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CD40 and RANK can activate the noncanonical NF-κB pathway that is dependent on NF-κB inducing kinase (NIK) expression levels. In unstimulated cells NIK forms a cytosolic complex with the ubiquitin ligases TRAF2, TRAF3 and cIAP1/2, which facilitates the K48-linked polyubiquitination and proteasomal degradation of NIK, keeping NIK levels low. Upon ligand binding, TRAF3 is recruited to the receptor, where TRAF2 directs nondegradative K63-linked polyubiquitination of cIAP1/2, resulting in their activation. Subsequently cIAP1/2 directs its K48-linked polyubiquitination to TRAF3, rather than NIK. As a result, TRAF3 is degraded and NIK is stabilised, resulting in increased NIK levels in the cell. NIK then phosphorylates and activates IKK1, which mediates NF-κB p100 phosphorylation. This is followed by K48-linked polyubiquitination and partial proteasomal degradation of p100 to p52, which forms a heterodimer with RelB to activate transcription. Next to TRAF3, TRAF1 has also been identified as a negative regulator of this pathway, most probably by competing with other TNF receptor-associated factors. cIAP, cellular inhibitor of apoptosis; IKK, IκB kinase; NF, nuclear factor; RANK, receptor activator of NF-κB; TRAF, TNF receptor-associated factor; TNF, tumour necrosis factor."}

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CD40 and RANK can activate the noncanonical NF-κB pathway that is dependent on NF-κB inducing kinase (NIK) expression levels. In unstimulated cells NIK forms a cytosolic complex with the ubiquitin ligases TRAF2, TRAF3 and cIAP1/2, which facilitates the K48-linked polyubiquitination and proteasomal degradation of NIK, keeping NIK levels low. Upon ligand binding, TRAF3 is recruited to the receptor, where TRAF2 directs nondegradative K63-linked polyubiquitination of cIAP1/2, resulting in their activation. Subsequently cIAP1/2 directs its K48-linked polyubiquitination to TRAF3, rather than NIK. As a result, TRAF3 is degraded and NIK is stabilised, resulting in increased NIK levels in the cell. NIK then phosphorylates and activates IKK1, which mediates NF-κB p100 phosphorylation. This is followed by K48-linked polyubiquitination and partial proteasomal degradation of p100 to p52, which forms a heterodimer with RelB to activate transcription. 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NF-κB signalling. CD40 and RANK can activate the noncanonical NF-κB pathway that is dependent on NF-κB inducing kinase (NIK) expression levels. In unstimulated cells NIK forms a cytosolic complex with the ubiquitin ligases TRAF2, TRAF3 and cIAP1/2, which facilitates the K48-linked polyubiquitination and proteasomal degradation of NIK, keeping NIK levels low. Upon ligand binding, TRAF3 is recruited to the receptor, where TRAF2 directs nondegradative K63-linked polyubiquitination of cIAP1/2, resulting in their activation. Subsequently cIAP1/2 directs its K48-linked polyubiquitination to TRAF3, rather than NIK. As a result, TRAF3 is degraded and NIK is stabilised, resulting in increased NIK levels in the cell. NIK then phosphorylates and activates IKK1, which mediates NF-κB p100 phosphorylation. This is followed by K48-linked polyubiquitination and partial proteasomal degradation of p100 to p52, which forms a heterodimer with RelB to activate transcription. Next to TRAF3, TRAF1 has also been identified as a negative regulator of this pathway, most probably by competing with other TNF receptor-associated factors. cIAP, cellular inhibitor of apoptosis; IKK, IκB kinase; NF, nuclear factor; RANK, receptor activator of NF-κB; TRAF, TNF receptor-associated factor; TNF, tumour necrosis factor."}

{"project":"GO-BP","denotations":[{"id":"T21763","span":{"begin":1301,"end":1309},"obj":"http://purl.obolibrary.org/obo/GO_0070265"},{"id":"T21762","span":{"begin":1301,"end":1309},"obj":"http://purl.obolibrary.org/obo/GO_0019835"},{"id":"T21761","span":{"begin":1301,"end":1309},"obj":"http://purl.obolibrary.org/obo/GO_0008219"},{"id":"T21760","span":{"begin":1301,"end":1309},"obj":"http://purl.obolibrary.org/obo/GO_0001906"},{"id":"T21759","span":{"begin":1231,"end":1249},"obj":"http://purl.obolibrary.org/obo/GO_0051092"},{"id":"T21758","span":{"begin":1179,"end":1182},"obj":"http://purl.obolibrary.org/obo/GO_0008384"},{"id":"T21757","span":{"begin":1168,"end":1177},"obj":"http://purl.obolibrary.org/obo/GO_0097194"},{"id":"T21756","span":{"begin":1168,"end":1177},"obj":"http://purl.obolibrary.org/obo/GO_0006915"},{"id":"T21755","span":{"begin":1146,"end":1154},"obj":"http://purl.obolibrary.org/obo/GO_0007349"},{"id":"T21754","span":{"begin":967,"end":980},"obj":"http://purl.obolibrary.org/obo/GO_0006351"},{"id":"T21753","span":{"begin":800,"end":815},"obj":"http://purl.obolibrary.org/obo/GO_0016310"},{"id":"T21752","span":{"begin":891,"end":902},"obj":"http://purl.obolibrary.org/obo/GO_0009056"},{"id":"T21751","span":{"begin":330,"end":341},"obj":"http://purl.obolibrary.org/obo/GO_0009056"},{"id":"T21750","span":{"begin":730,"end":733},"obj":"http://purl.obolibrary.org/obo/GO_0004704"},{"id":"T21749","span":{"begin":706,"end":709},"obj":"http://purl.obolibrary.org/obo/GO_0004704"},{"id":"T21748","span":{"begin":664,"end":667},"obj":"http://purl.obolibrary.org/obo/GO_0004704"},{"id":"T21747","span":{"begin":624,"end":627},"obj":"http://purl.obolibrary.org/obo/GO_0004704"},{"id":"T21746","span":{"begin":358,"end":361},"obj":"http://purl.obolibrary.org/obo/GO_0004704"},{"id":"T21745","span":{"begin":345,"end":348},"obj":"http://purl.obolibrary.org/obo/GO_0004704"},{"id":"T21744","span":{"begin":179,"end":182},"obj":"http://purl.obolibrary.org/obo/GO_0004704"},{"id":"T21743","span":{"begin":133,"end":136},"obj":"http://purl.obolibrary.org/obo/GO_0004704"},{"id":"T21742","span":{"begin":19,"end":29},"obj":"http://purl.obolibrary.org/obo/GO_0023052"}],"text":"Noncanonical NF-κB signalling. CD40 and RANK can activate the noncanonical NF-κB pathway that is dependent on NF-κB inducing kinase (NIK) expression levels. In unstimulated cells NIK forms a cytosolic complex with the ubiquitin ligases TRAF2, TRAF3 and cIAP1/2, which facilitates the K48-linked polyubiquitination and proteasomal degradation of NIK, keeping NIK levels low. Upon ligand binding, TRAF3 is recruited to the receptor, where TRAF2 directs nondegradative K63-linked polyubiquitination of cIAP1/2, resulting in their activation. Subsequently cIAP1/2 directs its K48-linked polyubiquitination to TRAF3, rather than NIK. As a result, TRAF3 is degraded and NIK is stabilised, resulting in increased NIK levels in the cell. NIK then phosphorylates and activates IKK1, which mediates NF-κB p100 phosphorylation. This is followed by K48-linked polyubiquitination and partial proteasomal degradation of p100 to p52, which forms a heterodimer with RelB to activate transcription. Next to TRAF3, TRAF1 has also been identified as a negative regulator of this pathway, most probably by competing with other TNF receptor-associated factors. cIAP, cellular inhibitor of apoptosis; IKK, IκB kinase; NF, nuclear factor; RANK, receptor activator of NF-κB; TRAF, TNF receptor-associated factor; TNF, tumour necrosis factor."}

{"project":"GO-MF","denotations":[{"id":"T21775","span":{"begin":1179,"end":1182},"obj":"http://purl.obolibrary.org/obo/GO_0008384"},{"id":"T21774","span":{"begin":386,"end":393},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T21773","span":{"begin":379,"end":385},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T21772","span":{"begin":218,"end":227},"obj":"http://purl.obolibrary.org/obo/GO_0031386"},{"id":"T21771","span":{"begin":730,"end":733},"obj":"http://purl.obolibrary.org/obo/GO_0004704"},{"id":"T21770","span":{"begin":706,"end":709},"obj":"http://purl.obolibrary.org/obo/GO_0004704"},{"id":"T21769","span":{"begin":664,"end":667},"obj":"http://purl.obolibrary.org/obo/GO_0004704"},{"id":"T21768","span":{"begin":624,"end":627},"obj":"http://purl.obolibrary.org/obo/GO_0004704"},{"id":"T21767","span":{"begin":358,"end":361},"obj":"http://purl.obolibrary.org/obo/GO_0004704"},{"id":"T21766","span":{"begin":345,"end":348},"obj":"http://purl.obolibrary.org/obo/GO_0004704"},{"id":"T21765","span":{"begin":179,"end":182},"obj":"http://purl.obolibrary.org/obo/GO_0004704"},{"id":"T21764","span":{"begin":133,"end":136},"obj":"http://purl.obolibrary.org/obo/GO_0004704"}],"text":"Noncanonical NF-κB signalling. CD40 and RANK can activate the noncanonical NF-κB pathway that is dependent on NF-κB inducing kinase (NIK) expression levels. In unstimulated cells NIK forms a cytosolic complex with the ubiquitin ligases TRAF2, TRAF3 and cIAP1/2, which facilitates the K48-linked polyubiquitination and proteasomal degradation of NIK, keeping NIK levels low. Upon ligand binding, TRAF3 is recruited to the receptor, where TRAF2 directs nondegradative K63-linked polyubiquitination of cIAP1/2, resulting in their activation. Subsequently cIAP1/2 directs its K48-linked polyubiquitination to TRAF3, rather than NIK. As a result, TRAF3 is degraded and NIK is stabilised, resulting in increased NIK levels in the cell. NIK then phosphorylates and activates IKK1, which mediates NF-κB p100 phosphorylation. This is followed by K48-linked polyubiquitination and partial proteasomal degradation of p100 to p52, which forms a heterodimer with RelB to activate transcription. Next to TRAF3, TRAF1 has also been identified as a negative regulator of this pathway, most probably by competing with other TNF receptor-associated factors. cIAP, cellular inhibitor of apoptosis; IKK, IκB kinase; NF, nuclear factor; RANK, receptor activator of NF-κB; TRAF, TNF receptor-associated factor; TNF, tumour necrosis factor."}

{"project":"GO-CC","denotations":[{"id":"T21779","span":{"begin":201,"end":235},"obj":"http://purl.obolibrary.org/obo/GO_0000153"},{"id":"T21778","span":{"begin":201,"end":235},"obj":"http://purl.obolibrary.org/obo/GO_0000151"},{"id":"T21777","span":{"begin":724,"end":728},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T21776","span":{"begin":173,"end":178},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T21785","span":{"begin":201,"end":235},"obj":"http://purl.obolibrary.org/obo/GO_0000836"},{"id":"T21784","span":{"begin":201,"end":235},"obj":"http://purl.obolibrary.org/obo/GO_0043494"},{"id":"T21783","span":{"begin":201,"end":235},"obj":"http://purl.obolibrary.org/obo/GO_0019005"},{"id":"T21782","span":{"begin":201,"end":235},"obj":"http://purl.obolibrary.org/obo/GO_0000152"},{"id":"T21781","span":{"begin":201,"end":235},"obj":"http://purl.obolibrary.org/obo/GO_0000837"},{"id":"T21780","span":{"begin":201,"end":235},"obj":"http://purl.obolibrary.org/obo/GO_0000835"}],"text":"Noncanonical NF-κB signalling. CD40 and RANK can activate the noncanonical NF-κB pathway that is dependent on NF-κB inducing kinase (NIK) expression levels. In unstimulated cells NIK forms a cytosolic complex with the ubiquitin ligases TRAF2, TRAF3 and cIAP1/2, which facilitates the K48-linked polyubiquitination and proteasomal degradation of NIK, keeping NIK levels low. Upon ligand binding, TRAF3 is recruited to the receptor, where TRAF2 directs nondegradative K63-linked polyubiquitination of cIAP1/2, resulting in their activation. Subsequently cIAP1/2 directs its K48-linked polyubiquitination to TRAF3, rather than NIK. As a result, TRAF3 is degraded and NIK is stabilised, resulting in increased NIK levels in the cell. NIK then phosphorylates and activates IKK1, which mediates NF-κB p100 phosphorylation. This is followed by K48-linked polyubiquitination and partial proteasomal degradation of p100 to p52, which forms a heterodimer with RelB to activate transcription. Next to TRAF3, TRAF1 has also been identified as a negative regulator of this pathway, most probably by competing with other TNF receptor-associated factors. cIAP, cellular inhibitor of apoptosis; IKK, IκB kinase; NF, nuclear factor; RANK, receptor activator of NF-κB; TRAF, TNF receptor-associated factor; TNF, tumour necrosis factor."}

{"project":"sentences","denotations":[{"id":"T21404","span":{"begin":374,"end":538},"obj":"Sentence"},{"id":"T21403","span":{"begin":157,"end":373},"obj":"Sentence"},{"id":"T21402","span":{"begin":31,"end":156},"obj":"Sentence"},{"id":"T21401","span":{"begin":0,"end":30},"obj":"Sentence"},{"id":"T21409","span":{"begin":982,"end":1317},"obj":"Sentence"},{"id":"T21408","span":{"begin":817,"end":981},"obj":"Sentence"},{"id":"T21407","span":{"begin":730,"end":816},"obj":"Sentence"},{"id":"T21406","span":{"begin":629,"end":729},"obj":"Sentence"},{"id":"T21405","span":{"begin":539,"end":628},"obj":"Sentence"},{"id":"T75","span":{"begin":31,"end":156},"obj":"Sentence"},{"id":"T76","span":{"begin":157,"end":373},"obj":"Sentence"},{"id":"T77","span":{"begin":374,"end":538},"obj":"Sentence"},{"id":"T78","span":{"begin":539,"end":628},"obj":"Sentence"},{"id":"T79","span":{"begin":629,"end":729},"obj":"Sentence"},{"id":"T80","span":{"begin":730,"end":816},"obj":"Sentence"},{"id":"T81","span":{"begin":817,"end":981},"obj":"Sentence"},{"id":"T82","span":{"begin":982,"end":1317},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Noncanonical NF-κB signalling. CD40 and RANK can activate the noncanonical NF-κB pathway that is dependent on NF-κB inducing kinase (NIK) expression levels. In unstimulated cells NIK forms a cytosolic complex with the ubiquitin ligases TRAF2, TRAF3 and cIAP1/2, which facilitates the K48-linked polyubiquitination and proteasomal degradation of NIK, keeping NIK levels low. Upon ligand binding, TRAF3 is recruited to the receptor, where TRAF2 directs nondegradative K63-linked polyubiquitination of cIAP1/2, resulting in their activation. Subsequently cIAP1/2 directs its K48-linked polyubiquitination to TRAF3, rather than NIK. As a result, TRAF3 is degraded and NIK is stabilised, resulting in increased NIK levels in the cell. NIK then phosphorylates and activates IKK1, which mediates NF-κB p100 phosphorylation. This is followed by K48-linked polyubiquitination and partial proteasomal degradation of p100 to p52, which forms a heterodimer with RelB to activate transcription. Next to TRAF3, TRAF1 has also been identified as a negative regulator of this pathway, most probably by competing with other TNF receptor-associated factors. cIAP, cellular inhibitor of apoptosis; IKK, IκB kinase; NF, nuclear factor; RANK, receptor activator of NF-κB; TRAF, TNF receptor-associated factor; TNF, tumour necrosis factor."}

{"project":"simple1","denotations":[{"id":"T21825","span":{"begin":236,"end":241},"obj":"Protein"},{"id":"T21824","span":{"begin":179,"end":182},"obj":"Protein"},{"id":"T21823","span":{"begin":133,"end":136},"obj":"Protein"},{"id":"T21822","span":{"begin":110,"end":131},"obj":"Protein"},{"id":"T21821","span":{"begin":40,"end":44},"obj":"Protein"},{"id":"T21820","span":{"begin":31,"end":35},"obj":"Protein"},{"id":"T21853","span":{"begin":1294,"end":1316},"obj":"Protein"},{"id":"T21852","span":{"begin":1289,"end":1292},"obj":"Protein"},{"id":"T21851","span":{"begin":1222,"end":1249},"obj":"Protein"},{"id":"T21850","span":{"begin":1216,"end":1220},"obj":"Protein"},{"id":"T21849","span":{"begin":997,"end":1002},"obj":"Protein"},{"id":"T21848","span":{"begin":990,"end":995},"obj":"Protein"},{"id":"T21847","span":{"begin":950,"end":954},"obj":"Protein"},{"id":"T21846","span":{"begin":914,"end":917},"obj":"Protein"},{"id":"T21845","span":{"begin":906,"end":910},"obj":"Protein"},{"id":"T21844","span":{"begin":795,"end":799},"obj":"Protein"},{"id":"T21843","span":{"begin":768,"end":772},"obj":"Protein"},{"id":"T21842","span":{"begin":730,"end":733},"obj":"Protein"},{"id":"T21841","span":{"begin":706,"end":709},"obj":"Protein"},{"id":"T21840","span":{"begin":664,"end":667},"obj":"Protein"},{"id":"T21839","span":{"begin":642,"end":647},"obj":"Protein"},{"id":"T21838","span":{"begin":624,"end":627},"obj":"Protein"},{"id":"T21837","span":{"begin":605,"end":610},"obj":"Protein"},{"id":"T21836","span":{"begin":558,"end":559},"obj":"Protein"},{"id":"T21835","span":{"begin":552,"end":557},"obj":"Protein"},{"id":"T21834","span":{"begin":505,"end":506},"obj":"Protein"},{"id":"T21833","span":{"begin":499,"end":504},"obj":"Protein"},{"id":"T21832","span":{"begin":437,"end":442},"obj":"Protein"},{"id":"T21831","span":{"begin":395,"end":400},"obj":"Protein"},{"id":"T21830","span":{"begin":358,"end":361},"obj":"Protein"},{"id":"T21829","span":{"begin":345,"end":348},"obj":"Protein"},{"id":"T21828","span":{"begin":259,"end":260},"obj":"Protein"},{"id":"T21827","span":{"begin":253,"end":258},"obj":"Protein"},{"id":"T21826","span":{"begin":243,"end":248},"obj":"Protein"}],"text":"Noncanonical NF-κB signalling. CD40 and RANK can activate the noncanonical NF-κB pathway that is dependent on NF-κB inducing kinase (NIK) expression levels. In unstimulated cells NIK forms a cytosolic complex with the ubiquitin ligases TRAF2, TRAF3 and cIAP1/2, which facilitates the K48-linked polyubiquitination and proteasomal degradation of NIK, keeping NIK levels low. Upon ligand binding, TRAF3 is recruited to the receptor, where TRAF2 directs nondegradative K63-linked polyubiquitination of cIAP1/2, resulting in their activation. Subsequently cIAP1/2 directs its K48-linked polyubiquitination to TRAF3, rather than NIK. As a result, TRAF3 is degraded and NIK is stabilised, resulting in increased NIK levels in the cell. NIK then phosphorylates and activates IKK1, which mediates NF-κB p100 phosphorylation. This is followed by K48-linked polyubiquitination and partial proteasomal degradation of p100 to p52, which forms a heterodimer with RelB to activate transcription. Next to TRAF3, TRAF1 has also been identified as a negative regulator of this pathway, most probably by competing with other TNF receptor-associated factors. cIAP, cellular inhibitor of apoptosis; IKK, IκB kinase; NF, nuclear factor; RANK, receptor activator of NF-κB; TRAF, TNF receptor-associated factor; TNF, tumour necrosis factor."}

{"project":"BioNLP16_DUT","denotations":[{"id":"T22376","span":{"begin":253,"end":258},"obj":"Protein"},{"id":"T22375","span":{"begin":243,"end":248},"obj":"Protein"},{"id":"T22374","span":{"begin":236,"end":241},"obj":"Protein"},{"id":"T22373","span":{"begin":179,"end":182},"obj":"Protein"},{"id":"T22372","span":{"begin":358,"end":361},"obj":"Protein"},{"id":"T22371","span":{"begin":345,"end":348},"obj":"Protein"},{"id":"T22370","span":{"begin":133,"end":136},"obj":"Protein"},{"id":"T22369","span":{"begin":110,"end":131},"obj":"Protein"},{"id":"T22368","span":{"begin":40,"end":44},"obj":"Protein"},{"id":"T22367","span":{"begin":31,"end":35},"obj":"Protein"},{"id":"T22418","span":{"begin":891,"end":902},"obj":"Protein_catabolism"},{"id":"T22417","span":{"begin":800,"end":815},"obj":"Phosphorylation"},{"id":"T22416","span":{"begin":758,"end":767},"obj":"Positive_regulation"},{"id":"T22415","span":{"begin":739,"end":753},"obj":"Phosphorylation"},{"id":"T22414","span":{"begin":780,"end":788},"obj":"Positive_regulation"},{"id":"T22413","span":{"begin":683,"end":692},"obj":"Positive_regulation"},{"id":"T22412","span":{"begin":634,"end":640},"obj":"Positive_regulation"},{"id":"T22411","span":{"begin":651,"end":659},"obj":"Protein_catabolism"},{"id":"T22410","span":{"begin":696,"end":705},"obj":"Positive_regulation"},{"id":"T22409","span":{"begin":671,"end":681},"obj":"Positive_regulation"},{"id":"T22408","span":{"begin":583,"end":601},"obj":"Binding"},{"id":"T22407","span":{"begin":404,"end":413},"obj":"Binding"},{"id":"T22406","span":{"begin":477,"end":495},"obj":"Binding"},{"id":"T22405","span":{"begin":295,"end":313},"obj":"Binding"},{"id":"T22404","span":{"begin":330,"end":341},"obj":"Protein_catabolism"},{"id":"T22403","span":{"begin":268,"end":279},"obj":"Positive_regulation"},{"id":"T22402","span":{"begin":97,"end":106},"obj":"Regulation"},{"id":"T22401","span":{"begin":138,"end":148},"obj":"Gene_expression"},{"id":"T22400","span":{"begin":1294,"end":1316},"obj":"Protein"},{"id":"T22399","span":{"begin":1289,"end":1292},"obj":"Protein"},{"id":"T22398","span":{"begin":1222,"end":1249},"obj":"Protein"},{"id":"T22397","span":{"begin":1216,"end":1220},"obj":"Protein"},{"id":"T22396","span":{"begin":997,"end":1002},"obj":"Protein"},{"id":"T22395","span":{"begin":990,"end":995},"obj":"Protein"},{"id":"T22394","span":{"begin":950,"end":954},"obj":"Protein"},{"id":"T22393","span":{"begin":914,"end":917},"obj":"Protein"},{"id":"T22392","span":{"begin":906,"end":910},"obj":"Protein"},{"id":"T22391","span":{"begin":795,"end":799},"obj":"Protein"},{"id":"T22390","span":{"begin":768,"end":772},"obj":"Protein"},{"id":"T22389","span":{"begin":730,"end":733},"obj":"Protein"},{"id":"T22388","span":{"begin":706,"end":709},"obj":"Protein"},{"id":"T22387","span":{"begin":664,"end":667},"obj":"Protein"},{"id":"T22386","span":{"begin":642,"end":647},"obj":"Protein"},{"id":"T22385","span":{"begin":624,"end":627},"obj":"Protein"},{"id":"T22384","span":{"begin":605,"end":610},"obj":"Protein"},{"id":"T22383","span":{"begin":558,"end":559},"obj":"Protein"},{"id":"T22382","span":{"begin":552,"end":557},"obj":"Protein"},{"id":"T22381","span":{"begin":505,"end":506},"obj":"Protein"},{"id":"T22380","span":{"begin":499,"end":504},"obj":"Protein"},{"id":"T22379","span":{"begin":437,"end":442},"obj":"Protein"},{"id":"T22378","span":{"begin":395,"end":400},"obj":"Protein"},{"id":"T22377","span":{"begin":259,"end":260},"obj":"Protein"}],"relations":[{"id":"R14569","pred":"themeOf","subj":"T22369","obj":"T22402"},{"id":"R14570","pred":"themeOf","subj":"T22369","obj":"T22401"},{"id":"R14571","pred":"themeOf","subj":"T22370","obj":"T22401"},{"id":"R14572","pred":"themeOf","subj":"T22371","obj":"T22405"},{"id":"R14573","pred":"themeOf","subj":"T22371","obj":"T22404"},{"id":"R14575","pred":"themeOf","subj":"T22380","obj":"T22406"},{"id":"R14591","pred":"themeOf","subj":"T22404","obj":"T22403"},{"id":"R14592","pred":"themeOf","subj":"T22405","obj":"T22403"},{"id":"R14574","pred":"themeOf","subj":"T22378","obj":"T22407"},{"id":"R14576","pred":"themeOf","subj":"T22381","obj":"T22406"},{"id":"R14577","pred":"themeOf","subj":"T22382","obj":"T22408"},{"id":"R14578","pred":"themeOf","subj":"T22384","obj":"T22408"},{"id":"R14579","pred":"themeOf","subj":"T22385","obj":"T22408"},{"id":"R14580","pred":"themeOf","subj":"T22386","obj":"T22411"},{"id":"R14581","pred":"themeOf","subj":"T22387","obj":"T22409"},{"id":"R14582","pred":"themeOf","subj":"T22388","obj":"T22413"},{"id":"R14583","pred":"themeOf","subj":"T22388","obj":"T22410"},{"id":"R14584","pred":"themeOf","subj":"T22389","obj":"T22415"},{"id":"R14585","pred":"causeOf","subj":"T22389","obj":"T22416"},{"id":"R14586","pred":"themeOf","subj":"T22390","obj":"T22415"},{"id":"R14587","pred":"themeOf","subj":"T22390","obj":"T22416"},{"id":"R14588","pred":"themeOf","subj":"T22391","obj":"T22417"},{"id":"R14589","pred":"themeOf","subj":"T22392","obj":"T22418"},{"id":"R14590","pred":"themeOf","subj":"T22393","obj":"T22418"},{"id":"R14593","pred":"themeOf","subj":"T22411","obj":"T22412"},{"id":"R14594","pred":"themeOf","subj":"T22417","obj":"T22414"}],"text":"Noncanonical NF-κB signalling. CD40 and RANK can activate the noncanonical NF-κB pathway that is dependent on NF-κB inducing kinase (NIK) expression levels. In unstimulated cells NIK forms a cytosolic complex with the ubiquitin ligases TRAF2, TRAF3 and cIAP1/2, which facilitates the K48-linked polyubiquitination and proteasomal degradation of NIK, keeping NIK levels low. Upon ligand binding, TRAF3 is recruited to the receptor, where TRAF2 directs nondegradative K63-linked polyubiquitination of cIAP1/2, resulting in their activation. Subsequently cIAP1/2 directs its K48-linked polyubiquitination to TRAF3, rather than NIK. As a result, TRAF3 is degraded and NIK is stabilised, resulting in increased NIK levels in the cell. NIK then phosphorylates and activates IKK1, which mediates NF-κB p100 phosphorylation. This is followed by K48-linked polyubiquitination and partial proteasomal degradation of p100 to p52, which forms a heterodimer with RelB to activate transcription. Next to TRAF3, TRAF1 has also been identified as a negative regulator of this pathway, most probably by competing with other TNF receptor-associated factors. cIAP, cellular inhibitor of apoptosis; IKK, IκB kinase; NF, nuclear factor; RANK, receptor activator of NF-κB; TRAF, TNF receptor-associated factor; TNF, tumour necrosis factor."}

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CD40 and RANK can activate the noncanonical NF-κB pathway that is dependent on NF-κB inducing kinase (NIK) expression levels. In unstimulated cells NIK forms a cytosolic complex with the ubiquitin ligases TRAF2, TRAF3 and cIAP1/2, which facilitates the K48-linked polyubiquitination and proteasomal degradation of NIK, keeping NIK levels low. Upon ligand binding, TRAF3 is recruited to the receptor, where TRAF2 directs nondegradative K63-linked polyubiquitination of cIAP1/2, resulting in their activation. Subsequently cIAP1/2 directs its K48-linked polyubiquitination to TRAF3, rather than NIK. As a result, TRAF3 is degraded and NIK is stabilised, resulting in increased NIK levels in the cell. NIK then phosphorylates and activates IKK1, which mediates NF-κB p100 phosphorylation. This is followed by K48-linked polyubiquitination and partial proteasomal degradation of p100 to p52, which forms a heterodimer with RelB to activate transcription. Next to TRAF3, TRAF1 has also been identified as a negative regulator of this pathway, most probably by competing with other TNF receptor-associated factors. cIAP, cellular inhibitor of apoptosis; IKK, IκB kinase; NF, nuclear factor; RANK, receptor activator of NF-κB; TRAF, TNF receptor-associated factor; TNF, tumour necrosis factor."}

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CD40 and RANK can activate the noncanonical NF-κB pathway that is dependent on NF-κB inducing kinase (NIK) expression levels. In unstimulated cells NIK forms a cytosolic complex with the ubiquitin ligases TRAF2, TRAF3 and cIAP1/2, which facilitates the K48-linked polyubiquitination and proteasomal degradation of NIK, keeping NIK levels low. Upon ligand binding, TRAF3 is recruited to the receptor, where TRAF2 directs nondegradative K63-linked polyubiquitination of cIAP1/2, resulting in their activation. Subsequently cIAP1/2 directs its K48-linked polyubiquitination to TRAF3, rather than NIK. As a result, TRAF3 is degraded and NIK is stabilised, resulting in increased NIK levels in the cell. NIK then phosphorylates and activates IKK1, which mediates NF-κB p100 phosphorylation. This is followed by K48-linked polyubiquitination and partial proteasomal degradation of p100 to p52, which forms a heterodimer with RelB to activate transcription. Next to TRAF3, TRAF1 has also been identified as a negative regulator of this pathway, most probably by competing with other TNF receptor-associated factors. cIAP, cellular inhibitor of apoptosis; IKK, IκB kinase; NF, nuclear factor; RANK, receptor activator of NF-κB; TRAF, TNF receptor-associated factor; TNF, tumour necrosis factor."}

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CD40 and RANK can activate the noncanonical NF-κB pathway that is dependent on NF-κB inducing kinase (NIK) expression levels. In unstimulated cells NIK forms a cytosolic complex with the ubiquitin ligases TRAF2, TRAF3 and cIAP1/2, which facilitates the K48-linked polyubiquitination and proteasomal degradation of NIK, keeping NIK levels low. Upon ligand binding, TRAF3 is recruited to the receptor, where TRAF2 directs nondegradative K63-linked polyubiquitination of cIAP1/2, resulting in their activation. Subsequently cIAP1/2 directs its K48-linked polyubiquitination to TRAF3, rather than NIK. As a result, TRAF3 is degraded and NIK is stabilised, resulting in increased NIK levels in the cell. NIK then phosphorylates and activates IKK1, which mediates NF-κB p100 phosphorylation. This is followed by K48-linked polyubiquitination and partial proteasomal degradation of p100 to p52, which forms a heterodimer with RelB to activate transcription. Next to TRAF3, TRAF1 has also been identified as a negative regulator of this pathway, most probably by competing with other TNF receptor-associated factors. cIAP, cellular inhibitor of apoptosis; IKK, IκB kinase; NF, nuclear factor; RANK, receptor activator of NF-κB; TRAF, TNF receptor-associated factor; TNF, tumour necrosis factor."}

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NF-κB signalling. CD40 and RANK can activate the noncanonical NF-κB pathway that is dependent on NF-κB inducing kinase (NIK) expression levels. In unstimulated cells NIK forms a cytosolic complex with the ubiquitin ligases TRAF2, TRAF3 and cIAP1/2, which facilitates the K48-linked polyubiquitination and proteasomal degradation of NIK, keeping NIK levels low. Upon ligand binding, TRAF3 is recruited to the receptor, where TRAF2 directs nondegradative K63-linked polyubiquitination of cIAP1/2, resulting in their activation. Subsequently cIAP1/2 directs its K48-linked polyubiquitination to TRAF3, rather than NIK. As a result, TRAF3 is degraded and NIK is stabilised, resulting in increased NIK levels in the cell. NIK then phosphorylates and activates IKK1, which mediates NF-κB p100 phosphorylation. This is followed by K48-linked polyubiquitination and partial proteasomal degradation of p100 to p52, which forms a heterodimer with RelB to activate transcription. Next to TRAF3, TRAF1 has also been identified as a negative regulator of this pathway, most probably by competing with other TNF receptor-associated factors. cIAP, cellular inhibitor of apoptosis; IKK, IκB kinase; NF, nuclear factor; RANK, receptor activator of NF-κB; TRAF, TNF receptor-associated factor; TNF, tumour necrosis factor."}