NDUFB10

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0045271 respiratory chain complex I	IBA GO_REF:0000033	ACCEPT	Summary: Phylogenetically inferred (IBA) membership in respiratory chain complex I. NDUFB10 is a bona fide, structurally resolved subunit of Complex I, so this cellular-component location is correct and represents a core aspect of the gene. Consistent with the experimental IDA/IPI annotations to the same term. Supporting Evidence: file:human/NDUFB10/NDUFB10-uniprot.txt Complex I is composed of 45 different subunits
GO:0005739 mitochondrion	IEA GO_REF:0000117	KEEP AS NON CORE	Summary: Electronic (ARBA) annotation to the parent term mitochondrion. Correct but less specific than the experimentally supported mitochondrial inner membrane / respiratory chain complex I locations. Kept as non-core because it is subsumed by the more precise localizations. Supporting Evidence: file:human/NDUFB10/NDUFB10-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion inner membrane
GO:0005743 mitochondrial inner membrane	IEA GO_REF:0000120	ACCEPT	Summary: Electronic annotation to mitochondrial inner membrane, matching the curated UniProt subcellular location and the experimental IDA/IMP annotations to the same term. NDUFB10 is a peripheral inner-membrane protein on the matrix/IMS interface as part of the Complex I membrane arm. Supporting Evidence: file:human/NDUFB10/NDUFB10-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion inner membrane
GO:1902600 proton transmembrane transport	IEA GO_REF:0000108	MARK AS OVER ANNOTATED	Summary: Logically inferred (GO_REF:0000108) from the complex-level NADH dehydrogenase activity term. Proton translocation is a property of the assembled Complex I holoenzyme carried out largely by the core ND4/ND5/ND2 antiporter-like subunits, not by this non-catalytic accessory subunit lacking a transmembrane domain. Over-attribution of a complex-level activity to a single supernumerary subunit. Supporting Evidence: PMID:28040730 does not contain a transmembrane domain
GO:0005515 protein binding	IPI PMID:17500595 Huntingtin interacting proteins are genetic modifiers of neu...	MARK AS OVER ANNOTATED	Summary: Bare "protein binding" from a large-scale huntingtin-interactor screen for genetic modifiers of neurodegeneration. The term is uninformative about NDUFB10's molecular function and the interaction does not inform its role as a Complex I subunit. Experimental IPI, so not removed; marked as over-annotated (uninformative).
GO:0005515 protein binding	IPI PMID:25416956 A proteome-scale map of the human interactome network.	MARK AS OVER ANNOTATED	Summary: Bare "protein binding" from a proteome-scale human binary interactome (high-throughput Y2H). Uninformative about molecular function; NDUFB10 appears as one of many nodes. Experimental IPI, retained but marked as over-annotated.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	MARK AS OVER ANNOTATED	Summary: Bare "protein binding" from the reference human binary interactome (HuRI, high-throughput Y2H). Does not specify an informative molecular function. Experimental IPI, retained but marked as over-annotated.
GO:0005515 protein binding	IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ...	MARK AS OVER ANNOTATED	Summary: Bare "protein binding" from a neurodegenerative-disease interactome map focused on protein aggregation. Uninformative about NDUFB10's molecular function. Experimental IPI, retained but marked as over-annotated.
GO:0045271 respiratory chain complex I	IEA GO_REF:0000120	ACCEPT	Summary: Electronic (IEA) membership in respiratory chain complex I. Correct and redundant with the experimental IDA/IPI annotations to the same term; represents the core cellular-component location. Supporting Evidence: file:human/NDUFB10/NDUFB10-uniprot.txt Complex I is composed of 45 different subunits
GO:0005743 mitochondrial inner membrane	IDA PMID:28844695 Architecture of Human Mitochondrial Respiratory Megacomplex ...	ACCEPT	Summary: Direct assay (ComplexPortal, cryo-EM of the human respiratory megacomplex) places NDUFB10 in the inner membrane as a resolved Complex I subunit. Correct and consistent with the curated UniProt location.
GO:0009060 aerobic respiration	NAS PMID:30030361 Assembly of mammalian oxidative phosphorylation complexes I-...	KEEP AS NON CORE	Summary: Author statement (ComplexPortal) that Complex I participates in aerobic respiration. True at the complex level; for NDUFB10 this is a broad downstream process rather than the gene's specific function. Kept as non-core; the more precise BP is mitochondrial electron transport, NADH to ubiquinone (GO:0006120).
GO:0042776 proton motive force-driven mitochondrial ATP synthesis	NAS PMID:30030361 Assembly of mammalian oxidative phosphorylation complexes I-...	MARK AS OVER ANNOTATED	Summary: Author statement (ComplexPortal) linking Complex I to proton-motive-force ATP synthesis. This is an OXPHOS system-level / downstream outcome, not a function of this non-catalytic accessory subunit (ATP synthesis is performed by Complex V). Over-attribution of a pathway-level process to a single subunit.
GO:0045271 respiratory chain complex I	IPI PMID:28844695 Architecture of Human Mitochondrial Respiratory Megacomplex ...	ACCEPT	Summary: ComplexPortal IPI assignment of NDUFB10 as a component of respiratory chain complex I, from the cryo-EM megacomplex structure. Correct core cellular-component annotation.
GO:0005739 mitochondrion	HTP PMID:34800366 Quantitative high-confidence human mitochondrial proteome an...	KEEP AS NON CORE	Summary: High-throughput mitochondrial proteome study confirming mitochondrial localization. Correct but less specific than the inner-membrane / Complex I locations; kept as non-core.
GO:0045271 respiratory chain complex I	IDA PMID:12611891 The subunit composition of the human NADH dehydrogenase obta...	ACCEPT	Summary: Direct identification of NDUFB10 as a subunit of the human NADH dehydrogenase (Complex I) by one-step immunopurification and mass spectrometry. Strong experimental support for this core cellular-component annotation. Supporting Evidence: PMID:12611891 we can resolve and identify the human homologues of 42 polypeptides
GO:0045271 respiratory chain complex I	IDA PMID:27626371 Accessory subunits are integral for assembly and function of...	ACCEPT	Summary: Direct identification of NDUFB10 within Complex I in the systematic accessory-subunit knockout study. Confirms NDUFB10 as an integral accessory subunit of the complex. Core cellular-component annotation. Supporting Evidence: PMID:27626371 Accessory subunits are integral for assembly and function of human mitochondrial complex I
GO:0045271 respiratory chain complex I	NAS PMID:9878551 cDNA of eight nuclear encoded subunits of NADH:ubiquinone ox...	ACCEPT	Summary: Non-traceable author statement from the cDNA characterization paper that NDUFB10 is a subunit of Complex I (localized within the hydrophobic protein fraction). Correct and redundant with the experimental IDA annotations to this term. Supporting Evidence: PMID:9878551 all located within the hydrophobic protein (HP) fraction of complex I
GO:0005515 protein binding	IPI PMID:28040730 Mutations in the accessory subunit NDUFB10 result in isolate...	MARK AS OVER ANNOTATED	Summary: IPI "protein binding" with interactor Q8N4Q1 (CHCHD4/MIA40). This is the one functionally meaningful interaction: NDUFB10 transiently binds the IMS disulfide-relay oxidoreductase CHCHD4 during import and oxidative folding. However, the bare "protein binding" term is uninformative; experimental IPI so retained, but marked over-annotated. The biology is captured in core_functions (structural molecule activity / Complex I assembly) and notes. Supporting Evidence: PMID:28040730 during its mitochondrial import and maturation NDUFB10 transiently interacts with CHCHD4 and acquires disulfide bonds
GO:0005743 mitochondrial inner membrane	IMP PMID:28040730 Mutations in the accessory subunit NDUFB10 result in isolate...	ACCEPT	Summary: IMP-supported inner-membrane localization from the disease study: wild-type NDUFB10 localizes completely to mitochondria (and integrates into the membrane-arm of Complex I), whereas the C107S variant is retained in the cytosol. Correct core localization. Supporting Evidence: PMID:28040730 the wild type protein was completely localized to mitochondria
GO:0005743 mitochondrial inner membrane	TAS Reactome:R-HSA-163217	ACCEPT	Summary: Reactome traceable annotation for the inner-membrane location in the context of the Complex I NADH to NAD+/CoQ reaction. Correct localization, redundant with experimental IDA/IMP annotations.
GO:0005743 mitochondrial inner membrane	TAS Reactome:R-HSA-6799178	ACCEPT	Summary: Reactome traceable annotation (Complex I biogenesis) for the inner-membrane location. Correct, redundant with experimental annotations.
GO:0005743 mitochondrial inner membrane	TAS Reactome:R-HSA-6799179	ACCEPT	Summary: Reactome traceable annotation (Complex I biogenesis) for the inner-membrane location. Correct, redundant with experimental annotations.
GO:0005743 mitochondrial inner membrane	TAS Reactome:R-HSA-6799191	ACCEPT	Summary: Reactome traceable annotation (Complex I biogenesis) for the inner-membrane location. Correct, redundant with experimental annotations.
GO:0005743 mitochondrial inner membrane	TAS Reactome:R-HSA-6799196	ACCEPT	Summary: Reactome traceable annotation (Complex I biogenesis) for the inner-membrane location. Correct, redundant with experimental annotations.
GO:0005743 mitochondrial inner membrane	TAS Reactome:R-HSA-6799197	ACCEPT	Summary: Reactome traceable annotation (Complex I biogenesis) for the inner-membrane location. Correct, redundant with experimental annotations.
GO:0005743 mitochondrial inner membrane	TAS Reactome:R-HSA-6799202	ACCEPT	Summary: Reactome traceable annotation (Complex I biogenesis) for the inner-membrane location. Correct, redundant with experimental annotations.
GO:0005515 protein binding	IPI PMID:14557246 AIP is a mitochondrial import mediator that binds to both im...	MARK AS OVER ANNOTATED	Summary: Bare "protein binding" from the AIP/Tom20 import study, where NDUFB10 was used as a control mitochondrial preprotein and shown to bind the import receptors Tom20 and Tom22 in vitro. A real import-machinery interaction but the bare term is uninformative about molecular function. Experimental IPI, retained but marked over-annotated. Supporting Evidence: PMID:14557246 other mitochondrial preproteins, ATP/ADP carrier protein and NDUFB10, which lack a cleavable presequence, also bound to AIP as well as to Tom20
GO:0006120 mitochondrial electron transport, NADH to ubiquinone	NAS PMID:9878551 cDNA of eight nuclear encoded subunits of NADH:ubiquinone ox...	ACCEPT	Summary: Author statement that NDUFB10, as a Complex I subunit, participates in the transfer of electrons from NADH to ubiquinone. This is the specific biological process of Complex I and an appropriate core BP for a genuine structural subunit, understood as contributory participation rather than NDUFB10 itself catalyzing electron transfer. Supporting Evidence: PMID:9878551 Its main function is the transport of electrons from NADH to ubiquinone
GO:0008137 NADH dehydrogenase (ubiquinone) activity	NAS PMID:9878551 cDNA of eight nuclear encoded subunits of NADH:ubiquinone ox...	MARK AS OVER ANNOTATED	Summary: Author statement assigning the complex-level NADH dehydrogenase (ubiquinone) catalytic activity directly to NDUFB10 via the "enables" qualifier. NDUFB10 is a non-catalytic accessory subunit lacking the redox cofactors (flavin, Fe-S clusters) required for this activity; the activity belongs to the assembled holoenzyme. NDUFB10 contributes_to but does not enable it. Best captured as contributes_to_molecular_function in core_functions; the direct "enables" annotation is an over-annotation. Supporting Evidence: PMID:27626371 Bacterial and human complex I share 14 core subunits that are essential for enzymatic function
GO:0005198 structural molecule activity	IDA PMID:28040730 Mutations in the accessory subunit NDUFB10 result in isolate...	NEW	Summary: Proposed new molecular-function annotation capturing the honest, subunit-specific MF of NDUFB10: it is a non-catalytic structural subunit that contributes to the structural integrity of Complex I. This replaces the over-annotated complex-level NADH dehydrogenase activity as the appropriate MF for this accessory subunit (it contributes_to GO:0008137). Supporting Evidence: PMID:28040730 the bovine homolog PDSW of human NDUFB10 appears to be located parallel to the membrane on the IMS face spanning ND4 and ND5
GO:0032981 mitochondrial respiratory chain complex I assembly	IMP PMID:28040730 Mutations in the accessory subunit NDUFB10 result in isolate...	NEW	Summary: Proposed new biological-process annotation. NDUFB10 is required for assembly of the Complex I holoenzyme: loss-of-function mutations perturb assembly at the ~830 kDa stage, and knockdown reduces the amount of fully assembled complex I. This is a core function of the gene not currently captured in GOA. Supporting Evidence: PMID:28040730 resulting in the perturbed assembly of the holoenzyme at the 830 kDa stage

Gene Description

Existing Annotations Review

Core Functions

References

📚 Additional Documentation

Notes

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