NEK7 is a small (302-residue) NIMA-related serine/threonine protein kinase consisting of little more than a catalytic domain, and the closest paralogue of NEK6. It has two separable roles. As a kinase it acts in the mitotic NEK9-NEK6/NEK7 cascade: NEK7 is held inactive in interphase by a Tyr-97 'Tyr-down' autoinhibitory conformation, and binding of the NEK9 C-terminal domain relieves that autoinhibition and promotes trans-autophosphorylation of the activation loop, so NEK7 activity rises in mitosis. Active NEK7 is concentrated at the centrosome and spindle poles, is required for gamma-tubulin recruitment and centrosomal microtubule nucleation, for bipolar spindle assembly and for completion of cytokinesis, and phosphorylates the microtubule-associated protein EML4 at Ser144/Ser146 to release it from spindle microtubules during chromosome congression. Loss of NEK7 in mouse causes late embryonic or perinatal lethality with chromosome lagging, cytokinesis failure and polyploidy. Separately, and without requiring catalytic activity, NEK7 binds the leucine-rich repeat domain of the innate-immune sensor NLRP3 and licenses inflammasome assembly: it opens the autoinhibited NLRP3 cage at the microtubule-organizing centre and is a stoichiometric structural subunit of the active NLRP3 disc, in which ten NEK7 molecules bridge adjacent NLRP3 subunits, permitting PYCARD/ASC recruitment and caspase-1 activation. Because the NEK9- and NLRP3-binding surfaces on NEK7 overlap and cellular NEK7 is limiting, mitosis and NLRP3 inflammasome activation are mutually exclusive. NEK7 is also reported to shuttle to the nucleus, a distribution modulated by ANKS3 binding.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000922 spindle pole | IEA GO_REF:0000044 | ACCEPT | Summary: Spindle pole localisation of NEK7, mapped electronically from the UniProt subcellular-location vocabulary. Reason: Independent experimental work places NEK7 at spindle poles in mitotic human cells, so the electronic mapping is correct even though it was not itself derived from an experiment. Supporting Evidence: PMID:19414596 while both kinases localize to spindle poles, only Nek6 obviously localizes to spindle microtubules PMID:17101132 We show here that the endogenous Nek7 protein is enriched at the centrosome in a microtubule-independent manner. |
| GO:0004672 protein kinase activity | IEA GO_REF:0000002 | ACCEPT | Summary: Generic protein kinase activity from InterPro domain mapping (protein kinase and serine/threonine kinase signatures). Reason: NEK7 is a bona fide protein kinase; the InterPro-derived term is a correct parent of the experimentally supported serine/threonine specificity, and an IEA being broader than the experimental annotation is acceptable. Supporting Evidence: PMID:19941817 bacterially expressed and purified kinases were incubated with 2 ΞΌCi 33P ATP in 38 ΞΌM ATP for 50 min at 30Β°C using Ξ²-casein as substrate PMID:26522158 In this study we elucidated the structural basis of the Nek7βNek9 interaction, which occurs at an unexpected site on the C-lobe of Nek7, and discovered that dimeric Nek9 stimulates Nek7 autophosphorylation. |
| GO:0004674 protein serine/threonine kinase activity | IBA GO_REF:0000033 | ACCEPT | Summary: Protein serine/threonine kinase activity inferred from the NEK/NIMA phylogenetic node (PANTHER:PTN001981567). Reason: The IBD node placement is sound: NEK7 is a catalytically active Ser/Thr kinase in direct assays, and the whole NIMA/NEK family shares this activity, so descent-based inheritance of the term is appropriate. NEK7's own appearance among the WITH/FROM sources reflects its experimental grounding and is expected. Supporting Evidence: PMID:19941817 bacterially expressed and purified kinases were incubated with 2 ΞΌCi 33P ATP in 38 ΞΌM ATP for 50 min at 30Β°C using Ξ²-casein as substrate PMID:26522158 In this study we elucidated the structural basis of the Nek7βNek9 interaction, which occurs at an unexpected site on the C-lobe of Nek7, and discovered that dimeric Nek9 stimulates Nek7 autophosphorylation. PMID:31409757 The mitotic kinases NEK6 and NEK7 phosphorylated the EML4 N-terminal domain at Ser144 and Ser146 in vitro, and depletion of these kinases in cells led to increased EML4 binding to microtubules in mitosis. |
| GO:0004674 protein serine/threonine kinase activity | IDA PMID:19941817 An autoinhibitory tyrosine motif in the cell-cycle-regulated... | ACCEPT | Summary: Direct kinase assay: purified NEK7 phosphorylates beta-casein, and activity is modulated by the Tyr-97 autoinhibitory motif and NEK9 binding. Reason: The paper measures NEK7 catalytic activity directly in vitro with a protein substrate and dissects its regulation, which is exactly what the term asserts. This is a core molecular function of NEK7. Supporting Evidence: PMID:19941817 bacterially expressed and purified kinases were incubated with 2 ΞΌCi 33P ATP in 38 ΞΌM ATP for 50 min at 30Β°C using Ξ²-casein as substrate PMID:19941817 Strikingly, Nek9-CTD did not significantly increase the activity of Nek7-Y97A, suggesting that the mechanism of Nek7 activation occurs through release of Tyr97 autoinhibition. PMID:19941817 From this we conclude that Tyr-down autoinhibition restricts the activity of Nek6 and Nek7 in interphase but is completely released in mitosis. |
| GO:0004674 protein serine/threonine kinase activity | IDA PMID:26522158 Mechanistic basis of Nek7 activation through Nek9 binding an... | ACCEPT | Summary: Direct demonstration of NEK7 catalytic activity and of NEK9-induced dimerisation driving NEK7 activation-loop autophosphorylation. Reason: Structural and enzymatic analysis of activated NEK7 supports the serine/threonine kinase assignment directly; NEK7 is the kinase being assayed. Supporting Evidence: PMID:26522158 In this study we elucidated the structural basis of the Nek7βNek9 interaction, which occurs at an unexpected site on the C-lobe of Nek7, and discovered that dimeric Nek9 stimulates Nek7 autophosphorylation. PMID:26522158 Autophosphorylation most likely occurs in trans between, not within, Nek7 back-to-back dimers. |
| GO:0005515 protein binding | IPI PMID:26188091 Anks3 alters the sub-cellular localization of the Nek7 kinas... | REMOVE | Summary: IPI annotation for the NEK7-ANKS3 interaction (Q6ZW76), annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. The cited study shows that ANKS3 binding retains NEK7 in the cytoplasm and that ANKS3 is modified in a NEK7-dependent but kinase-independent manner; neither observation yields a specific molecular-function term for NEK7, and the localisation consequence is a cellular-component rather than a molecular-function claim. Supporting Evidence: PMID:26188091 we show that Anks3, but not Anks6 interacted with the NIMA-related kinase Nek7 PMID:26188091 Importantly, Anks3 retained Nek7 in the cytoplasm, suggesting that, Nek7 triggers the modification of Anks3, which in turn prevents the nuclear localization of Nek7. |
| GO:0005515 protein binding | IPI PMID:26814970 NEK7 is an essential mediator of NLRP3 activation downstream... | MODIFY | Summary: IPI annotation recording the direct NEK7-NLRP3 interaction, mapped by IntAct to the generic protein binding term. Reason: The cited paper does not merely report an interaction: it shows that NEK7 binds the NLRP3 leucine-rich repeat domain and is required, downstream of potassium efflux, for NLRP3-ASC complex formation and caspase-1 activation, and that NEK7 catalytic activity is dispensable for this. That is a non-catalytic activator function, so the uninformative protein binding term should be replaced by GO:0140677 molecular function activator activity (with NLRP3 as input), which is already the term UniProt uses for the same biology from the structural papers. Proposed replacements: molecular function activator activity Supporting Evidence: PMID:26814970 We have shown that Nek7 is an essential factor that specifically and non-redundantly functions downstream of potassium efflux to regulate the activation of the NLRP3 inflammasome. PMID:26814970 Nek7 interacted with WT or mutant NLRP3 lacking the N-terminal Pyrin domain, but not NLRP3 with deletion of the C-terminal leucine-rich repeats (LRRs) PMID:26814970 In contrast, the catalytic activity of Nek7 is not required for NLRP3 activation. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:Q96D03 reported by the HuRI all-by-all binary yeast two-hybrid reference interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32296183 Here we present a human 'all-by-all' reference interactome map of human binary protein interactions, or 'HuRI'. |
| GO:0005515 protein binding | IPI PMID:32707033 Kinase Interaction Network Expands Functional and Disease Ro... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:P00558 reported by an affinity-purification kinase-interaction network study, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32707033 The experiment validated these interactions at NEK7 endogenous expression levels |
| GO:0005515 protein binding | IPI PMID:32707033 Kinase Interaction Network Expands Functional and Disease Ro... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:P42166 reported by an affinity-purification kinase-interaction network study, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32707033 The experiment validated these interactions at NEK7 endogenous expression levels |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:A0JP07 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:A2RUH7 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:F6Y2X3 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:O00214-2 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:O14829 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:O75175 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:O75317 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:O75874 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:O94983-5 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:P07437 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:P09382 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:P09471 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:P14060 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:P16422 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:P26715 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:P36382 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:P43356 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:P43686 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:P48775 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:P49184 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:P49746 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:P50749 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:P52756 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:P61224 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:P79483 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:Q02978 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:Q10981 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:Q13200 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:Q13428-5 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:Q13636 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:Q3SY56 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:Q68CL5-3 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:Q6P4D5-2 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:Q6P5S2 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:Q6UXH1-2 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:Q7Z434 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:Q7Z698 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:Q7Z6Z7-2 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:Q7Z780 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:Q8IY82 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:Q8N1W1-4 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:Q8N2W9 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:Q8N323 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:Q8NBT0 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:Q8NCF5-2 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:Q8NCR3 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:Q8TAB5 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:Q8TB02 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:Q96E17 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:Q96EF9 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:Q96EY8 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:Q96GK7 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:Q96I25 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:Q96JJ7-2 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:Q96L03 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Yeast two-hybrid interaction between NEK7 and NLRP3 (UniProtKB:Q96P20) from a large-scale screen, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. In this case the NLRP3 interaction is independently and far better characterised, and is already asserted as a non-catalytic activator function and as positive regulation of NLRP3 inflammasome complex assembly in other rows. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening PMID:26814970 Nek7 interacted with WT or mutant NLRP3 lacking the N-terminal Pyrin domain, but not NLRP3 with deletion of the C-terminal leucine-rich repeats (LRRs) |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:Q96QH2 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:Q99944 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:Q9BQ29 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:Q9BT49 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:Q9H2S6-2 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Yeast two-hybrid interaction between NEK7 and NEK9 (UniProtKB:Q9HC98-4) from a large-scale screen, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. The NEK9-NEK7 interaction is functionally important - NEK9 binding relieves Tyr-97 autoinhibition and stimulates NEK7 autophosphorylation - but in that relationship NEK7 is the regulated kinase, not the regulator, so the biology is already carried by the kinase-activity annotations rather than by a binding term on NEK7. Supporting Evidence: PMID:19941817 Strikingly, Nek9-CTD did not significantly increase the activity of Nek7-Y97A, suggesting that the mechanism of Nek7 activation occurs through release of Tyr97 autoinhibition. PMID:26522158 In this study we elucidated the structural basis of the Nek7βNek9 interaction, which occurs at an unexpected site on the C-lobe of Nek7, and discovered that dimeric Nek9 stimulates Nek7 autophosphorylation. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:Q9NPC7 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:Q9NVM1 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:Q9NX07 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:Q9ULR0 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:Q9ULW0 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:Q9Y3Y4 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Binary interaction between NEK7 and UniProtKB:Q9Y617 reported by systematic yeast two-hybrid screen of a neurodegenerative-disease-focused interactome, annotated to generic protein binding. Reason: GO:0005515 protein binding carries no functional information: it does not say what NEK7 does with the partner, in which direction the regulation runs, or in what process. Removing it does not question the reported interaction, and no informative molecular-function term can be derived from a binary interaction measurement alone. NEK7's functionally characterised interactions (NEK9, NLRP3) are captured by specific terms elsewhere in this review. Supporting Evidence: PMID:32814053 an interactome map that focuses on neurodegenerative disease (ND), connects βΌ5,000 human proteins via βΌ30,000 candidate interactions and is generated by systematic yeast two-hybrid interaction screening |
| GO:0005524 ATP binding | IEA GO_REF:0000002 | ACCEPT | Summary: ATP binding inferred electronically from the protein-kinase ATP-binding-site InterPro signatures. Reason: NEK7 is an ATP-dependent protein kinase with a canonical catalytic domain whose activity has been measured with radiolabelled ATP, so ATP binding is correct. Supporting Evidence: PMID:19941817 bacterially expressed and purified kinases were incubated with 2 ΞΌCi 33P ATP in 38 ΞΌM ATP for 50 min at 30Β°C using Ξ²-casein as substrate |
| GO:0005634 nucleus | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Nuclear localisation (is_active_in) inferred from the phylogenetic node PANTHER:PTN002878636. Reason: A nuclear pool of NEK7 is supported indirectly: ANKS3 binding is reported to prevent NEK7 nuclear localisation, which presupposes that NEK7 can enter the nucleus. This is a peripheral distribution rather than a site where NEK7's characterised functions occur - the kinase acts at the centrosome and spindle poles, and the inflammasome-licensing role occurs at the cytoplasmic microtubule-organizing centre - and no nuclear substrate or nuclear process has been identified. Keeping the annotation but flagging it as non-core reflects that evidence state. Supporting Evidence: PMID:26188091 Importantly, Anks3 retained Nek7 in the cytoplasm, suggesting that, Nek7 triggers the modification of Anks3, which in turn prevents the nuclear localization of Nek7. |
| GO:0005634 nucleus | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: Nuclear localisation transferred electronically from the mouse orthologue Nek7 (Q9ES74) and the UniProt subcellular-location vocabulary. Reason: A nuclear pool of NEK7 is supported indirectly: ANKS3 binding is reported to prevent NEK7 nuclear localisation, which presupposes that NEK7 can enter the nucleus. This is a peripheral distribution rather than a site where NEK7's characterised functions occur - the kinase acts at the centrosome and spindle poles, and the inflammasome-licensing role occurs at the cytoplasmic microtubule-organizing centre - and no nuclear substrate or nuclear process has been identified. Keeping the annotation but flagging it as non-core reflects that evidence state. Supporting Evidence: PMID:26188091 Importantly, Anks3 retained Nek7 in the cytoplasm, suggesting that, Nek7 triggers the modification of Anks3, which in turn prevents the nuclear localization of Nek7. |
| GO:0005634 nucleus | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Nuclear localisation transferred by curator judgement of sequence similarity from mouse Nek7 (Q9ES74). Reason: A nuclear pool of NEK7 is supported indirectly: ANKS3 binding is reported to prevent NEK7 nuclear localisation, which presupposes that NEK7 can enter the nucleus. This is a peripheral distribution rather than a site where NEK7's characterised functions occur - the kinase acts at the centrosome and spindle poles, and the inflammasome-licensing role occurs at the cytoplasmic microtubule-organizing centre - and no nuclear substrate or nuclear process has been identified. Keeping the annotation but flagging it as non-core reflects that evidence state. Supporting Evidence: PMID:26188091 Importantly, Anks3 retained Nek7 in the cytoplasm, suggesting that, Nek7 triggers the modification of Anks3, which in turn prevents the nuclear localization of Nek7. |
| GO:0005654 nucleoplasm | IDA GO_REF:0000052 | KEEP AS NON CORE | Summary: Nucleoplasm localisation from curated immunofluorescence imaging. Reason: Imaging-based nucleoplasmic staining is consistent with the reported nuclear pool of NEK7, but no nuclear function has been defined; NEK7's characterised activities are centrosomal/cytoplasmic. Retain as a non-core location. Supporting Evidence: PMID:26188091 Importantly, Anks3 retained Nek7 in the cytoplasm, suggesting that, Nek7 triggers the modification of Anks3, which in turn prevents the nuclear localization of Nek7. |
| GO:0005737 cytoplasm | EXP PMID:17586473 NEK7 is a centrosomal kinase critical for microtubule nuclea... | ACCEPT | Summary: Cytoplasmic localisation of NEK7 from direct experimental observation in human cells. Reason: NEK7 is a cytoplasmic protein concentrated at the centrosome throughout the cell cycle and at the midbody in late mitosis; cytoplasm is correct though general. Supporting Evidence: PMID:17586473 NEK7 was located at the centrosome throughout the cell cycle. PMID:17101132 We show here that the endogenous Nek7 protein is enriched at the centrosome in a microtubule-independent manner. |
| GO:0005737 cytoplasm | IEA GO_REF:0000120 | ACCEPT | Summary: Cytoplasmic localisation transferred electronically from mouse Nek7 and the UniProt subcellular-location vocabulary. Reason: Consistent with direct human data placing NEK7 in the cytoplasm at centrosomes and midbody. Supporting Evidence: PMID:17586473 NEK7 was located at the centrosome throughout the cell cycle. PMID:17586473 Temporal localization of NEK7 at midbody of the cytokinetic cell was also observed. |
| GO:0005737 cytoplasm | ISS GO_REF:0000024 | ACCEPT | Summary: Cytoplasmic localisation transferred by curator sequence-similarity judgement from mouse Nek7. Reason: Consistent with the direct human experimental evidence for cytoplasmic/centrosomal NEK7. Supporting Evidence: PMID:17586473 NEK7 was located at the centrosome throughout the cell cycle. |
| GO:0005813 centrosome | IEA GO_REF:0000044 | ACCEPT | Summary: Centrosome localisation mapped from the UniProt subcellular-location vocabulary. Reason: Endogenous NEK7 is enriched at the centrosome in a microtubule-independent manner in interphase and mitosis, so this is directly supported. Supporting Evidence: PMID:17101132 We show here that the endogenous Nek7 protein is enriched at the centrosome in a microtubule-independent manner. PMID:17727698 Importantly, Nek7 has been reported to localise to the centrosome in both interphase and mitotic U2OS and HeLa cells |
| GO:0005815 microtubule organizing center | IDA PMID:17586473 NEK7 is a centrosomal kinase critical for microtubule nuclea... | ACCEPT | Summary: NEK7 is active at the microtubule organizing center (IDA), where its depletion reduces centrosomal gamma-tubulin and microtubule regrowth. Reason: This is the site at which both of NEK7's characterised roles are executed: centrosomal microtubule nucleation in mitosis, and opening of the NLRP3 cage at the MTOC during inflammasome licensing. A core location. Supporting Evidence: PMID:17586473 NEK7 was located at the centrosome throughout the cell cycle. PMID:17586473 we observed a decrease in the centrosomal gamma-tubulin levels and reduction of the microtubule re-growth activity in the NEK7-suppressed cells PMID:36442502 its interaction with NEK7 at the MTOC disrupts the cage to allow formation of the active NLRP3 disc |
| GO:0006468 protein phosphorylation | IDA PMID:12840024 A mitotic cascade of NIMA family kinases. Nercc1/Nek9 activa... | ACCEPT | Summary: Protein phosphorylation (IDA) from the study defining the NEK9-NEK6/NEK7 mitotic kinase cascade. Reason: NEK7 is shown to be an activatable protein kinase in this work, so involvement in protein phosphorylation is correct; it is a general term, but accurate, and the specific substrate relationship is captured by later work on EML4. Supporting Evidence: PMID:12840024 Nercc1 activates Nek7 in vitro in a similar manner PMID:31409757 The mitotic kinases NEK6 and NEK7 phosphorylated the EML4 N-terminal domain at Ser144 and Ser146 in vitro, and depletion of these kinases in cells led to increased EML4 binding to microtubules in mitosis. |
| GO:0006468 protein phosphorylation | IDA PMID:31409757 Mitotic phosphorylation by NEK6 and NEK7 reduces the microtu... | ACCEPT | Summary: Protein phosphorylation (IDA) from the identification of EML4 Ser144/Ser146 as NEK6/NEK7 sites. Reason: Direct in vitro phosphorylation of a defined physiological substrate at mapped residues; NEK7 performs the catalytic step. Supporting Evidence: PMID:31409757 The mitotic kinases NEK6 and NEK7 phosphorylated the EML4 N-terminal domain at Ser144 and Ser146 in vitro, and depletion of these kinases in cells led to increased EML4 binding to microtubules in mitosis. PMID:31409757 NEK6- and NEK7-dependent phosphorylation promotes the dissociation of EML4 from microtubules in mitosis in a manner that is required for efficient chromosome congression |
| GO:0007346 regulation of mitotic cell cycle | IDA PMID:19941817 An autoinhibitory tyrosine motif in the cell-cycle-regulated... | ACCEPT | Summary: Regulation of the mitotic cell cycle (IDA), from the work showing that NEK7 activity is autoinhibited in interphase and released in mitosis. Reason: NEK7 activity is cell-cycle regulated and interfering with it arrests cells in mitosis, so NEK7 does act in mitotic progression. The term is general; the more specific spindle-assembly and chromosome-congression claims are carried by other rows in this review. Supporting Evidence: PMID:19941817 From this we conclude that Tyr-down autoinhibition restricts the activity of Nek6 and Nek7 in interphase but is completely released in mitosis. PMID:19414596 both Nek6 and Nek7 are activated in mitosis and that interfering with their activity by either depletion or expression of reduced-activity mutants leads to mitotic arrest and apoptosis |
| GO:0007346 regulation of mitotic cell cycle | TAS PMID:17727698 Mitotic regulation by NIMA-related kinases. | ACCEPT | Summary: Regulation of the mitotic cell cycle asserted by a review of NIMA-related kinases (TAS). Reason: The review accurately summarises the primary literature placing NEK7 in mitotic spindle organisation downstream of NEK9. A traceable author statement of a well-supported general claim. Supporting Evidence: PMID:17727698 it seems likely that these kinases exert their effects through organisation of the mitotic spindle PMID:17727698 Importantly, Nek7 has been reported to localise to the centrosome in both interphase and mitotic U2OS and HeLa cells |
| GO:0032206 positive regulation of telomere maintenance | IMP PMID:21531765 High-throughput RNAi screening reveals novel regulators of t... | UNDECIDED | Summary: Positive regulation of telomere maintenance (IMP) from a high-throughput kinase RNAi screen for telomerase modulators. Reason: Only the abstract of the cited screen is cached (no full text), and it names ERK8 rather than NEK7 as the highlighted hit, so I cannot see the NEK7-specific data the curator read. Screen hits of this kind are also frequently indirect - reduced telomerase activity is a common consequence of perturbing mitosis - and no follow-up work connects NEK7 to telomere biology. Per policy I leave an experimental annotation whose supporting text I cannot read as UNDECIDED rather than removing it. Supporting Evidence: PMID:21531765 we report the findings of a high-throughput functional RNA interference screen to globally profile the contribution of kinases to telomerase activity (TA) |
| GO:0035865 cellular response to potassium ion | IEA GO_REF:0000107 | ACCEPT | Summary: Cellular response to potassium ion, transferred electronically from mouse Nek7 (Q9ES74). Reason: NEK7 acts downstream of potassium efflux in NLRP3 activation: blocking K+ efflux with extracellular KCl prevents the NLRP3-NEK7 association and caspase-1 activation, while K+ efflux itself is unimpaired in NEK7-null macrophages. The annotation describes a genuine, experimentally defined position of NEK7 in a potassium-responsive pathway, and the orthologous mouse evidence transfers cleanly. Supporting Evidence: PMID:26814970 Notably, the association of NLRP3 with Nek7 as well as caspase-1 activation triggered by ATP were blocked in the presence of 50 mM KCl that inhibits potassium efflux and NLRP3 activation PMID:26814970 We have shown that Nek7 is an essential factor that specifically and non-redundantly functions downstream of potassium efflux to regulate the activation of the NLRP3 inflammasome. |
| GO:0035865 cellular response to potassium ion | ISS GO_REF:0000024 | ACCEPT | Summary: Cellular response to potassium ion, transferred from mouse Nek7 by curator sequence-similarity judgement. Reason: NEK7 acts downstream of potassium efflux in NLRP3 activation: blocking K+ efflux with extracellular KCl prevents the NLRP3-NEK7 association and caspase-1 activation, while K+ efflux itself is unimpaired in NEK7-null macrophages. The annotation describes a genuine, experimentally defined position of NEK7 in a potassium-responsive pathway, and the orthologous mouse evidence transfers cleanly. Supporting Evidence: PMID:26814970 Notably, the association of NLRP3 with Nek7 as well as caspase-1 activation triggered by ATP were blocked in the presence of 50 mM KCl that inhibits potassium efflux and NLRP3 activation PMID:26814970 We have shown that Nek7 is an essential factor that specifically and non-redundantly functions downstream of potassium efflux to regulate the activation of the NLRP3 inflammasome. |
| GO:0043549 regulation of kinase activity | IDA PMID:12840024 A mitotic cascade of NIMA family kinases. Nercc1/Nek9 activa... | UNDECIDED | Summary: Regulation of kinase activity (IDA) from the NEK9/NEK6/NEK7 cascade paper. Reason: In the cited work the regulatory direction runs the other way: NEK9 (Nercc1) phosphorylates and activates NEK6 and NEK7, so NEK7 is the regulated kinase rather than a regulator of one. Only the abstract is cached, so I cannot check whether the full text contains data in which NEK7 modulates another kinase's activity (NEK7 autophosphorylation in trans would be a borderline case). Because I cannot read the supporting text behind this experimental annotation, I flag it as UNDECIDED rather than removing it; if the annotation does reflect NEK9 acting on NEK7, it is misdirected and should be retired. Supporting Evidence: PMID:12840024 Nercc1 activates Nek7 in vitro in a similar manner PMID:12840024 Nek6 (314AA) and Nek7 (303AA), 76% identical, have little noncatalytic sequence but bind to the carboxyl-terminal noncatalytic tail of Nercc1/Nek9 |
| GO:0051225 spindle assembly | IEA GO_REF:0000117 | MODIFY | Summary: Spindle assembly predicted by an ARBA machine-learning model. Reason: Spindle assembly is correct for NEK7 but is the general, taxon-neutral parent: all of the evidence concerns the mitotic spindle specifically - NEK7 depletion gives monopolar, disorganised or multipolar mitotic spindles and prometaphase arrest, and NEK7 is activated in mitosis. GO:0090307 mitotic spindle assembly states that specificity, which matters for a protein whose activity is itself mitosis-restricted. Proposed replacements: mitotic spindle assembly Supporting Evidence: PMID:17586473 NEK7 knockdown by RNAi caused a prometaphase arrest of the cell cycle with monopolar or disorganized spindle. PMID:17101132 Down-regulation of Nek7 using a small interfering RNA approach resulted in a significant increase in mitotic cells presenting multipolar spindle phenotype. PMID:19414596 while completely inactive mutants and small interfering RNA-mediated depletion delay cells at metaphase with fragile mitotic spindles |
| GO:0051225 spindle assembly | TAS PMID:17727698 Mitotic regulation by NIMA-related kinases. | MODIFY | Summary: Spindle assembly asserted by a review of NIMA-related kinases (TAS). Reason: Spindle assembly is correct for NEK7 but is the general, taxon-neutral parent: all of the evidence concerns the mitotic spindle specifically - NEK7 depletion gives monopolar, disorganised or multipolar mitotic spindles and prometaphase arrest, and NEK7 is activated in mitosis. GO:0090307 mitotic spindle assembly states that specificity, which matters for a protein whose activity is itself mitosis-restricted. Proposed replacements: mitotic spindle assembly Supporting Evidence: PMID:17727698 it seems likely that these kinases exert their effects through organisation of the mitotic spindle PMID:17586473 NEK7 knockdown by RNAi caused a prometaphase arrest of the cell cycle with monopolar or disorganized spindle. |
| GO:0106310 protein serine kinase activity | EXP PMID:19941817 An autoinhibitory tyrosine motif in the cell-cycle-regulated... | ACCEPT | Summary: Protein serine kinase activity from direct experimental evidence of NEK7 catalytic activity. Reason: Direct kinase assays with protein substrates (beta-casein in vitro, and EML4 Ser144/Ser146 as a mapped physiological substrate) establish that NEK7 phosphorylates serine residues; the Rhea-backed serine-kinase term is the correct, specific catalytic assignment and is a core NEK7 function. Supporting Evidence: PMID:19941817 bacterially expressed and purified kinases were incubated with 2 ΞΌCi 33P ATP in 38 ΞΌM ATP for 50 min at 30Β°C using Ξ²-casein as substrate PMID:19941817 Strikingly, Nek9-CTD did not significantly increase the activity of Nek7-Y97A, suggesting that the mechanism of Nek7 activation occurs through release of Tyr97 autoinhibition. |
| GO:0106310 protein serine kinase activity | EXP PMID:26522158 Mechanistic basis of Nek7 activation through Nek9 binding an... | ACCEPT | Summary: Protein serine kinase activity from the structural/enzymatic analysis of NEK9-activated NEK7. Reason: Direct kinase assays with protein substrates (beta-casein in vitro, and EML4 Ser144/Ser146 as a mapped physiological substrate) establish that NEK7 phosphorylates serine residues; the Rhea-backed serine-kinase term is the correct, specific catalytic assignment and is a core NEK7 function. Supporting Evidence: PMID:26522158 In this study we elucidated the structural basis of the Nek7βNek9 interaction, which occurs at an unexpected site on the C-lobe of Nek7, and discovered that dimeric Nek9 stimulates Nek7 autophosphorylation. PMID:26522158 Autophosphorylation most likely occurs in trans between, not within, Nek7 back-to-back dimers. |
| GO:0106310 protein serine kinase activity | EXP PMID:31409757 Mitotic phosphorylation by NEK6 and NEK7 reduces the microtu... | ACCEPT | Summary: Protein serine kinase activity from the identification of EML4 Ser144/Ser146 as NEK7 phosphosites. Reason: Direct kinase assays with protein substrates (beta-casein in vitro, and EML4 Ser144/Ser146 as a mapped physiological substrate) establish that NEK7 phosphorylates serine residues; the Rhea-backed serine-kinase term is the correct, specific catalytic assignment and is a core NEK7 function. Supporting Evidence: PMID:31409757 The mitotic kinases NEK6 and NEK7 phosphorylated the EML4 N-terminal domain at Ser144 and Ser146 in vitro, and depletion of these kinases in cells led to increased EML4 binding to microtubules in mitosis. PMID:31409757 NEK6- and NEK7-dependent phosphorylation promotes the dissociation of EML4 from microtubules in mitosis in a manner that is required for efficient chromosome congression |
| GO:0106310 protein serine kinase activity | IEA GO_REF:0000116 | ACCEPT | Summary: Protein serine kinase activity mapped automatically from the Rhea reaction for protein serine phosphorylation. Reason: The Rhea mapping matches the EC 2.7.11.34 activity demonstrated for NEK7 in direct assays, including on a mapped physiological substrate. Supporting Evidence: PMID:31409757 The mitotic kinases NEK6 and NEK7 phosphorylated the EML4 N-terminal domain at Ser144 and Ser146 in vitro, and depletion of these kinases in cells led to increased EML4 binding to microtubules in mitosis. PMID:19941817 bacterially expressed and purified kinases were incubated with 2 ΞΌCi 33P ATP in 38 ΞΌM ATP for 50 min at 30Β°C using Ξ²-casein as substrate |
| GO:0140677 molecular function activator activity | IDA PMID:19941817 An autoinhibitory tyrosine motif in the cell-cycle-regulated... | UNDECIDED | Summary: Molecular function activator activity (IDA) attributed to NEK7 from the paper on Tyr-97 autoinhibition and NEK9-mediated release. Reason: In this paper the activation runs from NEK9 to NEK7: the NEK9 C-terminal domain relieves NEK7 Tyr-97 autoinhibition, and it is NEK9 that acts as the activator while NEK7 is the activated kinase. I can see no experiment in the cached full text in which NEK7 activates another protein's molecular function, and unlike the three NLRP3-based rows for this same term, this annotation carries no has_input extension naming an activated partner. The claim itself is well supported for NEK7 by the NLRP3 structural work, so nothing is lost by withholding judgement here; I flag the row as requiring curator attention to its direction rather than asserting removal of an experimental annotation whose supporting figure I cannot identify. Supporting Evidence: PMID:19941817 Strikingly, Nek9-CTD did not significantly increase the activity of Nek7-Y97A, suggesting that the mechanism of Nek7 activation occurs through release of Tyr97 autoinhibition. PMID:19941817 From this we conclude that Tyr-down autoinhibition restricts the activity of Nek6 and Nek7 in interphase but is completely released in mitosis. |
| GO:0140677 molecular function activator activity | IDA PMID:31189953 Structural mechanism for NEK7-licensed activation of NLRP3 i... | ACCEPT | Summary: Molecular function activator activity on NLRP3 (IDA, has_input NLRP3) from the cryo-EM structure of the NEK7-licensed inactive NLRP3 complex. Reason: NEK7 binds the NLRP3 leucine-rich repeat domain and relieves NLRP3 autoinhibition - structurally, it opens the inactive NLRP3 cage at the microtubule-organizing centre and bridges adjacent NLRP3 subunits in the active disc - without covalently modifying NLRP3 and without requiring its own catalytic activity, which is precisely the non-covalent direct activator relationship GO:0140677 is defined for. The has_input extension naming NLRP3 makes the claim unambiguous. This is a core NEK7 function and must be kept separate from its kinase activity. Supporting Evidence: PMID:31189953 In NLRP3, the LRR itself is too short to reach the adjacent LRR in the hypothetical oligomer, and NEK7 bridges the gap between adjacent NLRP3 subunits. PMID:31189953 consistent with the observation that both active and inactive NEK7 can support NLRP3 activation PMID:31189953 However, E280R did not rescue NLRP3 activation in NEK7KO iBMDMs whereas WT NEK7 did |
| GO:0140677 molecular function activator activity | IDA PMID:36442502 Cryo-EM structures of the active NLRP3 inflammasome disc. | ACCEPT | Summary: Molecular function activator activity on NLRP3 (IDA, has_input NLRP3) from the cryo-EM structures of the active NLRP3 inflammasome disc. Reason: NEK7 binds the NLRP3 leucine-rich repeat domain and relieves NLRP3 autoinhibition - structurally, it opens the inactive NLRP3 cage at the microtubule-organizing centre and bridges adjacent NLRP3 subunits in the active disc - without covalently modifying NLRP3 and without requiring its own catalytic activity, which is precisely the non-covalent direct activator relationship GO:0140677 is defined for. The has_input extension naming NLRP3 makes the claim unambiguous. This is a core NEK7 function and must be kept separate from its kinase activity. Supporting Evidence: PMID:36442502 its interaction with NEK7 at the MTOC disrupts the cage to allow formation of the active NLRP3 disc PMID:36442502 centrosomal NIMA-related kinase 7 (NEK7), important in mitosis, has been identified as a scaffolding protein in NLRP3 activation independent of its kinase activity PMID:36442502 Ten such subunits form a large flower-shaped disc of diameter about 32 nm from top and bottom views, in which the FISNAβNACHT domains interact near the centre of the disc and the LRR domains and bound NEK7 extend away from the centre |
| GO:0140677 molecular function activator activity | IDA PMID:39173637 Consecutive palmitoylation and phosphorylation orchestrates ... | ACCEPT | Summary: Molecular function activator activity on NLRP3 (IDA, has_input NLRP3, occurs_in MTOC) from the study of NLRP3 palmitoylation and LATS1/2 phosphorylation. Reason: NEK7 binds the NLRP3 leucine-rich repeat domain and relieves NLRP3 autoinhibition - structurally, it opens the inactive NLRP3 cage at the microtubule-organizing centre and bridges adjacent NLRP3 subunits in the active disc - without covalently modifying NLRP3 and without requiring its own catalytic activity, which is precisely the non-covalent direct activator relationship GO:0140677 is defined for. The has_input extension naming NLRP3 makes the claim unambiguous. This is a core NEK7 function and must be kept separate from its kinase activity. Supporting Evidence: PMID:39173637 LATS1/2, pre-recruited to MTOC during priming, phosphorylates NLRP3 to further facilitate its interaction with NIMA-related kinase 7 (NEK7), ultimately leading to full NLRP3 activation PMID:36442502 its interaction with NEK7 at the MTOC disrupts the cage to allow formation of the active NLRP3 disc |
| GO:0140677 molecular function activator activity | IEA GO_REF:0000107 | ACCEPT | Summary: Molecular function activator activity transferred electronically from mouse Nek7 (Q9ES74). Reason: The mouse evidence is the primary genetic and biochemical source for NEK7-dependent NLRP3 licensing, and the human protein performs the same function in human cells, so the orthology-based transfer is sound. Supporting Evidence: PMID:26814970 In contrast, the catalytic activity of Nek7 is not required for NLRP3 activation. PMID:36384135 showing that hsNEK7 is capable of priming NLRP3 |
| GO:1900227 positive regulation of NLRP3 inflammasome complex assembly | IBA GO_REF:0000033 | ACCEPT | Summary: Positive regulation of NLRP3 inflammasome complex assembly inferred from the phylogenetic node PANTHER:PTN002878636. Reason: NEK7 is required for NLRP3-ASC complex formation and caspase-1 activation downstream of potassium efflux, and it does part of the work of assembly itself rather than merely being necessary for it: NEK7 opens the autoinhibited NLRP3 cage and is a stoichiometric structural component of the assembled disc, where ten NEK7 molecules bridge adjacent NLRP3 subunits. Kinase-dead NEK7 rescues, so the contribution is structural rather than catalytic. The IBD node placement is well grounded, with experimental descendants in both human and mouse; NEK7's own presence in the WITH/FROM list reflects that direct grounding and is expected rather than circular. Supporting Evidence: PMID:31189953 In NLRP3, the LRR itself is too short to reach the adjacent LRR in the hypothetical oligomer, and NEK7 bridges the gap between adjacent NLRP3 subunits. PMID:26642356 when introduced by electroporation into Nek7Cu/Cu macrophages both wild-type NEK7 and NEK7K64M rescued IL-1Ξ² secretion in response to LPS priming plus nigericin or ATP |
| GO:1900227 positive regulation of NLRP3 inflammasome complex assembly | IDA PMID:31189953 Structural mechanism for NEK7-licensed activation of NLRP3 i... | ACCEPT | Summary: Positive regulation of NLRP3 inflammasome complex assembly (IDA) from the NEK7-NLRP3 structure and mutagenesis. Reason: NEK7 is required for NLRP3-ASC complex formation and caspase-1 activation downstream of potassium efflux, and it does part of the work of assembly itself rather than merely being necessary for it: NEK7 opens the autoinhibited NLRP3 cage and is a stoichiometric structural component of the assembled disc, where ten NEK7 molecules bridge adjacent NLRP3 subunits. Kinase-dead NEK7 rescues, so the contribution is structural rather than catalytic. Supporting Evidence: PMID:31189953 In NLRP3, the LRR itself is too short to reach the adjacent LRR in the hypothetical oligomer, and NEK7 bridges the gap between adjacent NLRP3 subunits. PMID:31189953 However, E280R did not rescue NLRP3 activation in NEK7KO iBMDMs whereas WT NEK7 did |
| GO:1900227 positive regulation of NLRP3 inflammasome complex assembly | IDA PMID:36442502 Cryo-EM structures of the active NLRP3 inflammasome disc. | ACCEPT | Summary: Positive regulation of NLRP3 inflammasome complex assembly (IDA) from the active NLRP3 inflammasome disc structures. Reason: NEK7 is required for NLRP3-ASC complex formation and caspase-1 activation downstream of potassium efflux, and it does part of the work of assembly itself rather than merely being necessary for it: NEK7 opens the autoinhibited NLRP3 cage and is a stoichiometric structural component of the assembled disc, where ten NEK7 molecules bridge adjacent NLRP3 subunits. Kinase-dead NEK7 rescues, so the contribution is structural rather than catalytic. Supporting Evidence: PMID:36442502 its interaction with NEK7 at the MTOC disrupts the cage to allow formation of the active NLRP3 disc PMID:36442502 Ten such subunits form a large flower-shaped disc of diameter about 32 nm from top and bottom views, in which the FISNAβNACHT domains interact near the centre of the disc and the LRR domains and bound NEK7 extend away from the centre |
| GO:1900227 positive regulation of NLRP3 inflammasome complex assembly | IDA PMID:39173637 Consecutive palmitoylation and phosphorylation orchestrates ... | ACCEPT | Summary: Positive regulation of NLRP3 inflammasome complex assembly (IDA) from the NLRP3 trafficking/phosphorylation study. Reason: NEK7 is required for NLRP3-ASC complex formation and caspase-1 activation downstream of potassium efflux, and it does part of the work of assembly itself rather than merely being necessary for it: NEK7 opens the autoinhibited NLRP3 cage and is a stoichiometric structural component of the assembled disc, where ten NEK7 molecules bridge adjacent NLRP3 subunits. Kinase-dead NEK7 rescues, so the contribution is structural rather than catalytic. Supporting Evidence: PMID:39173637 LATS1/2, pre-recruited to MTOC during priming, phosphorylates NLRP3 to further facilitate its interaction with NIMA-related kinase 7 (NEK7), ultimately leading to full NLRP3 activation |
| GO:1900227 positive regulation of NLRP3 inflammasome complex assembly | IEA GO_REF:0000107 | ACCEPT | Summary: Positive regulation of NLRP3 inflammasome complex assembly transferred electronically from mouse Nek7. Reason: NEK7 is required for NLRP3-ASC complex formation and caspase-1 activation downstream of potassium efflux, and it does part of the work of assembly itself rather than merely being necessary for it: NEK7 opens the autoinhibited NLRP3 cage and is a stoichiometric structural component of the assembled disc, where ten NEK7 molecules bridge adjacent NLRP3 subunits. Kinase-dead NEK7 rescues, so the contribution is structural rather than catalytic. Mouse macrophage genetics is the original and strongest evidence for this role, and it transfers to the human orthologue, which supports NLRP3 priming in the same way. Supporting Evidence: PMID:26642356 These results indicate that the kinase activity of NEK7 is nonessential for activation of the NLRP3 inflammasome. PMID:26642356 when introduced by electroporation into Nek7Cu/Cu macrophages both wild-type NEK7 and NEK7K64M rescued IL-1Ξ² secretion in response to LPS priming plus nigericin or ATP PMID:36384135 showing that hsNEK7 is capable of priming NLRP3 |
| GO:0046777 protein autophosphorylation | IDA PMID:26522158 Mechanistic basis of Nek7 activation through Nek9 binding an... | NEW | Summary: NEK7 autophosphorylates its own activation loop in trans between back-to-back dimers, a step stimulated by dimeric NEK9 binding. Reason: NEK7 itself performs the phosphotransfer onto NEK7 residues, so the participation test is met by the gene product doing the chemistry rather than being a substrate of another kinase. The observation is direct and is the mechanism by which NEK7 becomes catalytically competent in mitosis, and it is not covered by any existing row (the protein phosphorylation rows concern substrate phosphorylation; the regulation-of-kinase-activity row describes NEK9 acting on NEK7). Many protein kinases with activation-loop trans-autophosphorylation carry this term, so it is conventional rather than novel in kind. Supporting Evidence: PMID:26522158 In this study we elucidated the structural basis of the Nek7βNek9 interaction, which occurs at an unexpected site on the C-lobe of Nek7, and discovered that dimeric Nek9 stimulates Nek7 autophosphorylation. PMID:26522158 Autophosphorylation most likely occurs in trans between, not within, Nek7 back-to-back dimers. |
| GO:0030496 midbody | IDA PMID:17586473 NEK7 is a centrosomal kinase critical for microtubule nuclea... | NEW | Summary: NEK7 is observed at the midbody of cytokinetic cells, in addition to its centrosomal localisation through the cell cycle. Reason: A direct imaging observation of a discrete cellular location that no existing annotation captures (the current component set covers spindle pole, centrosome, MTOC, cytoplasm and nucleus). It is mechanistically coherent with the independent requirement for NEK7 in cytokinesis and with the cytokinesis failure and polyploidy of Nek7-null mouse cells. Supporting Evidence: PMID:17586473 Temporal localization of NEK7 at midbody of the cytokinetic cell was also observed. PMID:17586473 it was evident that NEK7 was directly involved in cytokinesis PMID:20473324 derived from Nek7(-/-) embryos show increase tendency for chromosomal lagging, micronuclei formation and cytokinesis failure |
| GO:0072559 NLRP3 inflammasome complex | IDA PMID:36442502 Cryo-EM structures of the active NLRP3 inflammasome disc. | NEW | Summary: Cryo-EM of the active human NLRP3 inflammasome resolves a ten-fold symmetric disc built from ten full-length NLRP3 and ten full-length NEK7 molecules, making NEK7 a structural subunit of the complex rather than only an upstream regulator. Reason: The participation test is met structurally: NEK7 is present in the assembled complex at defined stoichiometry and supplies the inter-subunit bridge that the short NLRP3 LRR cannot make, so it contributes structure the assembly depends on. The comparator check supports the term being used beyond its three definitional components - in human, GO:0072559 is already annotated to GSDMD, CARD8, DHX33 and DDX3X alongside NLRP3, PYCARD and CASP1 - and several of those rest on weaker evidence than an atomic model. Because the term definition enumerates only NLRP3, PYCARD and caspase-1, a curator may prefer to widen the definition before adding NEK7; that question is raised in suggested_questions rather than settled here. Supporting Evidence: PMID:36442502 Ten such subunits form a large flower-shaped disc of diameter about 32 nm from top and bottom views, in which the FISNAβNACHT domains interact near the centre of the disc and the LRR domains and bound NEK7 extend away from the centre PMID:31189953 In NLRP3, the LRR itself is too short to reach the adjacent LRR in the hypothetical oligomer, and NEK7 bridges the gap between adjacent NLRP3 subunits. PMID:36442502 its interaction with NEK7 at the MTOC disrupts the cage to allow formation of the active NLRP3 disc |
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Download this section (compressed HTML)Q: Should NEK7 be annotated as a component of GO:0072559 NLRP3 inflammasome complex, and should the term definition (which enumerates only NLRP3, PYCARD and caspase-1) be widened? The active disc contains ten NEK7 molecules at defined stoichiometry, and human annotations to this term already extend beyond the three definitional components.
Q: Is the GO:0140677 molecular function activator activity annotation from PMID:19941817, and the GO:0043549 regulation of kinase activity annotation from PMID:12840024, directionally correct? In both papers NEK9 activates NEK7, not the reverse, and neither annotation carries an extension naming an activated partner.
Q: How should the human-versus-mouse divergence in NEK7 dependence be represented? NEK7 is non-redundantly required for NLRP3 activation in mouse macrophages, but human BLaER1 and THP-1 cells deficient in NEK7 activate NLRP3 normally through an IKK-beta-dependent priming route, while human NEK7 can still prime NLRP3 when expressed.
Q: Does NEK7 have a function in the nucleus? Several annotations place it there and ANKS3 binding is reported to block its nuclear entry, but no nuclear substrate or nuclear process has been identified.
Q: Beyond EML4, what are the physiological substrates of NEK7 at the centrosome, and is the gamma-tubulin recruitment defect in NEK7-depleted cells the consequence of phosphorylating a specific pericentriolar substrate?
Q: Is the IMP annotation to positive regulation of telomere maintenance (PMID:21531765) a direct role, or a secondary consequence of perturbing mitosis in a kinase-wide RNAi screen?
Experiment: In NEK7-knockout human macrophages (and a NEK7-null monocytic line), re-express a panel of NEK7 alleles: wild type, kinase-dead (K64M), constitutively active (Y97A), the NLRP3-interface mutant E280R, and a NEK9-interface mutant. Score in parallel the mitotic phenotypes (centrosomal gamma-tubulin, microtubule regrowth, spindle polarity, EML4 Ser146 phosphorylation) and the inflammasome phenotypes (NLRP3-NEK7 co-immunoprecipitation, ASC oligomerisation, caspase-1 cleavage, IL-1beta release). A clean double dissociation, with E280R mitosis-competent but inflammasome-dead and K64M the converse, would fix the two activities as independent molecular functions of one protein.
Hypothesis: NEK7 catalytic activity and NLRP3 licensing are fully separable functions of the same surface-limited protein, so the two can be independently reconstituted in a NEK7-null human macrophage.
Experiment: Titrate NLRP3 expression over two orders of magnitude in NEK7-null and NEK7-competent human macrophages with and without IKK-beta inhibition, across K+-dependent (nigericin, ATP) and K+-independent (imiquimod) stimuli, reading out speck position relative to the pericentriolar material, caspase-1 activation and IL-1beta. Run the same matrix in mouse macrophages. If NEK7 dependence tracks with NLRP3 abundance and route rather than with species, the apparent species difference is a threshold effect.
Hypothesis: Human cells use NEK7-dependent and IKK-beta-dependent NLRP3 priming as alternative routes whose relative weight is set by NLRP3 abundance and stimulus, which would explain why mouse macrophages appear strictly NEK7-dependent and human lines do not.
Experiment: Reconstitute NLRP3 inflammasome assembly from purified components with sub-stoichiometric and saturating NEK7, and follow NEK7 occupancy during and after disc formation by mass photometry and quantitative cryo-EM classification; test whether NEK7 can be competed off an already-assembled disc by excess NEK9 C-terminal domain. Retention of NEK7 in the mature disc at one-to-one stoichiometry would support annotating NEK7 as a complex component.
Hypothesis: NEK7 is a stoichiometric structural subunit of the assembled inflammasome rather than a transient catalyst of its assembly.
Experiment: Apply analogue-sensitive NEK7 (gatekeeper mutant) with a bulky ATP analogue, or chemical-genetic thiophosphate labelling, in synchronised mitotic cells, and enrich labelled substrates from purified centrosomes by mass spectrometry. Validate candidates by phospho-site mutation and by asking whether the non-phosphorylatable allele reproduces the gamma-tubulin and microtubule-nucleation defect of NEK7 depletion.
Hypothesis: NEK7 has one or more unidentified centrosomal substrates whose phosphorylation mediates gamma-tubulin recruitment.
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