RING_1, 1 hit
PS50089 ZF_RING_2, 1 hit
PS50145 ZF_TRAF, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: P70196-1) [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
MSLLNCENSC GSSQSSSDCC AAMAASCSAA VKDDSVSGSA STGNLSSSFM
60 70 80 90 100
EEIQGYDVEF DPPLESKYEC PICLMALREA VQTPCGHRFC KACIIKSIRD
110 120 130 140 150
AGHKCPVDNE ILLENQLFPD NFAKREILSL TVKCPNKGCL QKMELRHLED
160 170 180 190 200
HQVHCEFALV NCPQCQRPFQ KCQVNTHIIE DCPRRQVSCV NCAVSMAYEE
210 220 230 240 250
KEIHDQSCPL ANIICEYCGT ILIREQMPNH YDLDCPTAPI PCTFSVFGCH
260 270 280 290 300
EKMQRNHLAR HLQENTQLHM RLLAQAVHNV NLALRPCDAA SPSRGCRPED
310 320 330 340 350
PNYEETIKQL ESRLVRQDHQ IRELTAKMET QSMYVGELKR TIRTLEDKVA
360 370 380 390 400
EMEAQQCNGI YIWKIGNFGM HLKSQEEERP VVIHSPGFYT GRPGYKLCMR
410 420 430 440 450
LHLQLPTAQR CANYISLFVH TMQGEYDSHL PWPFQGTIRL TILDQSEALI
460 470 480 490 500
RQNHEEVMDA KPELLAFQRP TIPRNPKGFG YVTFMHLEAL RQGTFIKDDT
510 520 530
LLVRCEVSTR FDMGGLRKEG FQPRSTDAGV
Length:530
Mass (Da):60,070
Last modified:February 9, 2010 - 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:iF8389250425E4E2D
GO
Isoform 2 (identifier: P70196-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     100-174: DAGHKCPVDN...CQRPFQKCQV → YLILRKHGAL...TQPPGKLQSP
     175-530: Missing.

Note: No experimental confirmation available.
Show »
Length:174
Mass (Da):18,961
Checksum:iF66189179AA9F9D3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti251E → Q in BAA12705 (PubMed:8910514).Curated1
Sequence conflicti251E → Q in BAC30850 (PubMed:16141072).Curated1
Sequence conflicti367N → K in BAA12705 (PubMed:8910514).Curated1
Sequence conflicti367N → K in BAC30850 (PubMed:16141072).Curated1

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_007404100 – 174DAGHK…QKCQV → YLILRKHGALQQPNVKSMLE TGHPKNRQTENTGQEHSRMD RNLRQLGSHPSLYYGMNRGL LPCLPTQPPGKLQSP in isoform 2. 1 PublicationAdd BLAST75
Alternative sequenceiVSP_007405175 – 530Missing in isoform 2. 1 PublicationAdd BLAST356

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
D84655 mRNA Translation: BAA12705.1
AK041172 mRNA Translation: BAC30850.1
AK155434 mRNA Translation: BAE33263.1
AL929571 Genomic DNA Translation: CAM20505.1
CH466519 Genomic DNA Translation: EDL27656.1
CH466519 Genomic DNA Translation: EDL27657.1
BC060705 mRNA Translation: AAH60705.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS16464.1 [P70196-1]

NCBI Reference Sequences

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RefSeqi
NP_001290202.1, NM_001303273.1 [P70196-1]
NP_033450.2, NM_009424.3 [P70196-1]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Mm.292729

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000004949; ENSMUSP00000004949; ENSMUSG00000027164 [P70196-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
22034

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:22034

UCSC genome browser

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UCSCi
uc008lhl.2 mouse [P70196-2]
uc008lhm.2 mouse [P70196-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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
D84655 mRNA Translation: BAA12705.1
AK041172 mRNA Translation: BAC30850.1
AK155434 mRNA Translation: BAE33263.1
AL929571 Genomic DNA Translation: CAM20505.1
CH466519 Genomic DNA Translation: EDL27656.1
CH466519 Genomic DNA Translation: EDL27657.1
BC060705 mRNA Translation: AAH60705.1
CCDSiCCDS16464.1 [P70196-1]
RefSeqiNP_001290202.1, NM_001303273.1 [P70196-1]
NP_033450.2, NM_009424.3 [P70196-1]
UniGeneiMm.292729

3D structure databases

ProteinModelPortaliP70196
SMRiP70196
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204307, 105 interactors
CORUMiP70196
DIPiDIP-29812N
IntActiP70196, 40 interactors
MINTiP70196
STRINGi10090.ENSMUSP00000004949

PTM databases

iPTMnetiP70196
PhosphoSitePlusiP70196

Proteomic databases

EPDiP70196
MaxQBiP70196
PaxDbiP70196
PeptideAtlasiP70196
PRIDEiP70196

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000004949; ENSMUSP00000004949; ENSMUSG00000027164 [P70196-1]
GeneIDi22034
KEGGimmu:22034
UCSCiuc008lhl.2 mouse [P70196-2]
uc008lhm.2 mouse [P70196-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
7189
MGIiMGI:108072 Traf6

Phylogenomic databases

eggNOGiENOG410ISDW Eukaryota
ENOG410XTXK LUCA
GeneTreeiENSGT00940000155426
HOGENOMiHOG000006625
HOVERGENiHBG060248
InParanoidiP70196
KOiK03175
OMAiIRQNHEE
OrthoDBi918518at2759
PhylomeDBiP70196
TreeFamiTF321154

Enzyme and pathway databases

UniPathwayi
UPA00143

ReactomeiR-MMU-1257604 PIP3 activates AKT signaling
R-MMU-166058 MyD88:MAL(TIRAP) cascade initiated on plasma membrane
R-MMU-168638 NOD1/2 Signaling Pathway
R-MMU-193692 Regulated proteolysis of p75NTR
R-MMU-202424 Downstream TCR signaling
R-MMU-205043 NRIF signals cell death from the nucleus
R-MMU-209543 p75NTR recruits signalling complexes
R-MMU-209560 NF-kB is activated and signals survival
R-MMU-2871837 FCERI mediated NF-kB activation
R-MMU-445989 TAK1 activates NFkB by phosphorylation and activation of IKKs complex
R-MMU-450302 activated TAK1 mediates p38 MAPK activation
R-MMU-450321 JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1
R-MMU-5607764 CLEC7A (Dectin-1) signaling
R-MMU-5689880 Ub-specific processing proteases
R-MMU-5689896 Ovarian tumor domain proteases
R-MMU-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-MMU-9020702 Interleukin-1 signaling
R-MMU-937039 IRAK1 recruits IKK complex
R-MMU-937041 IKK complex recruitment mediated by RIP1
R-MMU-937042 IRAK2 mediated activation of TAK1 complex
R-MMU-937072 TRAF6-mediated induction of TAK1 complex within TLR4 complex
R-MMU-975110 TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling
R-MMU-975138 TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation
R-MMU-975144 IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation
R-MMU-975155 MyD88 dependent cascade initiated on endosome
R-MMU-975163 IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation
R-MMU-975871 MyD88 cascade initiated on plasma membrane

Miscellaneous databases

Protein Ontology

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PROi
PR:P70196

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000027164 Expressed in 241 organ(s), highest expression level in lumbar subsegment of spinal cord
CleanExiMM_TRAF6
GenevisibleiP70196 MM

Family and domain databases

CDDicd03776 MATH_TRAF6, 1 hit
Gene3Di2.60.210.10, 1 hit
3.30.40.10, 3 hits
InterProiView protein in InterPro
IPR002083 MATH/TRAF_dom
IPR012227 TNF_rcpt--assoc_TRAF
IPR008974 TRAF-like
IPR027139 TRAF6
IPR037309 TRAF6_MATH
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
IPR017907 Znf_RING_CS
IPR001293 Znf_TRAF
PANTHERiPTHR10131:SF111 PTHR10131:SF111, 1 hit
PfamiView protein in Pfam
PF02176 zf-TRAF, 1 hit
PIRSFiPIRSF015614 TRAF, 1 hit
SMARTiView protein in SMART
SM00061 MATH, 1 hit
SM00184 RING, 1 hit
SUPFAMiSSF49599 SSF49599, 3 hits
PROSITEiView protein in PROSITE
PS50144 MATH, 1 hit
PS00518 ZF_RING_1, 1 hit
PS50089 ZF_RING_2, 1 hit
PS50145 ZF_TRAF, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

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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 nameiTRAF6_MOUSE
<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: P70196
Secondary accession number(s): Q6P9M0, Q8BLV2
<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 9, 2003
Last sequence update: February 9, 2010
Last modified: January 16, 2019
This is version 195 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

<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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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