DNMT3L

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0000792 heterochromatin	IEA GO_REF:0000107	ACCEPT	Summary: heterochromatin: DNMT3L supports chromatin repression and de novo DNA methylation through interactions with active methyltransferases. Heterochromatin, imprinting and transposon-silencing roles do not require it to catalyze methyl transfer itself. Reason: DNMT3L supports chromatin repression and de novo DNA methylation through interactions with active methyltransferases. Heterochromatin, imprinting and transposon-silencing roles do not require it to catalyze methyl transfer itself. Supporting Evidence: PMID:12202768 We find that Dnmt3L can repress transcription and that this repression is dependent on HDAC1 and is relieved by treatment with the HDAC inhibitor trichostatin A. file:human/DNMT3L/DNMT3L-uniprot.txt CC -!- FUNCTION: Catalytically inactive regulatory factor of DNA CC methyltransferases that can either promote or inhibit DNA methylation CC depending on the context (By similarity). Essential for the function of CC DNMT3A and DNMT3B: activates DNMT3A and DNMT3B by binding to their CC catalytic domain (PubMed:17687327). Acts by accelerating the binding of CC DNA and S-adenosyl-L-methionine (AdoMet) to the methyltransferases and CC dissociates from the complex after DNA binding to the CC methyltransferases (PubMed:17687327). Recognizes unmethylated histone CC H3 lysine 4 (H3K4me0) and induces de novo DNA methylation by CC recruitment or activation of DNMT3 (PubMed:17687327). Plays a key role CC in embryonic stem cells and germ cells (By similarity). In germ cells, CC required for the methylation of imprinted loci together with DNMT3A (By CC similarity). In male germ cells, specifically required to methylate CC retrotransposons, preventing their mobilization (By similarity). Plays CC a key role in embryonic stem cells (ESCs) by acting both as an positive CC and negative regulator of DNA methylation (By similarity). While it CC promotes DNA methylation of housekeeping genes together with DNMT3A and CC DNMT3B, it also acts as an inhibitor of DNA methylation at the promoter CC of bivalent genes (By similarity). Interacts with the EZH2 component of CC the PRC2/EED-EZH2 complex, preventing interaction of DNMT3A and DNMT3B CC with the PRC2/EED-EZH2 complex, leading to maintain low methylation CC levels at the promoters of bivalent genes (By similarity). Promotes CC differentiation of ESCs into primordial germ cells by inhibiting DNA CC methylation at the promoter of RHOX5, thereby activating its expression CC (By similarity). {ECO:0000250\|UniProtKB:Q9CWR8, CC ECO:0000269\|PubMed:17687327}. CC -!- SUBUNIT:
GO:0000794 condensed nuclear chromosome	IEA GO_REF:0000107	ACCEPT	Summary: condensed nuclear chromosome: DNMT3L supports chromatin repression and de novo DNA methylation through interactions with active methyltransferases. Heterochromatin, imprinting and transposon-silencing roles do not require it to catalyze methyl transfer itself. Reason: DNMT3L supports chromatin repression and de novo DNA methylation through interactions with active methyltransferases. Heterochromatin, imprinting and transposon-silencing roles do not require it to catalyze methyl transfer itself. Supporting Evidence: PMID:12202768 We find that Dnmt3L can repress transcription and that this repression is dependent on HDAC1 and is relieved by treatment with the HDAC inhibitor trichostatin A. file:human/DNMT3L/DNMT3L-uniprot.txt CC -!- FUNCTION: Catalytically inactive regulatory factor of DNA CC methyltransferases that can either promote or inhibit DNA methylation CC depending on the context (By similarity). Essential for the function of CC DNMT3A and DNMT3B: activates DNMT3A and DNMT3B by binding to their CC catalytic domain (PubMed:17687327). Acts by accelerating the binding of CC DNA and S-adenosyl-L-methionine (AdoMet) to the methyltransferases and CC dissociates from the complex after DNA binding to the CC methyltransferases (PubMed:17687327). Recognizes unmethylated histone CC H3 lysine 4 (H3K4me0) and induces de novo DNA methylation by CC recruitment or activation of DNMT3 (PubMed:17687327). Plays a key role CC in embryonic stem cells and germ cells (By similarity). In germ cells, CC required for the methylation of imprinted loci together with DNMT3A (By CC similarity). In male germ cells, specifically required to methylate CC retrotransposons, preventing their mobilization (By similarity). Plays CC a key role in embryonic stem cells (ESCs) by acting both as an positive CC and negative regulator of DNA methylation (By similarity). While it CC promotes DNA methylation of housekeeping genes together with DNMT3A and CC DNMT3B, it also acts as an inhibitor of DNA methylation at the promoter CC of bivalent genes (By similarity). Interacts with the EZH2 component of CC the PRC2/EED-EZH2 complex, preventing interaction of DNMT3A and DNMT3B CC with the PRC2/EED-EZH2 complex, leading to maintain low methylation CC levels at the promoters of bivalent genes (By similarity). Promotes CC differentiation of ESCs into primordial germ cells by inhibiting DNA CC methylation at the promoter of RHOX5, thereby activating its expression CC (By similarity). {ECO:0000250\|UniProtKB:Q9CWR8, CC ECO:0000269\|PubMed:17687327}. CC -!- SUBUNIT:
GO:0005515 protein binding	IPI PMID:12202768 Dnmt3L is a transcriptional repressor that recruits histone ...	UNDECIDED	Summary: protein binding: The PMID:12202768 interaction annotation does not by itself identify a molecular role for DNMT3L. 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:12202768 interaction annotation does not by itself identify a molecular role for DNMT3L. 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:16189514 Towards a proteome-scale map of the human protein-protein in...	UNDECIDED	Summary: protein binding: The PMID:16189514 interaction annotation does not by itself identify a molecular role for DNMT3L. 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:16189514 interaction annotation does not by itself identify a molecular role for DNMT3L. 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:17713477 Structure of Dnmt3a bound to Dnmt3L suggests a model for de ...	UNDECIDED	Summary: protein binding: The PMID:17713477 interaction annotation does not by itself identify a molecular role for DNMT3L. 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:17713477 interaction annotation does not by itself identify a molecular role for DNMT3L. 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:25416956 A proteome-scale map of the human interactome network.	UNDECIDED	Summary: protein binding: The PMID:25416956 interaction annotation does not by itself identify a molecular role for DNMT3L. 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:25416956 interaction annotation does not by itself identify a molecular role for DNMT3L. 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 DNMT3L. 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 DNMT3L. 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 DNMT3L. 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 DNMT3L. 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:0005634 nucleus	HDA PMID:16780588 Cell array-based intracellular localization screening reveal...	ACCEPT	Summary: nucleus: DNMT3L is a noncatalytic chromatin-associated regulator. Direct experiments support transcriptional repression via HDAC1 and activation of DNA methyltransferases through protein interaction; absence of intrinsic methyltransferase activity is compatible with these annotations. Reason: DNMT3L is a noncatalytic chromatin-associated regulator. Direct experiments support transcriptional repression via HDAC1 and activation of DNA methyltransferases through protein interaction; absence of intrinsic methyltransferase activity is compatible with these annotations. Supporting Evidence: PMID:12202768 We find that Dnmt3L can repress transcription and that this repression is dependent on HDAC1 and is relieved by treatment with the HDAC inhibitor trichostatin A. PMID:16543361 the two related methyltransferases DNMT3A and DNMT3B by regulatory factors including DNMT3L which has a stimulatory effect.
GO:0005634 nucleus	IBA GO_REF:0000033	ACCEPT	Summary: nucleus: DNMT3L is a noncatalytic chromatin-associated regulator. Direct experiments support transcriptional repression via HDAC1 and activation of DNA methyltransferases through protein interaction; absence of intrinsic methyltransferase activity is compatible with these annotations. Reason: DNMT3L is a noncatalytic chromatin-associated regulator. Direct experiments support transcriptional repression via HDAC1 and activation of DNA methyltransferases through protein interaction; absence of intrinsic methyltransferase activity is compatible with these annotations. Supporting Evidence: PMID:12202768 We find that Dnmt3L can repress transcription and that this repression is dependent on HDAC1 and is relieved by treatment with the HDAC inhibitor trichostatin A. PMID:16543361 the two related methyltransferases DNMT3A and DNMT3B by regulatory factors including DNMT3L which has a stimulatory effect.
GO:0005634 nucleus	IEA GO_REF:0000120	ACCEPT	Summary: nucleus: DNMT3L is a noncatalytic chromatin-associated regulator. Direct experiments support transcriptional repression via HDAC1 and activation of DNA methyltransferases through protein interaction; absence of intrinsic methyltransferase activity is compatible with these annotations. Reason: DNMT3L is a noncatalytic chromatin-associated regulator. Direct experiments support transcriptional repression via HDAC1 and activation of DNA methyltransferases through protein interaction; absence of intrinsic methyltransferase activity is compatible with these annotations. Supporting Evidence: PMID:12202768 We find that Dnmt3L can repress transcription and that this repression is dependent on HDAC1 and is relieved by treatment with the HDAC inhibitor trichostatin A. PMID:16543361 the two related methyltransferases DNMT3A and DNMT3B by regulatory factors including DNMT3L which has a stimulatory effect.
GO:0005634 nucleus	NAS PMID:12202768 Dnmt3L is a transcriptional repressor that recruits histone ...	ACCEPT	Summary: nucleus: DNMT3L is a noncatalytic chromatin-associated regulator. Direct experiments support transcriptional repression via HDAC1 and activation of DNA methyltransferases through protein interaction; absence of intrinsic methyltransferase activity is compatible with these annotations. Reason: DNMT3L is a noncatalytic chromatin-associated regulator. Direct experiments support transcriptional repression via HDAC1 and activation of DNA methyltransferases through protein interaction; absence of intrinsic methyltransferase activity is compatible with these annotations. Supporting Evidence: PMID:12202768 We find that Dnmt3L can repress transcription and that this repression is dependent on HDAC1 and is relieved by treatment with the HDAC inhibitor trichostatin A. PMID:16543361 the two related methyltransferases DNMT3A and DNMT3B by regulatory factors including DNMT3L which has a stimulatory effect.
GO:0005634 nucleus	NAS PMID:25383530 Structural insight into autoinhibition and histone H3-induce...	ACCEPT	Summary: nucleus: DNMT3L is a noncatalytic chromatin-associated regulator. Direct experiments support transcriptional repression via HDAC1 and activation of DNA methyltransferases through protein interaction; absence of intrinsic methyltransferase activity is compatible with these annotations. Reason: DNMT3L is a noncatalytic chromatin-associated regulator. Direct experiments support transcriptional repression via HDAC1 and activation of DNA methyltransferases through protein interaction; absence of intrinsic methyltransferase activity is compatible with these annotations. Supporting Evidence: PMID:12202768 We find that Dnmt3L can repress transcription and that this repression is dependent on HDAC1 and is relieved by treatment with the HDAC inhibitor trichostatin A. PMID:16543361 the two related methyltransferases DNMT3A and DNMT3B by regulatory factors including DNMT3L which has a stimulatory effect.
GO:0005634 nucleus	NAS PMID:32083663 Structural insights into CpG-specific DNA methylation by hum...	ACCEPT	Summary: nucleus: DNMT3L is a noncatalytic chromatin-associated regulator. Direct experiments support transcriptional repression via HDAC1 and activation of DNA methyltransferases through protein interaction; absence of intrinsic methyltransferase activity is compatible with these annotations. Reason: DNMT3L is a noncatalytic chromatin-associated regulator. Direct experiments support transcriptional repression via HDAC1 and activation of DNA methyltransferases through protein interaction; absence of intrinsic methyltransferase activity is compatible with these annotations. Supporting Evidence: PMID:12202768 We find that Dnmt3L can repress transcription and that this repression is dependent on HDAC1 and is relieved by treatment with the HDAC inhibitor trichostatin A. PMID:16543361 the two related methyltransferases DNMT3A and DNMT3B by regulatory factors including DNMT3L which has a stimulatory effect.
GO:0005737 cytoplasm	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: cytoplasm: This broad location or complex class is compatible with DNMT3L trafficking and interaction with catalytic enzymes; it does not imply that DNMT3L itself is catalytically active. Reason: This broad location or complex class is compatible with DNMT3L trafficking and interaction with catalytic enzymes; it does not imply that DNMT3L itself is catalytically active. Supporting Evidence: PMID:12202768 We find that Dnmt3L can repress transcription and that this repression is dependent on HDAC1 and is relieved by treatment with the HDAC inhibitor trichostatin A.
GO:0005737 cytoplasm	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: cytoplasm: This broad location or complex class is compatible with DNMT3L trafficking and interaction with catalytic enzymes; it does not imply that DNMT3L itself is catalytically active. Reason: This broad location or complex class is compatible with DNMT3L trafficking and interaction with catalytic enzymes; it does not imply that DNMT3L itself is catalytically active. Supporting Evidence: PMID:12202768 We find that Dnmt3L can repress transcription and that this repression is dependent on HDAC1 and is relieved by treatment with the HDAC inhibitor trichostatin A.
GO:0005829 cytosol	HDA PMID:16780588 Cell array-based intracellular localization screening reveal...	KEEP AS NON CORE	Summary: cytosol: This broad location or complex class is compatible with DNMT3L trafficking and interaction with catalytic enzymes; it does not imply that DNMT3L itself is catalytically active. Reason: This broad location or complex class is compatible with DNMT3L trafficking and interaction with catalytic enzymes; it does not imply that DNMT3L itself is catalytically active. Supporting Evidence: PMID:12202768 We find that Dnmt3L can repress transcription and that this repression is dependent on HDAC1 and is relieved by treatment with the HDAC inhibitor trichostatin A.
GO:0006346 DNA methylation-dependent constitutive heterochromatin formation	IEA GO_REF:0000107	ACCEPT	Summary: DNA methylation-dependent constitutive heterochromatin formation: DNMT3L supports chromatin repression and de novo DNA methylation through interactions with active methyltransferases. Heterochromatin, imprinting and transposon-silencing roles do not require it to catalyze methyl transfer itself. Reason: DNMT3L supports chromatin repression and de novo DNA methylation through interactions with active methyltransferases. Heterochromatin, imprinting and transposon-silencing roles do not require it to catalyze methyl transfer itself. Supporting Evidence: PMID:12202768 We find that Dnmt3L can repress transcription and that this repression is dependent on HDAC1 and is relieved by treatment with the HDAC inhibitor trichostatin A. file:human/DNMT3L/DNMT3L-uniprot.txt CC -!- FUNCTION: Catalytically inactive regulatory factor of DNA CC methyltransferases that can either promote or inhibit DNA methylation CC depending on the context (By similarity). Essential for the function of CC DNMT3A and DNMT3B: activates DNMT3A and DNMT3B by binding to their CC catalytic domain (PubMed:17687327). Acts by accelerating the binding of CC DNA and S-adenosyl-L-methionine (AdoMet) to the methyltransferases and CC dissociates from the complex after DNA binding to the CC methyltransferases (PubMed:17687327). Recognizes unmethylated histone CC H3 lysine 4 (H3K4me0) and induces de novo DNA methylation by CC recruitment or activation of DNMT3 (PubMed:17687327). Plays a key role CC in embryonic stem cells and germ cells (By similarity). In germ cells, CC required for the methylation of imprinted loci together with DNMT3A (By CC similarity). In male germ cells, specifically required to methylate CC retrotransposons, preventing their mobilization (By similarity). Plays CC a key role in embryonic stem cells (ESCs) by acting both as an positive CC and negative regulator of DNA methylation (By similarity). While it CC promotes DNA methylation of housekeeping genes together with DNMT3A and CC DNMT3B, it also acts as an inhibitor of DNA methylation at the promoter CC of bivalent genes (By similarity). Interacts with the EZH2 component of CC the PRC2/EED-EZH2 complex, preventing interaction of DNMT3A and DNMT3B CC with the PRC2/EED-EZH2 complex, leading to maintain low methylation CC levels at the promoters of bivalent genes (By similarity). Promotes CC differentiation of ESCs into primordial germ cells by inhibiting DNA CC methylation at the promoter of RHOX5, thereby activating its expression CC (By similarity). {ECO:0000250\|UniProtKB:Q9CWR8, CC ECO:0000269\|PubMed:17687327}. CC -!- SUBUNIT:
GO:0006346 DNA methylation-dependent constitutive heterochromatin formation	ISS GO_REF:0000024	ACCEPT	Summary: DNA methylation-dependent constitutive heterochromatin formation: DNMT3L supports chromatin repression and de novo DNA methylation through interactions with active methyltransferases. Heterochromatin, imprinting and transposon-silencing roles do not require it to catalyze methyl transfer itself. Reason: DNMT3L supports chromatin repression and de novo DNA methylation through interactions with active methyltransferases. Heterochromatin, imprinting and transposon-silencing roles do not require it to catalyze methyl transfer itself. Supporting Evidence: PMID:12202768 We find that Dnmt3L can repress transcription and that this repression is dependent on HDAC1 and is relieved by treatment with the HDAC inhibitor trichostatin A. file:human/DNMT3L/DNMT3L-uniprot.txt CC -!- FUNCTION: Catalytically inactive regulatory factor of DNA CC methyltransferases that can either promote or inhibit DNA methylation CC depending on the context (By similarity). Essential for the function of CC DNMT3A and DNMT3B: activates DNMT3A and DNMT3B by binding to their CC catalytic domain (PubMed:17687327). Acts by accelerating the binding of CC DNA and S-adenosyl-L-methionine (AdoMet) to the methyltransferases and CC dissociates from the complex after DNA binding to the CC methyltransferases (PubMed:17687327). Recognizes unmethylated histone CC H3 lysine 4 (H3K4me0) and induces de novo DNA methylation by CC recruitment or activation of DNMT3 (PubMed:17687327). Plays a key role CC in embryonic stem cells and germ cells (By similarity). In germ cells, CC required for the methylation of imprinted loci together with DNMT3A (By CC similarity). In male germ cells, specifically required to methylate CC retrotransposons, preventing their mobilization (By similarity). Plays CC a key role in embryonic stem cells (ESCs) by acting both as an positive CC and negative regulator of DNA methylation (By similarity). While it CC promotes DNA methylation of housekeeping genes together with DNMT3A and CC DNMT3B, it also acts as an inhibitor of DNA methylation at the promoter CC of bivalent genes (By similarity). Interacts with the EZH2 component of CC the PRC2/EED-EZH2 complex, preventing interaction of DNMT3A and DNMT3B CC with the PRC2/EED-EZH2 complex, leading to maintain low methylation CC levels at the promoters of bivalent genes (By similarity). Promotes CC differentiation of ESCs into primordial germ cells by inhibiting DNA CC methylation at the promoter of RHOX5, thereby activating its expression CC (By similarity). {ECO:0000250\|UniProtKB:Q9CWR8, CC ECO:0000269\|PubMed:17687327}. CC -!- SUBUNIT:
GO:0007141 male meiosis I	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: male meiosis I: The developmental/germ-cell phenotype is compatible with DNMT3L-dependent epigenetic regulation, but the mechanistic core is noncatalytic regulation of chromatin and DNA methyltransferases. Reason: The developmental/germ-cell phenotype is compatible with DNMT3L-dependent epigenetic regulation, but the mechanistic core is noncatalytic regulation of chromatin and DNA methyltransferases. Supporting Evidence: PMID:12202768 We find that Dnmt3L can repress transcription and that this repression is dependent on HDAC1 and is relieved by treatment with the HDAC inhibitor trichostatin A.
GO:0007141 male meiosis I	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: male meiosis I: The developmental/germ-cell phenotype is compatible with DNMT3L-dependent epigenetic regulation, but the mechanistic core is noncatalytic regulation of chromatin and DNA methyltransferases. Reason: The developmental/germ-cell phenotype is compatible with DNMT3L-dependent epigenetic regulation, but the mechanistic core is noncatalytic regulation of chromatin and DNA methyltransferases. Supporting Evidence: PMID:12202768 We find that Dnmt3L can repress transcription and that this repression is dependent on HDAC1 and is relieved by treatment with the HDAC inhibitor trichostatin A.
GO:0007283 spermatogenesis	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: spermatogenesis: The developmental/germ-cell phenotype is compatible with DNMT3L-dependent epigenetic regulation, but the mechanistic core is noncatalytic regulation of chromatin and DNA methyltransferases. Reason: The developmental/germ-cell phenotype is compatible with DNMT3L-dependent epigenetic regulation, but the mechanistic core is noncatalytic regulation of chromatin and DNA methyltransferases. Supporting Evidence: PMID:12202768 We find that Dnmt3L can repress transcription and that this repression is dependent on HDAC1 and is relieved by treatment with the HDAC inhibitor trichostatin A.
GO:0008047 enzyme activator activity	IBA GO_REF:0000033	ACCEPT	Summary: enzyme activator activity: DNMT3L is a noncatalytic chromatin-associated regulator. Direct experiments support transcriptional repression via HDAC1 and activation of DNA methyltransferases through protein interaction; absence of intrinsic methyltransferase activity is compatible with these annotations. Reason: DNMT3L is a noncatalytic chromatin-associated regulator. Direct experiments support transcriptional repression via HDAC1 and activation of DNA methyltransferases through protein interaction; absence of intrinsic methyltransferase activity is compatible with these annotations. Supporting Evidence: PMID:12202768 We find that Dnmt3L can repress transcription and that this repression is dependent on HDAC1 and is relieved by treatment with the HDAC inhibitor trichostatin A. PMID:16543361 the two related methyltransferases DNMT3A and DNMT3B by regulatory factors including DNMT3L which has a stimulatory effect.
GO:0008047 enzyme activator activity	IDA PMID:16543361 Mutations in DNA methyltransferase DNMT3B in ICF syndrome af...	ACCEPT	Summary: enzyme activator activity: DNMT3L is a noncatalytic chromatin-associated regulator. Direct experiments support transcriptional repression via HDAC1 and activation of DNA methyltransferases through protein interaction; absence of intrinsic methyltransferase activity is compatible with these annotations. Reason: DNMT3L is a noncatalytic chromatin-associated regulator. Direct experiments support transcriptional repression via HDAC1 and activation of DNA methyltransferases through protein interaction; absence of intrinsic methyltransferase activity is compatible with these annotations. Supporting Evidence: PMID:12202768 We find that Dnmt3L can repress transcription and that this repression is dependent on HDAC1 and is relieved by treatment with the HDAC inhibitor trichostatin A. PMID:16543361 the two related methyltransferases DNMT3A and DNMT3B by regulatory factors including DNMT3L which has a stimulatory effect.
GO:0008047 enzyme activator activity	IEA GO_REF:0000107	ACCEPT	Summary: enzyme activator activity: DNMT3L is a noncatalytic chromatin-associated regulator. Direct experiments support transcriptional repression via HDAC1 and activation of DNA methyltransferases through protein interaction; absence of intrinsic methyltransferase activity is compatible with these annotations. Reason: DNMT3L is a noncatalytic chromatin-associated regulator. Direct experiments support transcriptional repression via HDAC1 and activation of DNA methyltransferases through protein interaction; absence of intrinsic methyltransferase activity is compatible with these annotations. Supporting Evidence: PMID:12202768 We find that Dnmt3L can repress transcription and that this repression is dependent on HDAC1 and is relieved by treatment with the HDAC inhibitor trichostatin A. PMID:16543361 the two related methyltransferases DNMT3A and DNMT3B by regulatory factors including DNMT3L which has a stimulatory effect.
GO:0019899 enzyme binding	IPI PMID:12202768 Dnmt3L is a transcriptional repressor that recruits histone ...	KEEP AS NON CORE	Summary: enzyme binding: Binding to chromatin-modifying enzymes is a genuine component of DNMT3L regulation but enzyme binding alone omits the activation/repression mechanism. Reason: Binding to chromatin-modifying enzymes is a genuine component of DNMT3L regulation but enzyme binding alone omits the activation/repression mechanism. Supporting Evidence: PMID:12202768 We find that Dnmt3L can repress transcription and that this repression is dependent on HDAC1 and is relieved by treatment with the HDAC inhibitor trichostatin A.
GO:0035098 ESC/E(Z) complex	IEA GO_REF:0000107	UNDECIDED	Summary: ESC/E(Z) complex: The available evidence examined for DNMT3L does not resolve the exact claim of ESC/E(Z) complex. The specific experiment or traced orthology/phylogenetic inference behind GO_REF:0000107 is needed; the annotation is not rejected from absence in a summary or from a different main focus of the paper. Reason: The available evidence examined for DNMT3L does not resolve the exact claim of ESC/E(Z) complex. The specific experiment or traced orthology/phylogenetic inference behind GO_REF:0000107 is needed; the annotation is not rejected from absence in a summary or from a different main focus of the paper.
GO:0035098 ESC/E(Z) complex	ISS GO_REF:0000024	UNDECIDED	Summary: ESC/E(Z) complex: The available evidence examined for DNMT3L does not resolve the exact claim of ESC/E(Z) complex. The specific experiment or traced orthology/phylogenetic inference behind GO_REF:0000024 is needed; the annotation is not rejected from absence in a summary or from a different main focus of the paper. Reason: The available evidence examined for DNMT3L does not resolve the exact claim of ESC/E(Z) complex. The specific experiment or traced orthology/phylogenetic inference behind GO_REF:0000024 is needed; the annotation is not rejected from absence in a summary or from a different main focus of the paper.
GO:0045814 negative regulation of gene expression, epigenetic	IDA PMID:12202768 Dnmt3L is a transcriptional repressor that recruits histone ...	ACCEPT	Summary: negative regulation of gene expression, epigenetic: DNMT3L is a noncatalytic chromatin-associated regulator. Direct experiments support transcriptional repression via HDAC1 and activation of DNA methyltransferases through protein interaction; absence of intrinsic methyltransferase activity is compatible with these annotations. Reason: DNMT3L is a noncatalytic chromatin-associated regulator. Direct experiments support transcriptional repression via HDAC1 and activation of DNA methyltransferases through protein interaction; absence of intrinsic methyltransferase activity is compatible with these annotations. Supporting Evidence: PMID:12202768 We find that Dnmt3L can repress transcription and that this repression is dependent on HDAC1 and is relieved by treatment with the HDAC inhibitor trichostatin A. PMID:16543361 the two related methyltransferases DNMT3A and DNMT3B by regulatory factors including DNMT3L which has a stimulatory effect.
GO:0045892 negative regulation of DNA-templated transcription	IBA GO_REF:0000033	ACCEPT	Summary: negative regulation of DNA-templated transcription: DNMT3L is a noncatalytic chromatin-associated regulator. Direct experiments support transcriptional repression via HDAC1 and activation of DNA methyltransferases through protein interaction; absence of intrinsic methyltransferase activity is compatible with these annotations. Reason: DNMT3L is a noncatalytic chromatin-associated regulator. Direct experiments support transcriptional repression via HDAC1 and activation of DNA methyltransferases through protein interaction; absence of intrinsic methyltransferase activity is compatible with these annotations. Supporting Evidence: PMID:12202768 We find that Dnmt3L can repress transcription and that this repression is dependent on HDAC1 and is relieved by treatment with the HDAC inhibitor trichostatin A. PMID:16543361 the two related methyltransferases DNMT3A and DNMT3B by regulatory factors including DNMT3L which has a stimulatory effect.
GO:0048863 stem cell differentiation	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: stem cell differentiation: The developmental/germ-cell phenotype is compatible with DNMT3L-dependent epigenetic regulation, but the mechanistic core is noncatalytic regulation of chromatin and DNA methyltransferases. Reason: The developmental/germ-cell phenotype is compatible with DNMT3L-dependent epigenetic regulation, but the mechanistic core is noncatalytic regulation of chromatin and DNA methyltransferases. Supporting Evidence: PMID:12202768 We find that Dnmt3L can repress transcription and that this repression is dependent on HDAC1 and is relieved by treatment with the HDAC inhibitor trichostatin A.
GO:0048863 stem cell differentiation	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: stem cell differentiation: The developmental/germ-cell phenotype is compatible with DNMT3L-dependent epigenetic regulation, but the mechanistic core is noncatalytic regulation of chromatin and DNA methyltransferases. Reason: The developmental/germ-cell phenotype is compatible with DNMT3L-dependent epigenetic regulation, but the mechanistic core is noncatalytic regulation of chromatin and DNA methyltransferases. Supporting Evidence: PMID:12202768 We find that Dnmt3L can repress transcription and that this repression is dependent on HDAC1 and is relieved by treatment with the HDAC inhibitor trichostatin A.
GO:0071514 genomic imprinting	IEA GO_REF:0000107	ACCEPT	Summary: genomic imprinting: DNMT3L supports chromatin repression and de novo DNA methylation through interactions with active methyltransferases. Heterochromatin, imprinting and transposon-silencing roles do not require it to catalyze methyl transfer itself. Reason: DNMT3L supports chromatin repression and de novo DNA methylation through interactions with active methyltransferases. Heterochromatin, imprinting and transposon-silencing roles do not require it to catalyze methyl transfer itself. Supporting Evidence: PMID:12202768 We find that Dnmt3L can repress transcription and that this repression is dependent on HDAC1 and is relieved by treatment with the HDAC inhibitor trichostatin A. file:human/DNMT3L/DNMT3L-uniprot.txt CC -!- FUNCTION: Catalytically inactive regulatory factor of DNA CC methyltransferases that can either promote or inhibit DNA methylation CC depending on the context (By similarity). Essential for the function of CC DNMT3A and DNMT3B: activates DNMT3A and DNMT3B by binding to their CC catalytic domain (PubMed:17687327). Acts by accelerating the binding of CC DNA and S-adenosyl-L-methionine (AdoMet) to the methyltransferases and CC dissociates from the complex after DNA binding to the CC methyltransferases (PubMed:17687327). Recognizes unmethylated histone CC H3 lysine 4 (H3K4me0) and induces de novo DNA methylation by CC recruitment or activation of DNMT3 (PubMed:17687327). Plays a key role CC in embryonic stem cells and germ cells (By similarity). In germ cells, CC required for the methylation of imprinted loci together with DNMT3A (By CC similarity). In male germ cells, specifically required to methylate CC retrotransposons, preventing their mobilization (By similarity). Plays CC a key role in embryonic stem cells (ESCs) by acting both as an positive CC and negative regulator of DNA methylation (By similarity). While it CC promotes DNA methylation of housekeeping genes together with DNMT3A and CC DNMT3B, it also acts as an inhibitor of DNA methylation at the promoter CC of bivalent genes (By similarity). Interacts with the EZH2 component of CC the PRC2/EED-EZH2 complex, preventing interaction of DNMT3A and DNMT3B CC with the PRC2/EED-EZH2 complex, leading to maintain low methylation CC levels at the promoters of bivalent genes (By similarity). Promotes CC differentiation of ESCs into primordial germ cells by inhibiting DNA CC methylation at the promoter of RHOX5, thereby activating its expression CC (By similarity). {ECO:0000250\|UniProtKB:Q9CWR8, CC ECO:0000269\|PubMed:17687327}. CC -!- SUBUNIT:
GO:0071514 genomic imprinting	ISS GO_REF:0000024	ACCEPT	Summary: genomic imprinting: DNMT3L supports chromatin repression and de novo DNA methylation through interactions with active methyltransferases. Heterochromatin, imprinting and transposon-silencing roles do not require it to catalyze methyl transfer itself. Reason: DNMT3L supports chromatin repression and de novo DNA methylation through interactions with active methyltransferases. Heterochromatin, imprinting and transposon-silencing roles do not require it to catalyze methyl transfer itself. Supporting Evidence: PMID:12202768 We find that Dnmt3L can repress transcription and that this repression is dependent on HDAC1 and is relieved by treatment with the HDAC inhibitor trichostatin A. file:human/DNMT3L/DNMT3L-uniprot.txt CC -!- FUNCTION: Catalytically inactive regulatory factor of DNA CC methyltransferases that can either promote or inhibit DNA methylation CC depending on the context (By similarity). Essential for the function of CC DNMT3A and DNMT3B: activates DNMT3A and DNMT3B by binding to their CC catalytic domain (PubMed:17687327). Acts by accelerating the binding of CC DNA and S-adenosyl-L-methionine (AdoMet) to the methyltransferases and CC dissociates from the complex after DNA binding to the CC methyltransferases (PubMed:17687327). Recognizes unmethylated histone CC H3 lysine 4 (H3K4me0) and induces de novo DNA methylation by CC recruitment or activation of DNMT3 (PubMed:17687327). Plays a key role CC in embryonic stem cells and germ cells (By similarity). In germ cells, CC required for the methylation of imprinted loci together with DNMT3A (By CC similarity). In male germ cells, specifically required to methylate CC retrotransposons, preventing their mobilization (By similarity). Plays CC a key role in embryonic stem cells (ESCs) by acting both as an positive CC and negative regulator of DNA methylation (By similarity). While it CC promotes DNA methylation of housekeeping genes together with DNMT3A and CC DNMT3B, it also acts as an inhibitor of DNA methylation at the promoter CC of bivalent genes (By similarity). Interacts with the EZH2 component of CC the PRC2/EED-EZH2 complex, preventing interaction of DNMT3A and DNMT3B CC with the PRC2/EED-EZH2 complex, leading to maintain low methylation CC levels at the promoters of bivalent genes (By similarity). Promotes CC differentiation of ESCs into primordial germ cells by inhibiting DNA CC methylation at the promoter of RHOX5, thereby activating its expression CC (By similarity). {ECO:0000250\|UniProtKB:Q9CWR8, CC ECO:0000269\|PubMed:17687327}. CC -!- SUBUNIT:
GO:0090310 negative regulation of DNA methylation-dependent heterochromatin formation	IEA GO_REF:0000107	UNDECIDED	Summary: negative regulation of DNA methylation-dependent heterochromatin formation: The available evidence examined for DNMT3L does not resolve the exact claim of negative regulation of DNA methylation-dependent heterochromatin formation. The specific experiment or traced orthology/phylogenetic inference behind GO_REF:0000107 is needed; the annotation is not rejected from absence in a summary or from a different main focus of the paper. Reason: The available evidence examined for DNMT3L does not resolve the exact claim of negative regulation of DNA methylation-dependent heterochromatin formation. The specific experiment or traced orthology/phylogenetic inference behind GO_REF:0000107 is needed; the annotation is not rejected from absence in a summary or from a different main focus of the paper.
GO:0090310 negative regulation of DNA methylation-dependent heterochromatin formation	ISS GO_REF:0000024	UNDECIDED	Summary: negative regulation of DNA methylation-dependent heterochromatin formation: The available evidence examined for DNMT3L does not resolve the exact claim of negative regulation of DNA methylation-dependent heterochromatin formation. The specific experiment or traced orthology/phylogenetic inference behind GO_REF:0000024 is needed; the annotation is not rejected from absence in a summary or from a different main focus of the paper. Reason: The available evidence examined for DNMT3L does not resolve the exact claim of negative regulation of DNA methylation-dependent heterochromatin formation. The specific experiment or traced orthology/phylogenetic inference behind GO_REF:0000024 is needed; the annotation is not rejected from absence in a summary or from a different main focus of the paper.
GO:0141005 transposable element silencing by heterochromatin formation	ISS GO_REF:0000024	ACCEPT	Summary: transposable element silencing by heterochromatin formation: DNMT3L supports chromatin repression and de novo DNA methylation through interactions with active methyltransferases. Heterochromatin, imprinting and transposon-silencing roles do not require it to catalyze methyl transfer itself. Reason: DNMT3L supports chromatin repression and de novo DNA methylation through interactions with active methyltransferases. Heterochromatin, imprinting and transposon-silencing roles do not require it to catalyze methyl transfer itself. Supporting Evidence: PMID:12202768 We find that Dnmt3L can repress transcription and that this repression is dependent on HDAC1 and is relieved by treatment with the HDAC inhibitor trichostatin A. file:human/DNMT3L/DNMT3L-uniprot.txt CC -!- FUNCTION: Catalytically inactive regulatory factor of DNA CC methyltransferases that can either promote or inhibit DNA methylation CC depending on the context (By similarity). Essential for the function of CC DNMT3A and DNMT3B: activates DNMT3A and DNMT3B by binding to their CC catalytic domain (PubMed:17687327). Acts by accelerating the binding of CC DNA and S-adenosyl-L-methionine (AdoMet) to the methyltransferases and CC dissociates from the complex after DNA binding to the CC methyltransferases (PubMed:17687327). Recognizes unmethylated histone CC H3 lysine 4 (H3K4me0) and induces de novo DNA methylation by CC recruitment or activation of DNMT3 (PubMed:17687327). Plays a key role CC in embryonic stem cells and germ cells (By similarity). In germ cells, CC required for the methylation of imprinted loci together with DNMT3A (By CC similarity). In male germ cells, specifically required to methylate CC retrotransposons, preventing their mobilization (By similarity). Plays CC a key role in embryonic stem cells (ESCs) by acting both as an positive CC and negative regulator of DNA methylation (By similarity). While it CC promotes DNA methylation of housekeeping genes together with DNMT3A and CC DNMT3B, it also acts as an inhibitor of DNA methylation at the promoter CC of bivalent genes (By similarity). Interacts with the EZH2 component of CC the PRC2/EED-EZH2 complex, preventing interaction of DNMT3A and DNMT3B CC with the PRC2/EED-EZH2 complex, leading to maintain low methylation CC levels at the promoters of bivalent genes (By similarity). Promotes CC differentiation of ESCs into primordial germ cells by inhibiting DNA CC methylation at the promoter of RHOX5, thereby activating its expression CC (By similarity). {ECO:0000250\|UniProtKB:Q9CWR8, CC ECO:0000269\|PubMed:17687327}. CC -!- SUBUNIT:
GO:0141196 transposable element silencing by piRNA-mediated DNA methylation	IEA GO_REF:0000107	ACCEPT	Summary: transposable element silencing by piRNA-mediated DNA methylation: DNMT3L supports chromatin repression and de novo DNA methylation through interactions with active methyltransferases. Heterochromatin, imprinting and transposon-silencing roles do not require it to catalyze methyl transfer itself. Reason: DNMT3L supports chromatin repression and de novo DNA methylation through interactions with active methyltransferases. Heterochromatin, imprinting and transposon-silencing roles do not require it to catalyze methyl transfer itself. Supporting Evidence: PMID:12202768 We find that Dnmt3L can repress transcription and that this repression is dependent on HDAC1 and is relieved by treatment with the HDAC inhibitor trichostatin A. file:human/DNMT3L/DNMT3L-uniprot.txt CC -!- FUNCTION: Catalytically inactive regulatory factor of DNA CC methyltransferases that can either promote or inhibit DNA methylation CC depending on the context (By similarity). Essential for the function of CC DNMT3A and DNMT3B: activates DNMT3A and DNMT3B by binding to their CC catalytic domain (PubMed:17687327). Acts by accelerating the binding of CC DNA and S-adenosyl-L-methionine (AdoMet) to the methyltransferases and CC dissociates from the complex after DNA binding to the CC methyltransferases (PubMed:17687327). Recognizes unmethylated histone CC H3 lysine 4 (H3K4me0) and induces de novo DNA methylation by CC recruitment or activation of DNMT3 (PubMed:17687327). Plays a key role CC in embryonic stem cells and germ cells (By similarity). In germ cells, CC required for the methylation of imprinted loci together with DNMT3A (By CC similarity). In male germ cells, specifically required to methylate CC retrotransposons, preventing their mobilization (By similarity). Plays CC a key role in embryonic stem cells (ESCs) by acting both as an positive CC and negative regulator of DNA methylation (By similarity). While it CC promotes DNA methylation of housekeeping genes together with DNMT3A and CC DNMT3B, it also acts as an inhibitor of DNA methylation at the promoter CC of bivalent genes (By similarity). Interacts with the EZH2 component of CC the PRC2/EED-EZH2 complex, preventing interaction of DNMT3A and DNMT3B CC with the PRC2/EED-EZH2 complex, leading to maintain low methylation CC levels at the promoters of bivalent genes (By similarity). Promotes CC differentiation of ESCs into primordial germ cells by inhibiting DNA CC methylation at the promoter of RHOX5, thereby activating its expression CC (By similarity). {ECO:0000250\|UniProtKB:Q9CWR8, CC ECO:0000269\|PubMed:17687327}. CC -!- SUBUNIT:
GO:1902494 catalytic complex	IPI PMID:25383530 Structural insight into autoinhibition and histone H3-induce...	KEEP AS NON CORE	Summary: catalytic complex: This broad location or complex class is compatible with DNMT3L trafficking and interaction with catalytic enzymes; it does not imply that DNMT3L itself is catalytically active. Reason: This broad location or complex class is compatible with DNMT3L trafficking and interaction with catalytic enzymes; it does not imply that DNMT3L itself is catalytically active. Supporting Evidence: PMID:12202768 We find that Dnmt3L can repress transcription and that this repression is dependent on HDAC1 and is relieved by treatment with the HDAC inhibitor trichostatin A.
GO:1902494 catalytic complex	IPI PMID:32083663 Structural insights into CpG-specific DNA methylation by hum...	KEEP AS NON CORE	Summary: catalytic complex: This broad location or complex class is compatible with DNMT3L trafficking and interaction with catalytic enzymes; it does not imply that DNMT3L itself is catalytically active. Reason: This broad location or complex class is compatible with DNMT3L trafficking and interaction with catalytic enzymes; it does not imply that DNMT3L itself is catalytically active. Supporting Evidence: PMID:12202768 We find that Dnmt3L can repress transcription and that this repression is dependent on HDAC1 and is relieved by treatment with the HDAC inhibitor trichostatin A.

Gene Description

Existing Annotations Review

Core Functions

DNMT3L is a noncatalytic regulator of de novo DNA methyltransferases and chromatin-dependent gene repression.

References

Deep Research

Falcon

Manual

📚 Additional Documentation

Notes

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