{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P91133","uniProtkbId":"UBR1_CAEEL","entryAudit":{"firstPublicDate":"2005-08-16","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2010-10-05","entryVersion":159,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Caenorhabditis elegans","taxonId":6239,"lineage":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"E3 ubiquitin-protein ligase ubr-1"},"ecNumbers":[{"value":"2.3.2.27"}]},"alternativeNames":[{"fullName":{"value":"N-recognin-1"}},{"fullName":{"value":"RING-type E3 ubiquitin transferase ubr-1"}},{"fullName":{"value":"Ubiquitin-protein ligase E3-alpha"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"WormBase","id":"C32E8.11"}],"value":"ubr-1"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000312","source":"WormBase","id":"C32E8.11"}],"value":"C32E8.11"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8IWV7"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28602583"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29649217"}],"value":"E3 ubiquitin-protein ligase which is a component of the N-end rule pathway (By similarity). Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation (By similarity). In complex with ced-3, required for the ced-3-mediated cleavage and subsequent degradation of the heterochronic protein lin-28 to regulate seam cell fate patterning during larval development (PubMed:28602583). Negatively regulates glutamate metabolism through the aspartate aminotransferase got-1.2 (PubMed:29649217). Modulation of glutamate levels most likely controls locomotory behavior, in particular backwards locomotion or 'reversals' (PubMed:29649217)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.","ecNumber":"2.3.2.27"}},{"texts":[{"value":"Protein modification; protein ubiquitination"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28602583"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"14732404"}],"value":"Interacts with ubc-1 (Probable). Component of a complex containing at least ced-3, ubr-1 and possibly ate-1 (PubMed:28602583). Within complex interacts with ced-3 (via the p17 subunit); this interaction is required for the ced-3-mediated cleavage and subsequent degradation of the heterochronic protein lin-28 (PubMed:28602583)"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Membrane","id":"SL-0162"},"topology":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Single-pass membrane protein","id":"SL-9904"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29649217"}],"value":"Expressed in pharyngeal muscles, body wall muscles and a subset of neurons throughout postembryonic development (PubMed:29649217). Prominently expressed in premotor interneurons, but not expressed in ventral cord motor neurons (PubMed:29649217). Weakly expressed in hypodermal seam cells (PubMed:29649217)"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"value":"The RING-H2 zinc finger is an atypical RING finger with a His ligand in place of the fourth Cys of the classical motif"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28602583"}],"value":"RNAi-mediated knockdown enhances the excessive seam cell proliferation phenotype of the ain-1 ku322 mutant"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the E3 ubiquitin-protein ligase UBR1-like family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":2058,"modifier":"EXACT"}},"description":"E3 ubiquitin-protein ligase ubr-1","featureId":"PRO_0000056138"},{"type":"Transmembrane","location":{"start":{"value":1695,"modifier":"EXACT"},"end":{"value":1715,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Zinc finger","location":{"start":{"value":93,"modifier":"EXACT"},"end":{"value":164,"modifier":"EXACT"}},"description":"UBR-type","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00508"}]},{"type":"Zinc finger","location":{"start":{"value":1217,"modifier":"EXACT"},"end":{"value":1335,"modifier":"EXACT"}},"description":"RING-type; atypical"},{"type":"Region","location":{"start":{"value":1107,"modifier":"EXACT"},"end":{"value":1175,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":1381,"modifier":"EXACT"},"end":{"value":1416,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":1475,"modifier":"EXACT"},"end":{"value":1499,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1108,"modifier":"EXACT"},"end":{"value":1119,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1123,"modifier":"EXACT"},"end":{"value":1138,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1153,"modifier":"EXACT"},"end":{"value":1175,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1388,"modifier":"EXACT"},"end":{"value":1397,"modifier":"EXACT"}},"description":"Basic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1398,"modifier":"EXACT"},"end":{"value":1413,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1486,"modifier":"EXACT"},"end":{"value":1495,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Mutagenesis","location":{"start":{"value":18,"modifier":"EXACT"},"end":{"value":25,"modifier":"EXACT"}},"description":"In hp820; animals are viable, but display defective locomotion that progressively develops from the late larval stage into adulthood. Animals are capable of backwards locomotion or 'reversals' movements, but exhibit limited body flexing, with decreased body curvature during reversals, increased duration of reversals and a reduced frequency of reversal initiation compared to wild-type. Reduced bending is due to a defective activation pattern of A class motor neurons, whereby the posterior clusters of A class motor neurons DA7, VA10 and VA11, that innervate body wall muscles to execute reversals, are activated at the same time, which is in contrast to wild-type. Animals also display morphological and synaptic activity defects in AVA and AVE interneurons. Increases glutamate levels which is likely through increased got-1.2 activity. Defective reversals movement phenotype and increased glutamate levels are rescued in the got-1.2 hp731 mutant.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29649217"}],"alternativeSequence":{}},{"type":"Mutagenesis","location":{"start":{"value":34,"modifier":"EXACT"},"end":{"value":2058,"modifier":"EXACT"}},"description":"In hp821; animals are viable, but display defective locomotion that progressively develops from the late larval stage into adulthood. Animals are capable of backwards locomotion or 'reversals' movements, but exhibit limited body flexing, with decreased body curvature during reversals, increased duration of reversals and a reduced frequency of reversal initiation compared to wild-type. Reduced bending is due to a defective activation pattern of A class motor neurons, whereby the posterior clusters of A class motor neurons DA7, VA10 and VA11, that innervate body wall muscles to execute reversals, are activated at the same time, which is in contrast to wild-type. Animals also display morphological and synaptic activity defects in AVA and AVE interneurons. Increases glutamate levels which is likely through increased got-1.2 activity. Defective reversals movement phenotype and increased glutamate levels are rescued in the got-1.2 hp731 mutant.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29649217"}],"alternativeSequence":{}},{"type":"Mutagenesis","location":{"start":{"value":136,"modifier":"EXACT"},"end":{"value":163,"modifier":"EXACT"}},"description":"In tm5996; increases lin-28 protein levels 30 hours post feeding. Enhances the excessive seam cell proliferation phenotype and enhances the delay in temporal cell fate patterning of seam cells during the progression of larval development of the ain-1 ku322 mutant.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28602583"}],"alternativeSequence":{}},{"type":"Mutagenesis","location":{"start":{"value":1864,"modifier":"EXACT"},"end":{"value":2058,"modifier":"EXACT"}},"description":"In hp684; animals are viable, but display defective locomotion that progressively develops from the late larval stage into adulthood. Animals are capable of backwards locomotion or 'reversals' movements, but exhibit limited body flexing, with decreased body curvature during reversals, increased duration of reversals and a reduced frequency of reversal initiation compared to wild-type. Reduced bending is due to a defective activation pattern of A class motor neurons, whereby the posterior clusters of A class motor neurons DA7, VA10 and VA11, that innervate body wall muscles to execute reversals, are activated at the same time, which is in contrast to wild-type. Animals also display morphological and synaptic activity defects in AVA and AVE interneurons. Increases glutamate levels which is likely through increased got-1.2 activity. Defective reversals movement phenotype and increased glutamate levels are rescued in the got-1.2 hp731 mutant.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29649217"}],"alternativeSequence":{}}],"keywords":[{"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"id":"KW-0833","category":"Biological process","name":"Ubl conjugation pathway"},{"id":"KW-0862","category":"Ligand","name":"Zinc"},{"id":"KW-0863","category":"Domain","name":"Zinc-finger"}],"references":[{"referenceNumber":1,"citation":{"id":"9851916","citationType":"journal article","authoringGroup":["The C. elegans sequencing consortium"],"citationCrossReferences":[{"database":"PubMed","id":"9851916"},{"database":"DOI","id":"10.1126/science.282.5396.2012"}],"title":"Genome sequence of the nematode C. elegans: a platform for investigating biology.","publicationDate":"1998","journal":"Science","firstPage":"2012","lastPage":"2018","volume":"282"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"Bristol N2","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"14732404","citationType":"journal article","authors":["Crowe E.","Candido E.P.M."],"citationCrossReferences":[{"database":"PubMed","id":"14732404"},{"database":"DOI","id":"10.1016/j.ydbio.2003.09.037"}],"title":"Characterization of C. elegans RING finger protein 1, a binding partner of ubiquitin-conjugating enzyme 1.","publicationDate":"2004","journal":"Dev. 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