ID ABCE1_HUMAN Reviewed; 599 AA. AC P61221; O88793; Q13181; Q13864; Q6NR76; Q96AL0; Q96B10; Q99K66; DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2004, sequence version 1. DT 27-MAR-2024, entry version 187. DE RecName: Full=ATP-binding cassette sub-family E member 1; DE EC=3.6.5.- {ECO:0000269|PubMed:20122402}; DE AltName: Full=2'-5'-oligoadenylate-binding protein; DE AltName: Full=HuHP68; DE AltName: Full=RNase L inhibitor; DE AltName: Full=Ribonuclease 4 inhibitor; DE Short=RNS4I; GN Name=ABCE1; Synonyms=RLI, RNASEL1, RNASELI, RNS4I; GN ORFNames=OK/SW-cl.40; 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 [MRNA], CHARACTERIZATION, AND INTERACTION WITH RNASEL. RX PubMed=7539425; DOI=10.1074/jbc.270.22.13308; RA Bisbal C., Martinand C., Silhol M., Lebleu B., Salehzada T.; RT "Cloning and characterization of a RNase L inhibitor. A new component of RT the interferon-regulated 2-5A pathway."; RL J. Biol. Chem. 270:13308-13317(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=8641422; DOI=10.1016/0014-5793(96)00099-3; RA Aubry F., Mattei M.-G., Barque J.-P., Galibert F.; RT "Chromosomal localization and expression pattern of the RNase L inhibitor RT gene."; RL FEBS Lett. 381:135-139(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Colon adenocarcinoma; RA Shichijo S., Itoh K.; RT "Identification of immuno-peptidmics that are recognized by tumor-reactive RT CTL generated from TIL of colon cancer patients."; RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG SeattleSNPs variation discovery resource; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Duodenum, and Uterus; 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 [7] RP FUNCTION, FUNCTION (MICROBIAL INFECTION), AND INDUCTION BY EMCV. RX PubMed=9660177; DOI=10.1046/j.1432-1327.1998.2540248.x; RA Martinand C., Salehzada T., Silhol M., Lebleu B., Bisbal C.; RT "RNase L inhibitor (RLI) antisense constructions block partially the down RT regulation of the 2-5A/RNase L pathway in encephalomyocarditis-virus- RT (EMCV)-infected cells."; RL Eur. J. Biochem. 254:248-255(1998). RN [8] RP FUNCTION, FUNCTION (MICROBIAL INFECTION), AND INDUCTION BY HIV-1. RX PubMed=9847332; DOI=10.1128/jvi.73.1.290-296.1999; RA Martinand C., Montavon C., Salehzada T., Silhol M., Lebleu B., Bisbal C.; RT "RNase L inhibitor is induced during human immunodeficiency virus type 1 RT infection and down regulates the 2-5A/RNase L pathway in human T cells."; RL J. Virol. 73:290-296(1999). RN [9] RP SUBCELLULAR LOCATION, AND FUNCTION. RX PubMed=11585831; DOI=10.1074/jbc.m107482200; RA Le Roy F., Bisbal C., Silhol M., Martinand C., Lebleu B., Salehzada T.; RT "The 2-5A/RNase L/RNase L inhibitor (RNI) pathway regulates mitochondrial RT mRNAs stability in interferon alpha-treated H9 cells."; RL J. Biol. Chem. 276:48473-48482(2001). RN [10] RP INTERACTION WITH HIV-1 VIF AND GAG PROTEINS (MICROBIAL INFECTION). RX PubMed=11780123; DOI=10.1038/415088a; RA Zimmerman C., Klein K.C., Kiser P.K., Singh A.R., Firestein B.L., RA Riba S.C., Lingappa J.R.; RT "Identification of a host protein essential for assembly of immature HIV-1 RT capsids."; RL Nature 415:88-92(2002). RN [11] RP INTERACTION WITH HIV-2 PROTEIN GAG (MICROBIAL INFECTION). RX PubMed=14747530; DOI=10.1128/jvi.78.4.1645-1656.2004; RA Dooher J.E., Lingappa J.R.; RT "Conservation of a stepwise, energy-sensitive pathway involving HP68 for RT assembly of primate lentivirus capsids in cells."; RL J. Virol. 78:1645-1656(2004). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [13] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=20122402; DOI=10.1016/j.molcel.2009.12.034; RA Pisarev A.V., Skabkin M.A., Pisareva V.P., Skabkina O.V., RA Rakotondrafara A.M., Hentze M.W., Hellen C.U., Pestova T.V.; RT "The role of ABCE1 in eukaryotic posttermination ribosomal recycling."; RL Mol. Cell 37:196-210(2010). RN [14] RP FUNCTION. RX PubMed=21448132; DOI=10.1038/emboj.2011.93; RA Pisareva V.P., Skabkin M.A., Hellen C.U., Pestova T.V., Pisarev A.V.; RT "Dissociation by Pelota, Hbs1 and ABCE1 of mammalian vacant 80S ribosomes RT and stalled elongation complexes."; RL EMBO J. 30:1804-1817(2011). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417 AND THR-550, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [17] RP FUNCTION, INTERACTION WITH PINK1; CNOT4 AND PELO, UBIQUITINATION AT LYS-20, RP AND MUTAGENESIS OF LYS-20. RX PubMed=29861391; DOI=10.1016/j.cmet.2018.05.007; RA Wu Z., Wang Y., Lim J., Liu B., Li Y., Vartak R., Stankiewicz T., RA Montgomery S., Lu B.; RT "Ubiquitination of ABCE1 by NOT4 in Response to Mitochondrial Damage Links RT Co-translational Quality Control to PINK1-Directed Mitophagy."; RL Cell Metab. 28:130-144.e7(2018). RN [18] RP VARIANT CYS-489, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=17488105; DOI=10.1021/pr0700908; RA Bunger M.K., Cargile B.J., Sevinsky J.R., Deyanova E., Yates N.A., RA Hendrickson R.C., Stephenson J.L. Jr.; RT "Detection and validation of non-synonymous coding SNPs from orthogonal RT analysis of shotgun proteomics data."; RL J. Proteome Res. 6:2331-2340(2007). CC -!- FUNCTION: Nucleoside-triphosphatase (NTPase) involved in ribosome CC recycling by mediating ribosome disassembly (PubMed:20122402, CC PubMed:21448132). Able to hydrolyze ATP, GTP, UTP and CTP CC (PubMed:20122402). Splits ribosomes into free 60S subunits and CC tRNA- and mRNA-bound 40S subunits (PubMed:20122402, PubMed:21448132). CC Acts either after canonical termination facilitated by release factors CC (ETF1/eRF1) or after recognition of stalled and vacant ribosomes by CC mRNA surveillance factors (PELO/Pelota) (PubMed:20122402, CC PubMed:21448132). Involved in the No-Go Decay (NGD) pathway: recruited CC to stalled ribosomes by the Pelota-HBS1L complex, and drives the CC disassembly of stalled ribosomes, followed by degradation of damaged CC mRNAs as part of the NGD pathway (PubMed:21448132). Also plays a role CC in quality control of translation of mitochondrial outer membrane- CC localized mRNA (PubMed:29861391). As part of the PINK1-regulated CC signaling, ubiquitinated by CNOT4 upon mitochondria damage; this CC modification generates polyubiquitin signals that recruit autophagy CC receptors to the mitochondrial outer membrane and initiate mitophagy CC (PubMed:29861391). RNASEL-specific protein inhibitor which antagonizes CC the binding of 2-5A (5'-phosphorylated 2',5'-linked oligoadenylates) to CC RNASEL (PubMed:9660177). Negative regulator of the anti-viral effect of CC the interferon-regulated 2-5A/RNASEL pathway (PubMed:9660177, CC PubMed:9847332, PubMed:11585831). {ECO:0000269|PubMed:11585831, CC ECO:0000269|PubMed:20122402, ECO:0000269|PubMed:21448132, CC ECO:0000269|PubMed:29861391, ECO:0000269|PubMed:9660177, CC ECO:0000269|PubMed:9847332}. CC -!- FUNCTION: (Microbial infection) May act as a chaperone for post- CC translational events during HIV-1 capsid assembly. CC {ECO:0000269|PubMed:9847332}. CC -!- FUNCTION: (Microbial infection) Plays a role in the down-regulation of CC the 2-5A/RNASEL pathway during encephalomyocarditis virus (EMCV) and CC HIV-1 infections. {ECO:0000269|PubMed:9660177}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; CC Evidence={ECO:0000269|PubMed:20122402}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; CC Evidence={ECO:0000269|PubMed:20122402}; CC -!- CATALYTIC ACTIVITY: CC Reaction=CTP + H2O = CDP + H(+) + phosphate; Xref=Rhea:RHEA:29387, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37563, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58069; CC Evidence={ECO:0000269|PubMed:20122402}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + UTP = H(+) + phosphate + UDP; Xref=Rhea:RHEA:64900, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:46398, ChEBI:CHEBI:58223; CC Evidence={ECO:0000269|PubMed:20122402}; CC -!- SUBUNIT: Interacts with PINK1 (PubMed:29861391). Interacts with CNOT4 CC (PubMed:29861391). Interacts with PELO (PubMed:29861391). Probably CC heterodimerizes with RNASEL; this interaction inhibits RNASEL CC (PubMed:9660177) (Probable). {ECO:0000269|PubMed:29861391, CC ECO:0000305|PubMed:9660177}. CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 proteins Vif and CC Gag. {ECO:0000269|PubMed:11780123}. CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-2 protein Gag. CC {ECO:0000269|PubMed:14747530}. CC -!- INTERACTION: CC P61221; O75822: EIF3J; NbExp=3; IntAct=EBI-2510446, EBI-366647; CC P61221; P03347-1: gag; Xeno; NbExp=3; IntAct=EBI-2510446, EBI-10687478; CC P61221; Q9WH76: M; Xeno; NbExp=3; IntAct=EBI-2510446, EBI-10823897; CC P61221; P69479: P; Xeno; NbExp=3; IntAct=EBI-2510446, EBI-25568013; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11585831}. CC Mitochondrion {ECO:0000269|PubMed:11585831}. CC -!- INDUCTION: Activated by encephalomyocarditis virus (EMCV) and HIV-1. CC {ECO:0000269|PubMed:9660177, ECO:0000269|PubMed:9847332}. CC -!- PTM: Ubiquitinated by CNOT4 (PubMed:29861391). Ubiquitination mediates CC the recruitment of autophagy receptors to the mitochondrial outer CC membrane and initiates mitophagy (PubMed:29861391). CC {ECO:0000269|PubMed:29861391}. CC -!- MISCELLANEOUS: The ABC transporter domains seem not to be functional. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCE family. CC {ECO:0000305}. CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/abce1/"; CC -!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC proteins; CC URL="http://abcm2.hegelab.org/search"; 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; X76388; CAA53972.1; -; mRNA. DR EMBL; X74987; CAA52920.1; -; mRNA. DR EMBL; AB062293; BAB93476.1; -; mRNA. DR EMBL; BT009779; AAP88781.1; -; mRNA. DR EMBL; DQ148409; AAZ38723.1; -; Genomic_DNA. DR EMBL; BC016283; AAH16283.1; -; mRNA. DR EMBL; BC016988; AAH16988.1; -; mRNA. DR CCDS; CCDS34071.1; -. DR PIR; A57017; A57017. DR PIR; S63672; S63672. DR RefSeq; NP_001035809.1; NM_001040876.1. DR RefSeq; NP_002931.2; NM_002940.2. DR PDB; 6ZME; EM; 3.00 A; CI=1-599. DR PDB; 6ZVJ; EM; 3.80 A; 1=4-598. DR PDB; 7A09; EM; 3.50 A; J=1-599. DR PDBsum; 6ZME; -. DR PDBsum; 6ZVJ; -. DR PDBsum; 7A09; -. DR AlphaFoldDB; P61221; -. DR EMDB; EMD-11289; -. DR EMDB; EMD-11458; -. DR EMDB; EMD-11602; -. DR EMDB; EMD-3038; -. DR EMDB; EMD-3039; -. DR EMDB; EMD-3040; -. DR SMR; P61221; -. DR BioGRID; 111986; 387. DR IntAct; P61221; 49. DR MINT; P61221; -. DR STRING; 9606.ENSP00000296577; -. DR TCDB; 3.A.1.31.4; the atp-binding cassette (abc) superfamily. DR CarbonylDB; P61221; -. DR GlyGen; P61221; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P61221; -. DR MetOSite; P61221; -. DR PhosphoSitePlus; P61221; -. DR SwissPalm; P61221; -. DR BioMuta; ABCE1; -. DR DMDM; 47117664; -. DR EPD; P61221; -. DR jPOST; P61221; -. DR MassIVE; P61221; -. DR MaxQB; P61221; -. DR PaxDb; 9606-ENSP00000296577; -. DR PeptideAtlas; P61221; -. DR ProteomicsDB; 57276; -. DR Pumba; P61221; -. DR Antibodypedia; 27438; 356 antibodies from 31 providers. DR DNASU; 6059; -. DR Ensembl; ENST00000296577.9; ENSP00000296577.4; ENSG00000164163.11. DR GeneID; 6059; -. DR KEGG; hsa:6059; -. DR MANE-Select; ENST00000296577.9; ENSP00000296577.4; NM_002940.3; NP_002931.2. DR UCSC; uc003ijy.4; human. DR AGR; HGNC:69; -. DR CTD; 6059; -. DR DisGeNET; 6059; -. DR GeneCards; ABCE1; -. DR HGNC; HGNC:69; ABCE1. DR HPA; ENSG00000164163; Low tissue specificity. DR MIM; 601213; gene. DR neXtProt; NX_P61221; -. DR OpenTargets; ENSG00000164163; -. DR PharmGKB; PA24404; -. DR VEuPathDB; HostDB:ENSG00000164163; -. DR eggNOG; KOG0063; Eukaryota. DR GeneTree; ENSGT00390000015089; -. DR HOGENOM; CLU_017344_4_1_1; -. DR InParanoid; P61221; -. DR OMA; MVCIQNG; -. DR OrthoDB; 1110105at2759; -. DR PhylomeDB; P61221; -. DR TreeFam; TF105206; -. DR PathwayCommons; P61221; -. DR Reactome; R-HSA-8983711; OAS antiviral response. DR Reactome; R-HSA-909733; Interferon alpha/beta signaling. DR SignaLink; P61221; -. DR SIGNOR; P61221; -. DR BioGRID-ORCS; 6059; 807 hits in 1138 CRISPR screens. DR ChiTaRS; ABCE1; human. DR GenomeRNAi; 6059; -. DR Pharos; P61221; Tbio. DR PRO; PR:P61221; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; P61221; Protein. DR Bgee; ENSG00000164163; Expressed in primordial germ cell in gonad and 200 other cell types or tissues. DR ExpressionAtlas; P61221; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0022626; C:cytosolic ribosome; IDA:UniProt. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IBA:GO_Central. DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB. DR GO; GO:0043273; F:CTPase activity; IDA:UniProtKB. DR GO; GO:0060698; F:endoribonuclease inhibitor activity; IDA:GO_Central. DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB. DR GO; GO:0005506; F:iron ion binding; IBA:GO_Central. DR GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IDA:UniProt. DR GO; GO:0043024; F:ribosomal small subunit binding; IBA:GO_Central. DR GO; GO:0060702; P:negative regulation of endoribonuclease activity; IDA:GO_Central. DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW. DR GO; GO:0072344; P:rescue of stalled ribosome; IDA:UniProtKB. DR GO; GO:0000054; P:ribosomal subunit export from nucleus; IBA:GO_Central. DR GO; GO:0032790; P:ribosome disassembly; IDA:UniProtKB. DR GO; GO:0006413; P:translational initiation; IBA:GO_Central. DR GO; GO:0006415; P:translational termination; IDA:UniProt. DR CDD; cd03236; ABC_RNaseL_inhibitor_domain1; 1. DR CDD; cd03237; ABC_RNaseL_inhibitor_domain2; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like_ATP-bd. DR InterPro; IPR017871; ABC_transporter-like_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR013283; RLI1. DR InterPro; IPR034348; RLI_dom_1. DR InterPro; IPR007209; RNaseL-inhib-like_metal-bd_dom. DR PANTHER; PTHR19248:SF16; ATP-BINDING CASSETTE SUB-FAMILY E MEMBER 1; 1. DR PANTHER; PTHR19248; ATP-BINDING TRANSPORT PROTEIN-RELATED; 1. DR Pfam; PF00005; ABC_tran; 2. DR Pfam; PF00037; Fer4; 1. DR Pfam; PF04068; RLI; 1. DR PRINTS; PR01868; ABCEFAMILY. DR SMART; SM00382; AAA; 2. DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 2. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2. DR Genevisible; P61221; HS. PE 1: Evidence at protein level; KW 3D-structure; 4Fe-4S; ATP-binding; Chaperone; Cytoplasm; KW Host-virus interaction; Hydrolase; Iron; Iron-sulfur; Isopeptide bond; KW Metal-binding; Mitochondrion; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Repeat; Translation regulation; Ubl conjugation. FT CHAIN 1..599 FT /note="ATP-binding cassette sub-family E member 1" FT /id="PRO_0000093316" FT DOMAIN 7..37 FT /note="4Fe-4S ferredoxin-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT DOMAIN 46..75 FT /note="4Fe-4S ferredoxin-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT DOMAIN 79..315 FT /note="ABC transporter 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT DOMAIN 342..562 FT /note="ABC transporter 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT BINDING 110..117 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT BINDING 379..386 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT MOD_RES 417 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 550 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 20 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000269|PubMed:29861391" FT VARIANT 489 FT /note="S -> C (confirmed at protein level; FT dbSNP:rs3816497)" FT /evidence="ECO:0000269|PubMed:17488105" FT /id="VAR_068914" FT MUTAGEN 20 FT /note="K->R: Abolishes ubiquitination by CNOT4 and FT diminished the ability to recruit autophagy receptors to FT damaged mitochondria and to nuclear encoded respiratory FT chain component mRNA-ribonucleoproteins complexes." FT /evidence="ECO:0000269|PubMed:29861391" FT CONFLICT 118 FT /note="T -> A (in Ref. 1; CAA53972)" FT /evidence="ECO:0000305" FT CONFLICT 174..179 FT /note="DQIPKA -> ARFLRL (in Ref. 1; CAA53972)" FT /evidence="ECO:0000305" FT CONFLICT 471..473 FT /note="ALA -> RLR (in Ref. 1; CAA53972/CAA52920)" FT /evidence="ECO:0000305" SQ SEQUENCE 599 AA; 67314 MW; 5D582B62E95BC7A6 CRC64; MADKLTRIAI VNHDKCKPKK CRQECKKSCP VVRMGKLCIE VTPQSKIAWI SETLCIGCGI CIKKCPFGAL SIVNLPSNLE KETTHRYCAN AFKLHRLPIP RPGEVLGLVG TNGIGKSTAL KILAGKQKPN LGKYDDPPDW QEILTYFRGS ELQNYFTKIL EDDLKAIIKP QYVDQIPKAA KGTVGSILDR KDETKTQAIV CQQLDLTHLK ERNVEDLSGG ELQRFACAVV CIQKADIFMF DEPSSYLDVK QRLKAAITIR SLINPDRYII VVEHDLSVLD YLSDFICCLY GVPSAYGVVT MPFSVREGIN IFLDGYVPTE NLRFRDASLV FKVAETANEE EVKKMCMYKY PGMKKKMGEF ELAIVAGEFT DSEIMVMLGE NGTGKTTFIR MLAGRLKPDE GGEVPVLNVS YKPQKISPKS TGSVRQLLHE KIRDAYTHPQ FVTDVMKPLQ IENIIDQEVQ TLSGGELQRV ALALCLGKPA DVYLIDEPSA YLDSEQRLMA ARVVKRFILH AKKTAFVVEH DFIMATYLAD RVIVFDGVPS KNTVANSPQT LLAGMNKFLS QLEITFRRDP NNYRPRINKL NSIKDVEQKK SGNYFFLDD //