NDUFB3

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0006120 mitochondrial electron transport, NADH to ubiquinone	IBA GO_REF:0000033	ACCEPT	Summary: Phylogenetic (IBA) inference that NDUFB3 is involved in mitochondrial electron transport from NADH to ubiquinone, the defining process of Complex I. NDUFB3 is a stable subunit of Complex I, so its involvement in the complex's core process is appropriate. Core biological-process annotation. Supporting Evidence: PMID:9878551 Its main function is the transport of electrons from NADH to ubiquinone, which is accompanied by translocation of protons from the mitochondrial matrix to the intermembrane space.
GO:0045271 respiratory chain complex I	IBA GO_REF:0000033	ACCEPT	Summary: Phylogenetic (IBA) inference that NDUFB3 is part of respiratory chain complex I. Correct and strongly supported by direct experimental evidence: NDUFB3/B12 is a bona fide stable subunit of the Complex I holoenzyme. Core cellular-component annotation. Supporting Evidence: file:human/NDUFB3/NDUFB3-uniprot.txt Complex I is composed of 45 different subunits.
GO:0005739 mitochondrion	IEA GO_REF:0000002	KEEP AS NON CORE	Summary: InterPro2GO electronic annotation to mitochondrion, based on the NDUFB3 InterPro signature. Correct but less specific than the mitochondrial inner membrane annotations; retained as a valid, generic localization. Supporting Evidence: file:human/NDUFB3/NDUFB3-uniprot.txt Mitochondrion inner membrane
GO:0005743 mitochondrial inner membrane	IEA GO_REF:0000120	ACCEPT	Summary: Electronic annotation to mitochondrial inner membrane. Consistent with the authoritative UniProt subcellular location and with NDUFB3 being an inner-membrane-arm subunit of Complex I. Correct and the most specific membrane location. Supporting Evidence: file:human/NDUFB3/NDUFB3-uniprot.txt Mitochondrion inner membrane
GO:0022900 electron transport chain	IEA GO_REF:0000002	KEEP AS NON CORE	Summary: InterPro2GO electronic annotation to electron transport chain, the general parent process. Correct but less specific than mitochondrial electron transport, NADH to ubiquinone (GO:0006120), which is separately annotated and captures NDUFB3's role more precisely. Keep as non-core general process.
GO:1902600 proton transmembrane transport	IEA GO_REF:0000108	MARK AS OVER ANNOTATED	Summary: Inter-ontology (GO_REF:0000108) inference derived from the NADH dehydrogenase (ubiquinone) activity term (GO:0008137). NDUFB3 does not itself enable GO:0008137 (it is a non-catalytic accessory subunit) and does not itself translocate protons, so this inferred transport annotation over-propagates a complex-level function onto an accessory subunit. The complex-level essence (Complex I pumps protons) is not wrong, but attributing proton transport to this subunit over-annotates it. Reason: Automatically inferred from GO:0008137, which itself is a complex-level activity not independently enabled by this non-catalytic accessory subunit. Supporting Evidence: file:human/NDUFB3/NDUFB3-uniprot.txt that is believed not to be
GO:0045271 respiratory chain complex I	IEA GO_REF:0000120	ACCEPT	Summary: Electronic (UniProt/ARBA + Ensembl ortholog) transfer of Complex I membership. Correct; redundant with the experimental IDA/IPI and IBA annotations to the same term. Core cellular-component annotation.
GO:0005743 mitochondrial inner membrane	IDA PMID:28844695 Architecture of Human Mitochondrial Respiratory Megacomplex ...	ACCEPT	Summary: Direct-assay (IDA, ComplexPortal) localization to mitochondrial inner membrane, supported by the cryo-EM megacomplex structure in which NDUFB3 is assigned as a Complex I subunit. Correct and consistent with UniProt. Supporting Evidence: PMID:28844695 reveals the precise assignment of individual subunits of human CI
GO:0009060 aerobic respiration	NAS PMID:30030361 Assembly of mammalian oxidative phosphorylation complexes I-...	KEEP AS NON CORE	Summary: Complex/pathway-level biological process attributed by ComplexPortal (NAS). Aerobic respiration is a downstream consequence of Complex I function rather than the direct, subunit-specific function of NDUFB3. Correct as context but broader than this gene's core role; keep as non-core.
GO:0042776 proton motive force-driven mitochondrial ATP synthesis	NAS PMID:30030361 Assembly of mammalian oxidative phosphorylation complexes I-...	KEEP AS NON CORE	Summary: Complex/pathway-level process (ComplexPortal NAS). ATP synthesis is a downstream outcome of the proton-motive force generated by the respiratory chain, to which Complex I contributes, but it is not the direct function of this accessory subunit. Keep as non-core contextual annotation.
GO:0045271 respiratory chain complex I	IPI PMID:28844695 Architecture of Human Mitochondrial Respiratory Megacomplex ...	ACCEPT	Summary: Physical-interaction (IPI, ComplexPortal) evidence that NDUFB3 is part of respiratory chain complex I, from the cryo-EM structural assignment of human Complex I subunits. Strong direct evidence for complex membership. Core cellular-component annotation. Supporting Evidence: PMID:28844695 reveals the precise assignment of individual subunits of human CI
GO:0005739 mitochondrion	HTP PMID:34800366 Quantitative high-confidence human mitochondrial proteome an...	KEEP AS NON CORE	Summary: High-throughput (HTP) detection of NDUFB3 in the high-confidence human mitochondrial proteome. Confirms mitochondrial localization; less specific than the inner-membrane annotations. Keep as supporting, non-core evidence.
GO:0045271 respiratory chain complex I	IDA PMID:12611891 The subunit composition of the human NADH dehydrogenase obta...	ACCEPT	Summary: Direct-assay (IDA) identification of NDUFB3 as a subunit of immunopurified human NADH dehydrogenase (Complex I) by mass spectrometry. Primary experimental evidence for complex membership. Core cellular-component annotation. Supporting Evidence: PMID:12611891 we can resolve and identify the human homologues of 42 polypeptides detected so far in the more extensively studied
GO:0045271 respiratory chain complex I	IDA PMID:27626371 Accessory subunits are integral for assembly and function of...	ACCEPT	Summary: Direct experimental evidence (gene-editing/knockout plus quantitative proteomics) that NDUFB3 is a Complex I accessory subunit whose loss destabilizes co-module subunits. This is the FUNCTION-supporting reference in UniProt and provides strong support for complex membership and the assembly requirement. Core cellular-component annotation. Supporting Evidence: PMID:27626371 loss of each subunit affects the stability of other subunits residing in the same structural module.
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 assigning NDUFB3 to Complex I from the cDNA characterization of nuclear-encoded Complex I subunits. Correct, and corroborated by the multiple IDA/IPI annotations to the same term.
GO:0005743 mitochondrial inner membrane	TAS Reactome:R-HSA-163217	ACCEPT	Summary: Traceable-author (Reactome) localization to mitochondrial inner membrane, from the Complex I electron-transfer reaction event. Correct localization for this inner-membrane subunit.
GO:0005743 mitochondrial inner membrane	TAS Reactome:R-HSA-6799178	ACCEPT	Summary: Reactome TAS inner-membrane localization from a Complex I biogenesis event. Correct localization; redundant with other inner-membrane annotations.
GO:0005743 mitochondrial inner membrane	TAS Reactome:R-HSA-6799179	ACCEPT	Summary: Reactome TAS inner-membrane localization from a Complex I biogenesis event. Correct localization; redundant with other inner-membrane annotations.
GO:0005743 mitochondrial inner membrane	TAS Reactome:R-HSA-6799191	ACCEPT	Summary: Reactome TAS inner-membrane localization from a Complex I biogenesis event. Correct localization; redundant with other inner-membrane annotations.
GO:0005743 mitochondrial inner membrane	TAS Reactome:R-HSA-6799196	ACCEPT	Summary: Reactome TAS inner-membrane localization from a Complex I biogenesis event. Correct localization; redundant with other inner-membrane annotations.
GO:0005743 mitochondrial inner membrane	TAS Reactome:R-HSA-6799197	ACCEPT	Summary: Reactome TAS inner-membrane localization from a Complex I biogenesis event. Correct localization; redundant with other inner-membrane annotations.
GO:0005743 mitochondrial inner membrane	TAS Reactome:R-HSA-6799202	ACCEPT	Summary: Reactome TAS inner-membrane localization from a Complex I biogenesis event. Correct localization; redundant with other inner-membrane annotations.
GO:0006120 mitochondrial electron transport, NADH to ubiquinone	NAS PMID:9878551 cDNA of eight nuclear encoded subunits of NADH:ubiquinone ox...	ACCEPT	Summary: Non-traceable author statement that NDUFB3 is involved in mitochondrial electron transport from NADH to ubiquinone, the defining process of Complex I. This is the core biological process of the complex to which NDUFB3 belongs and is the appropriate BP for this subunit. Supporting Evidence: PMID:9878551 Its main function is the transport of electrons from NADH to ubiquinone, which is accompanied by translocation of protons from the mitochondrial matrix to the intermembrane space.
GO:0008137 NADH dehydrogenase (ubiquinone) activity	NAS PMID:9878551 cDNA of eight nuclear encoded subunits of NADH:ubiquinone ox...	MARK AS OVER ANNOTATED	Summary: This is the complex-level catalytic activity of Complex I. NDUFB3/B12 is a non-catalytic accessory subunit that is not one of the 14 core subunits and carries no redox cofactor, so it does not independently enable NADH dehydrogenase (ubiquinone) activity. A direct `enables` annotation over-annotates this subunit; the correct representation is that NDUFB3 contributes_to this complex-level activity (captured in core_functions) with its own function being structural. Not removed per policy (NAS, essence not entirely wrong at the complex level), but flagged as over-annotated. Reason: GO:0008137 is the activity of the whole Complex I holoenzyme; NDUFB3 is a non-catalytic accessory subunit and does not enable this activity on its own. Supporting Evidence: file:human/NDUFB3/NDUFB3-uniprot.txt that is believed not to be
GO:0006120 mitochondrial electron transport, NADH to ubiquinone	TAS PMID:9425316 Identification and primary structure of five human NADH-ubiq...	ACCEPT	Summary: Traceable-author statement that NDUFB3, as a Complex I subunit, is involved in mitochondrial electron transport from NADH to ubiquinone. Complex I is the first enzyme complex in the mitochondrial electron transport chain. Core biological-process annotation for this subunit. Supporting Evidence: PMID:9425316 complex I) is the first enzyme complex in the electron transport chain of mitochondria
GO:0008137 NADH dehydrogenase (ubiquinone) activity	TAS PMID:9425316 Identification and primary structure of five human NADH-ubiq...	MARK AS OVER ANNOTATED	Summary: Traceable-author `enables` of the complex-level NADH dehydrogenase (ubiquinone) activity. NDUFB3 is a non-catalytic accessory subunit and does not itself carry out this catalysis; it contributes_to the activity as part of the holoenzyme rather than enabling it (captured in core_functions). As with the NAS annotation to the same term, a direct `enables` over-annotates this accessory subunit. Flagged as over-annotated (not removed; TAS support and essence correct at the complex level). Reason: NDUFB3 is a non-catalytic accessory subunit; it contributes to rather than independently enables the complex-level GO:0008137 activity. Supporting Evidence: file:human/NDUFB3/NDUFB3-uniprot.txt that is believed not to be

Gene Description

Existing Annotations Review

Core Functions

References

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Notes

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