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0TRAF5_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameTRAF5
DescriptionTnf receptor-associated factor 5 (ring finger protein 84).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005515 protein binding (IPI)
0004871 signal transducer activity (IEP)
0043123 positive regulation of I-kappaB kinase/NF-k... (IEP)
0007165 signal transduction (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
The tumour necrosis factor receptor (TNFR) associated factors (TRAFs) act as signal transducers for both TNFRs and interleukin-1/Toll-like receptors. TRAFs function in immunity.mbryonic development.tress response and bone metabolism through their induction of cell proliferation.ifferentiation.nd apoptosis . TRAFs are characterised by two domains: an N-terminal domain containing RING and zinc finger motifs that is essential for the activation of downstream effectors.nd a C-terminal TRAF domain that is essential for self-association and receptor interaction . The TRAF-domain like fold is a beta-sandwich consisting of 8 strands in 2 beta sheets and has a circularly permuted greek-key immunoglobulin-fold topology that contains an extra strand. The substrate-binding domain (SBD) of the SIAH (seven in absentia homolog) family of proteins is structurally highly similar to the TRAF domain. The SIAH SBD interacts with a number of proteins.nd is involved in TNF-alpha-mediated NFkappaB activation . This entry represents the C-terminal portion of the SIAH substrate-binding domain.nd the TRAF domain.
  IPR013322:TRAF-type
Although apparently functionally unrelated.ntracellular TRAFs andextracellular meprins share a conserved region of about 180 residues.hemeprin and TRAF homology (MATH) domain .Meprins are mammalian tissue-specific metalloendopeptidases of the astacinfamily implicated in developmental.ormal and pathological processes byhydrolyzing a variety of proteins. Various growth factors.ytokines.ndextracellular matrix proteins are substrates for meprins. They are composed offive structural domains: an N-terminal endopeptidase domain. MAM domain (see). MATH domain.n EGF-like domain (see ) and aC-terminal transmembrane region. Meprin A and B form membrane boundhomotetramer whereas homooligomers of meprin A are secreted. A proteoliticsite adjacent to the MATH domain.nly present in meprin A.llows the releaseof the protein from the membrane .TRAF proteins were first isolated by their ability to interact with TNFreceptors . They promote cell survival by the activation of downstreamprotein kinases and.inally.ranscription factors of the NF-kB and AP-1family. The TRAF proteins are composed of 3 structural domains: a RING finger(see ) in the N-terminal part of the protein.ne to seven TRAFzinc fingers (see ) in the middle and the MATH domain in theC-terminal part . The MATH domain is necessary and sufficient forself-association and receptor interaction. From the structural analysis twoconsensus sequence recognized by the TRAF domain have been defined: a majorone.PSAT]x[QE]E and a minor one.xQxxD .The structure of the TRAF2 protein reveals a trimeric self-association of theMATH domain . The domain forms a new.ight-strandedantiparallel beta sandwich structure. A coiled-coil region adjacent to theMATH domain is also important for the trimerisation. The oligomerisation isessential for establishing appropriate connections to form signaling complexeswith TNF receptor-1. The ligand binding surface of TRAF proteins is located inbeta-strands 6 and 7 .
  IPR002083:MATH
Some of the proteins that have this domain are mammalian signal transducers associated with the cytoplasmic domain of the 75 kDa tumor necrosis factor receptor. A heterocomplex.omodimer or heterodimer of TRAF1 and TRAF2.inds to the N-terminal of the inhibitor of apoptosis proteins 1 and 2 (IAPS) and recruits them to the tumor necrosis factor receptor 2. Other proteins.45G2.6 protein from C. elegans and DG17 protein from slime mold also have this domain.
  IPR001293:Zinc finger, TRAF-type
Quality control of intracellular proteins is essential for cellular homeostasis. Molecular chaperones recognise and contribute to the refolding of misfolded or unfolded proteins.hereas the ubiquitin-proteasome system mediates the degradation of such abnormal proteins. Ubiquitin-protein ligases (E3s) determine the substrate specificity for ubiquitylation and have been classified into HECT and RING-finger families. More recently.owever.-box proteins.hich contain a domain (the U box) of about 70 amino acids that is conserved from yeast to humans.ave been identified as a new type of E3 .The RING-finger is a specialised type of Zn-finger of 40 to 60 residues that binds two atoms of zinc.nd is probably involved in mediating protein-protein interactions. . There are two different variants.he C3HC4-type and a C3H2C3-type.hich is clearly related despite the different cysteine/histidine pattern. The latter type is sometimes referred to as RING-H2 finger. The RING domain is a protein interaction domain which has been implicated in a range of diverse biological processes.E3 ubiquitin-protein ligase activity is intrinsic to the RING domain ofc-Cbl and is likely to be a general function of this domain; Various RINGfingers exhibit binding to E2 ubiquitin-conjugating enzymes (Ubcs) .Several 3D-structures for RING-fingers are known . The 3D structure of the zinc ligation system is unique to the RING domain and is referred to as the cross-brace motif. The spacing of the cysteines in such a domain is C-x(2)-C-x(9 to 39)-C-x(1 to 3)-H-x(2 to 3)-C-x(2)-C-x(4 to 48)-C-x(2)-C. Metal ligand pairs one and three co-ordinate to bind one zinc ion.hilst pairs two and four bind the second.s illustrated in the following schematic representation:Note that in the older literature.ome RING-fingers are denoted as LIM-domains. The LIM-domain Zn-finger is a fundamentally different family.lbeit with similar Cys-spacing (see ).
  IPR001841:Zinc finger, RING-type
The tumour necrosis factor receptor (TNFR) associated factors (TRAFs) act as signal transducers for both TNFRs and interleukin-1/Toll-like receptors. TRAFs function in immunity.mbryonic development.tress response and bone metabolism through their induction of cell proliferation.ifferentiation.nd apoptosis . TRAFs are characterised by two domains: an N-terminal domain containing RING and zinc finger motifs that is essential for the activation of downstream effectors.nd a C-terminal TRAF domain that is essential for self-association and receptor interaction . The TRAF-domain like fold is a beta-sandwich consisting of 8 strands in 2 beta sheets and has a circularly permuted greek-key immunoglobulin-fold topology that contains an extra strand. The substrate-binding domain (SBD) of the SIAH (seven in absentia homolog) family of proteins is structurally highly similar to the TRAF domain. The SIAH SBD interacts with a number of proteins.nd is involved in TNF-alpha-mediated NFkappaB activation .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR008974:TRAF-like
The tumour necrosis factor (TNF) receptor associated factors (TRAFs) are major signal transducers for the TNF receptor (TNFR) superfamily and the interleukin-1 receptor/Toll-like receptor superfamily in mammals . TRAFs constitute a family of genetically conserved adapter proteins found in mammals (TRAF1-6) as well as in other multicellular organisms such as Drosophila .. elegans . TRAF2 is the prototypical member of the family. Mammalian TRAF1 and TRAF2 were the first members initially identified by their association with TNFR2. The TRAF1/TRAF2 and TRAF3/TRAF5 gene pairs may have arisen from recent independent gene duplications and to share a common ancestral gene. TRAF4 and TRAF6 precursor genes may have arisen earlier during evolution.ith the divergence of the TRAF6 precursor occurring earliest of all. Except TRAF1.his PIRSF has a general domain architecture containing one N-terminal RING finger. variable number of middle region of TRAF-type zinc finger and C2H2 type of zinc finger.nd one C-terminal MATH domain. TRAF1 is unique in the family in that it lacks the N-terminal RING and zinc-finger domains . This has rendered TRAF1 unable to promote TNF receptor signalling and act as a "dominant negative" TRAF . Also TRAF1 is a substrate for caspases activated by TNF family death receptors . The larger C-terminal cleaved fragment can bind to and sequester TRAF2 from TNFR1 complex.herefore modulating TNF induced NFkB activation . A wide range of biological functions.uch as adaptive and innate immunity.mbryonic development.tress response and bone metabolism.re mediated by TRAFs through the induction of cell survival.roliferation.ifferentiation and death. TRAFs are functionally divergent from a perspective of both upstream and downstream TRAF signal transduction pathways and of signalling-dependent regulation of TRAF trafficking. Each TRAF protein interacts with and mediates the signal transduction of multiple receptors.nd in turn each receptor utilises multiple TRAFs for specific functions . About 40 interaction partners of TRAF have been described thus far.ncluding receptors.inases.egulators and adaptor proteins.TRAF proteins can be recruited to and activated by ligand-engaged receptors in least three distinct ways . 1) Members of the TNFR superfamily that do not contain intracellular death domains.uch as TNFR2 and CD40.ecruit TRAFs directly via short sequences in their intracellular tails . 2) Those that contain an intracellular death domain.uch as TNFR1.irst recruit an adapter protein.RADD.ia a death-domain-death-domain interaction.hich then serves as a central platform of the TNFR1 signalling complex.hich assembles TRAF2 and RIP for survival signalling.nd FADD and caspase-8 for the induction of apoptosis. 3) Members of the IL-1R/TLR superfamily contain a protein interaction module known as the TIR domain.hich recruits.equentially.yD88. TIR domain and death domain containing protein.nd IRAKs.dapter Ser/Thr kinases with death domains. IRAKs in turn associate with TRAF6 to elicit signalling by IL-1 and pathogenic components such as LPS. A common mechanism for the membrane-proximal event in TRAF signalling has been revealed by the conserved trimeric association in the crystal structure of the TRAF domain of TRAF2 .For additional information please see .
  IPR012227:TNF receptor-associated factor TRAF
The substrate-binding domain (SBD) of the SIAH (seven in absentia homolog) family of proteins is structurally highly similar to the TRAF domain. The SIAH SBD interacts with a number of proteins.nd is involved in TNF-alpha-mediated NFkappaB activation . This entry represents the N-terminal portion of the SIAH substrate-binding domain.nd the TRAF domain.
  IPR013323:SIAH-type
IPR013322:TRAF-type 
Evalue:-58.9208183288574 
Location:386-554IPR001293:zf-TRAF 
Evalue:-26.8239078521729 
Location:183-239IPR001293:zf-TRAF 
Evalue:-23.4948501586914 
Location:128-181IPR001841:zf-C3HC4 
Evalue:-3.17392516136169 
Location:45-81
SequencesProtein: TRAF5_HUMAN (557 aa)
mRNA: NM_004619
Local Annotation
Synapse Ontology
the generation of action potential at soma of neurons.
sdb:0313 generation of AP at soma  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 20 residues, 209566579-209566638Exon2: 75 residues, 209593203-209593422Exon3: 21 residues, 209594374-209594432Exon4: 36 residues, 209596331-209596433Exon5: 57 residues, 209599876-209600041Exon6: 28 residues, 209600666-209600744Exon7: 27 residues, 209601052-209601127Exon8: 33 residues, 209605340-209605433Exon9: 49 residues, 209609416-209609557Exon10: 58 residues, 209611266-209611435Exon11: 940 residues, 209612092-209614907Exon12: 2 residues, -Jump to TRAF5_HUMAN  
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