diff --git "a/target.jsonl" "b/target.jsonl"
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+++ "b/target.jsonl"
@@ -0,0 +1,1000 @@
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Modulates excitatory synaptic transmission and dendritic spine morphology. Binds to actin filaments (F-actin) and shows cross-linking activity. Binds along the sides of the F-actin. May play an important role in linking the actin cytoskeleton to the plasma membrane at the synaptic junction. Believed to target protein phosphatase 1/PP1 to dendritic spines, which are rich in F-actin, and regulates its specificity toward ion channels and other substrates, such as AMPA-type and NMDA-type glutamate receptors. Plays a role in regulation of G-protein coupled receptor signaling, including dopamine D2 receptors and alpha-adrenergic receptors. May establish a signaling complex for dopaminergic neurotransmission through D2 receptors by linking receptors downstream signaling molecules and the actin cytoskeleton. Binds to ADRA1B and RGS2 and mediates regulation of ADRA1B signaling. May confer to Rac signaling specificity by binding to both, RacGEFs and Rac effector proteins. Probably regulates p70 S6 kinase activity by forming a complex with TIAM1 (By similarity). Required for hepatocyte growth factor (HGF)-induced cell migration.","display_priority":1,"if_manual":0,"lang":"EN","source_info":[{"code":"Q96SB3","normalized_source_id":"96adf8c891514225a46927b3b16bd02a","source":"UNIPROT"}],"status":"ACTIVE"}],"paper_reference":[{"evidence_key":9,"evidence_type":"Protein Function","paper_id":"afedc958-bd66-32ba-8db8-7525d2701d8d","reference_id":"24114805","reference_type":"Pubmed","uniprot_id":"Q96SB3"},{"evidence_key":8,"evidence_type":"Protein Function","paper_id":"3b28955a-b3e2-3bd5-a0bf-782f643bf63f","reference_id":"19151759","reference_type":"Pubmed","uniprot_id":"Q96SB3"},{"evidence_key":7,"evidence_type":"Protein Function","paper_id":"2c828a7c-aa9a-32db-8ad3-3b1d59c1ccda","reference_id":"11278317","reference_type":"Pubmed","uniprot_id":"Q96SB3"}],"sequence_info":[{"related_target_id":"00523ac65a8448758ed9d1b8288df2f9","sequence_number":1293501,"uniprot_id":"Q96SB3"}],"is_leaf":1}
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The CX3CR1-CX3CL1 signaling exerts distinct functions in different tissue compartments, such as immune response, inflammation, cell adhesion and chemotaxis (PubMed:12055230, PubMed:9024663, PubMed:9177350, PubMed:9782118). Regulates leukocyte adhesion and migration processes at the endothelium (PubMed:9024663, PubMed:9177350). Can activate integrins in both a CX3CR1-dependent and CX3CR1-independent manner (PubMed:23125415, PubMed:24789099). In the presence of CX3CR1, activates integrins by binding to the classical ligand-binding site (site 1) in integrins (PubMed:23125415, PubMed:24789099). In the absence of CX3CR1, binds to a second site (site 2) in integrins which is distinct from site 1 and enhances the binding of other integrin ligands to site 1 (PubMed:23125415, PubMed:24789099).\n(Microbial infection) Mediates the cytoadherence of erythrocytes infected with parasite P.falciparum (strain 3D7) with endothelial cells by interacting with P.falciparum CBP1 and CBP2 expressed at the surface of erythrocytes (PubMed:27653778). The adhesion prevents the elimination of infected erythrocytes by the spleen (Probable).\nThe soluble form is chemotactic for T-cells and monocytes, but not for neutrophils.\nThe membrane-bound form promotes adhesion of those leukocytes to endothelial cells.","display_priority":1,"if_manual":0,"lang":"EN","source_info":[{"code":"P78423","normalized_source_id":"96adf8c891514225a46927b3b16bd02a","source":"UNIPROT"}],"status":"ACTIVE"}],"paper_reference":[{"evidence_key":15,"evidence_type":"Protein Function","paper_id":"b5d80dd3-a19e-3e85-b525-05abdb1aa48f","reference_id":"9782118","reference_type":"Pubmed","uniprot_id":"P78423"},{"evidence_key":7,"evidence_type":"Protein Function","paper_id":"8e75b885-fd56-35c2-9293-cf362eb18cb3","reference_id":"22171320","reference_type":"Pubmed","uniprot_id":"P78423"},{"evidence_key":14,"evidence_type":"Protein Function","paper_id":"23f6459a-e01d-3474-8bae-197bc431b06f","reference_id":"9177350","reference_type":"Pubmed","uniprot_id":"P78423"},{"evidence_key":3,"evidence_type":"Protein Function","paper_id":"1a6f0643-4518-3c2c-a019-67361f20fa41","reference_id":"10770945","reference_type":"Pubmed","uniprot_id":"P78423"},{"evidence_key":6,"evidence_type":"Protein Function","paper_id":"c1560bba-7b72-31c1-b004-bf7ba12fb776","reference_id":"21829356","reference_type":"Pubmed","uniprot_id":"P78423"},{"evidence_key":5,"evidence_type":"Protein Function","paper_id":"58d39ea0-535f-3cb4-bb7e-78559173ffc9","reference_id":"19838169","reference_type":"Pubmed","uniprot_id":"P78423"},{"evidence_key":10,"evidence_type":"Protein Function","paper_id":"45288331-4b05-316e-87ee-614533fc85cd","reference_id":"24789099","reference_type":"Pubmed","uniprot_id":"P78423"},{"evidence_key":12,"evidence_type":"Protein Function","paper_id":"878a42a3-bf30-3b36-b511-3b0d728d98fe","reference_id":"27653778","reference_type":"Pubmed","uniprot_id":"P78423"},{"evidence_key":11,"evidence_type":"Protein Function","paper_id":"c01ca680-3d68-3729-80f6-b7dc658d2e8b","reference_id":"25745166","reference_type":"Pubmed","uniprot_id":"P78423"},{"evidence_key":8,"evidence_type":"Protein Function","paper_id":"0b630950-371c-3a00-a772-533aea83bb8e","reference_id":"23125415","reference_type":"Pubmed","uniprot_id":"P78423"},{"evidence_key":13,"evidence_type":"Protein Function","paper_id":"8839fb8a-bd5b-3d72-9308-28f89dac11b1","reference_id":"9024663","reference_type":"Pubmed","uniprot_id":"P78423"},{"evidence_key":9,"evidence_type":"Protein Function","paper_id":"9eaa3d1d-4992-32fe-99e7-8a97c2011406","reference_id":"23765988","reference_type":"Pubmed","uniprot_id":"P78423"},{"evidence_key":4,"evidence_type":"Protein Function","paper_id":"9527c920-1832-3fe8-8347-3e0ed82faa10","reference_id":"12055230","reference_type":"Pubmed","uniprot_id":"P78423"},{"evidence_key":16,"evidence_type":"Protein Function","paper_id":"0ddfc4f7-e9b9-33b7-a254-2a74e8fb3210","reference_id":"9931005","reference_type":"Pubmed","uniprot_id":"P78423"}],"sequence_info":[{"related_target_id":"010c36dc4f9947cbb0acb4db64cb342a","sequence_number":14652,"uniprot_id":"P78423"}],"is_leaf":1}
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Key effector of the integrated stress response (ISR) to unfolded proteins: EIF2AK3/PERK specifically recognizes and binds misfolded proteins, leading to its activation and EIF2S1/eIF-2-alpha phosphorylation (PubMed:10677345, PubMed:27917829, PubMed:31023583). EIF2S1/eIF-2-alpha phosphorylation in response to stress converts EIF2S1/eIF-2-alpha in a global protein synthesis inhibitor, leading to a global attenuation of cap-dependent translation, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activators ATF4 and QRICH1, and hence allowing ATF4- and QRICH1-mediated reprogramming (PubMed:10026192, PubMed:10677345, PubMed:31023583, PubMed:33384352). The EIF2AK3/PERK-mediated unfolded protein response increases mitochondrial oxidative phosphorylation by promoting ATF4-mediated expression of COX7A2L/SCAF1, thereby increasing formation of respiratory chain supercomplexes (PubMed:31023583). In contrast to most subcellular compartments, mitochondria are protected from the EIF2AK3/PERK-mediated unfolded protein response due to EIF2AK3/PERK inhibition by ATAD3A at mitochondria-endoplasmic reticulum contact sites (PubMed:39116259). In addition to EIF2S1/eIF-2-alpha, also phosphorylates NFE2L2/NRF2 in response to stress, promoting release of NFE2L2/NRF2 from the BCR(KEAP1) complex, leading to nuclear accumulation and activation of NFE2L2/NRF2 (By similarity). Serves as a critical effector of unfolded protein response (UPR)-induced G1 growth arrest due to the loss of cyclin-D1 (CCND1) (By similarity). Involved in control of mitochondrial morphology and function (By similarity).","display_priority":1,"if_manual":0,"lang":"EN","source_info":[{"code":"Q9NZJ5","normalized_source_id":"96adf8c891514225a46927b3b16bd02a","source":"UNIPROT"}],"status":"ACTIVE"}],"paper_reference":[{"evidence_key":32,"evidence_type":"Protein Function","paper_id":"115d1ddb-7a98-4224-96f7-49e14dcf482a","reference_id":"39116259","reference_type":"Pubmed","uniprot_id":"Q9NZJ5"},{"evidence_key":21,"evidence_type":"Protein Function","paper_id":"22a8fcce-548f-3138-aa11-f6bbd0de5a12","reference_id":"26268696","reference_type":"Pubmed","uniprot_id":"Q9NZJ5"},{"evidence_key":10,"evidence_type":"Protein Function","paper_id":"516c68bb-6e1d-39e5-ae4e-1a1b7c958c7e","reference_id":"12086964","reference_type":"Pubmed","uniprot_id":"Q9NZJ5"},{"evidence_key":27,"evidence_type":"Protein 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PubMed:20151848, PubMed:24121512, PubMed:28387307, PubMed:35835865). Component of the ankyrin-1 complex of the erythrocyte membrane; required for normal flexibility and stability of the erythrocyte membrane and for normal erythrocyte shape via the interactions of its cytoplasmic domain with cytoskeletal proteins, glycolytic enzymes, and hemoglobin (PubMed:1538405, PubMed:20151848, PubMed:35835865). Functions as a transporter that mediates the 1:1 exchange of inorganic anions across the erythrocyte membrane. Mediates chloride-bicarbonate exchange in the kidney, and is required for normal acidification of the urine (PubMed:10926824, PubMed:14734552, PubMed:16227998, PubMed:24121512, PubMed:28387307).\n(Microbial infection) Acts as a receptor for P.falciparum (isolate 3D7) MSP9 and thus, facilitates merozoite invasion of erythrocytes (PubMed:14630931). Acts as a receptor for P.falciparum (isolate 3D7) MSP1 and thus, facilitates merozoite invasion of erythrocytes (PubMed:12692305).","display_priority":1,"if_manual":0,"lang":"EN","source_info":[{"code":"P02730","normalized_source_id":"96adf8c891514225a46927b3b16bd02a","source":"UNIPROT"}],"status":"ACTIVE"}],"paper_reference":[{"evidence_key":19,"evidence_type":"Protein Function","paper_id":"921a2b45-5199-319a-b01f-40bf469e3315","reference_id":"14734552","reference_type":"Pubmed","uniprot_id":"P02730"},{"evidence_key":42,"evidence_type":"Protein Function","paper_id":"dba6dc0e-59a3-39ac-8edc-debb52fef8a4","reference_id":"7506871","reference_type":"Pubmed","uniprot_id":"P02730"},{"evidence_key":11,"evidence_type":"Protein Function","paper_id":"5d46f3e9-60f0-3a86-ae4b-7fb2db7a0352","reference_id":"11049968","reference_type":"Pubmed","uniprot_id":"P02730"},{"evidence_key":31,"evidence_type":"Protein 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Acts either as activator (FLNB, HSPG2, LIPA1, MYOCD, PTPRF and PPFIBP1) or repressor (TPM1, ACTN1, ITGA7, PIEZO1, LSM14B, MBNL1 and MBML2) of splicing events on specific pre-mRNA targets (By similarity). Together with RNA binding proteins RBFOX2 and MBNL1/2, activates a splicing program associated with differentiated contractile vascular smooth muscle cells (SMC) by regulating AS of numerous pre-mRNA involved in actin cytoskeleton and focal adhesion machineries, suggesting a role in promoting a cell differentiated state (By similarity). Binds to introns, exons and 3'-UTR associated with tandem CAC trinucleotide motifs separated by a variable spacer region, at a minimum as a dimer. The minimal length of RNA required for RBPMS-binding tandem CAC motifs is 15 nt, with spacing ranging from 1 to 9 nt. Can also bind to CA dinucleotide repeats (PubMed:24860013, PubMed:26347403). Mediates repression of TPM1 exon 3 by binding to CAC tandem repeats in the flanking intronic regions, followed by higher-order oligomerization and heterotypic interactions with other splicing regulators including MBNL1 and RBFOX2, which prevents assembly of ATP-dependent splicing complexes (By similarity).\nActs as a regulator of pre-mRNA alternative splicing (AS) (By similarity). Binds mRNA (PubMed:17099224). Regulates AS of ACTN1, FLNB, although with lower efficiency than isoform A / RBPMSA (By similarity). Acts as coactivator of SMAD transcriptional activity in a TGFB1-dependent manner, possibly through increased phosphorylation of SMAD2 and SMAD3 at the C-terminal SSXS regions and promotion of the nuclear accumulation of SMAD proteins (PubMed:17099224).","display_priority":1,"if_manual":0,"lang":"EN","source_info":[{"code":"Q93062","normalized_source_id":"96adf8c891514225a46927b3b16bd02a","source":"UNIPROT"}],"status":"ACTIVE"}],"paper_reference":[{"evidence_key":5,"evidence_type":"Protein Function","paper_id":"1e41810c-6fd9-3224-b89a-a0fbc026e61c","reference_id":"17099224","reference_type":"Pubmed","uniprot_id":"Q93062"},{"evidence_key":8,"evidence_type":"Protein Function","paper_id":"935d82af-7642-3516-8a2d-6dcf71b304f6","reference_id":"8855282","reference_type":"Pubmed","uniprot_id":"Q93062"},{"evidence_key":4,"evidence_type":"Protein Function","paper_id":"eb2ac205-a4b7-4584-834c-4fc9ebffc5a8","reference_id":"14759258","reference_type":"Pubmed","uniprot_id":"Q93062"},{"evidence_key":6,"evidence_type":"Protein Function","paper_id":"851fd557-79fe-3780-bfae-ac61c8374b99","reference_id":"24860013","reference_type":"Pubmed","uniprot_id":"Q93062"},{"evidence_key":7,"evidence_type":"Protein Function","paper_id":"5e0b4293-8419-3cc0-a7be-e63d6f633174","reference_id":"26347403","reference_type":"Pubmed","uniprot_id":"Q93062"}],"sequence_info":[{"related_target_id":"016bf8c953cd4fd4a23d7ea0f8a6a254","sequence_number":923869,"uniprot_id":"Q93062"}],"is_leaf":1}
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The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation (PubMed:17403899). 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May play a role in the silencing of fetal globin genes (PubMed:20688955). Recruits the 5FMC complex to ZNF148, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes (By similarity). Plays an important role in the tumorigenicity of glioblastoma cells. Binds to 5-hydroxymethylcytosine (5hmC) and associates with the methylosome complex containing PRMT1, PRMT5, MEP50 and ERH. The CHTOP-methylosome complex associated with 5hmC is recruited to selective sites on the chromosome, where it methylates H4R3 and activates the transcription of genes involved in glioblastomagenesis (PubMed:25284789).\nRequired for effective mRNA nuclear export and is a component of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and specifically associates with spliced mRNA and not with unspliced pre-mRNA. 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Mainly converts arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate) to the specific bioactive lipid (12S)-hydroperoxyeicosatetraenoate/(12S)-HPETE (PubMed:17493578, PubMed:22984144, PubMed:24282679, PubMed:8319693, PubMed:8500694). Through the production of bioactive lipids like (12S)-HPETE it regulates different biological processes including platelet activation (PubMed:8319693, PubMed:8500694). It can also catalyze the epoxidation of double bonds of polyunsaturated fatty acids such as (14S)-hydroperoxy-docosahexaenoate/(14S)-HPDHA resulting in the formation of (13S,14S)-epoxy-DHA (PubMed:23504711). Furthermore, it may participate in the sequential oxidations of DHA ((4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate) to generate specialized pro-resolving mediators (SPMs) like resolvin D5 ((7S,17S)-diHPDHA) and (7S,14S)-diHPDHA, that actively down-regulate the immune response and have anti-aggregation properties with platelets (PubMed:32404334). An additional function involves a multistep process by which it transforms leukotriene A4/LTA4 into the bioactive lipids lipoxin A4/LXA4 and lipoxin B4/LXB4, both are vasoactive and LXA4 may regulate neutrophil function via occupancy of specific recognition sites (PubMed:8250832). Can also peroxidize linoleate ((9Z,12Z)-octadecadienoate) to (13S)-hydroperoxyoctadecadienoate/ (13S-HPODE) (By similarity). Due to its role in regulating both the expression of the vascular endothelial growth factor (VEGF, an angiogenic factor involved in the survival and metastasis of solid tumors) and the expression of integrin beta-1 (known to affect tumor cell migration and proliferation), it can be regarded as protumorigenic (PubMed:16638750, PubMed:22237009, PubMed:9751607). Important for cell survival, as it may play a role not only in proliferation but also in the prevention of apoptosis in vascular smooth muscle cells (PubMed:23578768).","display_priority":1,"if_manual":0,"lang":"EN","source_info":[{"code":"P18054","normalized_source_id":"96adf8c891514225a46927b3b16bd02a","source":"UNIPROT"}],"status":"ACTIVE"}],"paper_reference":[{"evidence_key":13,"evidence_type":"Protein Function","paper_id":"a349911a-a9f7-3686-b236-b27ee5d829de","reference_id":"18755188","reference_type":"Pubmed","uniprot_id":"P18054"},{"evidence_key":8,"evidence_type":"Protein Function","paper_id":"b18f1d52-1f62-300c-b6dc-dacd1835393f","reference_id":"17151091","reference_type":"Pubmed","uniprot_id":"P18054"},{"evidence_key":17,"evidence_type":"Protein Function","paper_id":"a014527a-fbeb-3e2c-a206-dfb4a6653059","reference_id":"22984144","reference_type":"Pubmed","uniprot_id":"P18054"},{"evidence_key":21,"evidence_type":"Protein Function","paper_id":"b4b499a3-4980-3734-815b-2a090061081f","reference_id":"24282679","reference_type":"Pubmed","uniprot_id":"P18054"},{"evidence_key":7,"evidence_type":"Protein Function","paper_id":"44767414-d4da-380f-b507-1f9765056bcf","reference_id":"16638750","reference_type":"Pubmed","uniprot_id":"P18054"},{"evidence_key":19,"evidence_type":"Protein Function","paper_id":"4a80e70d-bbb9-3df9-9210-7f33f5e972d6","reference_id":"23578768","reference_type":"Pubmed","uniprot_id":"P18054"},{"evidence_key":10,"evidence_type":"Protein Function","paper_id":"5ef9026b-4289-3c48-a5d4-0b29dfcca3c3","reference_id":"17493578","reference_type":"Pubmed","uniprot_id":"P18054"},{"evidence_key":16,"evidence_type":"Protein Function","paper_id":"5e589177-5971-34f6-a06a-32ed023b5e6a","reference_id":"2244907","reference_type":"Pubmed","uniprot_id":"P18054"},{"evidence_key":23,"evidence_type":"Protein Function","paper_id":"b5745087-8b5d-3add-8e40-8a9e3a60095d","reference_id":"32404334","reference_type":"Pubmed","uniprot_id":"P18054"},{"evidence_key":6,"evidence_type":"Protein Function","paper_id":"82743393-890d-4877-bc0f-2852a9d688c3","reference_id":"15489334","reference_type":"Pubmed","uniprot_id":"P18054"},{"evidence_key":24,"evidence_type":"Protein Function","paper_id":"8fbdef4c-594d-3ad6-a8eb-c04866a1a84a","reference_id":"8250832","reference_type":"Pubmed","uniprot_id":"P18054"},{"evidence_key":26,"evidence_type":"Protein Function","paper_id":"1a62df99-8172-3539-b9f8-d16bcd3cc33d","reference_id":"8500694","reference_type":"Pubmed","uniprot_id":"P18054"},{"evidence_key":15,"evidence_type":"Protein Function","paper_id":"fe609ce3-d6d9-3a2f-8719-9e180b110143","reference_id":"22237009","reference_type":"Pubmed","uniprot_id":"P18054"},{"evidence_key":20,"evidence_type":"Protein Function","paper_id":"d67eab7a-78cc-3b18-8ba1-25a29f22b493","reference_id":"2377602","reference_type":"Pubmed","uniprot_id":"P18054"},{"evidence_key":11,"evidence_type":"Protein Function","paper_id":"bde2a094-fdf7-3459-8d0a-9ab499ef9ca3","reference_id":"18311922","reference_type":"Pubmed","uniprot_id":"P18054"},{"evidence_key":9,"evidence_type":"Protein Function","paper_id":"3ad38ead-c06d-3fbc-a918-11ac364e1c6f","reference_id":"17460548","reference_type":"Pubmed","uniprot_id":"P18054"},{"evidence_key":14,"evidence_type":"Protein Function","paper_id":"a23b5e40-4a1c-38e4-ba97-8eece64b564c","reference_id":"2217179","reference_type":"Pubmed","uniprot_id":"P18054"},{"evidence_key":27,"evidence_type":"Protein Function","paper_id":"3e546c1b-e369-385c-95f9-6b29d45735a4","reference_id":"8912711","reference_type":"Pubmed","uniprot_id":"P18054"},{"evidence_key":22,"evidence_type":"Protein Function","paper_id":"8cb9eb58-399b-3620-b21a-175bfcd87a1b","reference_id":"25036362","reference_type":"Pubmed","uniprot_id":"P18054"},{"evidence_key":25,"evidence_type":"Protein Function","paper_id":"7e0947f7-9837-3c0c-a4fa-59092dbd3499","reference_id":"8319693","reference_type":"Pubmed","uniprot_id":"P18054"},{"evidence_key":12,"evidence_type":"Protein Function","paper_id":"44b384bd-4107-385d-a0ac-9be3d3695a8b","reference_id":"1851637","reference_type":"Pubmed","uniprot_id":"P18054"},{"evidence_key":5,"evidence_type":"Protein Function","paper_id":"81ffeca1-87f4-35e0-9ab7-f2364af6cb87","reference_id":"15308583","reference_type":"Pubmed","uniprot_id":"P18054"},{"evidence_key":18,"evidence_type":"Protein Function","paper_id":"a27499b4-c662-3d3d-a433-0e556f547bab","reference_id":"23504711","reference_type":"Pubmed","uniprot_id":"P18054"},{"evidence_key":28,"evidence_type":"Protein Function","paper_id":"c283d74f-e910-4eed-8faa-d61d85ab6915","reference_id":"9751607","reference_type":"Pubmed","uniprot_id":"P18054"}],"sequence_info":[{"related_target_id":"01d376c8f2e04c23a1e27339e36d9d61","sequence_number":449711,"uniprot_id":"P18054"}],"is_leaf":1}
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Involved in the biotransformation of 7-ethyl-10-hydroxycamptothecin (SN-38), the pharmacologically active metabolite of the anticancer drug irinotecan (PubMed:12181437, PubMed:18004212, PubMed:20610558, PubMed:23360619). 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PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein (PABP). PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenylation-dependent mRNA decapping and subsequent 5'-3' exonucleolytic degradation by XRN1. PAN3 acts as a regulator for PAN activity, recruiting the catalytic subunit PAN2 to mRNA via its interaction with RNA and PABP, and to miRNA targets via its interaction with GW182 family proteins.\nDecreases PAN2-mediated deadenylation, possibly by preventing progression into the second CCR4-NOT mediated stage of biphasic deadenylation. Has a significant effect on mRNA stability, generally stabilizing a subset of the transcriptome. Stabilizes mRNAs degraded by the AU-rich element (ARE)-mediated mRNA decay pathway but promotes degradation of mRNAs by the microRNA-mediated pathway (PubMed:28559491). Its activity influences mRNP remodeling, specifically reducing formation of a subset of P-bodies containing GW220, an isoform of TNRC6A (PubMed:28559491).\nEnhances PAN2 deadenylase activity and has an extensive effect on mRNA stability, generally enhancing mRNA decay across the transcriptome by multiple pathways, including the AU-rich element (ARE)-mediated pathway, microRNA-mediated pathway and the nonsense-mediated pathway (NMD) (PubMed:28559491). Its activity is required for efficient P-body formation (PubMed:28559491). May be involved in regulating mRNAs of genes involved in cell cycle progression and cell proliferation (PubMed:28559491).","display_priority":1,"if_manual":0,"lang":"EN","source_info":[{"code":"Q58A45","normalized_source_id":"96adf8c891514225a46927b3b16bd02a","source":"UNIPROT"}],"status":"ACTIVE"}],"paper_reference":[{"evidence_key":5,"evidence_type":"Protein Function","paper_id":"aed8c29d-ba79-3071-bdb1-86147719a3b4","reference_id":"17595167","reference_type":"Pubmed","uniprot_id":"Q58A45"},{"evidence_key":11,"evidence_type":"Protein Function","paper_id":"a11516e1-ce70-3a0a-b1cf-7f68526ca370","reference_id":"31570513","reference_type":"Pubmed","uniprot_id":"Q58A45"},{"evidence_key":10,"evidence_type":"Protein Function","paper_id":"afd7638d-0292-397c-b0e1-e92988cd7f8d","reference_id":"28559491","reference_type":"Pubmed","uniprot_id":"Q58A45"},{"evidence_key":4,"evidence_type":"Protein Function","paper_id":"61c1fca8-ddee-3a75-b5df-a57c8deb9783","reference_id":"14583602","reference_type":"Pubmed","uniprot_id":"Q58A45"},{"evidence_key":6,"evidence_type":"Protein Function","paper_id":"67560dcc-a5e6-3f16-927a-fe2a194d54af","reference_id":"18056425","reference_type":"Pubmed","uniprot_id":"Q58A45"},{"evidence_key":8,"evidence_type":"Protein Function","paper_id":"c7783703-9934-330e-874a-6680a69b80c3","reference_id":"21981923","reference_type":"Pubmed","uniprot_id":"Q58A45"},{"evidence_key":7,"evidence_type":"Protein Function","paper_id":"c3bb4068-4752-3116-b177-1f28372d4b8f","reference_id":"18625844","reference_type":"Pubmed","uniprot_id":"Q58A45"},{"evidence_key":9,"evidence_type":"Protein Function","paper_id":"b20eece2-d44a-36a9-bf12-b47d33a0b5af","reference_id":"23932717","reference_type":"Pubmed","uniprot_id":"Q58A45"}],"sequence_info":[{"related_target_id":"028195b39c34496cb25a1bb7ec50d130","sequence_number":9423390,"uniprot_id":"Q58A45"}],"is_leaf":1}
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Endoplasmic reticulum stress promotes processing of this form, releasing the transcription factor form that translocates into the nucleus, where it activates transcription of genes involved in the unfolded protein response (UPR) (PubMed:10564271, PubMed:11158310, PubMed:11779464).\nTranscription factor that initiates the unfolded protein response (UPR) during endoplasmic reticulum stress by activating transcription of genes involved in the UPR (PubMed:10564271, PubMed:11158310, PubMed:11163209, PubMed:11779464). Binds DNA on the 5'-CCAC[GA]-3'half of the ER stress response element (ERSE) (5'-CCAAT-N(9)-CCAC[GA]-3') and of ERSE II (5'-ATTGG-N-CCACG-3') (PubMed:10564271, PubMed:11158310, PubMed:11779464). Binding to ERSE requires binding of NF-Y to ERSE. Could also be involved in activation of transcription by the serum response factor (PubMed:10564271, PubMed:11158310, PubMed:11779464). May play a role in foveal development and cone function in the retina (PubMed:26029869).","display_priority":1,"if_manual":0,"lang":"EN","source_info":[{"code":"P18850","normalized_source_id":"96adf8c891514225a46927b3b16bd02a","source":"UNIPROT"}],"status":"ACTIVE"}],"paper_reference":[{"evidence_key":12,"evidence_type":"Protein Function","paper_id":"ff41ea15-5eb2-3c21-bc06-c21e97580cd4","reference_id":"17765680","reference_type":"Pubmed","uniprot_id":"P18850"},{"evidence_key":21,"evidence_type":"Protein Function","paper_id":"b4f4f5bb-2424-32d0-b4fc-9e4d65564510","reference_id":"9837962","reference_type":"Pubmed","uniprot_id":"P18850"},{"evidence_key":5,"evidence_type":"Protein Function","paper_id":"827bd4b7-4686-3b03-a76a-9e40a28ad9ff","reference_id":"10564271","reference_type":"Pubmed","uniprot_id":"P18850"},{"evidence_key":19,"evidence_type":"Protein Function","paper_id":"95666860-d51b-3b01-9239-9a235651f702","reference_id":"36739529","reference_type":"Pubmed","uniprot_id":"P18850"},{"evidence_key":13,"evidence_type":"Protein Function","paper_id":"e3a9ddfa-e6d8-32d5-b056-c9a179f5c31f","reference_id":"22682248","reference_type":"Pubmed","uniprot_id":"P18850"},{"evidence_key":18,"evidence_type":"Protein Function","paper_id":"e064058a-2446-3a94-b024-ac33b884cce6","reference_id":"34623328","reference_type":"Pubmed","uniprot_id":"P18850"},{"evidence_key":15,"evidence_type":"Protein Function","paper_id":"94c2e18c-4929-3256-8c98-53822af3e361","reference_id":"26029869","reference_type":"Pubmed","uniprot_id":"P18850"},{"evidence_key":8,"evidence_type":"Protein Function","paper_id":"94e8e730-0bd5-302c-aa1f-15919d16496c","reference_id":"11779464","reference_type":"Pubmed","uniprot_id":"P18850"},{"evidence_key":14,"evidence_type":"Protein Function","paper_id":"d95e5638-678e-39a7-99db-def18b21592f","reference_id":"2516827","reference_type":"Pubmed","uniprot_id":"P18850"},{"evidence_key":10,"evidence_type":"Protein Function","paper_id":"0106359d-8725-3992-97bb-c878451844d4","reference_id":"14699159","reference_type":"Pubmed","uniprot_id":"P18850"},{"evidence_key":17,"evidence_type":"Protein Function","paper_id":"394806f9-42a3-3e88-a4a1-e220686e7836","reference_id":"31875558","reference_type":"Pubmed","uniprot_id":"P18850"},{"evidence_key":9,"evidence_type":"Protein Function","paper_id":"3997170b-aa69-32dd-a614-ce5db6abfd9c","reference_id":"12782636","reference_type":"Pubmed","uniprot_id":"P18850"},{"evidence_key":16,"evidence_type":"Protein Function","paper_id":"b07a1921-aeb8-35f2-8cf1-423ae13379ec","reference_id":"26063662","reference_type":"Pubmed","uniprot_id":"P18850"},{"evidence_key":11,"evidence_type":"Protein Function","paper_id":"82743393-890d-4877-bc0f-2852a9d688c3","reference_id":"15489334","reference_type":"Pubmed","uniprot_id":"P18850"},{"evidence_key":6,"evidence_type":"Protein Function","paper_id":"8f3b81d8-11d6-385b-8447-3ca0ec3306d1","reference_id":"11158310","reference_type":"Pubmed","uniprot_id":"P18850"},{"evidence_key":20,"evidence_type":"Protein Function","paper_id":"cf0f9b36-f8b3-38e7-afe9-b301f1c58067","reference_id":"9271374","reference_type":"Pubmed","uniprot_id":"P18850"},{"evidence_key":7,"evidence_type":"Protein Function","paper_id":"e685a01f-227e-3fe4-890f-5a1925a19b80","reference_id":"11163209","reference_type":"Pubmed","uniprot_id":"P18850"}],"sequence_info":[{"related_target_id":"03fde1d920f24edbb0327ad3fbfbbc3d","sequence_number":451834,"uniprot_id":"P18850"}],"is_leaf":1}
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Can transport the statin pravastatin and may contribute to its disposition into the hepatocytes when the function of OATPs is compromised (PubMed:26239079). It is specifically activated by 3 to 5 carbons-containing short-chain fatty acids/SCFAs, including propionate (propanoate), butyrate (butanoate) and valerate (pentanoate) (PubMed:17393504). May operate the exchange of sulfated organic components against short-chain fatty acids/SCFAs, in particular butanoate, at the sinusoidal membrane of hepatocytes (PubMed:17393504).","display_priority":1,"if_manual":0,"lang":"EN","source_info":[{"code":"Q8IVM8","normalized_source_id":"96adf8c891514225a46927b3b16bd02a","source":"UNIPROT"}],"status":"ACTIVE"}],"paper_reference":[{"evidence_key":7,"evidence_type":"Protein Function","paper_id":"8df7e938-d28b-3487-9771-f578762b6dd2","reference_id":"28945155","reference_type":"Pubmed","uniprot_id":"Q8IVM8"},{"evidence_key":5,"evidence_type":"Protein Function","paper_id":"8dec0a2d-16f7-3ddd-82df-4002f3d987cc","reference_id":"17393504","reference_type":"Pubmed","uniprot_id":"Q8IVM8"},{"evidence_key":6,"evidence_type":"Protein Function","paper_id":"25b4126e-ca0a-3a35-9e8b-bdcf6f636efc","reference_id":"26239079","reference_type":"Pubmed","uniprot_id":"Q8IVM8"},{"evidence_key":3,"evidence_type":"Protein Function","paper_id":"bb75f3fe-0e81-3e8b-bea5-57fff59285b5","reference_id":"11327718","reference_type":"Pubmed","uniprot_id":"Q8IVM8"},{"evidence_key":4,"evidence_type":"Protein Function","paper_id":"eb0bc3b1-6ec0-3f52-9139-83306e6e052e","reference_id":"16959974","reference_type":"Pubmed","uniprot_id":"Q8IVM8"}],"sequence_info":[{"related_target_id":"0405cc4c1de148308ff7bd438d9936ec","sequence_number":646444,"uniprot_id":"Q8IVM8"}],"is_leaf":1}
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Both complexes regulate the spacing of nucleosomes along the chromatin and have the ability to slide mononucleosomes to the center of a DNA template (PubMed:28801535). Directly stimulates the ATPase activity of SMARCA5 in the NoRC-5 ISWI chromatin remodeling complex (PubMed:28801535). The NoRC-1 ISWI chromatin remodeling complex has a lower ATP hydrolysis rate than the NoRC-5 ISWI chromatin remodeling complex (PubMed:28801535). Within the NoRC-5 ISWI chromatin remodeling complex, mediates silencing of a fraction of rDNA by recruiting histone-modifying enzymes and DNA methyltransferases, leading to heterochromatin formation and transcriptional silencing (By similarity). In the complex, it plays a central role by being recruited to rDNA and by targeting chromatin modifying enzymes such as HDAC1, leading to repress RNA polymerase I transcription (By similarity). Recruited to rDNA via its interaction with TTF1 and its ability to recognize and bind histone H4 acetylated on 'Lys-16' (H4K16ac), leading to deacetylation of H4K5ac, H4K8ac, H4K12ac but not H4K16ac (By similarity). Specifically binds pRNAs, 150-250 nucleotide RNAs that are complementary in sequence to the rDNA promoter; pRNA-binding is required for heterochromatin formation and rDNA silencing (By similarity).","display_priority":1,"if_manual":0,"lang":"EN","source_info":[{"code":"Q9UIF9","normalized_source_id":"96adf8c891514225a46927b3b16bd02a","source":"UNIPROT"}],"status":"ACTIVE"}],"paper_reference":[{"evidence_key":9,"evidence_type":"Protein Function","paper_id":"0364b867-ed86-35b3-931a-9053025e6f12","reference_id":"19578370","reference_type":"Pubmed","uniprot_id":"Q9UIF9"},{"evidence_key":11,"evidence_type":"Protein Function","paper_id":"d8d2f6ee-490c-33a8-a73a-e8a80ec9da42","reference_id":"28801535","reference_type":"Pubmed","uniprot_id":"Q9UIF9"},{"evidence_key":10,"evidence_type":"Protein Function","paper_id":"328c9875-627d-3984-8d26-b7b07120d093","reference_id":"26100909","reference_type":"Pubmed","uniprot_id":"Q9UIF9"}],"sequence_info":[{"related_target_id":"0407d79a6282493881ce36a21fb7e247","sequence_number":1488665,"uniprot_id":"Q9UIF9"}],"is_leaf":1}
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Capable of transcription autoinactivation (By similarity). Binds to the consensus sequence 5'-C/GTAAT-3' in downstream activin regulatory elements (DARE) in the gene promoter, thereby repressing the transcription of CGA/alpha-GSU and GNRHR (By similarity). Represses transcription of myoblast differentiation factors (By similarity). Binds to core enhancer regions in target gene promoters of myoblast differentiation factors with binding specificity facilitated by interaction with PIAS1 (By similarity). Regulates, in a stage-specific manner, a developmental program of gene expression in the fetal tooth bud that controls odontoblast differentiation and proliferation of dental mesenchymal cells (By similarity). At the bud stage, required for mesenchymal molar tooth bud development via facilitating reciprocal signaling between dental epithelial and mesenchymal cells (By similarity). May also regulate expression of Wnt antagonists such as DKK2 and SFPR2 in the developing tooth mesenchyme (By similarity). Required for BMP4 expression in dental mesenchyme cells (By similarity). Also, in response to BMP4, required for BMP4 expression in neighboring dental epithelial cells (By similarity). Required for maximal FGF4-induced expression of SDC1 in dental mesenchyme cells (By similarity). Also in response to SDC1, required for SDC1 expression in neighboring dental epithelial cells (By similarity). At the early bell stage, acts to drive proliferation of dental mesenchyme cells, however during the late bell stage acts as an homeostatic regulator of the cell cycle (By similarity). Regulates proliferation and inhibits premature mesenchymal odontogenesis during the bell stage via inhibition of the Wnt signaling component CTNNB1 and subsequent repression of the odontoblast differentiation factors BMP2, BMP4, LEF1, ALPL and BGLAP/OCN (By similarity). Additionally, required for correct development and fusion of the palatal shelves and embryonic mandibular formation (By similarity). Plays a role in embryonic bone formation of the middle ear, skull and nasal bones (By similarity). Required for correct formation and thickness of the nail plate (By similarity). May play a role in limb-pattern formation (By similarity).","display_priority":1,"if_manual":0,"lang":"EN","source_info":[{"code":"P28360","normalized_source_id":"96adf8c891514225a46927b3b16bd02a","source":"UNIPROT"}],"status":"ACTIVE"}],"paper_reference":[{"evidence_key":6,"evidence_type":"Protein Function","paper_id":"f0054579-b2ba-330e-bff3-c8b79e96eaad","reference_id":"12807959","reference_type":"Pubmed","uniprot_id":"P28360"},{"evidence_key":4,"evidence_type":"Protein Function","paper_id":"d5c474ad-69f5-3d5b-9640-8760b2d1e20c","reference_id":"11369996","reference_type":"Pubmed","uniprot_id":"P28360"},{"evidence_key":8,"evidence_type":"Protein Function","paper_id":"dc67bb3c-c934-3902-81de-bc9bf71948c8","reference_id":"16600910","reference_type":"Pubmed","uniprot_id":"P28360"},{"evidence_key":5,"evidence_type":"Protein Function","paper_id":"3186f6c9-b6b3-3b2a-8d00-5b57f2f7f8be","reference_id":"12097313","reference_type":"Pubmed","uniprot_id":"P28360"},{"evidence_key":7,"evidence_type":"Protein Function","paper_id":"536c0722-3606-3189-9684-3739bcb30a2e","reference_id":"14702039","reference_type":"Pubmed","uniprot_id":"P28360"},{"evidence_key":9,"evidence_type":"Protein Function","paper_id":"e519f473-e2ba-3afb-822c-3e32a06520fa","reference_id":"8696335","reference_type":"Pubmed","uniprot_id":"P28360"}],"sequence_info":[{"related_target_id":"041c2a6423804bbf9e7cb78906457abb","sequence_number":1001180,"uniprot_id":"P28360"}],"is_leaf":1}
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Its role in cellular physiology is to improve mitochondrial performance (PubMed:32234310). CL is critical for the coassembly of lipids and proteins in mitochondrial membranes, for instance, remodeling of the acyl groups of CL in the mitochondrial inner membrane affects the assembly and stability of respiratory chain complex IV and its supercomplex forms (By similarity). Catalyzes the transacylation between phospholipids and lysophospholipids, with the highest rate being between phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) and CL. Catalyzes both 1-acyl-sn-glycero-3-phosphocholine (lysophosphatidylcholine or LPC) reacylation and PC-CL transacylation, that means, it exchanges acyl groups between CL and PC by a combination of forward and reverse transacylations. Also catalyzes transacylations between other phospholipids such as phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-phosphoethanolamine or PE) and CL, between PC and PE, and between PC and phosphatidate (1,2-diacyl-sn-glycero-3-phosphate or PA), although at lower rate. Not regiospecific, it transfers acyl groups into any of the sn-1 and sn-2 positions of the monolysocardiolipin (MLCL), which is an important prerequisite for uniformity and symmetry in CL acyl distribution. Cannot transacylate dilysocardiolipin (DLCL), thus, the role of MLCL is limited to that of an acyl acceptor. CoA-independent, it can reshuffle molecular species within a single phospholipid class. Redistributes fatty acids between MLCL, CL, and other lipids, which prolongs the half-life of CL. Its action is completely reversible, which allows for cyclic changes, such as fission and fusion or bending and flattening of the membrane. Hence, by contributing to the flexibility of the lipid composition, it plays an important role in the dynamics of mitochondria membranes. Essential for the final stage of spermatogenesis, spermatid individualization (By similarity). Required for the initiation of mitophagy (PubMed:33096711). Required to ensure progression of spermatocytes through meiosis (By similarity). Exon 7 of human tafazzin is essential for catalysis (PubMed:19700766).\nCatalyzes the transacylation between lysophosphatidate (such as 1-acyl-sn-glycero-3-phosphate) and phosphatidylglycerol (1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol)) (PubMed:19700766). Contributes to cardiolipin (1',3'-bis-[1,2-diacyl-sn-glycero-3-phospho]-glycerol or CL) remodeling (PubMed:12930833, PubMed:19700766).\nCatalyzes the transacylation between lysophospholipids and phospholipids, and plays a fundamental role in cardiolipin (1',3'-bis-[1,2-diacyl-sn-glycero-3-phospho]-glycerol or CL) metabolism and remodeling.\nCatalytically inactive.\nCatalytically inactive.","display_priority":1,"if_manual":0,"lang":"EN","source_info":[{"code":"Q16635","normalized_source_id":"96adf8c891514225a46927b3b16bd02a","source":"UNIPROT"}],"status":"ACTIVE"}],"paper_reference":[{"evidence_key":10,"evidence_type":"Protein Function","paper_id":"ca503665-acce-3fd5-b950-85e66aba0b86","reference_id":"19700766","reference_type":"Pubmed","uniprot_id":"Q16635"},{"evidence_key":12,"evidence_type":"Protein Function","paper_id":"d28ec4e4-9a62-3e43-95e8-dae6b50f92dd","reference_id":"25598000","reference_type":"Pubmed","uniprot_id":"Q16635"},{"evidence_key":13,"evidence_type":"Protein Function","paper_id":"b24a06a6-a751-3537-a97f-f696cfd32f4a","reference_id":"26908608","reference_type":"Pubmed","uniprot_id":"Q16635"},{"evidence_key":14,"evidence_type":"Protein Function","paper_id":"adfd0161-0d23-3edf-b785-5443b54255b9","reference_id":"29129703","reference_type":"Pubmed","uniprot_id":"Q16635"},{"evidence_key":11,"evidence_type":"Protein Function","paper_id":"b8822fa8-3a21-3a44-a7c8-efdd531091de","reference_id":"23409742","reference_type":"Pubmed","uniprot_id":"Q16635"},{"evidence_key":8,"evidence_type":"Protein Function","paper_id":"03f88004-c5a4-3943-9de4-c74e68a4f690","reference_id":"19164547","reference_type":"Pubmed","uniprot_id":"Q16635"},{"evidence_key":9,"evidence_type":"Protein Function","paper_id":"2cd0b48e-d697-3e70-8005-f2719c6b9f16","reference_id":"19416660","reference_type":"Pubmed","uniprot_id":"Q16635"},{"evidence_key":16,"evidence_type":"Protein Function","paper_id":"03f8c5da-b8de-3af5-acd9-ed9c0d20cdde","reference_id":"9382096","reference_type":"Pubmed","uniprot_id":"Q16635"},{"evidence_key":5,"evidence_type":"Protein Function","paper_id":"81f634ff-5530-35e5-b16d-2395df9d8e54","reference_id":"11238270","reference_type":"Pubmed","uniprot_id":"Q16635"},{"evidence_key":15,"evidence_type":"Protein Function","paper_id":"f9fa7d9c-0e88-3077-bd2b-63c391c45307","reference_id":"33096711","reference_type":"Pubmed","uniprot_id":"Q16635"},{"evidence_key":7,"evidence_type":"Protein Function","paper_id":"3bddb71a-2a62-38d7-ae32-922f2c327959","reference_id":"12930833","reference_type":"Pubmed","uniprot_id":"Q16635"},{"evidence_key":6,"evidence_type":"Protein Function","paper_id":"c783b594-2dbc-344d-9bef-46b5f353971d","reference_id":"12032589","reference_type":"Pubmed","uniprot_id":"Q16635"},{"evidence_key":17,"evidence_type":"Protein Function","paper_id":"927cb781-fce2-36ca-85e3-451c00405426","reference_id":"9382097","reference_type":"Pubmed","uniprot_id":"Q16635"}],"sequence_info":[{"related_target_id":"041c7afa57fd4f288d2c12a4e4176d2c","sequence_number":1316552,"uniprot_id":"Q16635"}],"is_leaf":1}
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Acts as a regulator of hypoxia-inducible gene expression (PubMed:11573933, PubMed:16126907, PubMed:19694616, PubMed:20416395, PubMed:21069422). Functions as an inhibitor of angiogenesis in hypoxic cells of the cornea. Plays a role in the development of the cardiorespiratory system. May also be involved in apoptosis (By similarity).\nAttenuates the ability of transcription factor HIF1A to bind to hypoxia-responsive elements (HRE) located within the enhancer/promoter of hypoxia-inducible target genes and hence inhibits HRE-driven transcriptional activation. Also inhibits hypoxia-inducible ARNT-mediated gene expression.\nAttenuates the ability of transcription factor HIF1A and EPAS1/HIF2A to bind to hypoxia-responsive elements (HRE) located within the enhancer/promoter of hypoxia-inducible target genes and hence inhibits HRE-driven transcriptional activation (PubMed:16126907, PubMed:17998805, PubMed:19694616, PubMed:20416395). May act as a tumor suppressor and inhibits malignant cell transformation (PubMed:17998805).\nAttenuates the ability of transcription factor HIF1A to bind to hypoxia-responsive elements (HRE) located within the enhancer/promoter of hypoxia-inducible target genes and hence inhibits HRE-driven transcriptional activation.\nAttenuates the ability of transcription factor HIF1A to bind to hypoxia-responsive elements (HRE) located within the enhancer/promoter of hypoxia-inducible target genes and hence inhibits HRE-driven transcriptional activation.","display_priority":1,"if_manual":0,"lang":"EN","source_info":[{"code":"Q9Y2N7","normalized_source_id":"96adf8c891514225a46927b3b16bd02a","source":"UNIPROT"}],"status":"ACTIVE"}],"paper_reference":[{"evidence_key":6,"evidence_type":"Protein Function","paper_id":"35716740-5b05-3569-bd5c-658210149b57","reference_id":"11573933","reference_type":"Pubmed","uniprot_id":"Q9Y2N7"},{"evidence_key":11,"evidence_type":"Protein Function","paper_id":"bbc950e6-8ccb-33f0-9a1a-faff5c508ee8","reference_id":"17998805","reference_type":"Pubmed","uniprot_id":"Q9Y2N7"},{"evidence_key":12,"evidence_type":"Protein Function","paper_id":"cc0ff940-cf1b-3c31-bf21-04294282bfb7","reference_id":"19694616","reference_type":"Pubmed","uniprot_id":"Q9Y2N7"},{"evidence_key":7,"evidence_type":"Protein Function","paper_id":"69d37ab6-59c7-30ef-90a3-8b665d77f6d8","reference_id":"12538644","reference_type":"Pubmed","uniprot_id":"Q9Y2N7"},{"evidence_key":9,"evidence_type":"Protein Function","paper_id":"5646205b-2d8f-39c5-987a-13be145ca0af","reference_id":"16126907","reference_type":"Pubmed","uniprot_id":"Q9Y2N7"},{"evidence_key":10,"evidence_type":"Protein Function","paper_id":"ad235ce9-60cc-3b15-b969-749ad43f380a","reference_id":"16775626","reference_type":"Pubmed","uniprot_id":"Q9Y2N7"},{"evidence_key":13,"evidence_type":"Protein Function","paper_id":"68838d0c-053a-3364-81fc-5cb0a0f57a5b","reference_id":"20416395","reference_type":"Pubmed","uniprot_id":"Q9Y2N7"},{"evidence_key":8,"evidence_type":"Protein Function","paper_id":"82743393-890d-4877-bc0f-2852a9d688c3","reference_id":"15489334","reference_type":"Pubmed","uniprot_id":"Q9Y2N7"},{"evidence_key":14,"evidence_type":"Protein Function","paper_id":"46094c95-2205-3d9d-ab39-3845355eb824","reference_id":"21069422","reference_type":"Pubmed","uniprot_id":"Q9Y2N7"}],"sequence_info":[{"related_target_id":"041d0616dbb043c28f472ca99df8c0e2","sequence_number":1293133,"uniprot_id":"Q9Y2N7"}],"is_leaf":1}
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Inhibits dissociation of IRAK1 and IRAK4 from the Toll-like receptor signaling complex by either inhibiting the phosphorylation of IRAK1 and IRAK4 or stabilizing the receptor complex (By similarity). 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Converts changes in the transmembrane electric potential into mechanical displacements resulting in the coupling of its expansion to movement of a charged voltage sensor across the lipid membrane (By similarity). The nature of the voltage sensor is not completely clear, and two models compete. In the first model, acts as an incomplete transporter where intracellular chloride anion acts as extrinsic voltage sensor that drives conformational change in the protein which is sufficient to produce a length change in the plane of the membrane and hence in the length of the OHC (By similarity). The second model in which multiple charged amino acid residues are distributed at the intracellular and extracellular membrane interfaces that form an intrinsic voltage sensor, whose movement produces the non-linear capacitance (NLC) (PubMed:34390643). However, the effective voltage sensor may be the result of a hybrid voltage sensor, assembled from intrinsic charge (charged residues) and extrinsic charge (bound anion) (By similarity). Notably, binding of anions to the anion-binding pocket partially neutralizes the intrinsic positive charge rather than to form an electrically negative sensor, therefore remaining charge may serve as voltage sensor that, after depolarization, moves from down (expanded state) to up (contracted) conformation, which is accompanied by an eccentric contraction of the intermembrane cross-sectional area of the protein as well as a major increase in the hydrophobic thickness of the protein having as consequences the plasma membrane thickening and the cell contraction after membrane depolarization (PubMed:34390643). The anion-binding pocket transits from the inward-open (Down) state, where it is exposed toward the intracellular solvent in the absence of anion, to the occluded (Up) state upon anion binding (PubMed:34390643). Salicylate competes for the anion-binding site and inhibits the voltage-sensor movement, and therefore inhibits the charge transfer and electromotility by displacing Cl(-) from the anion-binding site and by preventing the structural transitions to the contracted state (PubMed:34390643). In addition, can act as a weak Cl(-)/HCO3(-) antiporter across the cell membrane and so regulate the intracellular pH of the outer hair cells (OHCs), while firstly found as being unable to mediate electrogenic anion transport (By similarity). 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The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, BMAL1, BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and BMAL1 or BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-BMAL1|BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress BMAL1 transcription, respectively. BMAL1 positively regulates myogenesis and negatively regulates adipogenesis via the transcriptional control of the genes of the canonical Wnt signaling pathway. Plays a role in normal pancreatic beta-cell function; regulates glucose-stimulated insulin secretion via the regulation of antioxidant genes NFE2L2/NRF2 and its targets SESN2, PRDX3, CCLC and CCLM. Negatively regulates the mTORC1 signaling pathway; regulates the expression of MTOR and DEPTOR. Controls diurnal oscillations of Ly6C inflammatory monocytes; rhythmic recruitment of the PRC2 complex imparts diurnal variation to chemokine expression that is necessary to sustain Ly6C monocyte rhythms. Regulates the expression of HSD3B2, STAR, PTGS2, CYP11A1, CYP19A1 and LHCGR in the ovary and also the genes involved in hair growth. Plays an important role in adult hippocampal neurogenesis by regulating the timely entry of neural stem/progenitor cells (NSPCs) into the cell cycle and the number of cell divisions that take place prior to cell-cycle exit. Regulates the circadian expression of CIART and KLF11. The CLOCK-BMAL1 heterodimer regulates the circadian expression of SERPINE1/PAI1, VWF, B3, CCRN4L/NOC, NAMPT, DBP, MYOD1, PPARGC1A, PPARGC1B, SIRT1, GYS2, F7, NGFR, GNRHR, BHLHE40/DEC1, ATF4, MTA1, KLF10 and also genes implicated in glucose and lipid metabolism. Promotes rhythmic chromatin opening, regulating the DNA accessibility of other transcription factors. The NPAS2-BMAL1 heterodimer positively regulates the expression of MAOA, F7 and LDHA and modulates the circadian rhythm of daytime contrast sensitivity by regulating the rhythmic expression of adenylate cyclase type 1 (ADCY1) in the retina. The preferred binding motif for the CLOCK-BMAL1 heterodimer is 5'-CACGTGA-3', which contains a flanking adenine nucleotide at the 3-prime end of the canonical 6-nucleotide E-box sequence (PubMed:23229515). CLOCK specifically binds to the half-site 5'-CAC-3', while BMAL1 binds to the half-site 5'-GTGA-3' (PubMed:23229515). The CLOCK-BMAL1 heterodimer also recognizes the non-canonical E-box motifs 5'-AACGTGA-3' and 5'-CATGTGA-3' (PubMed:23229515). Essential for the rhythmic interaction of CLOCK with ASS1 and plays a critical role in positively regulating CLOCK-mediated acetylation of ASS1 (PubMed:28985504). Plays a role in protecting against lethal sepsis by limiting the expression of immune checkpoint protein CD274 in macrophages in a PKM2-dependent manner (By similarity). 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Controls the activity of the transcriptional regulators GLI1, GLI2 and GLI3 by opposing the effect of SUFU and promoting their nuclear localization (PubMed:10806483). GLI2 requires an additional function of STK36 to become transcriptionally active, but the enzyme does not need to possess an active kinase catalytic site for this to occur (PubMed:10806483). Required for postnatal development, possibly by regulating the homeostasis of cerebral spinal fluid or ciliary function. 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At physiologic concentrations, has higher specific activity in the presence of NADH (PubMed:23024808, PubMed:2722838, PubMed:6894153). Involved in cellular response to oxidative stress (PubMed:25865492). In some cell types, such as erythrocytes, its primary function may be the generation of NADP(+) (PubMed:2722838, PubMed:6894153).","display_priority":1,"if_manual":0,"lang":"EN","source_info":[{"code":"Q96C36","normalized_source_id":"96adf8c891514225a46927b3b16bd02a","source":"UNIPROT"}],"status":"ACTIVE"}],"paper_reference":[{"evidence_key":3,"evidence_type":"Protein Function","paper_id":"96623c48-99f5-324f-b082-8a8f9db3d603","reference_id":"23024808","reference_type":"Pubmed","uniprot_id":"Q96C36"},{"evidence_key":5,"evidence_type":"Protein Function","paper_id":"c4a915e3-2cfa-3388-b331-0da0e2eb51c4","reference_id":"25865492","reference_type":"Pubmed","uniprot_id":"Q96C36"},{"evidence_key":4,"evidence_type":"Protein Function","paper_id":"461e2c34-7f99-3a37-8538-9c2ddfd39c34","reference_id":"24930674","reference_type":"Pubmed","uniprot_id":"Q96C36"},{"evidence_key":7,"evidence_type":"Protein Function","paper_id":"508f33cf-90e3-3cfa-b41f-c8e1efffc883","reference_id":"6894153","reference_type":"Pubmed","uniprot_id":"Q96C36"},{"evidence_key":6,"evidence_type":"Protein Function","paper_id":"bfb3473d-b7af-4234-b385-138177d0536b","reference_id":"2722838","reference_type":"Pubmed","uniprot_id":"Q96C36"},{"evidence_key":6,"evidence_type":"Protein Function","paper_id":"f376ba06-0710-4210-980f-4eb3d2454752","reference_id":"2722838","reference_type":"Pubmed","uniprot_id":"Q96C36"}],"sequence_info":[{"related_target_id":"0499314d4f4340b3a0a6f974232d7e03","sequence_number":4648821,"uniprot_id":"Q96C36"}],"is_leaf":1}
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PubMed:28114273). In vitro also methylates unmodified 'Lys-20' (H4K20me0) of histone H4 and nucleosomes (PubMed:24396869). H4 'Lys-20' trimethylation represents a specific tag for epigenetic transcriptional repression. Mainly functions in pericentric heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin in these regions. KMT5B is targeted to histone H3 via its interaction with RB1 family proteins (RB1, RBL1 and RBL2) (By similarity). Plays a role in myogenesis by regulating the expression of target genes, such as EID3 (PubMed:23720823). Facilitates TP53BP1 foci formation upon DNA damage and proficient non-homologous end-joining (NHEJ)-directed DNA repair by catalyzing the di- and trimethylation of 'Lys-20' of histone H4 (PubMed:28114273). May play a role in class switch reconbination by catalyzing the di- and trimethylation of 'Lys-20' of histone H4 (By similarity).","display_priority":1,"if_manual":0,"lang":"EN","source_info":[{"code":"Q4FZB7","normalized_source_id":"96adf8c891514225a46927b3b16bd02a","source":"UNIPROT"}],"status":"ACTIVE"}],"paper_reference":[{"evidence_key":8,"evidence_type":"Protein Function","paper_id":"f9006f31-4be2-3434-a984-7d01711c0cc9","reference_id":"23720823","reference_type":"Pubmed","uniprot_id":"Q4FZB7"},{"evidence_key":6,"evidence_type":"Protein Function","paper_id":"82743393-890d-4877-bc0f-2852a9d688c3","reference_id":"15489334","reference_type":"Pubmed","uniprot_id":"Q4FZB7"},{"evidence_key":7,"evidence_type":"Protein Function","paper_id":"7e5b7ca9-1686-38bf-80d3-57aa4ef2504a","reference_id":"16322686","reference_type":"Pubmed","uniprot_id":"Q4FZB7"},{"evidence_key":9,"evidence_type":"Protein Function","paper_id":"65356c67-a5af-3a4d-ae89-9880ffa82444","reference_id":"24396869","reference_type":"Pubmed","uniprot_id":"Q4FZB7"},{"evidence_key":12,"evidence_type":"Protein Function","paper_id":"db0e4616-8410-35e2-946e-e683da2f3819","reference_id":"29276005","reference_type":"Pubmed","uniprot_id":"Q4FZB7"},{"evidence_key":10,"evidence_type":"Protein Function","paper_id":"35cf5f7b-8468-37ff-83ba-1baa8f1dd1ee","reference_id":"28114273","reference_type":"Pubmed","uniprot_id":"Q4FZB7"},{"evidence_key":11,"evidence_type":"Protein Function","paper_id":"1f823f85-8402-38a4-95d9-2a648f6ade42","reference_id":"28191889","reference_type":"Pubmed","uniprot_id":"Q4FZB7"}],"sequence_info":[{"related_target_id":"04add7f430d94579a4c45d3a6650c3c0","sequence_number":635724,"uniprot_id":"Q4FZB7"}],"is_leaf":1}
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When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in proteotoxic stress response and cell cycle; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling. During ubiquitination, the acceptor ubiquitin is positioned in the active site via direct interaction with the E2 ubiquitin-conjugating enzymes such as UBE2R2 (PubMed:38326650). 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Selectively transfers the sulfate group onto the terminal GlcNAc of alpha1,3-Man or alpha1,6-Man antenna of complex-type N-glycans depending on glycan composition. Only sulfates terminal GlcNAc of alpha1,3-Man antenna of G0 complex-type N-glycans. Can sulfate keratan-type N-acetyllactosamine (LacNAc) repeats generating epitopes for self versus non-self immune recognition by C-type lectins (PubMed:35939855, PubMed:38034954). Transfers the sulfate group primarily on core 2 GlcNAcbeta1-6(Galbeta1-3)GalNAcalpha-Ser/Thr and with lower efficiency on extended core 1 GlcNAcbeta1-3Galbeta1-3GalNAcalpha-Ser/Thr based O-linked glycans on peripheral node addressins (PNAds) expressed on the lumenal side of high endothelial venules (HEVs). Shares substrate specificity with CHST4 and both contribute to generate sialyl 6-sulfo Lewis X determinant (also known as MECA-79 epitope) for SELL recognition, a prerequisite for continuous lymphocyte homing into peripheral lymph nodes and antigen immune surveillance (By similarity) (PubMed:9722682). Has no activity toward alpha-linked GlcNAc moiety exposed at the non-reducing ends or to internally located GlcNAc residues (PubMed:11042394).","display_priority":1,"if_manual":0,"lang":"EN","source_info":[{"code":"Q9Y4C5","normalized_source_id":"96adf8c891514225a46927b3b16bd02a","source":"UNIPROT"}],"status":"ACTIVE"}],"paper_reference":[{"evidence_key":7,"evidence_type":"Protein Function","paper_id":"08373337-facc-33ec-8c3f-d1c3199e1e7a","reference_id":"11726653","reference_type":"Pubmed","uniprot_id":"Q9Y4C5"},{"evidence_key":11,"evidence_type":"Protein Function","paper_id":"a58b93ee-3273-3078-9768-9b1a899d2851","reference_id":"15632306","reference_type":"Pubmed","uniprot_id":"Q9Y4C5"},{"evidence_key":8,"evidence_type":"Protein Function","paper_id":"c3c75620-89bb-3461-94c9-48cea3d78c06","reference_id":"12501187","reference_type":"Pubmed","uniprot_id":"Q9Y4C5"},{"evidence_key":9,"evidence_type":"Protein Function","paper_id":"ddb9fb03-0246-3d56-85b3-dddf756c0746","reference_id":"12855678","reference_type":"Pubmed","uniprot_id":"Q9Y4C5"},{"evidence_key":6,"evidence_type":"Protein Function","paper_id":"be8eecd9-8908-3348-8d05-1656ec78e389","reference_id":"11310842","reference_type":"Pubmed","uniprot_id":"Q9Y4C5"},{"evidence_key":16,"evidence_type":"Protein Function","paper_id":"ddedea37-35ac-39e4-9516-cc096d5c7c2b","reference_id":"9722682","reference_type":"Pubmed","uniprot_id":"Q9Y4C5"},{"evidence_key":12,"evidence_type":"Protein Function","paper_id":"3631e5ee-be0d-37c7-b5ee-2aa142d6a151","reference_id":"19571171","reference_type":"Pubmed","uniprot_id":"Q9Y4C5"},{"evidence_key":13,"evidence_type":"Protein Function","paper_id":"865348e5-1811-3117-8187-f9d85a54e872","reference_id":"22260995","reference_type":"Pubmed","uniprot_id":"Q9Y4C5"},{"evidence_key":14,"evidence_type":"Protein Function","paper_id":"16bbe680-c21c-308b-bba3-95131a179c5c","reference_id":"35939855","reference_type":"Pubmed","uniprot_id":"Q9Y4C5"},{"evidence_key":4,"evidence_type":"Protein Function","paper_id":"8ef750c9-7041-3d97-9d28-360e57eae6ec","reference_id":"10049591","reference_type":"Pubmed","uniprot_id":"Q9Y4C5"},{"evidence_key":15,"evidence_type":"Protein Function","paper_id":"ace53178-f120-418c-9998-935700daff74","reference_id":"38034954","reference_type":"Pubmed","uniprot_id":"Q9Y4C5"},{"evidence_key":5,"evidence_type":"Protein Function","paper_id":"9279768f-6a12-3f2f-91db-44ca3ecf069e","reference_id":"11042394","reference_type":"Pubmed","uniprot_id":"Q9Y4C5"},{"evidence_key":10,"evidence_type":"Protein Function","paper_id":"c26a5f76-a373-3480-8a0a-1d0e8e0e1b87","reference_id":"15220337","reference_type":"Pubmed","uniprot_id":"Q9Y4C5"}],"sequence_info":[{"related_target_id":"05155fe6496948f49f821c47a2137eef","sequence_number":451608,"uniprot_id":"Q9Y4C5"}],"is_leaf":1}
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cytoskeleton (PubMed:15731758, PubMed:19605363, PubMed:19623537, PubMed:33713620, PubMed:34744632). Plays an important role in vesicular trafficking processes, namely clathrin-mediated endocytosis (CME), exocytic and clathrin-coated vesicle from the trans-Golgi network, and PDGF stimulated macropinocytosis (PubMed:15731758, PubMed:19623537, PubMed:33713620). During vesicular trafficking process, associates to the membrane, through lipid binding, and self-assembles into ring-like structure through oligomerization to form a helical polymer around the vesicle membrane and leading to vesicle scission (PubMed:17636067, PubMed:34744632, PubMed:36445308). Plays a role in organization of the actin cytoskeleton by mediating arrangement of stress fibers and actin bundles in podocytes (By similarity). During organization of the actin cytoskeleton, self-assembles into ring-like structure that directly bundles actin filaments to form typical membrane tubules decorated with dynamin spiral polymers (By similarity). Self-assembly increases GTPase activity and the GTP hydrolysis causes the rapid depolymerization of dynamin spiral polymers, and results in dispersion of actin bundles (By similarity). Remodels, through its interaction with CTTN, bundled actin filaments in a GTPase-dependent manner and plays a role in orchestrating the global actomyosin cytoskeleton (PubMed:19605363). The interaction with CTTN stabilizes the interaction of DNM2 and actin filaments and stimulates the intrinsic GTPase activity that results in actin filament-barbed ends and increases the sensitivity of filaments in bundles to the actin depolymerizing factor, CFL1 (By similarity). Plays a role in the autophagy process, by participating in the formation of ATG9A vesicles destined for the autophagosomes through its interaction with SNX18 (PubMed:29437695), by mediating recycling endosome scission leading to autophagosome release through MAP1LC3B interaction (PubMed:29437695, PubMed:32315611). Also regulates maturation of apoptotic cell corpse-containing phagosomes by recruiting PIK3C3 to the phagosome membrane (By similarity). Also plays a role in cytokinesis (By similarity). May participate in centrosome cohesion through its interaction with TUBG1 (By similarity). Plays a role in the regulation of neuron morphology, axon growth and formation of neuronal growth cones (By similarity). Involved in membrane tubulation (PubMed:24135484).","display_priority":1,"if_manual":0,"lang":"EN","source_info":[{"code":"P50570","normalized_source_id":"96adf8c891514225a46927b3b16bd02a","source":"UNIPROT"}],"status":"ACTIVE"}],"paper_reference":[{"evidence_key":37,"evidence_type":"Protein Function","paper_id":"8fb6e1e7-814b-3ab1-9300-7a4904e03ac9","reference_id":"36445308","reference_type":"Pubmed","uniprot_id":"P50570"},{"evidence_key":19,"evidence_type":"Protein Function","paper_id":"a5db70ba-5c53-3a81-b21d-1f2469960b79","reference_id":"18353773","reference_type":"Pubmed","uniprot_id":"P50570"},{"evidence_key":25,"evidence_type":"Protein Function","paper_id":"41acbd78-3e2c-3a4b-becc-46dff0b8bc8a","reference_id":"19932619","reference_type":"Pubmed","uniprot_id":"P50570"},{"evidence_key":11,"evidence_type":"Protein 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Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression and by phosphorylation and inhibition of proapoptotic proteins (BAD, MAP3K5, FOXO3) (PubMed:18593906). Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase of transcriptional activity (By similarity). The stabilization of MYC exerted by PIM1 might explain partly the strong synergism between these two oncogenes in tumorigenesis (By similarity). Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1 (By similarity). Phosphorylation of MAP3K5, another proapoptotic protein, by PIM1, significantly decreases MAP3K5 kinase activity and inhibits MAP3K5-mediated phosphorylation of JNK and JNK/p38MAPK subsequently reducing caspase-3 activation and cell apoptosis (PubMed:19749799). Stimulates cell cycle progression at the G1-S and G2-M transitions by phosphorylation of CDC25A and CDC25C (PubMed:16356754). Phosphorylation of CDKN1A, a regulator of cell cycle progression at G1, results in the relocation of CDKN1A to the cytoplasm and enhanced CDKN1A protein stability (PubMed:12431783). Promotes cell cycle progression and tumorigenesis by down-regulating expression of a regulator of cell cycle progression, CDKN1B, at both transcriptional and post-translational levels (PubMed:18593906). Phosphorylation of CDKN1B, induces 14-3-3 proteins binding, nuclear export and proteasome-dependent degradation (PubMed:18593906). May affect the structure or silencing of chromatin by phosphorylating HP1 gamma/CBX3 (PubMed:10664448). Also acts as a regulator of homing and migration of bone marrow cells involving functional interaction with the CXCL12-CXCR4 signaling axis (By similarity). Acts as a positive regulator of mTORC1 signaling by mediating phosphorylation and inhibition of DEPDC5 component of the GATOR1 complex (PubMed:31548394). Acts as a negative regulator of innate immunity by mediating phosphorylation and inactivation of GBP1 in absence of infection: phosphorylation of GBP1 induces interaction with 14-3-3 protein sigma (SFN) and retention in the cytosol (PubMed:37797010). Also phosphorylates and activates the ATP-binding cassette transporter ABCG2, allowing resistance to drugs through their excretion from cells (PubMed:18056989). Promotes brown adipocyte differentiation (By similarity).","display_priority":1,"if_manual":0,"lang":"EN","source_info":[{"code":"P11309","normalized_source_id":"96adf8c891514225a46927b3b16bd02a","source":"UNIPROT"}],"status":"ACTIVE"}],"paper_reference":[{"evidence_key":5,"evidence_type":"Protein Function","paper_id":"47a3d324-638f-3b86-b73b-7a2895623e35","reference_id":"12431783","reference_type":"Pubmed","uniprot_id":"P11309"},{"evidence_key":10,"evidence_type":"Protein Function","paper_id":"491bbb4f-0d7d-35ab-91d3-39a5231471c3","reference_id":"15798097","reference_type":"Pubmed","uniprot_id":"P11309"},{"evidence_key":4,"evidence_type":"Protein Function","paper_id":"eb521298-b5f8-3b5a-90f7-62066b9d2eec","reference_id":"10664448","reference_type":"Pubmed","uniprot_id":"P11309"},{"evidence_key":17,"evidence_type":"Protein Function","paper_id":"a6dedf7c-fb24-3828-b5e7-b1481e2d9b50","reference_id":"18593906","reference_type":"Pubmed","uniprot_id":"P11309"},{"evidence_key":12,"evidence_type":"Protein Function","paper_id":"a02c94aa-e8b4-3dd3-a66f-abbd40320c3f","reference_id":"16186805","reference_type":"Pubmed","uniprot_id":"P11309"},{"evidence_key":7,"evidence_type":"Protein Function","paper_id":"4f4676d3-0b14-3eed-9754-e0d72a14f863","reference_id":"15525646","reference_type":"Pubmed","uniprot_id":"P11309"},{"evidence_key":8,"evidence_type":"Protein Function","paper_id":"d8d6eb40-1135-3eb2-93b5-a458c299bf6a","reference_id":"15528381","reference_type":"Pubmed","uniprot_id":"P11309"},{"evidence_key":9,"evidence_type":"Protein Function","paper_id":"294121fb-ecca-30b9-a8fd-8fa693ff9875","reference_id":"15657054","reference_type":"Pubmed","uniprot_id":"P11309"},{"evidence_key":11,"evidence_type":"Protein Function","paper_id":"422ba984-c857-3275-9f82-c09414ab258d","reference_id":"15808862","reference_type":"Pubmed","uniprot_id":"P11309"},{"evidence_key":14,"evidence_type":"Protein Function","paper_id":"eba0a853-01a9-3dcf-92b0-2e92884aaca3","reference_id":"17344846","reference_type":"Pubmed","uniprot_id":"P11309"},{"evidence_key":16,"evidence_type":"Protein Function","paper_id":"5b415b4b-383c-3476-b9ab-167a4e61dcdf","reference_id":"1825810","reference_type":"Pubmed","uniprot_id":"P11309"},{"evidence_key":13,"evidence_type":"Protein Function","paper_id":"04feac00-f084-303f-aced-bf418324b665","reference_id":"16356754","reference_type":"Pubmed","uniprot_id":"P11309"},{"evidence_key":19,"evidence_type":"Protein Function","paper_id":"680214dd-0ac9-3ca0-b8fd-e0990217595f","reference_id":"25121590","reference_type":"Pubmed","uniprot_id":"P11309"},{"evidence_key":18,"evidence_type":"Protein Function","paper_id":"d823e9e8-5f82-309b-aa3f-0dba3c6b4253","reference_id":"19749799","reference_type":"Pubmed","uniprot_id":"P11309"},{"evidence_key":20,"evidence_type":"Protein Function","paper_id":"05752ed2-897f-3b82-9460-62bb2ccbd74a","reference_id":"31548394","reference_type":"Pubmed","uniprot_id":"P11309"},{"evidence_key":6,"evidence_type":"Protein Function","paper_id":"89f97125-8881-3752-82f6-25e7a0d98567","reference_id":"12473674","reference_type":"Pubmed","uniprot_id":"P11309"},{"evidence_key":15,"evidence_type":"Protein Function","paper_id":"dcfebde5-91bf-36b7-a5f2-8db9c44f0ecd","reference_id":"18056989","reference_type":"Pubmed","uniprot_id":"P11309"},{"evidence_key":21,"evidence_type":"Protein Function","paper_id":"29048cc7-c210-4bb9-8bde-13e2d0e98cd7","reference_id":"37797010","reference_type":"Pubmed","uniprot_id":"P11309"}],"sequence_info":[{"related_target_id":"02cc6decec0f4a8c8c6a5e1bea3b7c85","sequence_number":23758,"uniprot_id":"P11309"}],"is_leaf":1}
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Plays a major role in pre-mRNA alternative splicing regulation (PubMed:26990106, PubMed:29104163). Mediates preferentially muscle-specific exon inclusion in numerous mRNAs important for striated cardiac and skeletal muscle cell differentiation (PubMed:29104163). Binds to intronic splicing enhancer (ISE) composed of stretches of GU-rich motifs localized in flanking intron of exon that will be included by alternative splicing (By similarity). Involved in embryonic stem cell (ESC) transition to cardiac cell differentiation by promoting pre-mRNA alternative splicing events of several pluripotency and/or differentiation genes (PubMed:26990106). Plays a role in the regulation of mRNA stability (PubMed:20977548, PubMed:24356969, PubMed:24375645, PubMed:29104163). Binds to 3'-untranslated region (UTR) AU-rich elements in target transcripts, such as CDKN1A and MYOG, leading to maintain their stabilities (PubMed:20977548, PubMed:24356969). Involved in myogenic differentiation by regulating MYOG levels (PubMed:20977548). Binds to multiple regions in the mRNA 3'-UTR of TP63 isoform 2, hence inducing its destabilization (PubMed:24375645). Also promotes the destabilization of the CHRM2 mRNA via its binding to a region in the coding sequence (PubMed:29104163). Plays a role in the regulation of mRNA translation (PubMed:29358667). Mediates repression of p53/TP53 mRNA translation through its binding to U-rich element in the 3'-UTR, hence preventing EIF4E from binding to p53/TP53 mRNA and translation initiation (PubMed:29358667). Binds to a huge amount of mRNAs (PubMed:29104163). Required for embryonic heart development, sarcomer and M-band formation in striated muscles (By similarity). Together with RBM20, promotes the expression of short isoforms of PDLIM5/ENH in cardiomyocytes (By similarity).\n(Microbial infection) Promotes hepatitis C virus (HCV) replication over translation through the inhibition of viral protein expression. Decreases viral translation by linking viral 5'- and 3'-UTRs, blocking 80S ribosome assembly on the viral IRES and enhancing the interaction of the mature core protein and 5'-UTR.","display_priority":1,"if_manual":0,"lang":"EN","source_info":[{"code":"Q9BX46","normalized_source_id":"96adf8c891514225a46927b3b16bd02a","source":"UNIPROT"}],"status":"ACTIVE"}],"paper_reference":[{"evidence_key":9,"evidence_type":"Protein Function","paper_id":"3968e28c-6cde-314e-9ab0-7ff1d376999f","reference_id":"24375645","reference_type":"Pubmed","uniprot_id":"Q9BX46"},{"evidence_key":13,"evidence_type":"Protein Function","paper_id":"c135648b-6d3e-3ca8-9b40-e4fa6abfffa3","reference_id":"29358667","reference_type":"Pubmed","uniprot_id":"Q9BX46"},{"evidence_key":10,"evidence_type":"Protein Function","paper_id":"ca24f77e-3d2e-3ab5-af01-b9beaad22cfd","reference_id":"25313962","reference_type":"Pubmed","uniprot_id":"Q9BX46"},{"evidence_key":14,"evidence_type":"Protein Function","paper_id":"6cb43b14-8964-33be-89ca-62233349f024","reference_id":"29380205","reference_type":"Pubmed","uniprot_id":"Q9BX46"},{"evidence_key":8,"evidence_type":"Protein Function","paper_id":"5264394d-c8f9-341f-9c03-a6ac967ef11b","reference_id":"24356969","reference_type":"Pubmed","uniprot_id":"Q9BX46"},{"evidence_key":12,"evidence_type":"Protein Function","paper_id":"9305a809-916d-39b8-b876-9b5f327b5cbf","reference_id":"29104163","reference_type":"Pubmed","uniprot_id":"Q9BX46"},{"evidence_key":6,"evidence_type":"Protein Function","paper_id":"66bf9659-ba38-3f14-b52c-2dd9d65fec18","reference_id":"20977548","reference_type":"Pubmed","uniprot_id":"Q9BX46"},{"evidence_key":5,"evidence_type":"Protein Function","paper_id":"5e699a4d-5433-4026-9082-b8d8d5bcd81e","reference_id":"19658189","reference_type":"Pubmed","uniprot_id":"Q9BX46"},{"evidence_key":11,"evidence_type":"Protein Function","paper_id":"c7d4991f-47c3-3392-b9f1-49122d57783a","reference_id":"26990106","reference_type":"Pubmed","uniprot_id":"Q9BX46"},{"evidence_key":7,"evidence_type":"Protein Function","paper_id":"2afc912a-1ace-3be6-810c-d829fc6e4893","reference_id":"22345307","reference_type":"Pubmed","uniprot_id":"Q9BX46"}],"sequence_info":[{"related_target_id":"02e3dc9b16274affba795c2278d148e8","sequence_number":9423115,"uniprot_id":"Q9BX46"}],"is_leaf":1}
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Contributes to the renal and hepatic elimination of endogenous organic compounds from the systemic circulation into the urine and bile, respectively (PubMed:11327718, PubMed:25904762). Capable of transporting a wide range of purine and pyrimidine nucleobases, nucleosides and nucleotides, with cGMP, 2'deoxyguanosine and GMP being the preferred substrates (PubMed:11327718, PubMed:18216183, PubMed:26377792, PubMed:28945155). Functions as a pH- and chloride-independent cGMP bidirectional facilitative transporter that can regulate both intracellular and extracellular levels of cGMP and may be involved in cGMP signaling pathways (PubMed:18216183, PubMed:26377792). Mediates orotate/glutamate bidirectional exchange and most likely display a physiological role in hepatic release of glutamate into the blood (PubMed:21446918). Involved in renal secretion and possible reabsorption of creatinine (PubMed:25904762, PubMed:28945155). Able to uptake prostaglandin E2 (PGE2) and may contribute to PGE2 renal excretion (Probable). Also transports alpha-ketoglutarate and urate (PubMed:11327718, PubMed:26377792). 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Binds to the trophoblast-specific element 2 (TSE2) of the aromatase gene enhancer (PubMed:10542267). Binds to the SYDE1 promoter (PubMed:27917469). 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involved in peripheral immune surveillance in liver. May mediate the endocytosis of pathogens which are subsequently degraded in lysosomal compartments. Is a receptor for ICAM3, probably by binding to mannose-like carbohydrates.\n(Microbial infection) Acts as an attachment receptor for Ebolavirus.\n(Microbial infection) Acts as an attachment receptor for Human cytomegalovirus/HHV-5.\n(Microbial infection) Acts as an attachment receptor for HIV-1.\n(Microbial infection) Acts as an attachment receptor for Hepatitis C virus.\n(Microbial infection) Acts as an attachment receptor for SARS-CoV.\n(Microbial infection) Acts as an attachment receptor for West-nile virus.\n(Microbial infection) Acts as an attachment receptor for Marburg virus glycoprotein.\n(Microbial infection) Acts as an attachment receptor for Human coronavirus 229E.\n(Microbial infection) Acts as an attachment receptor for Influenzavirus.\n(Microbial infection) Recognition of M.bovis by dendritic cells may occur partially via this molecule.\n(Microbial infection) Acts as an attachment receptor for Japanese encephalitis virus.","display_priority":1,"if_manual":0,"lang":"EN","source_info":[{"code":"Q9H2X3","normalized_source_id":"96adf8c891514225a46927b3b16bd02a","source":"UNIPROT"}],"status":"ACTIVE"}],"paper_reference":[{"evidence_key":14,"evidence_type":"Protein Function","paper_id":"9db71d77-6370-33ba-9072-07de385afead","reference_id":"15496474","reference_type":"Pubmed","uniprot_id":"Q9H2X3"},{"evidence_key":9,"evidence_type":"Protein Function","paper_id":"a1640f8e-c7b5-3a0a-bc28-da9e14ea4532","reference_id":"12050398","reference_type":"Pubmed","uniprot_id":"Q9H2X3"},{"evidence_key":12,"evidence_type":"Protein Function","paper_id":"8c091f31-3e23-3c9b-9ad8-dffce0617cb6","reference_id":"15371595","reference_type":"Pubmed","uniprot_id":"Q9H2X3"},{"evidence_key":16,"evidence_type":"Protein Function","paper_id":"475a16cd-d65e-36d2-a008-223345f708cb","reference_id":"16816373","reference_type":"Pubmed","uniprot_id":"Q9H2X3"},{"evidence_key":5,"evidence_type":"Protein Function","paper_id":"d8fdfd89-4e21-388d-a5d3-a6edc4e1599b","reference_id":"11257134","reference_type":"Pubmed","uniprot_id":"Q9H2X3"},{"evidence_key":10,"evidence_type":"Protein Function","paper_id":"cac30d58-ca06-3aad-a955-4d147f977564","reference_id":"12433371","reference_type":"Pubmed","uniprot_id":"Q9H2X3"},{"evidence_key":21,"evidence_type":"Protein Function","paper_id":"505c680d-ee71-3d05-b206-e412aca874d9","reference_id":"24623090","reference_type":"Pubmed","uniprot_id":"Q9H2X3"},{"evidence_key":8,"evidence_type":"Protein Function","paper_id":"b6ee163d-ef50-333e-8a9f-403aedb78fac","reference_id":"11739956","reference_type":"Pubmed","uniprot_id":"Q9H2X3"},{"evidence_key":20,"evidence_type":"Protein Function","paper_id":"7b4e88ff-0776-3053-9be6-61de41774b1c","reference_id":"21277928","reference_type":"Pubmed","uniprot_id":"Q9H2X3"},{"evidence_key":4,"evidence_type":"Protein Function","paper_id":"eb7a1292-5264-3fb0-b9b9-abcc4f75c80b","reference_id":"11226297","reference_type":"Pubmed","uniprot_id":"Q9H2X3"},{"evidence_key":7,"evidence_type":"Protein Function","paper_id":"15bebc67-d596-395a-a78d-f0bee1e19f89","reference_id":"11384997","reference_type":"Pubmed","uniprot_id":"Q9H2X3"},{"evidence_key":17,"evidence_type":"Protein Function","paper_id":"a04ece9b-ffbe-375c-90a5-b62d93ea575a","reference_id":"17037540","reference_type":"Pubmed","uniprot_id":"Q9H2X3"},{"evidence_key":6,"evidence_type":"Protein Function","paper_id":"a127fdbe-8c6e-3371-80fb-8da8a79bd55a","reference_id":"11337487","reference_type":"Pubmed","uniprot_id":"Q9H2X3"},{"evidence_key":13,"evidence_type":"Protein Function","paper_id":"86c54d35-1044-3b05-b2b1-ee85c1d1dcd7","reference_id":"15479853","reference_type":"Pubmed","uniprot_id":"Q9H2X3"},{"evidence_key":18,"evidence_type":"Protein Function","paper_id":"e85234cf-0bf7-3f32-853d-fa62147762a9","reference_id":"21191006","reference_type":"Pubmed","uniprot_id":"Q9H2X3"},{"evidence_key":11,"evidence_type":"Protein Function","paper_id":"0dc77bf9-db6f-3695-b54f-d788cf7fffd2","reference_id":"12502850","reference_type":"Pubmed","uniprot_id":"Q9H2X3"},{"evidence_key":15,"evidence_type":"Protein Function","paper_id":"5a1456d7-a67d-3719-9383-4ce2c7b8d89c","reference_id":"16415006","reference_type":"Pubmed","uniprot_id":"Q9H2X3"},{"evidence_key":19,"evidence_type":"Protein Function","paper_id":"7bd0f597-0740-36e8-b308-03a18f533c57","reference_id":"21203928","reference_type":"Pubmed","uniprot_id":"Q9H2X3"}],"sequence_info":[{"related_target_id":"033f19e8cd8a483f91b47d6067064017","sequence_number":932541,"uniprot_id":"Q9H2X3"}],"is_leaf":1}
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In addition to its telomeric DNA-binding role, required to recruit a number of factors and enzymes required for telomere protection, including the shelterin complex, TERF2IP/RAP1 and DCLRE1B/Apollo (PubMed:16166375, PubMed:20655466). Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection (PubMed:16166375). Shelterin associates with arrays of double-stranded 5'-TTAGGG-3' repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways (PubMed:16166375). Together with DCLRE1B/Apollo, plays a key role in telomeric loop (T loop) formation by generating 3' single-stranded overhang at the leading end telomeres: T loops have been proposed to protect chromosome ends from degradation and repair (PubMed:20655466). Required both to recruit DCLRE1B/Apollo to telomeres and activate the exonuclease activity of DCLRE1B/Apollo (PubMed:20655466, PubMed:28216226). Preferentially binds to positive supercoiled DNA (PubMed:15608617, PubMed:20655466). Together with DCLRE1B/Apollo, required to control the amount of DNA topoisomerase (TOP1, TOP2A and TOP2B) needed for telomere replication during fork passage and prevent aberrant telomere topology (PubMed:20655466). 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Acts as a regulator of NaCl reabsorption in the distal nephron by mediating phosphorylation and activation of the thiazide-sensitive Na-Cl cotransporter SLC12A3/NCC in distal convoluted tubule cells of kidney downstream of WNK4 (PubMed:18270262). Also acts as a regulator of angiogenesis in endothelial cells downstream of WNK1 (PubMed:23386621, PubMed:25362046). Acts as an activator of inward rectifier potassium channels KCNJ2/Kir2.1 and KCNJ4/Kir2.3 downstream of WNK1: recognizes and binds the RXFXV/I variant motif on KCNJ2/Kir2.1 and KCNJ4/Kir2.3 and regulates their localization to the cell membrane without mediating their phosphorylation (PubMed:29581290). Phosphorylates RELL1, RELL2 and RELT (PubMed:16389068, PubMed:28688764). Phosphorylates PAK1 (PubMed:14707132). Phosphorylates PLSCR1 in the presence of RELT (PubMed:22052202).","display_priority":1,"if_manual":0,"lang":"EN","source_info":[{"code":"O95747","normalized_source_id":"96adf8c891514225a46927b3b16bd02a","source":"UNIPROT"}],"status":"ACTIVE"}],"paper_reference":[{"evidence_key":9,"evidence_type":"Protein Function","paper_id":"f196bb06-dcbc-3293-952f-efa9e529c8c4","reference_id":"17190791","reference_type":"Pubmed","uniprot_id":"O95747"},{"evidence_key":19,"evidence_type":"Protein Function","paper_id":"b107d90a-b612-3f07-84fb-c65a274f74f8","reference_id":"25362046","reference_type":"Pubmed","uniprot_id":"O95747"},{"evidence_key":6,"evidence_type":"Protein Function","paper_id":"6d6163c1-b852-3222-9773-cc2808d5d29a","reference_id":"16389068","reference_type":"Pubmed","uniprot_id":"O95747"},{"evidence_key":11,"evidence_type":"Protein Function","paper_id":"9a6aed7b-192e-37ac-b33d-c5017b582f15","reference_id":"17721439","reference_type":"Pubmed","uniprot_id":"O95747"},{"evidence_key":8,"evidence_type":"Protein Function","paper_id":"4a74ab5a-2cbd-3c78-96da-fb5373230b90","reference_id":"16832045","reference_type":"Pubmed","uniprot_id":"O95747"},{"evidence_key":5,"evidence_type":"Protein Function","paper_id":"aa197bfb-906e-3859-a961-82dbdc5001da","reference_id":"14707132","reference_type":"Pubmed","uniprot_id":"O95747"},{"evidence_key":17,"evidence_type":"Protein Function","paper_id":"5ce951f3-b184-3ce5-89ae-7ffa88a30969","reference_id":"22989884","reference_type":"Pubmed","uniprot_id":"O95747"},{"evidence_key":12,"evidence_type":"Protein Function","paper_id":"75e21dfe-6537-332d-8336-a20a50758f43","reference_id":"18270262","reference_type":"Pubmed","uniprot_id":"O95747"},{"evidence_key":18,"evidence_type":"Protein Function","paper_id":"5b776143-6afd-3e3a-a74a-17bab8597a35","reference_id":"23386621","reference_type":"Pubmed","uniprot_id":"O95747"},{"evidence_key":10,"evidence_type":"Protein Function","paper_id":"eba0a853-01a9-3dcf-92b0-2e92884aaca3","reference_id":"17344846","reference_type":"Pubmed","uniprot_id":"O95747"},{"evidence_key":16,"evidence_type":"Protein Function","paper_id":"e1efc590-0d4c-3a23-beb1-b992d4a847f4","reference_id":"22361696","reference_type":"Pubmed","uniprot_id":"O95747"},{"evidence_key":20,"evidence_type":"Protein Function","paper_id":"aabbab43-5af5-32c9-b83f-9e2f40a071c1","reference_id":"28688764","reference_type":"Pubmed","uniprot_id":"O95747"},{"evidence_key":7,"evidence_type":"Protein Function","paper_id":"c55f76be-48ee-31df-8141-61e94c9a31c0","reference_id":"16669787","reference_type":"Pubmed","uniprot_id":"O95747"},{"evidence_key":21,"evidence_type":"Protein Function","paper_id":"a6767451-e2c9-3f47-8e93-31d0dfe561d7","reference_id":"29581290","reference_type":"Pubmed","uniprot_id":"O95747"},{"evidence_key":4,"evidence_type":"Protein Function","paper_id":"5f73a06a-0880-36d4-8c8c-9343dd44aef0","reference_id":"10083736","reference_type":"Pubmed","uniprot_id":"O95747"},{"evidence_key":15,"evidence_type":"Protein Function","paper_id":"cb9b8ed8-ff1f-37cc-95a8-3383f73094e3","reference_id":"22052202","reference_type":"Pubmed","uniprot_id":"O95747"},{"evidence_key":13,"evidence_type":"Protein Function","paper_id":"0de11f2a-2d57-39de-9857-efe08d028ea7","reference_id":"19665974","reference_type":"Pubmed","uniprot_id":"O95747"},{"evidence_key":14,"evidence_type":"Protein Function","paper_id":"1307ad90-c627-3714-be56-83952180f831","reference_id":"21321328","reference_type":"Pubmed","uniprot_id":"O95747"},{"evidence_key":22,"evidence_type":"Protein Function","paper_id":"6963c93b-eef4-3cf2-9d3a-8a22a31e9b4d","reference_id":"34289367","reference_type":"Pubmed","uniprot_id":"O95747"}],"sequence_info":[{"related_target_id":"03455059889a4491943d9329c412d2b5","sequence_number":1043172,"uniprot_id":"O95747"}],"is_leaf":1}
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Also functions as an acyl-CoA ligase catalyzing the ATP-dependent formation of fatty acyl-CoA using LCFA and very-long-chain fatty acids (VLCFA) as substrates, which prevents fatty acid efflux from cells and might drive more fatty acid uptake (PubMed:10198260, PubMed:10749848, PubMed:11980911, PubMed:20530735, PubMed:22022213, PubMed:24269233). Plays a pivotal role in regulating available LCFA substrates from exogenous sources in tissues undergoing high levels of beta-oxidation or triglyceride synthesis (PubMed:20530735). Can also activate branched-chain fatty acids such as phytanic acid and pristanic acid (PubMed:10198260). May contribute to the synthesis of sphingosine-1-phosphate (PubMed:24269233). Does not activate C24 bile acids, cholate and chenodeoxycholate (PubMed:11980911). In vitro, activates 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanate (THCA), the C27 precursor of cholic acid deriving from the de novo synthesis from cholesterol (PubMed:11980911). 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Following SBF2/MTMT13-mediated activation in response to starvation-induced autophagy, binds to and regulates SNARE protein VAMP8 endolysosomal transport required for SNARE-mediated autophagosome-lysosome fusion (PubMed:25648148). 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