{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q8CCJ3","secondaryAccessions":["A2RSP7","B1AXU5","B1AXU6","Q3V145","Q6ZQ50","Q8BT70","Q8C484","Q9D8I8"],"uniProtkbId":"UFL1_MOUSE","entryAudit":{"firstPublicDate":"2005-06-21","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2005-06-21","entryVersion":156,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Mus musculus","commonName":"Mouse","taxonId":10090,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"E3 UFM1-protein ligase 1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O94874"}],"value":"2.3.2.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"E3 UFM1-protein transferase 1"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"20531390"}],"value":"Multiple alpha-helix protein located at ER"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"25952549"}],"value":"Regulator of C53/LZAP and DDRGK1"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"25952549"},{"evidenceCode":"ECO:0000312","source":"MGI","id":"MGI:1914740"}],"value":"Ufl1"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"14621295"}],"value":"Kiaa0776"},{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"20531390"}],"value":"Maxer"},{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"25952549"}],"value":"Rcad"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O94874"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25952549"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28575669"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29461087"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30701081"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37795761"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38377992"}],"value":"E3 protein ligase that mediates ufmylation, the covalent attachment of the ubiquitin-like modifier UFM1 to lysine residues on target proteins, and which plays a key role in various processes, such as ribosome recycling, response to DNA damage, interferon response or reticulophagy (also called ER-phagy) (PubMed:28575669, PubMed:37795761, PubMed:38377992). Catalyzes ufmylation of many protein, such as CD274/PD-L1, CDK5RAP3, CYB5R3, DDRGK1, EIF6, histone H4, MRE11, P4HB, PDCD1/PD-1, TRIP4, RPN1, RPS20/uS10, RPL10/uL16, RPL26/uL24, SYVN1/HRD1 and TP53/p53 (PubMed:28575669, PubMed:37795761, PubMed:38377992). As part of the UREL complex, plays a key role in ribosome recycling by catalyzing mono-ufmylation of RPL26/uL24 subunit of the 60S ribosome (By similarity). Ufmylation of RPL26/uL24 occurs on free 60S ribosomes following ribosome dissociation: it weakens the junction between post-termination 60S subunits and SEC61 translocons, promoting release and recycling of the large ribosomal subunit from the endoplasmic reticulum membrane (By similarity). Ufmylation of RPL26/uL24 and subsequent 60S ribosome recycling either take place after normal termination of translation or after ribosome stalling during cotranslational translocation at the endoplasmic reticulum (By similarity). Involved in reticulophagy in response to endoplasmic reticulum stress by mediating ufmylation of proteins such as CYB5R3 and RPN1, thereby promoting lysosomal degradation of ufmylated proteins (By similarity). Ufmylation in response to endoplasmic reticulum stress is essential for processes such as hematopoiesis, blood vessel morphogenesis or inflammatory response (PubMed:25952549, PubMed:29461087, PubMed:30701081). Mediates ufmylation of DDRGK1 and CDK5RAP3; the role of these modifications is however unclear: as both DDRGK1 and CDK5RAP3 act as substrate adapters for ufmylation, it is uncertain whether ufmylation of these proteins is a collateral effect or is required for ufmylation (By similarity). Acts as a negative regulator of T-cell activation by mediating ufmylation and stabilization of PDCD1/PD-1 (PubMed:38377992). Also involved in the response to DNA damage: recruited to double-strand break sites following DNA damage and mediates monoufmylation of histone H4 and ufmylation of MRE11 (By similarity). Mediates ufmylation of TP53/p53, promoting its stability (By similarity). Catalyzes ufmylation of TRIP4, thereby playing a role in nuclear receptor-mediated transcription (By similarity). Required for hematopoietic stem cell function and hematopoiesis (PubMed:25952549)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O94874"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21494687"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30635284"}],"value":"Catalytic component of the UFM1 ribosome E3 ligase (UREL) complex, composed of UFL1, DDRGK1 and CDK5RAP3 (PubMed:21494687, PubMed:30635284). Interacts with E2-like enzyme UFC1 (By similarity). Interacts with RELA (By similarity). Interacts with NBN; promoting recruitment to double-strand breaks following DNA damage (By similarity). Interacts (when phosphorylated) with YWHAG/14-3-3-gamma; sequestering UFL1 and preventing its association with PDCD1/PD-1 substrate (By similarity)"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O94874"}],"value":"Recruited to double-strand breaks by the MRE11-RAD50-NBN (MRN) complex following DNA damage"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37795761"}],"value":"Endoplasmic reticulum membrane","id":"SL-0097"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O94874"}],"value":"Cytoplasm, cytosol","id":"SL-0091"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O94874"}],"value":"Nucleus","id":"SL-0191"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O94874"}],"value":"Chromosome","id":"SL-0468"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["Q8CCJ3-3"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"isoformIds":["Q8CCJ3-1"],"sequenceIds":["VSP_014250","VSP_014251"],"isoformSequenceStatus":"Described"},{"name":{"value":"3"},"isoformIds":["Q8CCJ3-2"],"sequenceIds":["VSP_014249"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20228063"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20531390"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21494687"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30354401"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30701081"}],"value":"Ubiquitously expressed with higher expression in pancreatic islets and other secretory tissues (PubMed:20228063, PubMed:21494687). In the embryonic brain at 17 dpc, detected in Sox2-positive neural stem cells and in Slc1a3/GLAST-positive radial glia (PubMed:20531390). In perinatal brain, highly expressed in Slc1a3-positive Bergmann glia of the cerebellum (PubMed:20531390). Continues to be expressed in Bergmann glia of adult brain at 16 weeks (PubMed:20531390). Expressed in adult heart (PubMed:30354401). Highly expressed in the intestinal exocrine cells (PubMed:30701081)"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30354401"}],"value":"Up-regulated in hypertrophic hearts (at protein level)"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O94874"}],"value":"Ubiquitinated, leading to its degradation by the proteasome. Interaction with CDK5RAP3 protects both proteins against ubiquitination and degradation via the proteasome"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O94874"}],"value":"Phosphorylated at Ser-462 by ATM, enhancing protein ligase activity and promoting ATM activation in a positive feedback loop (By similarity). Phosphorylation at Thr-535 by AMPK promotes its interaction with YWHAG/14-3-3-gamma, thereby preventing UFL1 association with PDCD1/PD-1 substrate (By similarity)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25952549"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30354401"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30701081"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38377992"}],"value":"Embryonic lethality caused by impaired erythroid development (PubMed:25952549). Conditional deletion in adult mice results in severe anemia and cytopenia (PubMed:25952549). Cells show elevated endoplasmic reticulum stress and unfolded protein response in bone marrow cells and impaired autophagic degradation (PubMed:25952549). Conditional knockout in cardiomyocytes causes age-dependent cardiomyopathy and heart failure, characterized by elevated cardiac fetal gene expression, increased fibrosis, and impaired cardiac contractility (PubMed:30354401). When challenged with pressure overload, cardiac-specific knockout mice display greater hypertrophy, exacerbated fibrosis, and worsened cardiac contractility compared to wild-type mice counterparts (PubMed:30354401). Conditional knockout in adults causes a significant loss of both Paneth and goblet cells in intestine, which in turn results in dysbiotic microbiota and increased susceptibility to experimentally induced colitis (PubMed:30701081). Mice with conditional deletion in T-cells show improved antitumor immunity due to enhanced CD8(+) T-cell activation (PubMed:38377992)"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the UFL1 family"}],"commentType":"SIMILARITY"},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Erroneous initiation","sequence":"BAC98021.1","note":"Extended N-terminus.","evidences":[{"evidenceCode":"ECO:0000305"}]}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O94874"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":793,"modifier":"EXACT"}},"description":"E3 UFM1-protein ligase 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