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UniProtKB - Q9Y4K3 (TRAF6_HUMAN)

Entry version 213 (13 Feb 2019)
Sequence version 1 (01 Nov 1999)
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Protein

TNF receptor-associated factor 6

Gene

TRAF6

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

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. 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.11 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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

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

Molecular 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-HSA-1257604 PIP3 activates AKT signaling
R-HSA-166058 MyD88:MAL(TIRAP) cascade initiated on plasma membrane
R-HSA-168638 NOD1/2 Signaling Pathway
R-HSA-168927 TICAM1, RIP1-mediated IKK complex recruitment
R-HSA-193692 Regulated proteolysis of p75NTR
R-HSA-202424 Downstream TCR signaling
R-HSA-205043 NRIF signals cell death from the nucleus
R-HSA-209543 p75NTR recruits signalling complexes
R-HSA-209560 NF-kB is activated and signals survival
R-HSA-2871837 FCERI mediated NF-kB activation
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-5607764 CLEC7A (Dectin-1) signaling
R-HSA-5689880 Ub-specific processing proteases
R-HSA-5689896 Ovarian tumor domain proteases
R-HSA-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-HSA-9014325 TICAM1,TRAF6-dependent induction of TAK1 complex
R-HSA-9020702 Interleukin-1 signaling
R-HSA-933541 TRAF6 mediated IRF7 activation
R-HSA-933542 TRAF6 mediated NF-kB activation
R-HSA-937039 IRAK1 recruits IKK complex
R-HSA-937041 IKK complex recruitment mediated by RIP1
R-HSA-937042 IRAK2 mediated activation of TAK1 complex
R-HSA-937072 TRAF6-mediated induction of TAK1 complex within TLR4 complex
R-HSA-975110 TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling
R-HSA-975138 TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation
R-HSA-975144 IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation
R-HSA-975155 MyD88 dependent cascade initiated on endosome
R-HSA-975163 IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation
R-HSA-975871 MyD88 cascade initiated on plasma membrane

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

More...SignaLinki		Q9Y4K3

SIGNOR Signaling Network Open Resource

More...SIGNORi		Q9Y4K3

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

More...UniPathwayi
UPA00143

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

More...MoonDBi		Q9Y4K3 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:
TNF receptor-associated factor 6 (EC:2.3.2.27)
Alternative name(s):
E3 ubiquitin-protein ligase TRAF6
Interleukin-1 signal transducer
RING finger protein 85
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
Synonyms:RNF85
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 11

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000175104.14

Human Gene Nomenclature Database

More...HGNCi		HGNC:12036 TRAF6

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		602355 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q9Y4K3

<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

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>Mutagenesisi57D → K: Loss of interaction with UBE2N. 1 Publication1
Mutagenesisi70C → A: Loss of ligase activity, autoubiquitination and signaling capacity. 2 Publications1
Mutagenesisi72I → D: Loss of interaction with UBE2N. 1 Publication1
Mutagenesisi74L → E or K: Loss of interaction with UBE2N. 1 Publication1
Mutagenesisi88R → A: Loss of TRAF6 homodimerization and impaired polyubiquitin synthesis. Loss of TRAF6 homodimerization and impaired polyubiquitin synthesis; when associated with A-122. 1 Publication1
Mutagenesisi118F → A: Loss of TRAF6 homodimerization and impaired polyubiquitin synthesis. 1 Publication1
Mutagenesisi118F → W: Partially impaired polyubiquitin synthesis. 1 Publication1
Mutagenesisi118F → Y: Partially impaired polyubiquitin synthesis. 1 Publication1
Mutagenesisi122F → A: Loss of TRAF6 homodimerization and partially impaired polyubiquitin synthesis. Loss of TRAF6 homodimerization and impaired polyubiquitin synthesis; when associated with A-88. 1 Publication1
Mutagenesisi124K → R: Loss of SUMO1-modification and c-myb-mediated transcriptional repressive activation. 3 Publications1
Mutagenesisi142K → R: Loss of SUMO1-modification and c-myb-mediated transcriptional repressive activation. 1 Publication1
Mutagenesisi453K → R: Loss of SUMO1-modification and c-myb-mediated transcriptional repressive activation. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		7189

MalaCards human disease database

More...MalaCardsi		TRAF6

Open Targets

More...OpenTargetsi		ENSG00000175104

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

More...Orphaneti		1810 Autosomal dominant hypohidrotic ectodermal dysplasia

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA36713

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3588728

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		TRAF6

Domain mapping of disease mutations (DMDM)

More...DMDMi		30580642

<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_00000564071 – 522TNF receptor-associated factor 6Add BLAST522

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); alternate
Cross-linki124Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Cross-linki142Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Cross-linki453Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Sumoylated on Lys-124, Lys-142 and Lys-453 with SUMO1.1 Publication
Polyubiquitinated on Lys-124; 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 (PubMed:25861989).7 Publications

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q9Y4K3

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q9Y4K3

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q9Y4K3

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

More...PaxDbi		Q9Y4K3

PeptideAtlas

More...PeptideAtlasi		Q9Y4K3

PRoteomics IDEntifications database

More...PRIDEi		Q9Y4K3

ProteomicsDB human proteome resource

More...ProteomicsDBi		86225

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q9Y4K3

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

More...PhosphoSitePlusi		Q9Y4K3

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000175104 Expressed in 170 organ(s), highest expression level in secondary oocyte

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q9Y4K3 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB004605
HPA019805
HPA020599

<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. Homooligomer. 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. Associates with NGFR, TNFRSF17, IRAK2, IRAK3, RIPK2, MAP3K1, MAP3K5, MAP3K14, CSK, TRAF, TRAF-interacting protein TRIP and TNF receptor associated protein TDP2. Interacts with IL17R. Interacts with SQSTM1 bridging NTRK1 and NGFR. Forms a ternary complex with SQSTM1 and PRKCZ (By similarity). Interacts with PELI2 and PELI3. Binds UBE2V1. Interacts with TAX1BP1. Interacts with ZNF675. Interacts with ARRB1 and ARRB2. 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). Interacts with RBCK1. Interacts with TRAF3IP2. Interacts with LIMD1 (via LIM domains) (By similarity). Interacts with RSAD2/viperin (By similarity). Interacts (via C-terminus) with EIF2AK2/PKR (via the kinase catalytic domain) (By similarity). Interacts with ZFAND5. Interacts with IL1RL1. Interacts with TRAFD1. Interacts with AJUBA. Interacts with MAVS/IPS1. Interacts (via TRAF domains) with WDR34 (via WD domains). Interacts with IFIT3 (via N-terminus). Interacts with TICAM2. Interacts with CARD14. Interacts with CD40 and MAP3K8; the interaction is required for ERK activation (By similarity). Interacts with TICAM1 and this interaction is enhanced in the presence of WDFY1 (PubMed:25736436). Interacts with TANK; this interaction increases in response to DNA damage (PubMed:25861989). Interacts with USP10; this interaction increases in response to DNA damage (PubMed:25861989). Interacts with ZC3H12A; this interaction increases in response to DNA damage and is stimulated by TANK (PubMed:25861989). Interacts with WDFY3 (By similarity). Interacts with TRIM13 (PubMed:28087809). Interacts with GPS2 (By similarity).By similarity3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		113041, 318 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q9Y4K3

Database of interacting proteins

More...DIPi		DIP-27515N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		Q9Y4K3

Protein interaction database and analysis system

More...IntActi		Q9Y4K3, 114 interactors

Molecular INTeraction database

More...MINTi		Q9Y4K3

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000337853

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q9Y4K3

<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

1522
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LB4X-ray2.40A348-504[»]
1LB5X-ray2.40A347-504[»]
1LB6X-ray1.80A347-504[»]
2ECINMR-A50-128[»]
2JMDNMR-A67-124[»]
3HCSX-ray2.20A/B50-211[»]
3HCTX-ray2.10A50-159[»]
3HCUX-ray2.60A/C50-159[»]
4Z8MX-ray2.95A/B346-504[»]
5ZUJX-ray2.60A350-501[»]
6A33X-ray2.10A350-501[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		Q9Y4K3

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

More...SMRi		Q9Y4K3

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q9Y4K3

<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>Domaini350 – 499MATHPROSITE-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 – 354Interaction with TAX1BP11 PublicationAdd BLAST354
Regioni355 – 522Interaction with TANK1 PublicationAdd 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 coili288 – 348Sequence analysisAdd BLAST61

<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

Belongs to the TNF receptor-associated factor family. A subfamily.Curated

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

More...eggNOGi		ENOG410ISDW Eukaryota
ENOG410XTXK LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000155426

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000006625

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG060248

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q9Y4K3

KEGG Orthology (KO)

More...KOi		K03175

Identification of Orthologs from Complete Genome Data

More...OMAi		IRQNHEE

Database of Orthologous Groups

More...OrthoDBi		1465912at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q9Y4K3

TreeFam database of animal gene trees

More...TreeFami		TF321154

Family and domain databases

Conserved Domains Database

More...CDDi		cd03776 MATH_TRAF6, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.60.210.10, 1 hit
3.30.40.10, 3 hits

Integrated resource of protein families, domains and functional sites

More...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

More...PANTHERi		PTHR10131:SF111 PTHR10131:SF111, 1 hit

Pfam protein domain database

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

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF015614 TRAF, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF49599 SSF49599, 3 hits

PROSITE; a protein domain and family database

More...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>Sequencei

<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.

Q9Y4K3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSLLNCENSC GSSQSESDCC VAMASSCSAV TKDDSVGGTA STGNLSSSFM 
        60         70         80         90        100
EEIQGYDVEF DPPLESKYEC PICLMALREA VQTPCGHRFC KACIIKSIRD 
       110        120        130        140        150
AGHKCPVDNE ILLENQLFPD NFAKREILSL MVKCPNEGCL HKMELRHLED 
       160        170        180        190        200
HQAHCEFALM DCPQCQRPFQ KFHINIHILK DCPRRQVSCD NCAASMAFED 
       210        220        230        240        250
KEIHDQNCPL ANVICEYCNT ILIREQMPNH YDLDCPTAPI PCTFSTFGCH 
       260        270        280        290        300
EKMQRNHLAR HLQENTQSHM RMLAQAVHSL SVIPDSGYIS EVRNFQETIH 
       310        320        330        340        350
QLEGRLVRQD HQIRELTAKM ETQSMYVSEL KRTIRTLEDK VAEIEAQQCN 
       360        370        380        390        400
GIYIWKIGNF GMHLKCQEEE KPVVIHSPGF YTGKPGYKLC MRLHLQLPTA 
       410        420        430        440        450
QRCANYISLF VHTMQGEYDS HLPWPFQGTI RLTILDQSEA PVRQNHEEIM 
       460        470        480        490        500
DAKPELLAFQ RPTIPRNPKG FGYVTFMHLE ALRQRTFIKD DTLLVRCEVS 
       510        520 
TRFDMGSLRR EGFQPRSTDA GV
Length:522
Mass (Da):59,573
Last modified:November 1, 1999 - 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:i5AB9C255CCFEE749
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 conflicti12S → F in AAH31052 (PubMed:15489334).Curated1

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
U78798 mRNA Translation: AAB38751.1
AY228337 Genomic DNA Translation: AAO38054.1
AK292978 mRNA Translation: BAF85667.1
AC009656 Genomic DNA No translation available.
AC061999 Genomic DNA No translation available.
CH471064 Genomic DNA Translation: EAW68119.1
CH471064 Genomic DNA Translation: EAW68120.1
CH471064 Genomic DNA Translation: EAW68122.1
BC031052 mRNA Translation: AAH31052.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS7901.1

Protein sequence database of the Protein Information Resource

More...PIRi		S71821

NCBI Reference Sequences

More...RefSeqi		NP_004611.1, NM_004620.3
NP_665802.1, NM_145803.2

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.444172
Hs.591983

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000348124; ENSP00000337853; ENSG00000175104
ENST00000526995; ENSP00000433623; ENSG00000175104

Database of genes from NCBI RefSeq genomes

More...GeneIDi		7189

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:7189

UCSC genome browser

More...UCSCi		uc001mwq.3 human

<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

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U78798 mRNA Translation: AAB38751.1
AY228337 Genomic DNA Translation: AAO38054.1
AK292978 mRNA Translation: BAF85667.1
AC009656 Genomic DNA No translation available.
AC061999 Genomic DNA No translation available.
CH471064 Genomic DNA Translation: EAW68119.1
CH471064 Genomic DNA Translation: EAW68120.1
CH471064 Genomic DNA Translation: EAW68122.1
BC031052 mRNA Translation: AAH31052.1
CCDSiCCDS7901.1
PIRiS71821
RefSeqiNP_004611.1, NM_004620.3
NP_665802.1, NM_145803.2
UniGeneiHs.444172
Hs.591983

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LB4X-ray2.40A348-504[»]
1LB5X-ray2.40A347-504[»]
1LB6X-ray1.80A347-504[»]
2ECINMR-A50-128[»]
2JMDNMR-A67-124[»]
3HCSX-ray2.20A/B50-211[»]
3HCTX-ray2.10A50-159[»]
3HCUX-ray2.60A/C50-159[»]
4Z8MX-ray2.95A/B346-504[»]
5ZUJX-ray2.60A350-501[»]
6A33X-ray2.10A350-501[»]
ProteinModelPortaliQ9Y4K3
SMRiQ9Y4K3
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113041, 318 interactors
CORUMiQ9Y4K3
DIPiDIP-27515N
ELMiQ9Y4K3
IntActiQ9Y4K3, 114 interactors
MINTiQ9Y4K3
STRINGi9606.ENSP00000337853

Chemistry databases

BindingDBiQ9Y4K3
ChEMBLiCHEMBL3588728

Protein family/group databases

MoonDBiQ9Y4K3 Predicted

PTM databases

iPTMnetiQ9Y4K3
PhosphoSitePlusiQ9Y4K3

Polymorphism and mutation databases

BioMutaiTRAF6
DMDMi30580642

Proteomic databases

EPDiQ9Y4K3
jPOSTiQ9Y4K3
MaxQBiQ9Y4K3
PaxDbiQ9Y4K3
PeptideAtlasiQ9Y4K3
PRIDEiQ9Y4K3
ProteomicsDBi86225

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		7189
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000348124; ENSP00000337853; ENSG00000175104
ENST00000526995; ENSP00000433623; ENSG00000175104
GeneIDi7189
KEGGihsa:7189
UCSCiuc001mwq.3 human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		7189
DisGeNETi7189
EuPathDBiHostDB:ENSG00000175104.14

GeneCards: human genes, protein and diseases

More...GeneCardsi		TRAF6
HGNCiHGNC:12036 TRAF6
HPAiCAB004605
HPA019805
HPA020599
MalaCardsiTRAF6
MIMi602355 gene
neXtProtiNX_Q9Y4K3
OpenTargetsiENSG00000175104
Orphaneti1810 Autosomal dominant hypohidrotic ectodermal dysplasia
PharmGKBiPA36713

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiENOG410ISDW Eukaryota
ENOG410XTXK LUCA
GeneTreeiENSGT00940000155426
HOGENOMiHOG000006625
HOVERGENiHBG060248
InParanoidiQ9Y4K3
KOiK03175
OMAiIRQNHEE
OrthoDBi1465912at2759
PhylomeDBiQ9Y4K3
TreeFamiTF321154

Enzyme and pathway databases

UniPathwayi
UPA00143

ReactomeiR-HSA-1257604 PIP3 activates AKT signaling
R-HSA-166058 MyD88:MAL(TIRAP) cascade initiated on plasma membrane
R-HSA-168638 NOD1/2 Signaling Pathway
R-HSA-168927 TICAM1, RIP1-mediated IKK complex recruitment
R-HSA-193692 Regulated proteolysis of p75NTR
R-HSA-202424 Downstream TCR signaling
R-HSA-205043 NRIF signals cell death from the nucleus
R-HSA-209543 p75NTR recruits signalling complexes
R-HSA-209560 NF-kB is activated and signals survival
R-HSA-2871837 FCERI mediated NF-kB activation
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-5607764 CLEC7A (Dectin-1) signaling
R-HSA-5689880 Ub-specific processing proteases
R-HSA-5689896 Ovarian tumor domain proteases
R-HSA-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-HSA-9014325 TICAM1,TRAF6-dependent induction of TAK1 complex
R-HSA-9020702 Interleukin-1 signaling
R-HSA-933541 TRAF6 mediated IRF7 activation
R-HSA-933542 TRAF6 mediated NF-kB activation
R-HSA-937039 IRAK1 recruits IKK complex
R-HSA-937041 IKK complex recruitment mediated by RIP1
R-HSA-937042 IRAK2 mediated activation of TAK1 complex
R-HSA-937072 TRAF6-mediated induction of TAK1 complex within TLR4 complex
R-HSA-975110 TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling
R-HSA-975138 TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation
R-HSA-975144 IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation
R-HSA-975155 MyD88 dependent cascade initiated on endosome
R-HSA-975163 IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation
R-HSA-975871 MyD88 cascade initiated on plasma membrane
SignaLinkiQ9Y4K3
SIGNORiQ9Y4K3

Miscellaneous databases

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

More...ChiTaRSi		TRAF6 human
EvolutionaryTraceiQ9Y4K3

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		TRAF6

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

More...GenomeRNAii		7189

Protein Ontology

More...PROi		PR:Q9Y4K3

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000175104 Expressed in 170 organ(s), highest expression level in secondary oocyte
GenevisibleiQ9Y4K3 HS

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

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 nameiTRAF6_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: Q9Y4K3
Secondary accession number(s): A6NKI7
, A8KAB3, D3DR16, Q8NEH5
<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: November 1, 1999
Last modified: February 13, 2019
This is version 213 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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