HOG1

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0001100 negative regulation of exit from mitosis	IDA PMID:32265285 Hog1 activation delays mitotic exit via phosphorylation of N...	KEEP AS NON CORE	Summary: Hog1 phosphorylates the nucleolar Cdc14 inhibitor Net1 and delays mitotic exit when cells are osmostressed in metaphase (Tognetti et al. 2020). Reason: Direct, well-supported experimental annotation (in vitro and in vivo Net1 phosphorylation, nonphosphorylatable Net1 mutant reduces viability). Hog1 carries out the regulatory step itself by phosphorylating Net1, so the regulation annotation is appropriate. It is one of several stress-coupled cell-cycle checkpoints downstream of Hog1 rather than the core osmosignaling function, so kept as non-core. Supporting Evidence: PMID:32265285 Here we show that Hog1 delays mitotic exit when cells are stressed during metaphase. PMID:32265285 Hog1 phosphorylates Net1 on T62 and S385 in vitro and in vivo.
GO:0003682 chromatin binding	IDA PMID:24508389 Control of Cdc28 CDK1 by a stress-induced lncRNA.	KEEP AS NON CORE	Summary: ChIP shows Hog1 associating with chromatin at stress-induced lncRNA promoters and at the CDC28 3' UTR / +1 nucleosome upon osmostress. Reason: Hog1 is recruited to chromatin of osmostress genes (via Hot1, Sko1 and other factors) and ChIP supports chromatin association. Hog1 has no known DNA- or histone-binding domain, so this MF reflects recruitment by transcription factors rather than an intrinsic chromatin-binding activity; the chromatin location is better expressed as a CC. The SGD curator annotation is kept, but as non-core. Supporting Evidence: PMID:24508389 Therefore, Hog1 associates to and stimulates the recruitment of RNA Pol II at the promoters of stress-induced lncRNAs. PMID:12743037 In response to high osmolarity, Hot1 targets Hog1 to specific osmostress-responsive promoters.
GO:0004672 protein kinase activity	IEA GO_REF:0000002	ACCEPT	Summary: InterPro-based protein kinase activity; Hog1 is a bona fide Ser/Thr MAP kinase. Reason: Correct though general; the more specific MAP kinase activity (GO:0004707) is annotated experimentally. Supporting Evidence: PMID:10805732 Taken together, these results indicate that Rck2 is a direct substrate for the MAPK Hog1. file:yeast/HOG1/HOG1-deep-research-falcon.md Pbs2 is the immediate upstream MAPK kinase and phosphorylates Hog1 at Thr174 and Tyr176.
GO:0004674 protein serine/threonine kinase activity	IBA GO_REF:0000033	ACCEPT	Summary: Phylogenetic inference of protein serine/threonine kinase activity for the MAPK family. Reason: Hog1 phosphorylates Ser and Thr residues on many substrates (Rck2 Ser519, Sic1, Net1 T62/S385, Dot1); the IBA placement at the MAPK node is sound. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000622075 · PANTHER:PTN000622075 SUPPORTS TRANSFER The broad PTHR24055 MAPK-family node carries generic protein Ser/Thr kinase activity across intact MAPKs and related CMGC kinases; budding yeast Hog1 retains the MAPK domain and direct Ser/Thr phosphorylation activity. Supporting Evidence: PMID:32265285 Hog1 phosphorylates Net1 on T62 and S385 in vitro and in vivo. PMID:10805732 Taken together, these results indicate that Rck2 is a direct substrate for the MAPK Hog1.
GO:0004674 protein serine/threonine kinase activity	IDA PMID:38270553 Proline-directed yeast and human MAP kinases phosphorylate t...	ACCEPT	Summary: In vitro kinase assays show Pbs2-activated Hog1 phosphorylating Dot1 at proline-adjacent Ser/Thr sites; hog1 deletion reduces Dot1 phosphorylation in vivo. Reason: Direct kinase assay evidence for Ser/Thr kinase activity; consistent with MAP kinase activity. Supporting Evidence: PMID:38270553 In vitro kinase assays showed that Hog1p phosphorylates Dot1p at multiple sites, including at several proline-adjacent sites that are consistent with known Hog1p substrate preferences.
GO:0004707 MAP kinase activity	IDA PMID:10805732 Rck2 kinase is a substrate for the osmotic stress-activated ...	ACCEPT	Summary: Pbs2-activated Hog1 directly phosphorylates Rck2 at Ser519 in vitro, increasing Rck2 activity. Reason: Core molecular function. Hog1 is the terminal MAPK of the HOG cascade, activated by Pbs2 dual phosphorylation of the TGY motif, and directly phosphorylates downstream substrates. Supporting Evidence: PMID:10805732 Taken together, these results indicate that Rck2 is a direct substrate for the MAPK Hog1. file:yeast/HOG1/HOG1-deep-research-falcon.md Pbs2 is the immediate upstream MAPK kinase and phosphorylates Hog1 at Thr174 and Tyr176.
GO:0004707 MAP kinase activity	IDA PMID:32265285 Hog1 activation delays mitotic exit via phosphorylation of N...	ACCEPT	Summary: Hog1 phosphorylates Net1 on T62 and S385 in vitro and in vivo. Reason: Core molecular function; direct substrate phosphorylation by the activated MAPK. Supporting Evidence: PMID:32265285 Hog1 phosphorylates Net1 on T62 and S385 in vitro and in vivo.
GO:0004707 MAP kinase activity	IEA GO_REF:0000120	ACCEPT	Summary: Combined automated inference (InterPro MAPK signatures, EC 2.7.11.24) of MAP kinase activity. Reason: Consistent with the experimental evidence; Hog1 is a TGY-type MAPK. Supporting Evidence: file:yeast/HOG1/HOG1-deep-research-falcon.md Pbs2 is the immediate upstream MAPK kinase and phosphorylates Hog1 at Thr174 and Tyr176.
GO:0005515 protein binding	IPI PMID:10409737 Osmotic stress-induced gene expression in Saccharomyces cere...	MODIFY	Summary: Two-hybrid interaction of Hog1 with the osmostress transcription factor Hot1. Reason: Bare protein binding is uninformative. The partner Hot1 is a Pol II-specific DNA-binding transcription activator that later work showed recruits Hog1 to osmostress promoters, so the informative MF is RNA polymerase II-specific DNA-binding transcription factor binding. Note the original paper itself could not confirm the interaction biochemically. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding Supporting Evidence: PMID:10409737 In an attempt to find target proteins of the Hog1p MAP kinase, we carried out a two-hybrid screen with HOG1 coding sequences as bait. PMID:10409737 Various attempts to obtain biochemical evidence for Hog1p-Hot1p interaction by coprecipitation assays or by immunokinase assays failed (data not shown). PMID:12743037 In response to high osmolarity, Hot1 targets Hog1 to specific osmostress-responsive promoters.
GO:0005515 protein binding	IPI PMID:11805837 Systematic identification of protein complexes in Saccharomy...	MODIFY	Summary: High-throughput affinity purification/MS co-purification of Hog1 with the protein kinase Rck2. Reason: Bare protein binding is uninformative. Rck2 is a CaMK-like protein kinase that binds Hog1 via its C-terminal Hog1-binding domain and is a direct Hog1 substrate; protein kinase binding captures the interaction. Proposed replacements: protein kinase binding Supporting Evidence: PMID:11805837 Beginning with 10% of predicted yeast proteins as baits, we detected 3,617 associated proteins covering 25% of the yeast proteome. PMID:10805732 Both two-hybrid analyses and coprecipitation assays demonstrated that Hog1 binds strongly to the C-terminal region of Rck2.
GO:0005515 protein binding	IPI PMID:15448699 Hog1 mediates cell-cycle arrest in G1 phase by the dual targ...	REMOVE	Summary: Hog1 physically interacts with the CDK inhibitor Sic1 and phosphorylates it, contributing to G1 arrest under osmostress. Reason: Bare protein binding is uninformative, and Sic1 is a substrate rather than a partner defining a distinct Hog1 binding function; there is no informative binding MF for Hog1 here. Removing this generic row does not mean the interaction is false; the contact is a kinase-substrate interaction whose functional content is already carried by the MAP kinase activity annotations and the downstream process annotations. Supporting Evidence: PMID:15448699 Hog1 interacts physically with Sic1 in vivo and in vitro, and phosphorylates a single residue at the carboxyl terminus of Sic1
GO:0005515 protein binding	IPI PMID:16688223 Phosphorylation of Hsl1 by Hog1 leads to a G2 arrest essenti...	MODIFY	Summary: Activated Hog1 interacts with and phosphorylates the Hsl1 checkpoint kinase, leading to G2 arrest. Reason: Bare protein binding is uninformative. Hsl1 is a protein kinase, so protein kinase binding is the informative replacement for this kinase-kinase contact. Proposed replacements: protein kinase binding Supporting Evidence: PMID:16688223 Activated Hog1 interacts and directly phosphorylates a residue within the Hsl7-docking site of the Hsl1 checkpoint kinase
GO:0005515 protein binding	IPI PMID:18467557 An in vivo map of the yeast protein interactome.	MODIFY	Summary: Protein-fragment complementation (PCA) detects in vivo Hog1-Rck2 interaction. Reason: Bare protein binding is uninformative; Rck2 is a protein kinase and a direct Hog1 substrate, so protein kinase binding is the informative MF. Proposed replacements: protein kinase binding Supporting Evidence: PMID:18467557 We identified 2770 interactions among 1124 endogenously expressed proteins. PMID:10805732 Both two-hybrid analyses and coprecipitation assays demonstrated that Hog1 binds strongly to the C-terminal region of Rck2.
GO:0005515 protein binding	IPI PMID:20489023 A global protein kinase and phosphatase interaction network ...	MODIFY	Summary: Kinase-phosphatase interaction network (AP-MS) links Hog1 with the MAPKK Ste7. Reason: Bare protein binding is uninformative. Ste7 is a protein kinase (the pheromone/filamentous-growth MAPKK), so protein kinase binding is the informative replacement; the physiological significance of a Hog1-Ste7 contact is not established. Proposed replacements: protein kinase binding Supporting Evidence: PMID:20489023 We identified a kinase and phosphatase interaction (KPI) network of 1844 interactions in budding yeast by mass spectrometric analysis of protein complexes.
GO:0005515 protein binding	IPI PMID:20489023 A global protein kinase and phosphatase interaction network ...	MODIFY	Summary: Kinase-phosphatase interaction network (AP-MS) recovers the Hog1-Rck2 interaction. Reason: Bare protein binding is uninformative; Rck2 is a protein kinase that binds Hog1 and is its substrate, so protein kinase binding is the informative MF. Proposed replacements: protein kinase binding Supporting Evidence: PMID:20489023 We identified a kinase and phosphatase interaction (KPI) network of 1844 interactions in budding yeast by mass spectrometric analysis of protein complexes. PMID:10805732 Both two-hybrid analyses and coprecipitation assays demonstrated that Hog1 binds strongly to the C-terminal region of Rck2.
GO:0005515 protein binding	IPI PMID:20489023 A global protein kinase and phosphatase interaction network ...	MODIFY	Summary: Kinase-phosphatase interaction network (AP-MS) recovers Hog1 association with Hot1. Reason: Bare protein binding is uninformative. Hot1 is a Pol II-specific DNA-binding transcription factor that targets Hog1 to osmostress promoters, so RNA polymerase II-specific DNA-binding transcription factor binding is the informative MF. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding Supporting Evidence: PMID:20489023 We identified a kinase and phosphatase interaction (KPI) network of 1844 interactions in budding yeast by mass spectrometric analysis of protein complexes. PMID:12743037 In response to high osmolarity, Hot1 targets Hog1 to specific osmostress-responsive promoters.
GO:0005515 protein binding	IPI PMID:21743437 Control of Ubp3 ubiquitin protease activity by the Hog1 SAPK...	REMOVE	Summary: Hog1 interacts with and phosphorylates the ubiquitin protease Ubp3 at Ser695 to modulate osmostress transcription. Reason: Bare protein binding is uninformative; Ubp3 is a Hog1 substrate and no specific binding MF of Hog1 is implied beyond its kinase activity (generic enzyme binding would be no more informative). Removing this generic row does not mean the interaction is false; the contact is a kinase-substrate interaction whose functional content is already carried by the MAP kinase activity annotations and the downstream process annotations. Supporting Evidence: PMID:21743437 Hog1 interacts with and phosphorylates Ubp3 at serine 695, which is essential to determine the extent of transcriptional activation in response to osmostress.
GO:0005515 protein binding	IPI PMID:23178807 Coordinated control of replication and transcription by a SA...	REMOVE	Summary: Hog1 interacts with and phosphorylates the replication checkpoint mediator Mrc1. Reason: Bare protein binding is uninformative; Mrc1 is a Hog1 substrate and the functional consequence is captured by GO:0033262 from the same paper. Removing this generic row does not mean the interaction is false; the contact is a kinase-substrate interaction whose functional content is already carried by the MAP kinase activity annotations and the downstream process annotations. Supporting Evidence: PMID:23178807 Hog1 interacts with and phosphorylates Mrc1, a component of the replication complex.
GO:0005515 protein binding	IPI PMID:37968396 The social and structural architecture of the yeast protein ...	MODIFY	Summary: Proteome-wide affinity enrichment-MS interactome recovers Hog1-Rck2. Reason: Bare protein binding is uninformative; Rck2 is a protein kinase and direct Hog1 substrate, so protein kinase binding is the informative MF. Proposed replacements: protein kinase binding Supporting Evidence: PMID:37968396 The 4,159 pull-downs generated a highly structured network of 3,927 proteins connected by 31,004 interactions PMID:10805732 Both two-hybrid analyses and coprecipitation assays demonstrated that Hog1 binds strongly to the C-terminal region of Rck2.
GO:0005516 calmodulin binding	IPI PMID:27421986 Regulation of MAP kinase Hog1 by calmodulin during hyperosmo...	KEEP AS NON CORE	Summary: Hog1 reported as a calmodulin (Cmd1)-binding protein; CaM binding implicated in hyperosmotic signaling. Reason: Single-study finding (abstract only available here) that has not been widely replicated; plausible as a regulatory interaction but not part of the core MAPK function. The SGD curator read the full text, so the annotation is kept as non-core rather than challenged. Supporting Evidence: PMID:27421986 we demonstrate that Hog1 is a novel CaM-binding protein, and that CaM-binding to Hog1 is involved in the mediation of the hyperosmotic stress signaling pathway.
GO:0005524 ATP binding	IEA GO_REF:0000002	ACCEPT	Summary: ATP binding inferred from the protein kinase domain / ATP-binding site signatures. Reason: Hog1 is an active ATP-dependent protein kinase; ATP binding is intrinsic to its catalytic function. Supporting Evidence: file:yeast/HOG1/HOG1-deep-research-falcon.md Pbs2 is the immediate upstream MAPK kinase and phosphorylates Hog1 at Thr174 and Tyr176.
GO:0005634 nucleus	IBA GO_REF:0000033	ACCEPT	Summary: Phylogenetic inference that MAPKs are active in the nucleus. Reason: Hog1 accumulates in the nucleus on activation and acts at osmostress promoters; consistent with experimental evidence. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000622075 · PANTHER:PTN000622075 SUPPORTS TRANSFER The nucleus IBD is placed on the broad PTHR24055 MAPK node, and budding yeast Hog1 is a direct experimental descendant with stress-triggered nuclear accumulation and promoter-bound transcriptional output. Supporting Evidence: PMID:10817757 The MAP kinase Hog1 transiently accumulates in the nucleus upon activation. PMID:12743037 In response to high osmolarity, Hot1 targets Hog1 to specific osmostress-responsive promoters.
GO:0005634 nucleus	IDA PMID:10817757 Two protein tyrosine phosphatases, Ptp2 and Ptp3, modulate t...	ACCEPT	Summary: Hog1-GFP transiently accumulates in the nucleus after osmotic activation; retention modulated by nuclear Ptp2. Reason: Nuclear localization is central to Hog1 function in transcriptional reprogramming. Supporting Evidence: PMID:10817757 The MAP kinase Hog1 transiently accumulates in the nucleus upon activation.
GO:0005634 nucleus	IEA GO_REF:0000044	ACCEPT	Summary: UniProt subcellular location mapping to nucleus. Reason: Consistent with experimental data. Supporting Evidence: PMID:10817757 The MAP kinase Hog1 transiently accumulates in the nucleus upon activation.
GO:0005737 cytoplasm	HDA PMID:11914276 Subcellular localization of the yeast proteome.	ACCEPT	Summary: Proteome-scale immunolocalization places Hog1 in the cytoplasm. Reason: Hog1 is predominantly cytoplasmic in unstressed cells, consistent with this high-throughput call. Supporting Evidence: PMID:11914276 By high-throughput immunolocalization of tagged gene products, we have determined the subcellular localization of 2744 yeast proteins. file:yeast/HOG1/HOG1-deep-research-falcon.md In unstressed cells, Hog1 continuously cycles between cytoplasmic and nuclear compartments.
GO:0005737 cytoplasm	IBA GO_REF:0000033	ACCEPT	Summary: Phylogenetic inference that MAPKs are active in the cytoplasm. Reason: Hog1 is activated by Pbs2 in the cytoplasm and acts on cytoplasmic targets (e.g. Rck2, Fps1 regulators). Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000622075 · PANTHER:PTN000622075 SUPPORTS TRANSFER The cytoplasmic activity call is broad across PTHR24055, but it fits Hog1, which cycles through the cytoplasm and acts on cytoplasmic osmostress targets before and after activation. Supporting Evidence: file:yeast/HOG1/HOG1-deep-research-falcon.md In unstressed cells, Hog1 continuously cycles between cytoplasmic and nuclear compartments. PMID:10817757 In support of this result PTP2 overexpression sequestered Hog1 in the nucleus while PTP3 overexpression restricted Hog1 to the cytoplasm.
GO:0005737 cytoplasm	IDA PMID:10817757 Two protein tyrosine phosphatases, Ptp2 and Ptp3, modulate t...	ACCEPT	Summary: Hog1 is cytoplasmic in resting cells and is anchored there by Ptp3. Reason: Correct experimental localization. Supporting Evidence: PMID:10817757 In support of this result PTP2 overexpression sequestered Hog1 in the nucleus while PTP3 overexpression restricted Hog1 to the cytoplasm.
GO:0005737 cytoplasm	IEA GO_REF:0000044	ACCEPT	Summary: UniProt subcellular location mapping to cytoplasm. Reason: Consistent with experimental data. Supporting Evidence: PMID:10817757 In support of this result PTP2 overexpression sequestered Hog1 in the nucleus while PTP3 overexpression restricted Hog1 to the cytoplasm.
GO:0006357 regulation of transcription by RNA polymerase II	IDA PMID:23178807 Coordinated control of replication and transcription by a SA...	ACCEPT	Summary: Hog1 induces hundreds of stress-responsive genes, including during S phase, while coordinating replication. Reason: Hog1 regulates Pol II transcription of osmostress genes; correct, though the more specific positive regulation term (GO:0045944) is also annotated. Supporting Evidence: PMID:23178807 In response to osmostress, hundreds of stress-responsive genes are rapidly induced by the stress-activated protein kinase (SAPK) Hog1 PMID:23178807 Here we show in Saccharomyces cerevisae that a single signalling molecule, Hog1, coordinates both replication and transcription upon osmostress.
GO:0006972 hyperosmotic response	IMP PMID:7681220 An osmosensing signal transduction pathway in yeast.	ACCEPT	Summary: HOG1 was isolated as a gene required to restore the osmotic gradient in response to increased external osmolarity. Reason: Founding genetic evidence for the core role of Hog1 in the hyperosmotic response. Supporting Evidence: PMID:7681220 Yeast genes were isolated that are required for restoring the osmotic gradient across the cell membrane in response to increased external osmolarity. PMID:7681220 A rapid, PBS2-dependent tyrosine phosphorylation of HOG1 protein occurred in response to increases in extracellular osmolarity.
GO:0007231 osmosensory signaling pathway	IBA GO_REF:0000033	ACCEPT	Summary: Phylogenetic inference of osmosensory signaling for the Hog1/Sty1 clade. Reason: Core process: Hog1 is the MAPK tier of the yeast osmosensory HOG pathway. The target appearing among its own sources reflects its experimental grounding. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN001172058 · PANTHER:PTN001172058 SUPPORTS TRANSFER PTN001172058 is the fungal HOG/Sty1 stress-MAPK node; the osmosensory signaling assertion matches the experimentally grounded budding yeast HOG pathway and is inherited by Hog1 without evidence of loss. Supporting Evidence: PMID:7681220 A rapid, PBS2-dependent tyrosine phosphorylation of HOG1 protein occurred in response to increases in extracellular osmolarity. file:yeast/HOG1/HOG1-deep-research-falcon.md Pbs2 is the immediate upstream MAPK kinase and phosphorylates Hog1 at Thr174 and Tyr176.
GO:0007231 osmosensory signaling pathway	IMP PMID:7681220 An osmosensing signal transduction pathway in yeast.	ACCEPT	Summary: hog1 mutants are defective in osmoadaptation and Hog1 is tyrosine-phosphorylated in a PBS2-dependent manner on osmotic shift. Reason: Core process; defines the osmosensing signal transduction pathway. Supporting Evidence: PMID:7681220 A rapid, PBS2-dependent tyrosine phosphorylation of HOG1 protein occurred in response to increases in extracellular osmolarity.
GO:0016241 regulation of macroautophagy	IMP PMID:16874103 Deletion of HOG1 leads to Osmosensitivity in starvation-indu...	KEEP AS NON CORE	Summary: hog1 deletion renders starvation-induced (but not rapamycin-induced) autophagy osmosensitive. Reason: Mutant phenotype supports a Hog1 contribution to autophagy regulation under osmotic conditions; mechanism unclear and peripheral to the core osmosignaling role. Cached text is abstract only; defer to curator but keep as non-core. Supporting Evidence: PMID:16874103 Recent work shows that in yeast, loss of Hog1, the yeast orthologue of p38(MAPK), leads to osmosensitivity of starvation-induced autophagy
GO:0033262 regulation of nuclear cell cycle DNA replication	IDA PMID:23178807 Coordinated control of replication and transcription by a SA...	KEEP AS NON CORE	Summary: Hog1 phosphorylates Mrc1 to delay origin firing and replication-fork progression upon osmostress. Reason: Direct regulatory action of Hog1 (Mrc1 phosphorylation) establishes a replication checkpoint during osmostress; a real but secondary, stress-coupled cell-cycle output. Supporting Evidence: PMID:23178807 Mrc1 phosphorylation by Hog1 delays early and late origin firing by preventing Cdc45 loading, as well as slowing down replication-complex progression. PMID:23178807 Hog1 interacts with and phosphorylates Mrc1, a component of the replication complex.
GO:0034599 cellular response to oxidative stress	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: Phylogenetic inference of a role in cellular response to oxidative stress (Sty1/Hog1 clade). Reason: In fission yeast Sty1 the oxidative stress role is central; in S. cerevisiae Hog1 contributes to hydrogen peroxide responses but osmostress is the dominant input. Node placement is reasonable, kept as non-core. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN001172058 · PANTHER:PTN001172058 SUPPORTS TRANSFER The oxidative-stress IBD is placed on the fungal HOG/Sty1 node and is compatible with budding yeast Hog1's peroxide and organic-acid stress inputs, but oxidative stress is a contextual output rather than the dominant osmosensory role of S. cerevisiae Hog1. Supporting Evidence: file:yeast/HOG1/HOG1-uniprot.txt hydrogen peroxide response, adaptation to citric acid PMID:15177185 Mutants in either pathway are sensitive to hydrogen peroxide and the double mutants exhibit a near perfectly additive phenotype.
GO:0045944 positive regulation of transcription by RNA polymerase II	IDA PMID:12743037 Osmostress-induced transcription by Hot1 depends on a Hog1-m...	ACCEPT	Summary: Hog1 recruited to promoters by Hot1 is required for Pol II recruitment and activates transcription when tethered to a promoter. Reason: Core nuclear output of Hog1: direct positive regulation of osmostress gene transcription at chromatin. Supporting Evidence: PMID:12743037 Thus, anchoring of active Hog1 to promoters by the Hot1 activator is essential for recruitment and activation of RNA Pol II. PMID:12743037 In response to high osmolarity, Hot1 targets Hog1 to specific osmostress-responsive promoters.
GO:0045944 positive regulation of transcription by RNA polymerase II	IMP PMID:23435728 Activator and repressor functions of the Mot3 transcription ...	ACCEPT	Summary: A Mot3/Msn2/Msn4-dependent group of osmostress-inducible genes requires Hog1 for induction. Reason: Consistent with Hog1's established role as a positive regulator of osmostress gene transcription. Supporting Evidence: PMID:23435728 As expected, we found this group of stress-responsive genes to be dependent on the MAP kinase Hog1
GO:0045944 positive regulation of transcription by RNA polymerase II	IMP PMID:24508389 Control of Cdc28 CDK1 by a stress-induced lncRNA.	ACCEPT	Summary: Hog1 induces stress lncRNAs and CDC28 expression by recruiting Pol II and RSC. Reason: Hog1 associates with promoters and stimulates Pol II recruitment; supports positive regulation of Pol II transcription. Supporting Evidence: PMID:24508389 Therefore, Hog1 associates to and stimulates the recruitment of RNA Pol II at the promoters of stress-induced lncRNAs. PMID:24508389 Using whole-genome tiling arrays, we found that Hog1 induces a set of lncRNAs upon stress.
GO:0051403 stress-activated MAPK cascade	IBA GO_REF:0000033	ACCEPT	Summary: Phylogenetic inference of stress-activated MAPK cascade for the Hog1/Sty1 clade. Reason: Hog1 is the terminal kinase of the Ssk2/Ssk22 (and Ste11) -> Pbs2 -> Hog1 stress-activated MAPK cascade. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN001172058 · PANTHER:PTN001172058 SUPPORTS TRANSFER PTN001172058 is the fungal HOG/Sty1 node, and its stress-activated MAPK cascade assertion matches the Ssk2/Ssk22/Ste11-Pbs2-Hog1 cascade. Supporting Evidence: file:yeast/HOG1/HOG1-deep-research-falcon.md Pbs2 is the immediate upstream MAPK kinase and phosphorylates Hog1 at Thr174 and Tyr176. PMID:7681220 A rapid, PBS2-dependent tyrosine phosphorylation of HOG1 protein occurred in response to increases in extracellular osmolarity.
GO:0051403 stress-activated MAPK cascade	IEA GO_REF:0000002	ACCEPT	Summary: InterPro Sty1/Hog1 family mapping to stress-activated MAPK cascade. Reason: Correct; consistent with IBA and experimental data. Supporting Evidence: file:yeast/HOG1/HOG1-deep-research-falcon.md Pbs2 is the immediate upstream MAPK kinase and phosphorylates Hog1 at Thr174 and Tyr176.
GO:0071470 cellular response to osmotic stress	IDA PMID:10805732 Rck2 kinase is a substrate for the osmotic stress-activated ...	ACCEPT	Summary: Rck2 is phosphorylated by Hog1 upon osmotic stress and mediates a subset of Hog1 osmostress responses. Reason: Correct; GO:0071474 cellular hyperosmotic response (also annotated) is the more precise sibling-descendant. Supporting Evidence: PMID:10805732 Taken together, our data suggest that Rck2 acts downstream of Hog1, controlling a subset of the responses induced by the MAPK upon osmotic stress.
GO:0071470 cellular response to osmotic stress	IDA PMID:12743037 Osmostress-induced transcription by Hot1 depends on a Hog1-m...	ACCEPT	Summary: Hog1 drives osmostress-induced transcription via Hot1-dependent Pol II recruitment. Reason: Correct core process. Supporting Evidence: PMID:12743037 In response to high osmolarity, Hot1 targets Hog1 to specific osmostress-responsive promoters.
GO:0071470 cellular response to osmotic stress	IDA PMID:23178807 Coordinated control of replication and transcription by a SA...	ACCEPT	Summary: Hog1 coordinates replication and transcription upon osmostress. Reason: Correct core process. Supporting Evidence: PMID:23178807 Here we show in Saccharomyces cerevisae that a single signalling molecule, Hog1, coordinates both replication and transcription upon osmostress.
GO:0071470 cellular response to osmotic stress	IDA PMID:24508389 Control of Cdc28 CDK1 by a stress-induced lncRNA.	ACCEPT	Summary: Hog1 associates with chromatin and induces lncRNAs and CDC28 upon osmostress. Reason: Correct core process. Supporting Evidence: PMID:24508389 Using whole-genome tiling arrays, we found that Hog1 induces a set of lncRNAs upon stress.
GO:0071470 cellular response to osmotic stress	IMP PMID:16874103 Deletion of HOG1 leads to Osmosensitivity in starvation-indu...	ACCEPT	Summary: hog1 deletion makes starvation-induced autophagy sensitive to osmotic conditions. Reason: Hog1 is required for the cellular response to osmotic stress; the annotation is correct even though this particular paper addresses an autophagy readout. Supporting Evidence: PMID:16874103 Recent work shows that in yeast, loss of Hog1, the yeast orthologue of p38(MAPK), leads to osmosensitivity of starvation-induced autophagy
GO:0071470 cellular response to osmotic stress	IMP PMID:23435728 Activator and repressor functions of the Mot3 transcription ...	ACCEPT	Summary: Osmostress-induced genes controlled by Mot3 require Hog1. Reason: Correct core process. Supporting Evidence: PMID:23435728 As expected, we found this group of stress-responsive genes to be dependent on the MAP kinase Hog1
GO:0071470 cellular response to osmotic stress	IMP PMID:24508389 Control of Cdc28 CDK1 by a stress-induced lncRNA.	ACCEPT	Summary: Hog1 is required for osmostress induction of lncRNAs and CDC28. Reason: Correct core process. Supporting Evidence: PMID:24508389 Using whole-genome tiling arrays, we found that Hog1 induces a set of lncRNAs upon stress.
GO:0071474 cellular hyperosmotic response	IDA PMID:32265285 Hog1 activation delays mitotic exit via phosphorylation of N...	ACCEPT	Summary: Hog1 activation under osmostress delays mitotic exit via Net1 phosphorylation, promoting survival. Reason: Hog1 is the effector of the cellular hyperosmotic response; precise and correct. Supporting Evidence: PMID:32265285 Here we show that Hog1 delays mitotic exit when cells are stressed during metaphase.
GO:0071474 cellular hyperosmotic response	IPI PMID:27421986 Regulation of MAP kinase Hog1 by calmodulin during hyperosmo...	ACCEPT	Summary: Calmodulin binding to Hog1 reported to participate in hyperosmotic stress signaling. Reason: Hog1's involvement in the cellular hyperosmotic response is firmly established; the process term is correct regardless of the specific CaM mechanism. Supporting Evidence: PMID:27421986 we demonstrate that Hog1 is a novel CaM-binding protein, and that CaM-binding to Hog1 is involved in the mediation of the hyperosmotic stress signaling pathway.
GO:0106310 protein serine kinase activity	EXP PMID:10805732 Rck2 kinase is a substrate for the osmotic stress-activated ...	ACCEPT	Summary: Hog1 phosphorylates Rck2 on Ser519. Reason: Direct evidence of serine kinase activity; MAP kinase activity (GO:0004707) is the more specific and informative term. Supporting Evidence: PMID:10805732 Taken together, these results indicate that Rck2 is a direct substrate for the MAPK Hog1.
GO:0106310 protein serine kinase activity	EXP PMID:11230135 Regulation of the Sko1 transcriptional repressor by the Hog1...	ACCEPT	Summary: Hog1 phosphorylates Sko1 in vitro at multiple N-terminal sites. Reason: Direct evidence of serine kinase activity on a key transcriptional target. Supporting Evidence: PMID:11230135 Hog1 phosphorylates Sko1 in vitro at multiple sites within the N-terminal region.
GO:0106310 protein serine kinase activity	EXP PMID:12482976 Targeting the MEF2-like transcription factor Smp1 by the str...	ACCEPT	Summary: Hog1 phosphorylates Smp1 in vitro at the C-terminal region. Reason: Direct evidence of Ser/Thr kinase activity on a transcriptional target. Supporting Evidence: PMID:12482976 Hog1 phosphorylated Smp1 in vitro at the C-terminal region.
GO:0106310 protein serine kinase activity	EXP PMID:38270553 Proline-directed yeast and human MAP kinases phosphorylate t...	ACCEPT	Summary: Hog1 phosphorylates Dot1 at multiple Ser sites in vitro. Reason: Direct kinase assay evidence. Supporting Evidence: PMID:38270553 In vitro kinase assays showed that Hog1p phosphorylates Dot1p at multiple sites, including at several proline-adjacent sites that are consistent with known Hog1p substrate preferences.
GO:0106310 protein serine kinase activity	IEA GO_REF:0000116	ACCEPT	Summary: Rhea-based mapping (RHEA:17989, protein-serine phosphorylation). Reason: Consistent with experimental data. Supporting Evidence: PMID:11230135 Hog1 phosphorylates Sko1 in vitro at multiple sites within the N-terminal region.
GO:0000785 chromatin	IDA PMID:24508389 Control of Cdc28 CDK1 by a stress-induced lncRNA.	NEW	Summary: ChIP shows Hog1 associating with chromatin at osmostress-responsive promoters and at the CDC28 locus upon stress; Hot1 and other factors recruit it there. Reason: Hog1 function in transcriptional activation is exerted at chromatin of stress-responsive genes, where it is anchored by transcription factors and stimulates Pol II recruitment. The existing chromatin binding MF (GO:0003682) from the same paper describes this as an intrinsic binding activity, which Hog1 is not known to have; a chromatin location captures the ChIP observation more accurately. Supporting Evidence: PMID:24508389 Therefore, Hog1 associates to and stimulates the recruitment of RNA Pol II at the promoters of stress-induced lncRNAs. PMID:12743037 In response to high osmolarity, Hot1 targets Hog1 to specific osmostress-responsive promoters.
GO:0071243 cellular response to arsenic-containing substance	IMP PMID:31772124 Thiol-based direct threat sensing by the stress-activated pr...	NEW	Summary: Guerra-Moreno et al. 2019 showed that Hog1 binds arsenic directly through three conserved cysteines adjacent to the catalytic loop; mutating them makes cells arsenic sensitive without affecting the osmotic response, and Hog1 drives Yap8 phosphorylation, Yap8 nuclear localization and ARR2/ARR3 expression. GOA has no arsenic-response row for HOG1, although its downstream factor Yap8 (ARR1) carries this term. Reason: Hog1 does part of the work of the response, sensing arsenic and signalling to Yap8, so this is participation, not mere requirement. The term is not an ancestor or descendant of the osmotic-stress terms the gene carries. Kept out of core functions, which centre on osmostress signalling. Supporting Evidence: PMID:31772124 we identified a mode of Hog1 function whereby Hog1 senses arsenic through a direct physical interaction that requires three conserved cysteine residues located adjacent to the catalytic loop. PMID:31772124 Hog1 promoted arsenic detoxification by stimulating phosphorylation of the transcription factor Yap8, promoting Yap8 nuclear localization, and stimulating the transcription of the only known Yap8 targets, ARR2 and ARR3

Gene Description

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Core Functions

Terminal MAP kinase of the HOG osmostress cascade: activated by Pbs2 dual phosphorylation, it relays the osmosensory signal by phosphorylating cytoplasmic and nuclear substrates to execute the cellular hyperosmotic response.

Nuclear Hog1, recruited to osmostress promoters by transcription factors such as Hot1 and Sko1, phosphorylates these factors and promotes RNA polymerase II recruitment, driving induction of osmostress genes.

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SGD

SGD gene description for HOG1 (yeast)

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