AATF

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0005730 nucleolus	IBA GO_REF:0000033	ACCEPT	Summary: IBA annotation placing AATF in the nucleolus, supported by phylogenetic inference across multiple orthologs. AATF nucleolar localization is strongly supported by nucleolar proteomics (PMID:12429849), HPA immunofluorescence (GO_REF:0000052), cryo-EM SSU processome structure (PMID:34516797), and UniProt subcellular location annotation. Reason: Nucleolar localization is one of the best-established features of AATF. The IBA annotation is consistent with multiple lines of experimental evidence including cryo-EM structural data showing AATF as part of the nucleolar SSU processome (PMID:34516797) and nucleolar proteomics (PMID:12429849). UniProt states "Nucleus, nucleolus" as subcellular location. Supporting Evidence: PMID:34516797 The human small subunit processome mediates early maturation of the small ribosomal subunit PMID:12429849 we have carried out a proteomic analysis to draw up a list of proteins present within nucleoli of HeLa cells
GO:0045893 positive regulation of DNA-templated transcription	IEA GO_REF:0000108	ACCEPT	Summary: IEA annotation inferred from GO:0003713 (transcription coactivator activity) via inter-ontology logical links. AATF functions as a transcriptional cofactor that activates transcription of multiple target genes including p21/CDKN1A (PMID:12847090), p53/TP53 (PMID:17157788), and NRF-1 target OXPHOS genes (Sorino et al. 2026). Reason: This is a reasonable logical inference from transcription coactivator activity. AATF clearly positively regulates transcription: it displaces HDAC1 from promoters leading to activation of p21 (PMID:12847090), promotes p53 transcription after DNA damage (PMID:17157788), and the original identification showed "a Gal4-BD-AATF fusion protein exhibited strong transactivation activity" (PMID:10580117). Supporting Evidence: PMID:12847090 Che-1 activates p21WAF1/Cip1 by displacing histone deacetylase (HDAC)1 from the Sp1 binding sites of the p21WAF1/Cip1 gene promoter PMID:17157788 These Che-1 modifications induce a specific recruitment of Che-1 on the TP53 and p21 promoters PMID:10580117 a Gal4-BD-AATF fusion protein exhibited strong transactivation activity file:human/AATF/AATF-deep-research-falcon.md AATF physically interacts with NRF-1 and is required for NRF-1-mediated transcription of nuclear-encoded OXPHOS genes by affecting RNA polymerase II recruitment (Sorino et al. 2026)
GO:0003713 transcription coactivator activity	IEA GO_REF:0000107	ACCEPT	Summary: IEA annotation transferred from mouse ortholog via Ensembl Compara. AATF/Che-1 acts as a transcriptional cofactor that binds RNA polymerase II subunit POLR2J (PMID:10783144), displaces HDAC1 from promoters to activate transcription of p21 (PMID:12847090), and cooperates with NRF-1 for OXPHOS gene transcription (Sorino et al. 2026). Reason: Transcription coactivator activity is a well-supported core function of AATF. The protein binds RNA Pol II via POLR2J, interacts with sequence-specific transcription factors (SP1, NRF-1, Rb family), and activates transcription from multiple promoters. The original Gal4-AATF fusion showed "strong transactivation activity" (PMID:10580117). Supporting Evidence: PMID:10783144 Here we describe Che-1, a novel human protein that interacts with hRPB11 PMID:12847090 Che-1 is a recently identified human RNA polymerase II binding protein involved in the regulation of gene transcription and cell proliferation
GO:0005667 transcription regulator complex	IEA GO_REF:0000107	ACCEPT	Summary: IEA annotation transferred from mouse ortholog. AATF interacts with SAGA/ATAC HAT module subunits (ADA2A, ADA2B, GCN5/KAT2A) (PMID:29232376) and with Rb/E2F complexes (PMID:10783144, PMID:12450794), consistent with participation in transcription regulator complexes. Reason: AATF is documented to interact with components of SAGA/ATAC complexes (PMID:29232376) and with Rb-containing transcriptional regulatory complexes. The term is appropriately broad to capture these associations. However, the SSU processome (GO:0032040) is the more structurally defined complex membership, covered by a separate annotation. Supporting Evidence: PMID:29232376 Co-immunoprecipitation and co-localization experiments were used to demonstrate association of AATF both with two ADA2 isoforms, ADA2A and ADA2B and with GCN5 proteins PMID:10783144 these results identify a novel protein that binds Rb and the core of pol II, and suggest that Che-1 may be part of transcription regulatory complex
GO:0005737 cytoplasm	IEA GO_REF:0000107	ACCEPT	Summary: IEA annotation transferred from mouse ortholog. Cytoplasmic localization of AATF has been shown by IDA in PMID:14627703 and PMID:15207272, and PMID:22909821 showed that AATF is sequestered in the cytoplasm by MRLC3 and released to the nucleus upon MK2 phosphorylation after genotoxic stress. Reason: Cytoplasmic localization is supported by multiple IDA annotations from focused studies. The IEA annotation is consistent with the experimental evidence. Supporting Evidence: PMID:14627703 AATF colocalizes with Par-4 in both cytoplasmic and nuclear compartments PMID:22909821 AATF is phosphorylated by the checkpoint kinase MK2. Phosphorylation results in the release of AATF from cytoplasmic MRLC3 and subsequent nuclear translocation
GO:0030968 endoplasmic reticulum unfolded protein response	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: IEA annotation transferred from mouse ortholog via Ensembl Compara. The role of AATF in the UPR is directly supported by Ishigaki et al. 2010 (PMID:19911006), which showed that AATF is induced by ER stress through the PERK-eIF2alpha pathway and acts as an antiapoptotic transcriptional cofactor that drives AKT1 expression via STAT3 in pancreatic beta-cells. Knockdown of AATF sensitizes cells to ER stress-mediated death. Reason: The UPR/antiapoptotic role is well-supported experimentally (PMID:19911006) but is a context-specific secondary function of AATF rather than a core activity. AATF's core functions are SSU processome / 40S ribosome biogenesis (PMID:34516797) and transcription coactivator activity at TP53/CDKN1A and other promoters (PMID:12847090, PMID:17157788). The UPR contribution is downstream of the more general transcription coactivator activity acting on the AKT1 promoter via STAT3, so it is appropriately retained as non-core rather than promoted to a core function. In a proteostasis-network context, this evidence supports a stress-response regulatory role only; it does not justify annotating AATF as a chaperone, protein-folding factor, or core ER protein-quality-control component. Supporting Evidence: PMID:19911006 AATF is induced by ER stress through the PERK-eIF2alpha pathway and transcriptionally activates the v-akt murine thymoma viral oncogene homolog 1 (AKT1) gene through signal transducer and activator of transcription 3 (Stat3), which sustains Akt1 activation and promotes cell survival PMID:19911006 RNAi-mediated knockdown of AATF or AKT1 renders cells sensitive to ER stress
GO:0005515 protein binding	IPI PMID:12847090 Che-1 arrests human colon carcinoma cell proliferation by di...	MODIFY	Summary: Protein binding annotation based on interaction with SP1 (UniProtKB:P08047) from PMID:12847090. Che-1/AATF interacts with SP1 at the p21 promoter and displaces HDAC1 from SP1 binding sites. Reason: The interaction with SP1 is well-documented and functionally significant -- AATF displaces HDAC1 from SP1-bound promoter regions. However, "protein binding" is uninformative per curation guidelines. A more specific term should capture the transcription cofactor nature of this interaction. Proposed replacements: transcription coactivator activity Supporting Evidence: PMID:12847090 Che-1 activates p21WAF1/Cip1 by displacing histone deacetylase (HDAC)1 from the Sp1 binding sites of the p21WAF1/Cip1 gene promoter and accumulating acetylated histone H3 on these sites
GO:0005515 protein binding	IPI PMID:17157788 Che-1 phosphorylation by ATM/ATR and Chk2 kinases activates ...	KEEP AS NON CORE	Summary: Protein binding annotation covering interactions with CHEK2 (O96017), RELA (Q04206), and ATM (Q13315) from PMID:17157788. The checkpoint kinases ATM/ATR and Chk2 interact with and phosphorylate Che-1 in response to DNA damage, promoting its accumulation and recruitment to TP53 and p21 promoters. Reason: The interactions with ATM, ATR, and CHEK2 are well-documented and functionally important for the DNA damage response. These represent kinase-substrate relationships rather than core molecular function of AATF. The interactions are real but "protein binding" does not capture the biology. These are better described by the BP annotation for DNA damage response context. Keeping as non-core since these reflect AATF being a substrate of checkpoint kinases rather than defining AATF's own molecular function. Supporting Evidence: PMID:17157788 The checkpoint kinases ATM/ATR and Chk2 interact with Che-1 and promote its phosphorylation and accumulation in response to DNA damage
GO:0005515 protein binding	IPI PMID:22909821 AATF/Che-1 acts as a phosphorylation-dependent molecular mod...	KEEP AS NON CORE	Summary: Protein binding annotation based on interaction with MRLC3/Myl12a (Q6ZWQ9) from PMID:22909821. AATF is sequestered in the cytoplasm by MRLC3, and MK2-dependent phosphorylation releases AATF for nuclear translocation after genotoxic stress. Reason: This is a genuine interaction with a cytoplasmic sequestration partner. The interaction with MRLC3 is specific and functionally characterized -- it regulates AATF nucleocytoplasmic distribution. However, this reflects regulation of AATF localization rather than a core molecular function. Supporting Evidence: PMID:22909821 Phosphorylation results in the release of AATF from cytoplasmic MRLC3 and subsequent nuclear translocation
GO:0005515 protein binding	IPI PMID:25416956 A proteome-scale map of the human interactome network.	KEEP AS NON CORE	Summary: Protein binding annotation based on interaction with NGDN (Q8NEJ9) from the HI-II-14 proteome-scale human interactome map (PMID:25416956). NGDN (Neuroguidin/Ngd1) is a ribosome biogenesis factor. This interaction is supported by multiple independent studies (also PMID:30021884, PMID:33961781, PMID:35271311). Reason: The AATF-NGDN interaction is notable because NGDN is also a component of the SSU processome, consistent with AATF's role in ribosome biogenesis. The interaction is reproduced across four independent high-throughput studies. However, "protein binding" is uninformative. This interaction likely reflects their co-participation in the SSU processome complex. Supporting Evidence: PMID:25416956 a systematic map of ~14,000 high-quality human binary protein-protein interactions
GO:0005515 protein binding	IPI PMID:29232376 Che1/AATF interacts with subunits of the histone acetyltrans...	KEEP AS NON CORE	Summary: Protein binding annotations based on interactions with SAGA/ATAC HAT module subunits TADA2A (O75478), TADA3 (O75528), TADA2B (Q86TJ2), and KAT2A/GCN5 (Q92830) from PMID:29232376. The study used co-immunoprecipitation, co-localization, and yeast two-hybrid assays to demonstrate these interactions. Reason: These interactions with SAGA/ATAC complex subunits are well-supported by multiple experimental approaches (co-IP, co-localization, Y2H). They suggest AATF participates in HAT-containing transcriptional regulatory complexes. While these support the transcription regulator complex (GO:0005667) CC annotation, the generic "protein binding" term does not add informative annotation beyond what is already captured by the MF and CC terms. Supporting Evidence: PMID:29232376 Co-immunoprecipitation and co-localization experiments were used to demonstrate association of AATF both with two ADA2 isoforms, ADA2A and ADA2B and with GCN5 proteins in human cells
GO:0005515 protein binding	IPI PMID:30021884 Histone Interaction Landscapes Visualized by Crosslinking Ma...	KEEP AS NON CORE	Summary: Protein binding annotation based on interaction with NGDN (Q8NEJ9) detected by crosslinking mass spectrometry in intact cell nuclei (PMID:30021884). Reason: Duplicate interaction partner (NGDN) as PMID:25416956. This crosslinking MS study provides independent confirmation of the AATF-NGDN interaction in a nuclear context, consistent with their shared role in the SSU processome.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	KEEP AS NON CORE	Summary: Protein binding annotation based on interaction with MNS1 (Q8NEH6) from a binary protein interactome reference map (PMID:32296183). MNS1 (meiosis-specific nuclear structural protein 1) is involved in cilium assembly. Reason: This interaction is from a large-scale binary interactome study. MNS1 is a meiosis/cilia protein and the biological relevance of its interaction with nuclear AATF is unclear. Keeping as non-core since the interaction is detected in a high-quality systematic screen but may not reflect a biologically meaningful interaction in normal cellular context.
GO:0005515 protein binding	IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ...	KEEP AS NON CORE	Summary: Protein binding annotations based on interactions with APP (P05067), PIK3R1 isoform 2 (P27986-2), and RAC1 (P63000) from a neurodegenerative disease-focused interactome mapping study (PMID:32814053). The AATF-APP interaction is consistent with AATF's documented role in antagonizing amyloid beta production (PMID:14627703). Reason: The APP interaction is plausible given AATF's documented role in inhibiting aberrant Abeta production through interaction with Par-4/PAWR (PMID:14627703). The PIK3R1 and RAC1 interactions are from a neurodegenerative disease-focused screen and their biological significance for AATF function is less clear. These are non-core interactions that may reflect disease-context-specific associations. Supporting Evidence: PMID:14627703 AATF inhibits aberrant production of amyloid beta peptide 1-42 by interacting directly with Par-4
GO:0005515 protein binding	IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling...	KEEP AS NON CORE	Summary: Protein binding annotation based on interaction with NGDN (Q8NEJ9) from dual proteome-scale networks (PMID:33961781). This is the third independent study detecting the AATF-NGDN interaction. Reason: Another independent confirmation of the AATF-NGDN interaction, consistent with their co-participation in the SSU processome. The reproducibility across studies strongly supports this interaction but "protein binding" remains uninformative.
GO:0005515 protein binding	IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce...	KEEP AS NON CORE	Summary: Protein binding annotation based on interaction with NGDN (Q8NEJ9) from OpenCell endogenous tagging study (PMID:35271311). Fourth independent detection of AATF-NGDN interaction. Reason: Yet another confirmation of the AATF-NGDN interaction. The repeated detection across four independent high-throughput studies (PMID:25416956, PMID:30021884, PMID:33961781, PMID:35271311) strongly validates this interaction, consistent with co-participation in the SSU processome.
GO:0005634 nucleus	IEA GO_REF:0000120	ACCEPT	Summary: IEA annotation for nuclear localization based on combined automated methods including ortholog transfer and InterPro domain mapping. Nuclear localization of AATF is extremely well established by multiple IDA studies (PMID:10580117, PMID:14627703, PMID:15207272, PMID:12429849). Reason: Nuclear localization is one of the most robustly supported features of AATF, confirmed by multiple independent IDA studies. The IEA annotation is correct and consistent with experimental data.
GO:0005730 nucleolus	IEA GO_REF:0000120	ACCEPT	Summary: IEA annotation for nucleolar localization based on combined automated methods. Nucleolar localization is well supported by proteomics (PMID:12429849), HPA immunofluorescence, and cryo-EM structure (PMID:34516797). Reason: Correct IEA annotation consistent with multiple lines of experimental evidence. Nucleolus is a key site of AATF function as part of the SSU processome.
GO:0005730 nucleolus	NAS PMID:34516797 Nucleolar maturation of the human small subunit processome.	ACCEPT	Summary: NAS annotation from ComplexPortal based on the cryo-EM SSU processome paper (PMID:34516797). The structures were obtained from nucleolar particles, firmly placing AATF in the nucleolus as part of the SSU processome. Reason: The cryo-EM structures of the human SSU processome (PMID:34516797) directly demonstrate AATF as a structural component of this nucleolar complex. The paper title itself states "Nucleolar maturation of the human small subunit processome." Supporting Evidence: PMID:34516797 this 4.5-megadalton nucleolar assembly with the distinctive ability to mature the small ribosomal subunit from within
GO:0030490 maturation of SSU-rRNA	NAS PMID:34516797 Nucleolar maturation of the human small subunit processome.	ACCEPT	Summary: NAS annotation from ComplexPortal for SSU rRNA maturation based on the SSU processome cryo-EM paper. The SSU processome mediates early maturation of the small ribosomal subunit by coupling RNA folding to RNA cleavage and processing. Reason: AATF is a structural component of the SSU processome, which mediates "early maturation of the small ribosomal subunit by coupling RNA folding to subsequent RNA cleavage and processing steps" (PMID:34516797). SSU-rRNA maturation is a core function of this complex and AATF's participation is demonstrated by the cryo-EM structure. Supporting Evidence: PMID:34516797 The human small subunit processome mediates early maturation of the small ribosomal subunit by coupling RNA folding to subsequent RNA cleavage and processing steps
GO:0005730 nucleolus	IDA GO_REF:0000052	ACCEPT	Summary: IDA annotation from HPA based on immunofluorescence data showing AATF localizes to the nucleolus. Reason: HPA immunofluorescence provides direct experimental evidence for nucleolar localization, consistent with all other evidence sources.
GO:0032040 small-subunit processome	IDA PMID:34516797 Nucleolar maturation of the human small subunit processome.	ACCEPT	Summary: IDA annotation placing AATF as part of the small-subunit processome based on cryo-EM structures at 2.7 to 3.9 angstrom resolution (PMID:34516797). AATF is directly resolved in the SSU processome particle structures. Reason: This is one of the strongest annotations for AATF. The cryo-EM structures at high resolution directly show AATF as a structural component of the SSU processome, a 4.5-MDa nucleolar assembly. The SSU processome is listed in ComplexPortal as CPX-2511 with AATF as a component. This is a core cellular component annotation. Supporting Evidence: PMID:34516797 We report the high-resolution cryo-electron microscopy structures of maturing human small subunit (SSU) processomes at resolutions of 2.7 to 3.9 angstroms
GO:0032040 small-subunit processome	NAS PMID:34516797 Nucleolar maturation of the human small subunit processome.	ACCEPT	Summary: NAS annotation from ComplexPortal placing AATF in the small-subunit (SSU) processome (CPX-2511), citing PMID:34516797 — the same cryo-EM SSU processome paper that supports the existing IDA row for GO:0032040 on this gene. Reason: The term and citation are correct and reinforce one of AATF's core functions. ComplexPortal curates AATF as a stoichiometric component of CPX-2511 (SSU processome). This NAS row duplicates the existing higher-strength IDA annotation for GO:0032040 from the same PMID; both are accepted because the term placement is unambiguous from the cryo-EM structures. Supporting Evidence: PMID:34516797 The human small subunit processome mediates early maturation of the small ribosomal subunit by coupling RNA folding to subsequent RNA cleavage and processing steps
GO:0042274 ribosomal small subunit biogenesis	IDA PMID:34516797 Nucleolar maturation of the human small subunit processome.	ACCEPT	Summary: IDA annotation for ribosomal small subunit biogenesis based on the cryo-EM SSU processome structures (PMID:34516797). As a structural component of the SSU processome, AATF participates in the maturation process that generates the small ribosomal subunit. Reason: AATF is a bona fide component of the SSU processome, which is the first precursor of the small eukaryotic ribosomal subunit. The processome mediates RNA folding, modifications, rearrangements, cleavage, and targeted degradation of pre-ribosomal RNA. This is a core biological process for AATF. Supporting Evidence: PMID:34516797 These conserved mechanisms highlight the SSU processome's impressive structural plasticity, which endows this 4.5-megadalton nucleolar assembly with the distinctive ability to mature the small ribosomal subunit from within
GO:0003723 RNA binding	HDA PMID:22658674 Insights into RNA biology from an atlas of mammalian mRNA-bi...	ACCEPT	Summary: HDA annotation for RNA binding from the mRNA interactome capture study (PMID:22658674). AATF was identified among 860 mRNA-binding proteins in HeLa cells using UV crosslinking and oligo(dT) purification. Reason: RNA binding is consistent with AATF's role as a component of the SSU processome, which processes pre-rRNA. The interactome capture identifies proteins crosslinked to poly(A) RNA, indicating mRNA binding. This is further supported by AATF's nuclear/nucleolar localization and involvement in ribosome biogenesis. The HDA evidence from a systematic mRNA interactome study is appropriate. Supporting Evidence: PMID:22658674 We identify 860 proteins that qualify as RBPs by biochemical and statistical criteria
GO:0003723 RNA binding	HDA PMID:22681889 The mRNA-bound proteome and its global occupancy profile on ...	ACCEPT	Summary: HDA annotation for RNA binding from a second independent mRNA-bound proteome study (PMID:22681889). AATF was identified among ~800 mRNA-binding proteins using photoreactive nucleotide-enhanced UV crosslinking in HEK293 cells. Reason: Independent confirmation of AATF RNA binding from a second systematic study using a different cell line (HEK293 vs HeLa in PMID:22658674). The convergent evidence from two independent high-throughput RNA interactome studies strengthens the RNA binding annotation. Supporting Evidence: PMID:22681889 Application to a human embryonic kidney cell line identified close to 800 proteins
GO:0005515 protein binding	IPI PMID:10783144 Identification of a novel partner of RNA polymerase II subun...	MODIFY	Summary: Protein binding annotation based on interactions with POLR2J (P52435) and RB1 (P06400) from PMID:10783144. Che-1/AATF was identified as a binding partner of hRPB11 (POLR2J) and shown to interact with Rb through two distinct domains, repressing Rb growth suppression by counteracting Rb-mediated inhibition of E2F1 transactivation. Reason: The interaction with POLR2J is the defining molecular function of Che-1/AATF and represents its core role as a transcriptional cofactor. "Protein binding" is uninformative. The POLR2J interaction is better captured by transcription coactivator activity, and the Rb interaction modulates transcriptional regulation. Proposed replacements: transcription coactivator activity Supporting Evidence: PMID:10783144 Here we describe Che-1, a novel human protein that interacts with hRPB11 PMID:10783144 Che-1 represses the growth suppression function of Rb, counteracting the inhibitory action of Rb on the trans-activation function of E2F1
GO:0005634 nucleus	IDA PMID:10580117 AATF, a novel transcription factor that interacts with Dlk/Z...	ACCEPT	Summary: IDA annotation for nuclear localization from the original AATF identification paper (PMID:10580117). AATF was described as a "nuclear phosphoprotein." Reason: The original identification of AATF described it as a nuclear phosphoprotein, and nuclear localization is one of the most well-established features of AATF across all subsequent studies. Supporting Evidence: PMID:10580117 we identified apoptosis antagonizing transcription factor (AATF), a nuclear phosphoprotein of 523 amino acids
GO:0005634 nucleus	IDA PMID:14627703 AATF inhibits aberrant production of amyloid beta peptide 1-...	ACCEPT	Summary: IDA annotation for nuclear localization from PMID:14627703. AATF was observed to colocalize with Par-4 in both nuclear and cytoplasmic compartments in neural cells. Reason: Direct experimental observation of AATF in the nucleus. The colocalization with Par-4 in nuclear compartments is well documented in this study. Supporting Evidence: PMID:14627703 AATF colocalizes with Par-4 in both cytoplasmic and nuclear compartments
GO:0005634 nucleus	IDA PMID:15207272 AATF protects neural cells against oxidative damage induced ...	ACCEPT	Summary: IDA annotation for nuclear localization from PMID:15207272. AATF expression was observed in cortical neurons and PC12 cells, with nuclear localization. Reason: Consistent with all other nuclear localization evidence for AATF. Supporting Evidence: PMID:15207272 AATF (apoptosis-antagonizing transcription factor), a leucine zipper protein initially identified as an interaction partner of DAP like kinase (Dlk, a member of the pro-apoptotic Death-Associated Protein kinase family), is expressed in cortical neurons and in neural PC12 cells
GO:0005737 cytoplasm	IDA PMID:14627703 AATF inhibits aberrant production of amyloid beta peptide 1-...	ACCEPT	Summary: IDA annotation for cytoplasmic localization from PMID:14627703. AATF colocalizes with Par-4 in cytoplasmic compartments in neural cells. Reason: Cytoplasmic localization is experimentally demonstrated and functionally relevant. PMID:22909821 later showed that AATF is sequestered in the cytoplasm by MRLC3 and released to the nucleus upon phosphorylation, indicating regulated nucleocytoplasmic distribution. Supporting Evidence: PMID:14627703 AATF colocalizes with Par-4 in both cytoplasmic and nuclear compartments
GO:0005737 cytoplasm	IDA PMID:15207272 AATF protects neural cells against oxidative damage induced ...	ACCEPT	Summary: IDA annotation for cytoplasmic localization from PMID:15207272. AATF was detected in cytoplasm in neural cell contexts. Reason: Consistent with cytoplasmic detection in PMID:14627703 and the regulated nucleocytoplasmic shuttling mechanism described in PMID:22909821.
GO:0043522 leucine zipper domain binding	IPI PMID:10580117 AATF, a novel transcription factor that interacts with Dlk/Z...	ACCEPT	Summary: IPI annotation for leucine zipper domain binding based on interaction with Dlk/ZIP kinase (DAPK3, O43293) from PMID:10580117. AATF was identified as an interaction partner of Dlk/ZIP kinase and contains a putative leucine zipper domain. Reason: The interaction with Dlk/ZIP kinase via the leucine zipper domain is the original basis for AATF identification. AATF "contains an extremely acidic domain and a putative leucine zipper characteristic of transcription factors" (PMID:10580117). The leucine zipper mediates the interaction with Dlk and with Par-4/PAWR. Supporting Evidence: PMID:10580117 AATF contains an extremely acidic domain and a putative leucine zipper characteristic of transcription factors
GO:0043522 leucine zipper domain binding	IPI PMID:14627703 AATF inhibits aberrant production of amyloid beta peptide 1-...	ACCEPT	Summary: IPI annotation for leucine zipper domain binding based on interaction with Par-4/PAWR (Q96IZ0) from PMID:14627703. AATF interacts directly and selectively with Par-4 via the leucine zipper domain. Reason: The leucine zipper-mediated interaction with Par-4 is well characterized and functionally significant -- the AATF/Par-4 complex formation is essential for AATF's inhibitory effect on aberrant Abeta secretion. Supporting Evidence: PMID:14627703 it interacts directly and selectively with Par-4 via the leucine zipper domain in neural cells PMID:14627703 AATF/Par-4 complex formation was essential for the inhibitory effect of AATF on aberrant Abeta secretion
GO:0005634 nucleus	IDA PMID:12429849 Functional proteomic analysis of human nucleolus.	ACCEPT	Summary: IDA annotation for nuclear localization from nucleolar proteomics study (PMID:12429849). AATF was identified among 213 nucleolar proteins in HeLa cells, which are by definition also nuclear proteins. Reason: Nucleolar proteins are a subset of nuclear proteins. The proteomic identification of AATF in purified nucleoli confirms nuclear localization. Supporting Evidence: PMID:12429849 we have carried out a proteomic analysis to draw up a list of proteins present within nucleoli of HeLa cells. This analysis allowed the identification of 213 different nucleolar proteins
GO:0006355 regulation of DNA-templated transcription	IDA PMID:12847090 Che-1 arrests human colon carcinoma cell proliferation by di...	NEW	Summary: AATF/Che-1 regulates transcription by displacing HDAC1 from promoters (PMID:12847090), modulating E2F target gene expression via Rb interaction (PMID:10783144, PMID:12450794), and activating p53 transcription after DNA damage (PMID:17157788). This is a core biological process for AATF that is not explicitly annotated in GOA at an appropriate level. Reason: While GO:0045893 (positive regulation of DNA-templated transcription) is present as IEA, there is strong direct experimental evidence for AATF in regulation of transcription. AATF can both activate (p21, p53 promoters) and repress (pro-apoptotic PUMA, BAX, BAK promoters per PMID:22909821) transcription depending on context. The parent term "regulation of DNA-templated transcription" better captures the bidirectional nature of AATF transcriptional regulation. Supporting Evidence: PMID:12847090 Che-1 arrests human colon carcinoma cell proliferation by displacing HDAC1 from the p21WAF1/CIP1 promoter PMID:22909821 AATF binds to the PUMA, BAX and BAK promoter regions to repress p53-driven expression of these pro-apoptotic genes PMID:17157788 These Che-1 modifications induce a specific recruitment of Che-1 on the TP53 and p21 promoters

Gene Description

Existing Annotations Review

Core Functions

References

Deep Research

Falcon

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