DPM2

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0005783 endoplasmic reticulum	IBA GO_REF:0000033	ACCEPT	Summary: Phylogenetic (IBA) assignment that DPM2 is active in the endoplasmic reticulum. This is correct but less specific than the well-supported ER membrane localization; retained as an accurate, broader localization. Reason: DPM2 is an ER membrane protein and the Dol-P-Man synthase complex acts in the ER. The more specific GO:0005789 (ER membrane) is separately annotated and preferred for the core localization. Supporting Evidence: PMID:9724629 DPM2, an 84 amino acid file:human/DPM2/DPM2-uniprot.txt Endoplasmic reticulum membrane; Multi-pass
GO:0006488 dolichol-linked oligosaccharide biosynthetic process	IBA GO_REF:0000033	ACCEPT	Summary: Phylogenetic (IBA) assignment linking DPM2 to biosynthesis of the dolichol-linked oligosaccharide N-glycan precursor. Dol-P-Man produced by the DPM synthase complex is the mannosyl donor for elongation of the lipid-linked oligosaccharide, so DPM2's regulatory role is upstream of and required for this process. Reason: Consistent with the established role of Dol-P-Man synthase in supplying mannose to the dolichol-linked oligosaccharide (LLO) pathway. Supporting Evidence: PMID:10835346 Dolichol-phosphate-mannose (DPM) synthase generates mannosyl donors for
GO:0033185 dolichol-phosphate-mannose synthase complex	IBA GO_REF:0000033	ACCEPT	Summary: Phylogenetic (IBA) assignment of DPM2 as part of the dolichol-phosphate-mannose synthase complex. This is the core structural context of DPM2 and is strongly supported experimentally. Reason: DPM2 is a bona fide subunit of the three-subunit human DPM synthase complex (DPM1/DPM2/DPM3). Supporting Evidence: PMID:10835346 mammalian DPM synthase contains catalytic DPM1 and regulatory DPM2
GO:0030234 enzyme regulator activity	IBA GO_REF:0000033	ACCEPT	Summary: Phylogenetic (IBA) assignment of enzyme regulator activity, capturing DPM2's non-catalytic regulatory role in the DPM synthase complex. DPM2 enhances DPM synthase activity and substrate (dolichyl phosphate) binding without itself being catalytic. Reason: Matches the experimentally supported function of DPM2 as a regulatory subunit. The more specific GO:0008047 (enzyme activator activity), separately annotated by IDA, better reflects the activating nature of this regulation. Supporting Evidence: PMID:10835346 DPM synthase activity was 10 times PMID:9724629 DPM2 enhances binding of dolichol phosphate, a substrate of DPM
GO:0005789 endoplasmic reticulum membrane	IEA GO_REF:0000120	ACCEPT	Summary: Electronic (IEA) assignment of ER membrane localization from InterPro/UniProt subcellular-location mapping. Correct and consistent with the experimentally determined multi-pass ER membrane topology of DPM2. Reason: DPM2 is a multi-pass ER membrane protein; this is the core cellular location. Supporting Evidence: file:human/DPM2/DPM2-uniprot.txt Endoplasmic reticulum membrane; Multi-pass
GO:0030234 enzyme regulator activity	IEA GO_REF:0000002	ACCEPT	Summary: Electronic (IEA) InterPro2GO assignment of enzyme regulator activity based on the DPM2 domain (IPR009914). Consistent with the experimental IDA/IBA evidence for DPM2's regulatory role. Reason: Correct molecular-function class for the DPM2 regulatory subunit; the more specific enzyme activator activity (GO:0008047) is also annotated. Supporting Evidence: PMID:10835346 mammalian DPM synthase contains catalytic DPM1 and regulatory DPM2
GO:0180047 dolichol phosphate mannose biosynthetic process	IEA GO_REF:0000002	ACCEPT	Summary: Electronic (IEA) InterPro2GO assignment to Dol-P-Man biosynthesis. This is the core biological process that the DPM synthase complex, and hence DPM2 as its regulatory subunit, carries out. Reason: Directly matches DPM2's function as regulatory subunit of Dol-P-Man synthase; also supported by an experimental IDA annotation (PMID:10835346). Supporting Evidence: PMID:9724629 DPM2 enhances binding of dolichol phosphate, a substrate of DPM
GO:0005515 protein binding	IPI PMID:10835346 Human dolichol-phosphate-mannose synthase consists of three ...	MARK AS OVER ANNOTATED	Summary: IPI protein-binding annotation from co-purification/interaction of DPM2 with DPM3 (UniProtKB:Q9P2X0) in the DPM synthase complex. The interaction is real and biologically meaningful for complex assembly, but the bare "protein binding" term is uninformative about molecular function. Reason: Per curation guidelines, bare protein binding (GO:0005515) is uninformative and is not retained as a core function. The underlying DPM2-DPM3 interaction is better captured by complex membership (GO:0033185) and by enzyme regulator/ activator activity. Experimental IPI is kept, not removed. Supporting Evidence: PMID:10835346 with DPM2 via its N-terminal portion
GO:0005515 protein binding	IPI PMID:10944123 Initial enzyme for glycosylphosphatidylinositol biosynthesis...	MARK AS OVER ANNOTATED	Summary: IPI protein-binding annotations from interactions of DPM2 with GPI-GnT components (PIGA/P37287, PIGC/Q92535, PIGQ/Q9BRB3). These interactions underlie DPM2's association with, and enhancement of, the GPI-GnT complex, but the bare term itself is uninformative. Reason: Bare protein binding is not retained as a core function per curation guidelines. The interactions are more informatively represented by GPI-GnT complex membership (GO:0000506) and enzyme regulator activity. Experimental IPI kept. Supporting Evidence: PMID:10944123 associates with GPI-GnT through interactions with PIG-A, PIG-C and
GO:0005515 protein binding	IPI PMID:16162815 The initial enzyme for glycosylphosphatidylinositol biosynth...	MARK AS OVER ANNOTATED	Summary: IPI protein-binding annotation from DPM2's identification as a component of the seven-subunit GPI-GnT complex (with PIGA/P37287). Real interaction but the bare term is uninformative. Reason: Bare protein binding is not retained as a core function per curation guidelines; complex membership (GO:0000506) captures the biology. Experimental IPI kept. Supporting Evidence: PMID:16162815 complex GPI-N-acetylglucosaminyltransferase (GPI-GnT)
GO:0005789 endoplasmic reticulum membrane	NAS PMID:9724629 DPM2 regulates biosynthesis of dolichol phosphate-mannose in...	ACCEPT	Summary: NAS assignment of ER membrane localization based on the original DPM2 characterization. DPM2 was shown to be an ER-expressed membrane protein. Reason: Consistent with experimental IDA/IEA support for ER membrane localization; this is the core cellular location of DPM2. Supporting Evidence: PMID:9724629 DPM2, an 84 amino acid
GO:0033185 dolichol-phosphate-mannose synthase complex	IPI PMID:10835346 Human dolichol-phosphate-mannose synthase consists of three ...	ACCEPT	Summary: IPI (ComplexPortal) annotation of DPM2 as part of the DPM synthase complex, based on the physical characterization of the three-subunit human complex. This is a core annotation for DPM2. Reason: Direct experimental support for DPM2 membership in the DPM1/DPM2/DPM3 complex. Supporting Evidence: PMID:10835346 The third subunit, DPM3, comprises 92 amino acids associated with DPM1
GO:0043048 dolichyl monophosphate biosynthetic process	IDA PMID:10835346 Human dolichol-phosphate-mannose synthase consists of three ...	MARK AS OVER ANNOTATED	Summary: IDA annotation to "dolichyl monophosphate biosynthetic process". PMID:10835346 concerns dolichol-phosphate-MANNOSE (Dol-P-Man) synthesis, i.e. the transfer of mannose onto dolichyl phosphate, rather than the biosynthesis of dolichyl monophosphate itself. The chosen term is therefore an imprecise/misleading match for the underlying experiment. Reason: DPM2 regulates addition of mannose to dolichyl phosphate to form Dol-P-Man; it is not shown to be involved in synthesis of the dolichyl monophosphate acceptor. Kept (experimental, not removed) but flagged; the accurate BP is GO:0180047 (dolichol phosphate mannose biosynthetic process), which is separately annotated. Supporting Evidence: PMID:10835346 Dolichol-phosphate-mannose (DPM) synthase generates mannosyl donors for
GO:0180047 dolichol phosphate mannose biosynthetic process	IDA PMID:10835346 Human dolichol-phosphate-mannose synthase consists of three ...	ACCEPT	Summary: IDA annotation to Dol-P-Man biosynthesis, the core biological process of the DPM synthase complex. DPM2 was shown to be required for and to enhance this activity (~10-fold), and to be required for the ER localization/stability of the catalytic subunit DPM1. Reason: Strong experimental support; this is the central biological process DPM2 participates in as regulatory subunit of Dol-P-Man synthase. Supporting Evidence: PMID:10835346 DPM synthase activity was 10 times PMID:9724629 that is essential for the ER localization and stable expression of
GO:0000506 glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex	IPI PMID:16162815 The initial enzyme for glycosylphosphatidylinositol biosynth...	KEEP AS NON CORE	Summary: IPI (ComplexPortal) annotation of DPM2 as a component of the GPI-GnT complex. DPM2 co-purifies with the GPI-GnT machinery, but it is a secondary/moonlighting membership: DPM2 is not essential for GPI-GnT and its primary role is in the DPM synthase complex. Reason: Real, experimentally supported association, but non-core relative to DPM2's primary role as regulatory subunit of Dol-P-Man synthase; DPM2 is dispensable for GPI-GnT activity (though it enhances it). Supporting Evidence: PMID:16162815 complex GPI-N-acetylglucosaminyltransferase (GPI-GnT) PMID:10944123 indicating that DPM2 is not essential for GPI-GnT; however, the enzyme activity
GO:0005789 endoplasmic reticulum membrane	IDA PMID:16162815 The initial enzyme for glycosylphosphatidylinositol biosynth...	ACCEPT	Summary: IDA (ComplexPortal) annotation of ER membrane localization, consistent with the ER-membrane topology of DPM2 and the ER location of the GPI-GnT and DPM synthase complexes. Reason: Core cellular location, well supported across multiple lines of evidence. Supporting Evidence: file:human/DPM2/DPM2-uniprot.txt Endoplasmic reticulum membrane; Multi-pass
GO:0000506 glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex	IDA PMID:16162815 The initial enzyme for glycosylphosphatidylinositol biosynth...	KEEP AS NON CORE	Summary: IDA (UniProt) annotation of DPM2 as a component of the GPI-GnT complex, from the seven-component characterization of GPI-GnT (PIGA/PIGC/PIGH/PIGP/PIGQ/PIGY/DPM2). Secondary/moonlighting membership relative to DPM2's DPM-synthase role. Reason: Experimentally supported but non-core; DPM2 is not essential for GPI-GnT. Supporting Evidence: PMID:16162815 complex GPI-N-acetylglucosaminyltransferase (GPI-GnT)
GO:0006506 GPI anchor biosynthetic process	IDA PMID:16162815 The initial enzyme for glycosylphosphatidylinositol biosynth...	KEEP AS NON CORE	Summary: IDA annotation linking DPM2 to GPI anchor biosynthesis via its membership in GPI-GnT, the first enzyme of the GPI pathway. This is a genuine but secondary role; DPM2 also contributes to GPI biosynthesis indirectly by supplying Dol-P-Man as a mannosyl donor. Reason: Real involvement but non-core; DPM2 enhances rather than is essential for GPI-GnT, and its core role is Dol-P-Man synthesis. Supporting Evidence: PMID:10944123 DPM2, which regulates PMID:16162815 Biosynthesis of glycosylphosphatidylinositol (GPI) is initiated by an unusually
GO:0008047 enzyme activator activity	IDA PMID:10835346 Human dolichol-phosphate-mannose synthase consists of three ...	ACCEPT	Summary: IDA annotation of enzyme activator activity. DPM2 increases Dol-P-Man synthase activity ~10-fold and enhances dolichyl phosphate substrate binding, acting as a positive (activating) regulator of the catalytic DPM1 subunit. This is the most precise molecular-function term for DPM2. Reason: Directly supported by the ~10x activation of DPM synthase in the presence of DPM2 and by enhanced substrate (dolichyl phosphate) binding; this is DPM2's core molecular function. Supporting Evidence: PMID:10835346 DPM synthase activity was 10 times PMID:9724629 DPM2 enhances binding of dolichol phosphate, a substrate of DPM
GO:0005789 endoplasmic reticulum membrane	TAS Reactome:R-HSA-4719375	ACCEPT	Summary: TAS (Reactome) ER membrane localization from the "Defective DPM2 does not transfer mannose to DOLP to form DOLPman" reaction. Correct localization. Reason: Consistent with the well-established ER membrane localization of DPM2. Supporting Evidence: file:human/DPM2/DPM2-uniprot.txt Endoplasmic reticulum membrane; Multi-pass
GO:0005789 endoplasmic reticulum membrane	TAS Reactome:R-HSA-162721	ACCEPT	Summary: TAS (Reactome) ER membrane localization from the dolichyl phosphate + GDP-mannose -> Dol-P-Man reaction. Correct localization. Reason: Consistent with the ER membrane localization of DPM2 and the DPM synthase complex. Supporting Evidence: file:human/DPM2/DPM2-uniprot.txt Endoplasmic reticulum membrane; Multi-pass
GO:0005789 endoplasmic reticulum membrane	TAS Reactome:R-HSA-162730	ACCEPT	Summary: TAS (Reactome) ER membrane localization from the GPI-GnT reaction (PI + UDP-GlcNAc -> GlcNAc-PI + UDP). Correct localization. Reason: Consistent with the ER membrane localization of DPM2 and the GPI-GnT complex. Supporting Evidence: file:human/DPM2/DPM2-uniprot.txt Endoplasmic reticulum membrane; Multi-pass
GO:0005789 endoplasmic reticulum membrane	TAS Reactome:R-HSA-4717406	ACCEPT	Summary: TAS (Reactome) ER membrane localization from the "Defective DPM1 does not transfer mannose to DOLP to form DOLPman" reaction. Correct localization. Reason: Consistent with the ER membrane localization of DPM2. Supporting Evidence: file:human/DPM2/DPM2-uniprot.txt Endoplasmic reticulum membrane; Multi-pass
GO:0005789 endoplasmic reticulum membrane	TAS Reactome:R-HSA-4719354	ACCEPT	Summary: TAS (Reactome) ER membrane localization from the "Defective DPM3 does not transfer mannose to DOLP to form DOLPman" reaction. Correct localization. Reason: Consistent with the ER membrane localization of DPM2. Supporting Evidence: file:human/DPM2/DPM2-uniprot.txt Endoplasmic reticulum membrane; Multi-pass
GO:0000506 glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex	IDA PMID:10944123 Initial enzyme for glycosylphosphatidylinositol biosynthesis...	KEEP AS NON CORE	Summary: IDA (MGI) annotation of DPM2 as a component of the GPI-GnT complex, from the demonstration that DPM2 associates with GPI-GnT via PIG-A, PIG-C and GPI1. Secondary/moonlighting membership. Reason: Experimentally supported but non-core relative to DPM2's DPM synthase role; DPM2 is not essential for GPI-GnT. Supporting Evidence: PMID:10944123 associates with GPI-GnT through interactions with PIG-A, PIG-C and
GO:0033185 dolichol-phosphate-mannose synthase complex	IDA PMID:10835346 Human dolichol-phosphate-mannose synthase consists of three ...	ACCEPT	Summary: IDA (UniProt) annotation of DPM2 as part of the DPM synthase complex, from the physical characterization of the three-subunit human complex. Core annotation. Reason: Directly supported experimental evidence for DPM2 membership in the DPM1/DPM2/ DPM3 complex. Supporting Evidence: PMID:10835346 mammalian DPM synthase contains catalytic DPM1 and regulatory DPM2
GO:0000506 glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex	TAS PMID:16280320 DPM1, the catalytic subunit of dolichol-phosphate mannose sy...	KEEP AS NON CORE	Summary: TAS annotation of GPI-GnT complex membership. PMID:16280320 focuses on DPM3 tethering/stabilizing DPM1 and notes DPM3 was co-purified with DPM1 and DPM2; the GPI-GnT membership of DPM2 is more directly established elsewhere (PMID:10944123, PMID:16162815). Secondary/moonlighting membership. Reason: Real but non-core association; DPM2's primary complex is the DPM synthase complex. Supporting Evidence: PMID:16280320 co-purified with DPM1 and DPM2
GO:0005789 endoplasmic reticulum membrane	TAS PMID:16280320 DPM1, the catalytic subunit of dolichol-phosphate mannose sy...	ACCEPT	Summary: TAS ER membrane localization. Consistent with the ER-membrane setting of the DPM synthase and GPI-GnT complexes. Reason: Consistent with the well-established ER membrane localization of DPM2. Supporting Evidence: PMID:16280320 tethered file:human/DPM2/DPM2-uniprot.txt Endoplasmic reticulum membrane; Multi-pass
GO:0005789 endoplasmic reticulum membrane	TAS PMID:9724629 DPM2 regulates biosynthesis of dolichol phosphate-mannose in...	ACCEPT	Summary: TAS ER membrane localization from the original DPM2 characterization, which described DPM2 as an ER-expressed membrane protein. Reason: Core cellular location, supported by the primary DPM2 paper and consistent with multi-pass ER membrane topology. Supporting Evidence: PMID:9724629 DPM2, an 84 amino acid file:human/DPM2/DPM2-uniprot.txt Endoplasmic reticulum membrane; Multi-pass

Gene Description

Existing Annotations Review

Core Functions

References

📚 Additional Documentation

Notes

📄 View Raw YAML