DARS2

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0000049 tRNA binding	TAS PMID:15779907 Toward the full set of human mitochondrial aminoacyl-tRNA sy...	ACCEPT	Summary: tRNA binding: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Reason: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Supporting Evidence: PMID:15779907 Both belong to the expected class of synthetases, have a dimeric organization, and aminoacylate Escherichia coli tRNAs as well as in vitro transcribed human mitochondrial tRNAs.
GO:0000166 nucleotide binding	IEA GO_REF:0000002	KEEP AS NON CORE	Summary: nucleotide binding: This is a broad compatible binding or cellular-compartment annotation; the core function is ATP-dependent mitochondrial tRNA(Asp) aminoacylation. Cytoplasm does not mean specifically cytosol and need not exclude mitochondria. Reason: This is a broad compatible binding or cellular-compartment annotation; the core function is ATP-dependent mitochondrial tRNA(Asp) aminoacylation. Cytoplasm does not mean specifically cytosol and need not exclude mitochondria. Supporting Evidence: PMID:15779907 Both belong to the expected class of synthetases, have a dimeric organization, and aminoacylate Escherichia coli tRNAs as well as in vitro transcribed human mitochondrial tRNAs.
GO:0003676 nucleic acid binding	IEA GO_REF:0000002	KEEP AS NON CORE	Summary: nucleic acid binding: This is a broad compatible binding or cellular-compartment annotation; the core function is ATP-dependent mitochondrial tRNA(Asp) aminoacylation. Cytoplasm does not mean specifically cytosol and need not exclude mitochondria. Reason: This is a broad compatible binding or cellular-compartment annotation; the core function is ATP-dependent mitochondrial tRNA(Asp) aminoacylation. Cytoplasm does not mean specifically cytosol and need not exclude mitochondria. Supporting Evidence: PMID:15779907 Both belong to the expected class of synthetases, have a dimeric organization, and aminoacylate Escherichia coli tRNAs as well as in vitro transcribed human mitochondrial tRNAs.
GO:0004812 aminoacyl-tRNA ligase activity	IEA GO_REF:0000120	MODIFY	Summary: aminoacyl-tRNA ligase activity: The broad ligase activity is correct, but the experimentally established aspartate-tRNA ligase activity identifies both the amino acid and substrate class. Reason: The broad ligase activity is correct, but the experimentally established aspartate-tRNA ligase activity identifies both the amino acid and substrate class. Proposed replacements: aspartate-tRNA ligase activity Supporting Evidence: PMID:15779907 Both belong to the expected class of synthetases, have a dimeric organization, and aminoacylate Escherichia coli tRNAs as well as in vitro transcribed human mitochondrial tRNAs.
GO:0004815 aspartate-tRNA ligase activity	EXP PMID:15779907 Toward the full set of human mitochondrial aminoacyl-tRNA sy...	ACCEPT	Summary: aspartate-tRNA ligase activity: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Reason: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Supporting Evidence: PMID:15779907 Both belong to the expected class of synthetases, have a dimeric organization, and aminoacylate Escherichia coli tRNAs as well as in vitro transcribed human mitochondrial tRNAs.
GO:0004815 aspartate-tRNA ligase activity	IBA GO_REF:0000033	ACCEPT	Summary: aspartate-tRNA ligase activity: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Reason: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Supporting Evidence: PMID:15779907 Both belong to the expected class of synthetases, have a dimeric organization, and aminoacylate Escherichia coli tRNAs as well as in vitro transcribed human mitochondrial tRNAs.
GO:0004815 aspartate-tRNA ligase activity	IDA PMID:23275545 Thermodynamic properties distinguish human mitochondrial asp...	ACCEPT	Summary: aspartate-tRNA ligase activity: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Reason: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Supporting Evidence: PMID:15779907 Both belong to the expected class of synthetases, have a dimeric organization, and aminoacylate Escherichia coli tRNAs as well as in vitro transcribed human mitochondrial tRNAs.
GO:0004815 aspartate-tRNA ligase activity	IDA PMID:40814755 Biallelic Variants in the DARS2 Gene as a Novel Cause of Axo...	ACCEPT	Summary: aspartate-tRNA ligase activity: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Reason: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Supporting Evidence: PMID:15779907 Both belong to the expected class of synthetases, have a dimeric organization, and aminoacylate Escherichia coli tRNAs as well as in vitro transcribed human mitochondrial tRNAs.
GO:0004815 aspartate-tRNA ligase activity	IEA GO_REF:0000120	ACCEPT	Summary: aspartate-tRNA ligase activity: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Reason: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Supporting Evidence: PMID:15779907 Both belong to the expected class of synthetases, have a dimeric organization, and aminoacylate Escherichia coli tRNAs as well as in vitro transcribed human mitochondrial tRNAs.
GO:0005515 protein binding	IPI PMID:15779907 Toward the full set of human mitochondrial aminoacyl-tRNA sy...	UNDECIDED	Summary: protein binding: The PMID:15779907 interaction annotation does not by itself identify a molecular role for DARS2. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title. Reason: The PMID:15779907 interaction annotation does not by itself identify a molecular role for DARS2. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title.
GO:0005515 protein binding	IPI PMID:28514442 Architecture of the human interactome defines protein commun...	UNDECIDED	Summary: protein binding: The PMID:28514442 interaction annotation does not by itself identify a molecular role for DARS2. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title. Reason: The PMID:28514442 interaction annotation does not by itself identify a molecular role for DARS2. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title.
GO:0005515 protein binding	IPI PMID:28514442 Architecture of the human interactome defines protein commun...	UNDECIDED	Summary: protein binding: The PMID:28514442 interaction annotation does not by itself identify a molecular role for DARS2. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title. Reason: The PMID:28514442 interaction annotation does not by itself identify a molecular role for DARS2. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title.
GO:0005515 protein binding	IPI PMID:29568061 An AP-MS- and BioID-compatible MAC-tag enables comprehensive...	UNDECIDED	Summary: protein binding: The PMID:29568061 interaction annotation does not by itself identify a molecular role for DARS2. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title. Reason: The PMID:29568061 interaction annotation does not by itself identify a molecular role for DARS2. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title.
GO:0005515 protein binding	IPI PMID:30021884 Histone Interaction Landscapes Visualized by Crosslinking Ma...	UNDECIDED	Summary: protein binding: The PMID:30021884 interaction annotation does not by itself identify a molecular role for DARS2. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title. Reason: The PMID:30021884 interaction annotation does not by itself identify a molecular role for DARS2. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	UNDECIDED	Summary: protein binding: The PMID:32296183 interaction annotation does not by itself identify a molecular role for DARS2. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title. Reason: The PMID:32296183 interaction annotation does not by itself identify a molecular role for DARS2. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	UNDECIDED	Summary: protein binding: The PMID:32296183 interaction annotation does not by itself identify a molecular role for DARS2. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title. Reason: The PMID:32296183 interaction annotation does not by itself identify a molecular role for DARS2. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	UNDECIDED	Summary: protein binding: The PMID:32296183 interaction annotation does not by itself identify a molecular role for DARS2. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title. Reason: The PMID:32296183 interaction annotation does not by itself identify a molecular role for DARS2. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	UNDECIDED	Summary: protein binding: The PMID:32296183 interaction annotation does not by itself identify a molecular role for DARS2. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title. Reason: The PMID:32296183 interaction annotation does not by itself identify a molecular role for DARS2. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	UNDECIDED	Summary: protein binding: The PMID:32296183 interaction annotation does not by itself identify a molecular role for DARS2. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title. Reason: The PMID:32296183 interaction annotation does not by itself identify a molecular role for DARS2. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	UNDECIDED	Summary: protein binding: The PMID:32296183 interaction annotation does not by itself identify a molecular role for DARS2. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title. Reason: The PMID:32296183 interaction annotation does not by itself identify a molecular role for DARS2. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	UNDECIDED	Summary: protein binding: The PMID:32296183 interaction annotation does not by itself identify a molecular role for DARS2. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title. Reason: The PMID:32296183 interaction annotation does not by itself identify a molecular role for DARS2. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	UNDECIDED	Summary: protein binding: The PMID:32296183 interaction annotation does not by itself identify a molecular role for DARS2. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title. Reason: The PMID:32296183 interaction annotation does not by itself identify a molecular role for DARS2. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	UNDECIDED	Summary: protein binding: The PMID:32296183 interaction annotation does not by itself identify a molecular role for DARS2. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title. Reason: The PMID:32296183 interaction annotation does not by itself identify a molecular role for DARS2. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	UNDECIDED	Summary: protein binding: The PMID:32296183 interaction annotation does not by itself identify a molecular role for DARS2. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title. Reason: The PMID:32296183 interaction annotation does not by itself identify a molecular role for DARS2. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	UNDECIDED	Summary: protein binding: The PMID:32296183 interaction annotation does not by itself identify a molecular role for DARS2. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title. Reason: The PMID:32296183 interaction annotation does not by itself identify a molecular role for DARS2. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title.
GO:0005515 protein binding	IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling...	UNDECIDED	Summary: protein binding: The PMID:33961781 interaction annotation does not by itself identify a molecular role for DARS2. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title. Reason: The PMID:33961781 interaction annotation does not by itself identify a molecular role for DARS2. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title.
GO:0005515 protein binding	IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling...	UNDECIDED	Summary: protein binding: The PMID:33961781 interaction annotation does not by itself identify a molecular role for DARS2. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title. Reason: The PMID:33961781 interaction annotation does not by itself identify a molecular role for DARS2. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title.
GO:0005515 protein binding	IPI PMID:35156780 CFTR interactome mapping using the mammalian membrane two-hy...	UNDECIDED	Summary: protein binding: The PMID:35156780 interaction annotation does not by itself identify a molecular role for DARS2. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title. Reason: The PMID:35156780 interaction annotation does not by itself identify a molecular role for DARS2. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title.
GO:0005515 protein binding	IPI PMID:36012204 Differential CFTR-Interactome Proximity Labeling Procedures ...	UNDECIDED	Summary: protein binding: The PMID:36012204 interaction annotation does not by itself identify a molecular role for DARS2. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title. Reason: The PMID:36012204 interaction annotation does not by itself identify a molecular role for DARS2. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title.
GO:0005524 ATP binding	IEA GO_REF:0000002	ACCEPT	Summary: ATP binding: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Reason: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Supporting Evidence: PMID:15779907 Both belong to the expected class of synthetases, have a dimeric organization, and aminoacylate Escherichia coli tRNAs as well as in vitro transcribed human mitochondrial tRNAs.
GO:0005524 ATP binding	TAS PMID:15779907 Toward the full set of human mitochondrial aminoacyl-tRNA sy...	ACCEPT	Summary: ATP binding: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Reason: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Supporting Evidence: PMID:15779907 Both belong to the expected class of synthetases, have a dimeric organization, and aminoacylate Escherichia coli tRNAs as well as in vitro transcribed human mitochondrial tRNAs.
GO:0005737 cytoplasm	IEA GO_REF:0000120	KEEP AS NON CORE	Summary: cytoplasm: This is a broad compatible binding or cellular-compartment annotation; the core function is ATP-dependent mitochondrial tRNA(Asp) aminoacylation. Cytoplasm does not mean specifically cytosol and need not exclude mitochondria. Reason: This is a broad compatible binding or cellular-compartment annotation; the core function is ATP-dependent mitochondrial tRNA(Asp) aminoacylation. Cytoplasm does not mean specifically cytosol and need not exclude mitochondria. Supporting Evidence: PMID:15779907 Both belong to the expected class of synthetases, have a dimeric organization, and aminoacylate Escherichia coli tRNAs as well as in vitro transcribed human mitochondrial tRNAs.
GO:0005739 mitochondrion	HTP PMID:34800366 Quantitative high-confidence human mitochondrial proteome an...	ACCEPT	Summary: mitochondrion: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Reason: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Supporting Evidence: PMID:15779907 Both belong to the expected class of synthetases, have a dimeric organization, and aminoacylate Escherichia coli tRNAs as well as in vitro transcribed human mitochondrial tRNAs.
GO:0005739 mitochondrion	IBA GO_REF:0000033	ACCEPT	Summary: mitochondrion: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Reason: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Supporting Evidence: PMID:15779907 Both belong to the expected class of synthetases, have a dimeric organization, and aminoacylate Escherichia coli tRNAs as well as in vitro transcribed human mitochondrial tRNAs.
GO:0005739 mitochondrion	IDA GO_REF:0000052	ACCEPT	Summary: mitochondrion: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Reason: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Supporting Evidence: PMID:15779907 Both belong to the expected class of synthetases, have a dimeric organization, and aminoacylate Escherichia coli tRNAs as well as in vitro transcribed human mitochondrial tRNAs.
GO:0005739 mitochondrion	TAS PMID:15779907 Toward the full set of human mitochondrial aminoacyl-tRNA sy...	ACCEPT	Summary: mitochondrion: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Reason: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Supporting Evidence: PMID:15779907 Both belong to the expected class of synthetases, have a dimeric organization, and aminoacylate Escherichia coli tRNAs as well as in vitro transcribed human mitochondrial tRNAs.
GO:0005759 mitochondrial matrix	EXP PMID:15779907 Toward the full set of human mitochondrial aminoacyl-tRNA sy...	ACCEPT	Summary: mitochondrial matrix: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Reason: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Supporting Evidence: PMID:15779907 Both belong to the expected class of synthetases, have a dimeric organization, and aminoacylate Escherichia coli tRNAs as well as in vitro transcribed human mitochondrial tRNAs.
GO:0005759 mitochondrial matrix	IEA GO_REF:0000044	ACCEPT	Summary: mitochondrial matrix: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Reason: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Supporting Evidence: PMID:15779907 Both belong to the expected class of synthetases, have a dimeric organization, and aminoacylate Escherichia coli tRNAs as well as in vitro transcribed human mitochondrial tRNAs.
GO:0005759 mitochondrial matrix	IMP PMID:30006346 Three human aminoacyl-tRNA synthetases have distinct sub-mit...	ACCEPT	Summary: mitochondrial matrix: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Reason: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Supporting Evidence: PMID:15779907 Both belong to the expected class of synthetases, have a dimeric organization, and aminoacylate Escherichia coli tRNAs as well as in vitro transcribed human mitochondrial tRNAs.
GO:0005759 mitochondrial matrix	TAS Reactome:R-HSA-380229	ACCEPT	Summary: mitochondrial matrix: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Reason: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Supporting Evidence: PMID:15779907 Both belong to the expected class of synthetases, have a dimeric organization, and aminoacylate Escherichia coli tRNAs as well as in vitro transcribed human mitochondrial tRNAs.
GO:0006418 tRNA aminoacylation for protein translation	IEA GO_REF:0000002	ACCEPT	Summary: tRNA aminoacylation for protein translation: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Reason: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Supporting Evidence: PMID:15779907 Both belong to the expected class of synthetases, have a dimeric organization, and aminoacylate Escherichia coli tRNAs as well as in vitro transcribed human mitochondrial tRNAs.
GO:0006422 obsolete aspartyl-tRNA aminoacylation	IBA GO_REF:0000033	ACCEPT	Summary: obsolete aspartyl-tRNA aminoacylation: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Reason: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Supporting Evidence: PMID:15779907 Both belong to the expected class of synthetases, have a dimeric organization, and aminoacylate Escherichia coli tRNAs as well as in vitro transcribed human mitochondrial tRNAs.
GO:0016874 ligase activity	IEA GO_REF:0000002	MODIFY	Summary: ligase activity: The broad ligase activity is correct, but the experimentally established aspartate-tRNA ligase activity identifies both the amino acid and substrate class. Reason: The broad ligase activity is correct, but the experimentally established aspartate-tRNA ligase activity identifies both the amino acid and substrate class. Proposed replacements: aspartate-tRNA ligase activity Supporting Evidence: PMID:15779907 Both belong to the expected class of synthetases, have a dimeric organization, and aminoacylate Escherichia coli tRNAs as well as in vitro transcribed human mitochondrial tRNAs.
GO:0031966 mitochondrial membrane	IDA PMID:40814755 Biallelic Variants in the DARS2 Gene as a Novel Cause of Axo...	ACCEPT	Summary: Human cell fractionation and chemical extraction directly identify both soluble and membrane-associated mt-AspRS. The membrane pool is peripherally anchored through electrostatic interactions, so mitochondrial membrane is a supported location without implying an integral transmembrane protein. Reason: Human cell fractionation and chemical extraction directly identify both soluble and membrane-associated mt-AspRS. The membrane pool is peripherally anchored through electrostatic interactions, so mitochondrial membrane is a supported location without implying an integral transmembrane protein. Supporting Evidence: PMID:30006346 mt-AspRS being present in both. Chemical treatments revealed that mt-AspRs is anchored in the mitochondrial membrane through electrostatic interactions
GO:0031966 mitochondrial membrane	IEA GO_REF:0000044	ACCEPT	Summary: Human cell fractionation and chemical extraction directly identify both soluble and membrane-associated mt-AspRS. The membrane pool is peripherally anchored through electrostatic interactions, so mitochondrial membrane is a supported location without implying an integral transmembrane protein. Reason: Human cell fractionation and chemical extraction directly identify both soluble and membrane-associated mt-AspRS. The membrane pool is peripherally anchored through electrostatic interactions, so mitochondrial membrane is a supported location without implying an integral transmembrane protein. Supporting Evidence: PMID:30006346 mt-AspRS being present in both. Chemical treatments revealed that mt-AspRs is anchored in the mitochondrial membrane through electrostatic interactions
GO:0031966 mitochondrial membrane	IMP PMID:30006346 Three human aminoacyl-tRNA synthetases have distinct sub-mit...	ACCEPT	Summary: Human cell fractionation and chemical extraction directly identify both soluble and membrane-associated mt-AspRS. The membrane pool is peripherally anchored through electrostatic interactions, so mitochondrial membrane is a supported location without implying an integral transmembrane protein. Reason: Human cell fractionation and chemical extraction directly identify both soluble and membrane-associated mt-AspRS. The membrane pool is peripherally anchored through electrostatic interactions, so mitochondrial membrane is a supported location without implying an integral transmembrane protein. Supporting Evidence: PMID:30006346 mt-AspRS being present in both. Chemical treatments revealed that mt-AspRs is anchored in the mitochondrial membrane through electrostatic interactions
GO:0042803 protein homodimerization activity	IPI PMID:15779907 Toward the full set of human mitochondrial aminoacyl-tRNA sy...	ACCEPT	Summary: protein homodimerization activity: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Reason: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Supporting Evidence: PMID:15779907 Both belong to the expected class of synthetases, have a dimeric organization, and aminoacylate Escherichia coli tRNAs as well as in vitro transcribed human mitochondrial tRNAs.
GO:0042803 protein homodimerization activity	IPI PMID:23275545 Thermodynamic properties distinguish human mitochondrial asp...	ACCEPT	Summary: protein homodimerization activity: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Reason: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Supporting Evidence: PMID:15779907 Both belong to the expected class of synthetases, have a dimeric organization, and aminoacylate Escherichia coli tRNAs as well as in vitro transcribed human mitochondrial tRNAs.
GO:0043039 tRNA charging	IDA PMID:15779907 Toward the full set of human mitochondrial aminoacyl-tRNA sy...	ACCEPT	Summary: tRNA charging: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Reason: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Supporting Evidence: PMID:15779907 Both belong to the expected class of synthetases, have a dimeric organization, and aminoacylate Escherichia coli tRNAs as well as in vitro transcribed human mitochondrial tRNAs.
GO:0043039 tRNA charging	IDA PMID:17384640 Mitochondrial aspartyl-tRNA synthetase deficiency causes leu...	ACCEPT	Summary: tRNA charging: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Reason: Human DARS2 is a dimeric mitochondrial aspartate-tRNA synthetase, with direct aminoacylation and structural evidence. Binding ATP and tRNA and producing charged mitochondrial tRNA(Asp) are parts of this core reaction; mitochondrial localization is independently supported. Supporting Evidence: PMID:15779907 Both belong to the expected class of synthetases, have a dimeric organization, and aminoacylate Escherichia coli tRNAs as well as in vitro transcribed human mitochondrial tRNAs.
GO:0050560 aspartate-tRNA(Asn) ligase activity	IDA PMID:15779907 Toward the full set of human mitochondrial aminoacyl-tRNA sy...	UNDECIDED	Summary: aspartate-tRNA(Asn) ligase activity: The exact tRNA(Asn) claim requires the original substrate-specificity experiments. The cached 2005 and disease-paper abstracts do not resolve it, and the accessible structural study documents mitochondrial/bacterial tRNA(Asp) accommodation rather than tRNA(Asn) charging. Existing experimental annotations are not rejected from this incomplete evidence. Reason: The exact tRNA(Asn) claim requires the original substrate-specificity experiments. The cached 2005 and disease-paper abstracts do not resolve it, and the accessible structural study documents mitochondrial/bacterial tRNA(Asp) accommodation rather than tRNA(Asn) charging. Existing experimental annotations are not rejected from this incomplete evidence. Supporting Evidence: PMID:15779907 Both belong to the expected class of synthetases, have a dimeric organization, and aminoacylate Escherichia coli tRNAs as well as in vitro transcribed human mitochondrial tRNAs.
GO:0050560 aspartate-tRNA(Asn) ligase activity	IDA PMID:17384640 Mitochondrial aspartyl-tRNA synthetase deficiency causes leu...	UNDECIDED	Summary: aspartate-tRNA(Asn) ligase activity: The exact tRNA(Asn) claim requires the original substrate-specificity experiments. The cached 2005 and disease-paper abstracts do not resolve it, and the accessible structural study documents mitochondrial/bacterial tRNA(Asp) accommodation rather than tRNA(Asn) charging. Existing experimental annotations are not rejected from this incomplete evidence. Reason: The exact tRNA(Asn) claim requires the original substrate-specificity experiments. The cached 2005 and disease-paper abstracts do not resolve it, and the accessible structural study documents mitochondrial/bacterial tRNA(Asp) accommodation rather than tRNA(Asn) charging. Existing experimental annotations are not rejected from this incomplete evidence. Supporting Evidence: PMID:15779907 Both belong to the expected class of synthetases, have a dimeric organization, and aminoacylate Escherichia coli tRNAs as well as in vitro transcribed human mitochondrial tRNAs.
GO:0070145 obsolete mitochondrial asparaginyl-tRNA aminoacylation	IC PMID:15779907 Toward the full set of human mitochondrial aminoacyl-tRNA sy...	UNDECIDED	Summary: obsolete mitochondrial asparaginyl-tRNA aminoacylation: The exact tRNA(Asn) claim requires the original substrate-specificity experiments. The cached 2005 and disease-paper abstracts do not resolve it, and the accessible structural study documents mitochondrial/bacterial tRNA(Asp) accommodation rather than tRNA(Asn) charging. Existing experimental annotations are not rejected from this incomplete evidence. Reason: The exact tRNA(Asn) claim requires the original substrate-specificity experiments. The cached 2005 and disease-paper abstracts do not resolve it, and the accessible structural study documents mitochondrial/bacterial tRNA(Asp) accommodation rather than tRNA(Asn) charging. Existing experimental annotations are not rejected from this incomplete evidence. Supporting Evidence: PMID:15779907 Both belong to the expected class of synthetases, have a dimeric organization, and aminoacylate Escherichia coli tRNAs as well as in vitro transcribed human mitochondrial tRNAs.
GO:0070145 obsolete mitochondrial asparaginyl-tRNA aminoacylation	IDA PMID:23275545 Thermodynamic properties distinguish human mitochondrial asp...	UNDECIDED	Summary: obsolete mitochondrial asparaginyl-tRNA aminoacylation: The exact tRNA(Asn) claim requires the original substrate-specificity experiments. The cached 2005 and disease-paper abstracts do not resolve it, and the accessible structural study documents mitochondrial/bacterial tRNA(Asp) accommodation rather than tRNA(Asn) charging. Existing experimental annotations are not rejected from this incomplete evidence. Reason: The exact tRNA(Asn) claim requires the original substrate-specificity experiments. The cached 2005 and disease-paper abstracts do not resolve it, and the accessible structural study documents mitochondrial/bacterial tRNA(Asp) accommodation rather than tRNA(Asn) charging. Existing experimental annotations are not rejected from this incomplete evidence. Supporting Evidence: PMID:15779907 Both belong to the expected class of synthetases, have a dimeric organization, and aminoacylate Escherichia coli tRNAs as well as in vitro transcribed human mitochondrial tRNAs.

Gene Description

Existing Annotations Review

Core Functions

DARS2 is the nuclear-encoded mitochondrial aspartate-tRNA ligase.

References

Deep Research

Falcon

📚 Additional Documentation

Notes

📄 View Raw YAML