ID PTH_HUMAN Reviewed; 214 AA. AC Q86Y79; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 24-JAN-2024, entry version 149. DE RecName: Full=Peptidyl-tRNA hydrolase {ECO:0000305}; DE Short=PTH; DE EC=3.1.1.29 {ECO:0000269|PubMed:30244831}; GN Name=PTRH1 {ECO:0000303|PubMed:30244831, ECO:0000312|HGNC:HGNC:27039}; GN Synonyms=C9orf115 {ECO:0000312|HGNC:HGNC:27039}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF HIS-46 AND ASP-121. RX PubMed=30244831; DOI=10.1016/j.molcel.2018.08.022; RA Kuroha K., Zinoviev A., Hellen C.U.T., Pestova T.V.; RT "Release of ubiquitinated and non-ubiquitinated nascent chains from stalled RT mammalian ribosomal complexes by ANKZF1 and Ptrh1."; RL Mol. Cell 72:286-302(2018). CC -!- FUNCTION: Peptidyl-tRNA hydrolase that cleaves nascent chains-tRNAs CC that are not stably fixed in the P-site of 60S ribosome-nascent chain CC complexes (PubMed:30244831). Acts downstream of the ribosome-associated CC quality control (RQC) pathway to release non-ubiquitinated nascent CC chains from 60S and 80S ribosome-nascent chain complexes CC (PubMed:30244831). Does not act on ubiquitinated nascent chains, which CC are cleaved by ANKZF1 for degradation (PubMed:30244831). CC {ECO:0000269|PubMed:30244831}. CC -!- CATALYTIC ACTIVITY: CC Reaction=an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L- CC amino acid + H(+); Xref=Rhea:RHEA:54448, Rhea:RHEA-COMP:10123, CC Rhea:RHEA-COMP:13883, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:59874, ChEBI:CHEBI:78442, ChEBI:CHEBI:138191; CC EC=3.1.1.29; Evidence={ECO:0000269|PubMed:30244831}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54449; CC Evidence={ECO:0000269|PubMed:30244831}; CC -!- INTERACTION: CC Q86Y79; O15084: ANKRD28; NbExp=3; IntAct=EBI-2602515, EBI-359567; CC Q86Y79; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-2602515, EBI-10175124; CC Q86Y79; P80188: LCN2; NbExp=3; IntAct=EBI-2602515, EBI-11911016; CC Q86Y79; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-2602515, EBI-79165; CC -!- SIMILARITY: Belongs to the PTH family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC047012; AAH47012.1; -; mRNA. DR CCDS; CCDS35147.1; -. DR RefSeq; NP_001002913.1; NM_001002913.2. DR AlphaFoldDB; Q86Y79; -. DR SMR; Q86Y79; -. DR BioGRID; 126512; 28. DR IntAct; Q86Y79; 14. DR STRING; 9606.ENSP00000418661; -. DR iPTMnet; Q86Y79; -. DR PhosphoSitePlus; Q86Y79; -. DR BioMuta; PTRH1; -. DR DMDM; 74750555; -. DR EPD; Q86Y79; -. DR jPOST; Q86Y79; -. DR MassIVE; Q86Y79; -. DR MaxQB; Q86Y79; -. DR PaxDb; 9606-ENSP00000418661; -. DR PeptideAtlas; Q86Y79; -. DR ProteomicsDB; 70381; -. DR Pumba; Q86Y79; -. DR Antibodypedia; 17102; 125 antibodies from 17 providers. DR DNASU; 138428; -. DR Ensembl; ENST00000419060.5; ENSP00000418661.1; ENSG00000187024.15. DR Ensembl; ENST00000543175.5; ENSP00000439469.1; ENSG00000187024.15. DR GeneID; 138428; -. DR KEGG; hsa:138428; -. DR MANE-Select; ENST00000543175.5; ENSP00000439469.1; NM_001002913.3; NP_001002913.1. DR UCSC; uc004bro.4; human. DR AGR; HGNC:27039; -. DR CTD; 138428; -. DR DisGeNET; 138428; -. DR GeneCards; PTRH1; -. DR HGNC; HGNC:27039; PTRH1. DR HPA; ENSG00000187024; Low tissue specificity. DR neXtProt; NX_Q86Y79; -. DR OpenTargets; ENSG00000187024; -. DR PharmGKB; PA134917129; -. DR VEuPathDB; HostDB:ENSG00000187024; -. DR eggNOG; KOG2255; Eukaryota. DR GeneTree; ENSGT00390000004247; -. DR InParanoid; Q86Y79; -. DR OMA; HVLSKFH; -. DR OrthoDB; 66431at2759; -. DR PhylomeDB; Q86Y79; -. DR TreeFam; TF332601; -. DR PathwayCommons; Q86Y79; -. DR SignaLink; Q86Y79; -. DR BioGRID-ORCS; 138428; 27 hits in 1155 CRISPR screens. DR ChiTaRS; PTRH1; human. DR GenomeRNAi; 138428; -. DR Pharos; Q86Y79; Tbio. DR PRO; PR:Q86Y79; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q86Y79; Protein. DR Bgee; ENSG00000187024; Expressed in right adrenal gland and 129 other cell types or tissues. DR ExpressionAtlas; Q86Y79; baseline and differential. DR Genevisible; Q86Y79; HS. DR GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0072344; P:rescue of stalled ribosome; IDA:UniProtKB. DR CDD; cd00462; PTH; 1. DR Gene3D; 3.40.50.1470; Peptidyl-tRNA hydrolase; 1. DR InterPro; IPR001328; Pept_tRNA_hydro. DR InterPro; IPR018171; Pept_tRNA_hydro_CS. DR InterPro; IPR036416; Pept_tRNA_hydro_sf. DR NCBIfam; TIGR00447; pth; 1. DR PANTHER; PTHR17224; PEPTIDYL-TRNA HYDROLASE; 1. DR PANTHER; PTHR17224:SF1; PEPTIDYL-TRNA HYDROLASE-RELATED; 1. DR Pfam; PF01195; Pept_tRNA_hydro; 1. DR SUPFAM; SSF53178; Peptidyl-tRNA hydrolase-like; 1. DR PROSITE; PS01196; PEPT_TRNA_HYDROL_2; 1. PE 1: Evidence at protein level; KW Hydrolase; Reference proteome. FT CHAIN 1..214 FT /note="Peptidyl-tRNA hydrolase" FT /id="PRO_0000240441" FT MUTAGEN 46 FT /note="H->N: Abolished peptidyl-tRNA activity." FT /evidence="ECO:0000269|PubMed:30244831" FT MUTAGEN 121 FT /note="D->A: Abolished peptidyl-tRNA activity." FT /evidence="ECO:0000269|PubMed:30244831" SQ SEQUENCE 214 AA; 22937 MW; DBA3959411DA8248 CRC64; MRPGGFLGAG QRLSRAMSRC VLEPRPPGKR WMVAGLGNPG LPGTRHSVGM AVLGQLARRL GVAESWTRDR HCAADLALAP LGDAQLVLLR PRRLMNANGR SVARAAELFG LTAEEVYLVH DELDKPLGRL ALKLGGSARG HNGVRSCISC LNSNAMPRLR VGIGRPAHPE AVQAHVLGCF SPAEQELLPL LLDRATDLIL DHIRERSQGP SLGP //