{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Warmack RA"],"funding":["Division of Molecular and Cellular Biosciences","University of California, Los Angeles","National Institute of General Medical Sciences","NIGMS NIH HHS","Life Extension Foundation, Inc.","Division of Graduate Education"],"pagination":["879-894"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9875861"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["61(10)"],"pubmed_abstract":["The spontaneous l-isoaspartate protein modification has been observed to negatively affect protein function. However, this modification can be reversed in many proteins in reactions initiated by the protein-l-isoaspartyl (d-aspartyl) <i>O</i>-methyltransferase (PCMT1). It has been hypothesized that an additional mechanism exists in which l-isoaspartate-damaged proteins are recognized and proteolytically degraded. Herein, we describe the protein-l-isoaspartate <i>O</i>-methyltransferase domain-containing protein 1 (PCMTD1) as a putative E3 ubiquitin ligase substrate adaptor protein. The N-terminal domain of PCMTD1 contains l-isoaspartate and <i>S</i>-adenosylmethionine (AdoMet) binding motifs similar to those in PCMT1. This protein also has a C-terminal domain containing suppressor of cytok"],"journal":["Biochemistry"],"pubmed_title":["Human Protein-l-isoaspartate <i>O</i>-Methyltransferase Domain-Containing Protein 1 (PCMTD1) Associates with Cullin-RING Ligase Proteins."],"pmcid":["PMC9875861"],"funding_grant_id":["T32 GM136614","DGE-1650604","T32 GM007185","R35 GM139539","GM007185","R35GM139539","MCB-1714569"],"pubmed_authors":["Warmack RA","Lowenson JD","Peluso E","Ong JY","Pang EZ","Torres JZ","Clarke SG"],"additional_accession":[]},"is_claimable":false,"name":"Human Protein-l-isoaspartate <i>O</i>-Methyltransferase Domain-Containing Protein 1 (PCMTD1) Associates with Cullin-RING Ligase Proteins.","description":"The spontaneous l-isoaspartate protein modification has been observed to negatively affect protein function. However, this modification can be reversed in many proteins in reactions initiated by the protein-l-isoaspartyl (d-aspartyl) <i>O</i>-methyltransferase (PCMT1). It has been hypothesized that an additional mechanism exists in which l-isoaspartate-damaged proteins are recognized and proteolytically degraded. Herein, we describe the protein-l-isoaspartate <i>O</i>-methyltransferase domain-containing protein 1 (PCMTD1) as a putative E3 ubiquitin ligase substrate adaptor protein. The N-terminal domain of PCMTD1 contains l-isoaspartate and <i>S</i>-adenosylmethionine (AdoMet) binding motifs similar to those in PCMT1. This protein also has a C-terminal domain containing suppressor of cytok","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 May","modification":"2025-04-04T08:06:40.465Z","creation":"2025-04-04T08:06:40.465Z"},"accession":"S-EPMC9875861","cross_references":{"pubmed":["35486881"],"doi":["10.1021/acs.biochem.2c00130"]}}