{"metadata":{"accession":"PF23248","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR057043","hierarchy":null,"name":{"name":"PARP14, second type I KH domain","short":"KH_PARP14_2"},"description":[{"text":"<p>This domain is found in human Protein mono-ADP-ribosyltransferase PARP14 and related proteins. PARP14 is a large multidomain protein which in the N-terminal half contains a series of consecutive RRM and KH domains that are known to be nucleic acid-binding. PARP14 is involved in multiple signaling pathways linked to cancer, inflammation, and infection. PARP14 is an ADP-ribosyltransferase that mediates mono-ADP-ribosylation of glutamate residues on target proteins [[cite:PUB00083477],[cite:PUB00155694],[cite:PUB00146699]]. In contrast to PARP1 and PARP2, it is not able to mediate poly-ADP-ribosylation [[cite:PUB00146699]]. The domain represented by this entry is a KH domain found second in the human PARP14.</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00083477":{"PMID":16061477,"ISBN":null,"volume":"280","issue":"40","year":2005,"title":"B-aggressive lymphoma family proteins have unique domains that modulate transcription and exhibit poly(ADP-ribose) polymerase activity.","URL":null,"raw_pages":"33756-65","medline_journal":"J Biol Chem","ISO_journal":"J. Biol. Chem.","authors":["Aguiar RC","Takeyama K","He C","Kreinbrink K","Shipp MA."],"DOI_URL":"http://dx.doi.org/10.1074/jbc.M505408200"},"PUB00155694":{"PMID":18851833,"ISBN":null,"volume":"32","issue":"1","year":2008,"title":"Substrate-assisted catalysis by PARP10 limits its activity to mono-ADP-ribosylation.","URL":null,"raw_pages":"57-69","medline_journal":"Mol Cell","ISO_journal":"Mol Cell","authors":["Kleine H","Poreba E","Lesniewicz K","Hassa PO","Hottiger MO","Litchfield DW","Shilton BH","Luscher B."],"DOI_URL":"https://doi.org/10.1016/j.molcel.2008.08.009"},"PUB00146699":{"PMID":25043379,"ISBN":null,"volume":"5","issue":null,"year":2014,"title":"Family-wide analysis of poly(ADP-ribose) polymerase activity.","URL":null,"raw_pages":"4426","medline_journal":"Nat Commun","ISO_journal":"Nat Commun","authors":["Vyas S","Matic I","Uchima L","Rood J","Zaja R","Hay RT","Ahel I","Chang P."],"DOI_URL":null}},"set_info":{"accession":"CL0007","name":"KH"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":241,"interactions":0,"matches":1750,"pathways":0,"proteins":1712,"proteomes":650,"sets":1,"structural_models":{"alphafold":108,"bfvd":0},"structures":0,"taxa":2062},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":188,"alignment:full":1293},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}