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Entry version 233 (13 Nov 2019)
Sequence version 2 (19 Sep 2002)
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Protein

TNF receptor-associated factor 2

Gene

TRAF2

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

Regulates activation of NF-kappa-B and JNK and plays a central role in the regulation of cell survival and apoptosis. Required for normal antibody isotype switching from IgM to IgG. Has E3 ubiquitin-protein ligase activity and promotes 'Lys-63'-linked ubiquitination of target proteins, such as BIRC3, RIPK1 and TICAM1. Is an essential constituent of several E3 ubiquitin-protein ligase complexes, where it promotes the ubiquitination of target proteins by bringing them into contact with other E3 ubiquitin ligases. Regulates BIRC2 and BIRC3 protein levels by inhibiting their autoubiquitination and subsequent degradation; this does not depend on the TRAF2 RING-type zinc finger domain. Plays a role in mediating activation of NF-kappa-B by EIF2AK2/PKR. In complex with BIRC2 or BIRC3, promotes ubiquitination of IKBKE.17 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 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

Has very low E3 ubiquitin ligase activity in the absence of sphingosine-1-phosphate. E3 ubiquitin ligase activity is strongly activated by cytoplasmic sphingosine-1-phosphate.1 Publication

<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 <a href="http://www.uniprot.org/help/function_section">Function</a> 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 fingeri34 – 73RING-typePROSITE-ProRule annotationAdd BLAST40
Zinc fingeri124 – 180TRAF-type 1PROSITE-ProRule annotationAdd BLAST57
Zinc fingeri177 – 233TRAF-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 processApoptosis, Ubl conjugation pathway
LigandLipid-binding, Metal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-140534 Caspase activation via Death Receptors in the presence of ligand
R-HSA-3371378 Regulation by c-FLIP
R-HSA-5213460 RIPK1-mediated regulated necrosis
R-HSA-5218900 CASP8 activity is inhibited
R-HSA-5357786 TNFR1-induced proapoptotic signaling
R-HSA-5357905 Regulation of TNFR1 signaling
R-HSA-5357956 TNFR1-induced NFkappaB signaling pathway
R-HSA-5668541 TNFR2 non-canonical NF-kB pathway
R-HSA-5675482 Regulation of necroptotic cell death
R-HSA-5676594 TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway
R-HSA-5689880 Ub-specific processing proteases
R-HSA-69416 Dimerization of procaspase-8
R-HSA-75893 TNF signaling
R-HSA-933541 TRAF6 mediated IRF7 activation
R-HSA-933542 TRAF6 mediated NF-kB activation

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

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SignaLinki
Q12933

SIGNOR Signaling Network Open Resource

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SIGNORi
Q12933

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

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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 2 (EC:2.3.2.27)
Alternative name(s):
E3 ubiquitin-protein ligase TRAF2
RING-type E3 ubiquitin transferase TRAF2Curated
Tumor necrosis factor type 2 receptor-associated protein 3
<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:TRAF2
Synonyms:TRAP3
<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 9

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:12032 TRAF2

Online Mendelian Inheritance in Man (OMIM)

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MIMi
601895 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q12933

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

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

Keywords - Cellular componenti

Cytoplasm

<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>Mutagenesisi11S → A: Reduces global phosphorylation. Partial reduction of TNF-dependent activation of NF-kappa-B and activation of JNK. 1 Publication1
Mutagenesisi11S → D: Slight increase of TNF-dependent activation of NF-kappa-B and activation of JNK. 1 Publication1
Mutagenesisi31K → R: Abolishes 'Lys-63'-linked polyubiquitination. 1
Mutagenesisi117T → A: Loss of phosphorylation site. Abolishes activation of NF-kappa-B. 1 Publication1
Mutagenesisi285I → A: Strongly reduced interaction with BIRC3. 1 Publication1
Mutagenesisi288V → A: Strongly reduced interaction with BIRC3. 1 Publication1
Mutagenesisi292E → A: Strongly reduced interaction with BIRC3. 1 Publication1

Organism-specific databases

DisGeNET

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DisGeNETi
7186

Open Targets

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OpenTargetsi
ENSG00000127191

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA164742666

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
Q12933

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
TRAF2

Domain mapping of disease mutations (DMDM)

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DMDMi
23503103

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000563992 – 501TNF receptor-associated factor 2Add BLAST500

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineCombined sources1
Modified residuei5PhosphoserineCombined sources1
Modified residuei7PhosphothreonineCombined sources1
Modified residuei11PhosphoserineCombined sources1 Publication1
Modified residuei22PhosphothreonineCombined sources1
<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-linki31Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei117Phosphothreonine; by PKC1 Publication1

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

Phosphorylated at several serine residues within the first 128 amino acid residues. Phosphorylated at Thr-117 in response to signaling via TNF and TNFRSF1A. Phosphorylation at Thr-117 is required for 'Lys-63'-linked polyubiquitination, but not for 'Lys-48'-linked polyubiquitination. Phosphorylation at Thr-117 is important for interaction with IKKA and IKKB, activation of IKK and subsequent activation of NF-kappa-B.1 Publication
Undergoes both 'Lys-48'-linked and 'Lys-63'-linked polyubiquitination. Polyubiquitinated via 'Lys-63'-linked ubiquitin in response to TNF signaling; this requires prior phosphorylation at Thr-117. 'Lys-63'-linked polyubiquitination promotes TRAF2-mediated activation of NF-kappa-B. Can be polyubiquitinated at several Lys residues via 'Lys-48'-linked ubiquitin chains in response to TNF signaling, leading to proteasomal degradation. Autoubiquitinated, leading to its subsequent proteasomal degradation. Polyubiquitinated by BIRC2 and SIAH2, leading to its subsequent proteasomal degradation. Deubiquitinated by CYLD, a protease that specifically cleaves 'Lys-63'-linked polyubiquitin chains.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q12933

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q12933

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
Q12933

MaxQB - The MaxQuant DataBase

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MaxQBi
Q12933

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

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PaxDbi
Q12933

PeptideAtlas

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PeptideAtlasi
Q12933

PRoteomics IDEntifications database

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PRIDEi
Q12933

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
59035 [Q12933-1]
59036 [Q12933-2]
59037 [Q12933-3]
59038 [Q12933-4]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q12933

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

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PhosphoSitePlusi
Q12933

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000127191 Expressed in 156 organ(s), highest expression level in cerebellar hemisphere

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q12933 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q12933 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB004603
HPA009972
HPA010634

<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 (PubMed:8069916). Heterotrimer with TRAF1 (PubMed:8069916). Heterotrimer with TRAF3 (via TRAF domain) (PubMed:15383523, PubMed:20447407). The domain containing the RING-type and the first TRAF-type zinc finger can also form homodimers (in vitro) (PubMed:19810754).

Interacts with TNFRSF1B/TNFR2 (PubMed:7639698, PubMed:8069916, PubMed:10206649).

Interacts with TNFRSF5/CD40 (PubMed:9718306).

Interacts with TNFRSF4, TNFRSF7/CD27, TNFRSF8/CD30, TNFRSF9/CD137, TNFRSF11A/RANK, TNFRSF13B/TACI, TNFRSF14, TNFRSF16/NGFR, TNFRSF17/BCMA, TNFRSF18/AITR, TNFRSF19/TROY, TNFRSF19L/RELT, EDAR and IL15RA (PubMed:8627180, PubMed:9153189, PubMed:9692890, PubMed:9488716, PubMed:9774460, PubMed:9607925, PubMed:9418902, PubMed:10463949, PubMed:10037686, PubMed:10514511, PubMed:10809768, PubMed:10880535, PubMed:11035039, PubMed:10411888). Stimulation of TNF-alpha receptor TNFRSF1A leads to the formation of two distinct signaling complexes. Plasma membrane-bound complex I is composed of TNFRSF1A, TRADD, RIPK1, TRAF2 and BIRC2/c-IAP1 or BIRC3 which interacts with CHUCK/IKK-alpha, IKBKB/IKK-beta and IKBKG/IKK-gamma promoting cell survival (PubMed:21307340, PubMed:18981220). Subsequently, TRADD, RIPK1 and TRAF2 dissociate from TNFRSF1A and form cytoplasmic complex II with FADD and caspase CASP8 promoting cell apoptosis (PubMed:21307340).

Interacts with TRADD (PubMed:10892748).

Identified in a complex with TNFRSF1A, RIPK1 and IKBKB/IKK-beta (PubMed:18981220).

Interacts with RIPK2 (PubMed:9705938).

Interacts with BIRC2 and BIRC3 N-terminus; a single BIRC2 or BIRC3 molecule interacts with a heterotrimer formed by TRAF1 and TRAF2, or a TRAF2 homotrimer (PubMed:11907583, PubMed:19506082, PubMed:20447407, PubMed:20385093).

Identified in a complex composed of TRAF2, TRAF3, BIRC2 and BIRC3 (By similarity).

Interacts with BIRC2; the interaction promotes BIRC2 stability (PubMed:19506082). Interaction with BIRC2 and/or BIRC3 is essential for ubiquitination of IKBKE, degradation of NFKBIA and activation of NF-kappa-B (By similarity). Within complex I, phosphorylated TRAF2 interacts (via 'Lys-63'-linked polyubiquitin chains) with CHUCK/IKK-alpha, IKBKB/IKK-beta, IKBKG/IKK-gamma TAB2, TAB3 and TAK1 in response to TNF-alpha stimulation (PubMed:19150425). Within complex I, interacts with UXT isoform 1 (via TPQE motif); the interaction prevents the recruitment of FADD and CASP8/caspase 8 to complex I (PubMed:21307340).

Forms a complex composed of TNFRSF8/CD30 or TNFRSF1B/TNFR2, and TRAF1, TRAF2 and E3 ligase TRAIP (PubMed:9104814). Within the complex, interacts with TRAIP; the interaction inhibits TRAF2-mediated NF-kappa B activation (PubMed:9104814).

Component of a complex composed of TANK and TBK1 (PubMed:10581243).

Interacts with TRPC4AP (By similarity).

Interacts with MAP3K1/MEKK1, MAP3K5/ASK1 and MAP3K11/MLK3 in response to TNF-alpha stimulation; the interaction leads to JNK activation (PubMed:10346818, PubMed:19918265, PubMed:9774977).

Component of a complex composed of MAP3K14/NIK BIRC3 and TRAF3; the interaction leads to BIRC2/3-mediated ubiquitination of TRAF3 upon CD40 engagement in a TRAF2-dependent manner (By similarity).

Interacts with MAP3K14/NIK in response to TNF-alpha stimulation; the interaction leads to NF-kappa B activation (PubMed:9020361).

Interacts with PEG3; the interaction may promote TRAF2-mediated NF-kappa B activation (By similarity).

Interacts with HIVEP3; the interaction may inhibit TNF-alpha-TRAF2-mediated NF-kappa B and JNK activation (By similarity).

Interacts with TANK/ITRAF; the interaction prevents interaction between TNFRSF1B/TNFR2 and TRAF2 (PubMed:8710854).

Interacts with deubiquitinating enzyme CYLD; the interaction results in the deubiquitination and inactivation of TRAF2 (PubMed:12917691).

Interacts with SIAH2; the interaction leads to TRAF2 ubiquitination and degradation (PubMed:12411493).

Interacts with E2 conjugating enzyme UBE2N/Ubc13, E3 ligase ITCH and RNF11 in response to TNF-alpha stimulation (By similarity).

Interacts with ubiquitin-editing enzyme TNFAIP3/A20 in response to TNF-alpha stimulation; the interaction promotes TRAF2 dissociation from UBE2N/Ubc13, ITCH, RNF11 and TAX1BP1 and prevents prolonged TRAF-2 ubiquitination (By similarity).

Interacts with TAX1BP1 in response to TNF-alpha stimulation; the interaction promotes TRAF2 dissociation from UBE2N/Ubc13 and TNFAIP3/A20, and prevents prolonged TRAF-2 ubiquitination (By similarity).

Interacts (via C-terminus) with EIF2AK2/PKR (via the kinase catalytic domain) (PubMed:15121867).

Interacts with deubiquitinating enzyme USP48 (PubMed:16214042).

Interacts with PTPN2; probably involved in TNF-mediated signaling (PubMed:15696169).

Interacts with Toll-like receptor TLR4/3 adapter TICAM1/TRIF; the interaction may promotes TICAM1 ubiquitination (PubMed:20047764).

Interacts with kinase/endoribonuclease ERN1/IRE1 and DAB2IP in response to ER stress; the interaction requires DAB2IP (By similarity).

Interacts with ERN1/IRE1 and TAOK3 in response to ER stress; the interaction may promote TRAF2 phosphorylation (PubMed:11278723).

Interacts (via zinc fingers) with DAB2IP (via C-terminus PER domain)in response to TNF-alpha stimulation (PubMed:15310755, PubMed:17389591).

Interacts with CASP8AP2/FLASH (By similarity).

Interacts with NFATC2IP; the interaction may repress IL-4 production in T cells (By similarity).

Interacts with kinase CDK9 (PubMed:9827693).

Interacts with sphingosine kinase 1 SPHK1 (PubMed:20577214).

Interacts with kinase TNIK (PubMed:10521462).

Interacts with TRAFD1 (By similarity).

Interacts with DNA phosphodiesterase TDP2 (PubMed:10764746).

Interacts with MAVS/IPS1 (PubMed:16153868).

Interacts with CARD14 (PubMed:21302310).

Interacts with Epstein-Barr virus LMP1/BNFL1 (PubMed:10411888).

Interacts with GPS2 (By similarity).

Interacts with XPNPEP3 (PubMed:25609706).

Interacts with RIPK3 (PubMed:29883609).

Interacts with RELL2 (PubMed:19969290).

By similarity54 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

WithEntry#Exp.IntActNotes
itself9EBI-355744,EBI-355744
B2R8Y43EBI-355744,EBI-10175581
P889613EBI-355744,EBI-7907665From Human herpesvirus 8 type M.
Q9NRN76EBI-355744,EBI-740884
P632612EBI-355744,EBI-351292
Q9UHB73EBI-355744,EBI-395282
Q9UHB7-23EBI-355744,EBI-10261324
Q9Y2J4-43EBI-355744,EBI-10187270
X5D7783EBI-355744,EBI-17183751
Q96IX96EBI-355744,EBI-744859
Q9UKG12EBI-355744,EBI-741243
P299723EBI-355744,EBI-745213
Q8N5N63EBI-355744,EBI-10266832
Q8N9N23EBI-355744,EBI-10268317
P542537EBI-355744,EBI-930964
O151693EBI-355744,EBI-710484
Q8TBE03EBI-355744,EBI-742750
B4DE543EBI-355744,EBI-16429313
Q8N9N54EBI-355744,EBI-744695
Q8N9N5-73EBI-355744,EBI-16429296
O959998EBI-355744,EBI-958922
Q9BXY85EBI-355744,EBI-745073
Q1349016EBI-355744,EBI-514538
Q134897EBI-355744,EBI-517709
Q86X595EBI-355744,EBI-8465536
O087366EBI-355744,EBI-6140033From Mus musculus.
Q8NEC53EBI-355744,EBI-744545
Q9HC525EBI-355744,EBI-712912
Q9NVL83EBI-355744,EBI-10238351
Q8TD31-35EBI-355744,EBI-10175300
F6RF563EBI-355744,EBI-10177725
P2594211EBI-355744,EBI-525714
Q86Y333EBI-355744,EBI-10260504
Q996186EBI-355744,EBI-739534
P465275EBI-355744,EBI-519280
Q8IYX8-23EBI-355744,EBI-10181988
Q02930-35EBI-355744,EBI-10192698
Q6BCY43EBI-355744,EBI-744761
O609414EBI-355744,EBI-740402
Q8WWZ35EBI-355744,EBI-2949647
A0A0S2Z3V13EBI-355744,EBI-16434097
Q1280511EBI-355744,EBI-536772
Q5JVL45EBI-355744,EBI-743105
P005333EBI-355744,EBI-297353
Q9H0I26EBI-355744,EBI-744099
O754603EBI-355744,EBI-371750
A0A0S2Z3N63EBI-355744,EBI-16434659
Q018443EBI-355744,EBI-739737
Q8N2X66EBI-355744,EBI-749333
Q96EK73EBI-355744,EBI-739883
Q9GZU83EBI-355744,EBI-2371956
Q86YD75EBI-355744,EBI-6658203
Q9NVF75EBI-355744,EBI-740282
Q9BRP75EBI-355744,EBI-10297077
Q53EP0-33EBI-355744,EBI-10242151
Q065476EBI-355744,EBI-618165
Q9H8Y86EBI-355744,EBI-739467
Q929175EBI-355744,EBI-746309
Q2KHT43EBI-355744,EBI-10239244
P092115EBI-355744,EBI-353467
Q5T8I93EBI-355744,EBI-9675710
P090223EBI-355744,EBI-3957603From Mus musculus.
Q8NA543EBI-355744,EBI-10220600
Q9BVG83EBI-355744,EBI-2125614
P576825EBI-355744,EBI-8472267
Q8TBB13EBI-355744,EBI-739832
Q132332EBI-355744,EBI-49776
Q629252EBI-355744,EBI-636664From Rattus norvegicus.
Q995587EBI-355744,EBI-358011
Q996834EBI-355744,EBI-476263
Q7Z4344EBI-355744,EBI-995373
Q6PF185EBI-355744,EBI-9675802
Q8N6N63EBI-355744,EBI-8656665
O760415EBI-355744,EBI-2880203
Q166493EBI-355744,EBI-3951858
P071743EBI-355744,EBI-1038810From Rattus norvegicus.
Q9GZQ43EBI-355744,EBI-10303844
Q166563EBI-355744,EBI-2547810
P890553EBI-355744,EBI-9522973From Rotavirus sp..
Q9BRJ75EBI-355744,EBI-2949792
Q86SE93EBI-355744,EBI-2827999
Q96JS36EBI-355744,EBI-10290053
Q135266EBI-355744,EBI-714158
O604375EBI-355744,EBI-368321
Q6NYC85EBI-355744,EBI-2557469
O437417EBI-355744,EBI-1053424
Q9H8753EBI-355744,EBI-744488
P547256EBI-355744,EBI-746453
Q8WWW03EBI-355744,EBI-367390
Q96IZ55EBI-355744,EBI-740773
Q9P2K34EBI-355744,EBI-743428
P483803EBI-355744,EBI-742557
Q135467EBI-355744,EBI-358507
Q0D2K35EBI-355744,EBI-10226430
Q9NTX73EBI-355744,EBI-722397
Q9H7885EBI-355744,EBI-747035
Q9H0W85EBI-355744,EBI-2872322
Q9BV903EBI-355744,EBI-9675976
Q9NZD86EBI-355744,EBI-742688
G2XKQ03EBI-355744,EBI-10175576
Q9BSW75EBI-355744,EBI-745392
Q928448EBI-355744,EBI-356349
Q9H2K82EBI-355744,EBI-1384100
Q9UHD26EBI-355744,EBI-356402
Q155606EBI-355744,EBI-710310
Q9BXF95EBI-355744,EBI-8644516
Q9BT498EBI-355744,EBI-741350
Q96CV83EBI-355744,EBI-6137619
Q96CG37EBI-355744,EBI-740711
Q081173EBI-355744,EBI-717810
P215808EBI-355744,EBI-527670
Q9Y6Q62EBI-355744,EBI-525675
Q9Y6Q6-25EBI-355744,EBI-20899422
Q9NP843EBI-355744,EBI-2851995
Q929564EBI-355760,EBI-1056653
P194385EBI-355744,EBI-299451
P203333EBI-355744,EBI-358983
Q9UKE52EBI-355744,EBI-1051794
Q1562812EBI-355744,EBI-359215
Q130776EBI-355744,EBI-359224
P701912EBI-355744,EBI-523899From Mus musculus.
Q9Y4K310EBI-355744,EBI-359276
Q8IWZ53EBI-355744,EBI-5235829
Q128155EBI-355744,EBI-2349743
Q63HK53EBI-355744,EBI-9053916
Q9Y5U23EBI-355744,EBI-717229
Q5T1245EBI-355744,EBI-746004
P224153EBI-355744,EBI-1054489
O756046EBI-355744,EBI-743272
Q70EK83EBI-355744,EBI-742050
Q5GFL63EBI-355744,EBI-10243723
P079473EBI-355744,EBI-515331
Q055164EBI-355744,EBI-711925
P242784EBI-355744,EBI-739899
Q53FD03EBI-355744,EBI-740767
Q6FIF07EBI-355744,EBI-724630
Q96NC05EBI-355744,EBI-2682299
Q86VK43EBI-355744,EBI-720304
Q96MN93EBI-355744,EBI-948288
Q32MK93EBI-355744,EBI-10239929
Q6NX493EBI-355744,EBI-2841978
Q8N7203EBI-355744,EBI-625509
Q6ZS27-33EBI-355744,EBI-10255155
A0A0S2Z6P03EBI-355744,EBI-16429989
Q3MJ624EBI-355744,EBI-5667532
Q9NX653EBI-355744,EBI-739949

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
113038, 378 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q12933

Database of interacting proteins

More...
DIPi
DIP-6223N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
Q12933

Protein interaction database and analysis system

More...
IntActi
Q12933, 425 interactors

Molecular INTeraction database

More...
MINTi
Q12933

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000247668

<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

1501
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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SMRi
Q12933

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q12933

<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>Domaini351 – 496MATHPROSITE-ProRule annotationAdd BLAST146

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>Regioni283 – 293Important for interaction with BIRC2 and BIRC3By similarityAdd BLAST11

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 – 3481 PublicationAdd BLAST50

<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.1 Publication
The MATH/TRAF domain binds to receptor cytoplasmic domains.1 Publication
The RING-type zinc finger domain is essential for E3 ubiquitin-protein ligase activity. It is not essential for the stabilization of BIRC2, or for the ubiquitination of RIPK1 in response to TNFR1 signaling.1 Publication

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri34 – 73RING-typePROSITE-ProRule annotationAdd BLAST40
Zinc fingeri124 – 180TRAF-type 1PROSITE-ProRule annotationAdd BLAST57
Zinc fingeri177 – 233TRAF-type 2PROSITE-ProRule annotationAdd BLAST57

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410ISDM Eukaryota
ENOG4111M70 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000156621

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000231558

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q12933

KEGG Orthology (KO)

More...
KOi
K03173

Identification of Orthologs from Complete Genome Data

More...
OMAi
CRFHAVG

Database of Orthologous Groups

More...
OrthoDBi
918518at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q12933

TreeFam database of animal gene trees

More...
TreeFami
TF321154

Family and domain databases

Conserved Domains Database

More...
CDDi
cd03778 MATH_TRAF2, 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
IPR027133 TRAF2
IPR037305 TRAF2_MATH
IPR032070 TRAF_BIRC3-bd
IPR018957 Znf_C3HC4_RING-type
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
IPR017907 Znf_RING_CS
IPR001293 Znf_TRAF

The PANTHER Classification System

More...
PANTHERi
PTHR10131:SF21 PTHR10131:SF21, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF16673 TRAF_BIRC3_bd, 1 hit
PF00097 zf-C3HC4, 1 hit
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, 1 hit

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>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (4+)i

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

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 4 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q12933-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
MAAASVTPPG SLELLQPGFS KTLLGTKLEA KYLCSACRNV LRRPFQAQCG
60 70 80 90 100
HRYCSFCLAS ILSSGPQNCA ACVHEGIYEE GISILESSSA FPDNAARREV
110 120 130 140 150
ESLPAVCPSD GCTWKGTLKE YESCHEGRCP LMLTECPACK GLVRLGEKER
160 170 180 190 200
HLEHECPERS LSCRHCRAPC CGADVKAHHE VCPKFPLTCD GCGKKKIPRE
210 220 230 240 250
KFQDHVKTCG KCRVPCRFHA IGCLETVEGE KQQEHEVQWL REHLAMLLSS
260 270 280 290 300
VLEAKPLLGD QSHAGSELLQ RCESLEKKTA TFENIVCVLN REVERVAMTA
310 320 330 340 350
EACSRQHRLD QDKIEALSSK VQQLERSIGL KDLAMADLEQ KVLEMEASTY
360 370 380 390 400
DGVFIWKISD FARKRQEAVA GRIPAIFSPA FYTSRYGYKM CLRIYLNGDG
410 420 430 440 450
TGRGTHLSLF FVVMKGPNDA LLRWPFNQKV TLMLLDQNNR EHVIDAFRPD
460 470 480 490 500
VTSSSFQRPV NDMNIASGCP LFCPVSKMEA KNSYVRDDAI FIKAIVDLTG

L
Length:501
Mass (Da):55,859
Last modified:September 19, 2002 - 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:iC508BE185B783B20
GO
Isoform 2 (identifier: Q12933-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     122-122: E → EVKMPACGMVTEAPAVGSRPRSPSSYDLVLHVPLTGAEACLMSVEEETELLLR

Note: No experimental confirmation available.
Show »
Length:553
Mass (Da):61,384
Checksum:iE5000CF242B2F404
GO
Isoform 3 (identifier: Q12933-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     53-63: Missing.

Note: No experimental confirmation available.
Show »
Length:490
Mass (Da):54,671
Checksum:i9CAF6DDAB0DE64DD
GO
Isoform 4 (identifier: Q12933-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     176-200: Missing.

Note: No experimental confirmation available.
Show »
Length:476
Mass (Da):53,055
Checksum:iBB290C92E8D33D79
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B1AMX8B1AMX8_HUMAN
TNF receptor-associated factor 2
TRAF2
193Annotation 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>
B1AMX7B1AMX7_HUMAN
TNF receptor-associated factor 2
TRAF2
171Annotation 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>
B1AMY1B1AMY1_HUMAN
TNF receptor-associated factor 2
TRAF2
121Annotation 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>

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 conflicti205 – 310Missing in BAB70792 (PubMed:14702039).CuratedAdd BLAST106
Sequence conflicti343 – 365LEMEA…FARKR → RPFQAQCGHRYCSFCLASIL RKL in AAA87706 (PubMed:7639698).CuratedAdd BLAST23

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_03968753 – 63Missing in isoform 3. 1 PublicationAdd BLAST11
Alternative sequenceiVSP_007401122E → EVKMPACGMVTEAPAVGSRP RSPSSYDLVLHVPLTGAEAC LMSVEEETELLLR in isoform 2. 1 Publication1
Alternative sequenceiVSP_039688176 – 200Missing in isoform 4. 1 PublicationAdd BLAST25

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
U12597 mRNA Translation: AAA87706.1
AK054686 mRNA Translation: BAB70792.1
AK289722 mRNA Translation: BAF82411.1
AK298370 mRNA Translation: BAG60609.1
BX538160 mRNA Translation: CAD98040.1
AY623660 Genomic DNA Translation: AAT27320.1
AL355987 Genomic DNA No translation available.
AL449425 Genomic DNA No translation available.
CH471090 Genomic DNA Translation: EAW88299.1
BC032410 mRNA Translation: AAH32410.1
BC033810 mRNA Translation: AAH33810.1
BC043492 mRNA Translation: AAH43492.1
BC064662 mRNA Translation: AAH64662.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS7013.1 [Q12933-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
S56163

NCBI Reference Sequences

More...
RefSeqi
NP_066961.2, NM_021138.3 [Q12933-1]
XP_011517276.1, XM_011518974.2 [Q12933-1]
XP_011517277.1, XM_011518975.2
XP_011517278.1, XM_011518976.2 [Q12933-1]
XP_011517279.1, XM_011518977.2 [Q12933-1]
XP_011517280.1, XM_011518978.2
XP_016870584.1, XM_017015095.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000247668; ENSP00000247668; ENSG00000127191 [Q12933-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
7186

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:7186

UCSC genome browser

More...
UCSCi
uc004cjv.4 human [Q12933-1]

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

<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
U12597 mRNA Translation: AAA87706.1
AK054686 mRNA Translation: BAB70792.1
AK289722 mRNA Translation: BAF82411.1
AK298370 mRNA Translation: BAG60609.1
BX538160 mRNA Translation: CAD98040.1
AY623660 Genomic DNA Translation: AAT27320.1
AL355987 Genomic DNA No translation available.
AL449425 Genomic DNA No translation available.
CH471090 Genomic DNA Translation: EAW88299.1
BC032410 mRNA Translation: AAH32410.1
BC033810 mRNA Translation: AAH33810.1
BC043492 mRNA Translation: AAH43492.1
BC064662 mRNA Translation: AAH64662.1
CCDSiCCDS7013.1 [Q12933-1]
PIRiS56163
RefSeqiNP_066961.2, NM_021138.3 [Q12933-1]
XP_011517276.1, XM_011518974.2 [Q12933-1]
XP_011517277.1, XM_011518975.2
XP_011517278.1, XM_011518976.2 [Q12933-1]
XP_011517279.1, XM_011518977.2 [Q12933-1]
XP_011517280.1, XM_011518978.2
XP_016870584.1, XM_017015095.1

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
1CA4X-ray2.20A/B/C/D/E/F334-501[»]
1CA9X-ray2.30A/B/C/D/E/F310-501[»]
1CZYX-ray2.00A/B/C334-501[»]
1CZZX-ray2.70A/B/C315-501[»]
1D00X-ray2.00A/B/C/D/E/F/G/H334-501[»]
1D01X-ray2.00A/B/C/D/E/F334-501[»]
1D0AX-ray2.00A/B/C/D/E/F334-501[»]
1D0JX-ray2.50A/B/C/D/E/F334-501[»]
1F3VX-ray2.00B331-501[»]
1QSCX-ray2.40A/B/C311-501[»]
3KNVX-ray1.90A1-133[»]
3M06X-ray2.67A/B/C/D/E/F266-329[»]
3M0AX-ray2.61A/B/C266-329[»]
3M0DX-ray2.80A/B266-329[»]
SMRiQ12933
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi113038, 378 interactors
CORUMiQ12933
DIPiDIP-6223N
ELMiQ12933
IntActiQ12933, 425 interactors
MINTiQ12933
STRINGi9606.ENSP00000247668

PTM databases

iPTMnetiQ12933
PhosphoSitePlusiQ12933

Polymorphism and mutation databases

BioMutaiTRAF2
DMDMi23503103

Proteomic databases

EPDiQ12933
jPOSTiQ12933
MassIVEiQ12933
MaxQBiQ12933
PaxDbiQ12933
PeptideAtlasiQ12933
PRIDEiQ12933
ProteomicsDBi59035 [Q12933-1]
59036 [Q12933-2]
59037 [Q12933-3]
59038 [Q12933-4]

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
7186

Genome annotation databases

EnsembliENST00000247668; ENSP00000247668; ENSG00000127191 [Q12933-1]
GeneIDi7186
KEGGihsa:7186
UCSCiuc004cjv.4 human [Q12933-1]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
7186
DisGeNETi7186

GeneCards: human genes, protein and diseases

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GeneCardsi
TRAF2
HGNCiHGNC:12032 TRAF2
HPAiCAB004603
HPA009972
HPA010634
MIMi601895 gene
neXtProtiNX_Q12933
OpenTargetsiENSG00000127191
PharmGKBiPA164742666

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410ISDM Eukaryota
ENOG4111M70 LUCA
GeneTreeiENSGT00940000156621
HOGENOMiHOG000231558
InParanoidiQ12933
KOiK03173
OMAiCRFHAVG
OrthoDBi918518at2759
PhylomeDBiQ12933
TreeFamiTF321154

Enzyme and pathway databases

UniPathwayiUPA00143
ReactomeiR-HSA-140534 Caspase activation via Death Receptors in the presence of ligand
R-HSA-3371378 Regulation by c-FLIP
R-HSA-5213460 RIPK1-mediated regulated necrosis
R-HSA-5218900 CASP8 activity is inhibited
R-HSA-5357786 TNFR1-induced proapoptotic signaling
R-HSA-5357905 Regulation of TNFR1 signaling
R-HSA-5357956 TNFR1-induced NFkappaB signaling pathway
R-HSA-5668541 TNFR2 non-canonical NF-kB pathway
R-HSA-5675482 Regulation of necroptotic cell death
R-HSA-5676594 TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway
R-HSA-5689880 Ub-specific processing proteases
R-HSA-69416 Dimerization of procaspase-8
R-HSA-75893 TNF signaling
R-HSA-933541 TRAF6 mediated IRF7 activation
R-HSA-933542 TRAF6 mediated NF-kB activation
SignaLinkiQ12933
SIGNORiQ12933

Miscellaneous databases

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

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ChiTaRSi
TRAF2 human
EvolutionaryTraceiQ12933

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
TRAF2

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

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GenomeRNAii
7186
PharosiQ12933

Protein Ontology

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PROi
PR:Q12933

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000127191 Expressed in 156 organ(s), highest expression level in cerebellar hemisphere
ExpressionAtlasiQ12933 baseline and differential
GenevisibleiQ12933 HS

Family and domain databases

CDDicd03778 MATH_TRAF2, 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
IPR027133 TRAF2
IPR037305 TRAF2_MATH
IPR032070 TRAF_BIRC3-bd
IPR018957 Znf_C3HC4_RING-type
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
IPR017907 Znf_RING_CS
IPR001293 Znf_TRAF
PANTHERiPTHR10131:SF21 PTHR10131:SF21, 1 hit
PfamiView protein in Pfam
PF16673 TRAF_BIRC3_bd, 1 hit
PF00097 zf-C3HC4, 1 hit
PF02176 zf-TRAF, 1 hit
PIRSFiPIRSF015614 TRAF, 1 hit
SMARTiView protein in SMART
SM00061 MATH, 1 hit
SM00184 RING, 1 hit
SUPFAMiSSF49599 SSF49599, 1 hit
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...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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 nameiTRAF2_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: Q12933
Secondary accession number(s): A8K107
, B4DPJ7, Q7Z337, Q96NT2
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: September 19, 2002
Last modified: November 13, 2019
This is version 233 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
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