UniProt:P61221 ABCE1

chain
  • chain:1-599
checksum 5D582B62E95BC7A6
comment
  • FUNCTION Nucleoside-triphosphatase (NTPase) involved in ribosome recycling by mediating ribosome disassembly (PubMed:20122402, PubMed:21448132). Able to hydrolyze ATP, GTP, UTP and CTP (PubMed:20122402). Splits ribosomes into free 60S subunits and tRNA- and mRNA-bound 40S subunits (PubMed:20122402, PubMed:21448132). Acts either after canonical termination facilitated by release factors (ETF1/eRF1) or after recognition of stalled and vacant ribosomes by mRNA surveillance factors (PELO/Pelota) (PubMed:20122402, PubMed:21448132). Involved in the No-Go Decay (NGD) pathway: recruited to stalled ribosomes by the Pelota-HBS1L complex, and drives the disassembly of stalled ribosomes, followed by degradation of damaged mRNAs as part of the NGD pathway (PubMed:21448132). Also plays a role in quality control of translation of mitochondrial outer membrane-localized mRNA (PubMed:29861391). As part of the PINK1-regulated signaling, ubiquitinated by CNOT4 upon mitochondria damage; this modification generates polyubiquitin signals that recruit autophagy receptors to the mitochondrial outer membrane and initiate mitophagy (PubMed:29861391). RNASEL-specific protein inhibitor which antagonizes the binding of 2-5A (5'-phosphorylated 2',5'-linked oligoadenylates) to RNASEL (PubMed:9660177). Negative regulator of the anti-viral effect of the interferon-regulated 2-5A/RNASEL pathway (PubMed:11585831, PubMed:9660177, PubMed:9847332).FUNCTION (Microbial infection) May act as a chaperone for post-translational events during HIV-1 capsid assembly.FUNCTION (Microbial infection) Plays a role in the down-regulation of the 2-5A/RNASEL pathway during encephalomyocarditis virus (EMCV) and HIV-1 infections.CATALYTIC ACTIVITY GTP + H2O = GDP + phosphate + H(+)CATALYTIC ACTIVITY ATP + H2O = ADP + phosphate + H(+)CATALYTIC ACTIVITY CTP + H2O = CDP + phosphate + H(+)CATALYTIC ACTIVITY UTP + H2O = UDP + phosphate + H(+)SUBUNIT (Microbial infection) Interacts with Chandipura virus matrix protein.SUBUNIT Interacts with PINK1 (PubMed:29861391). Interacts with CNOT4 (PubMed:29861391). Interacts with PELO (PubMed:29861391). Probably heterodimerizes with RNASEL; this interaction inhibits RNASEL (Probable) (PubMed:9660177).SUBUNIT (Microbial infection) Interacts with HIV-1 proteins Vif and Gag.SUBUNIT (Microbial infection) Interacts with HIV-2 protein Gag.INTERACTION Activated by encephalomyocarditis virus (EMCV) and HIV-1.PTM Ubiquitinated by CNOT4 (PubMed:29861391). Ubiquitination mediates the recruitment of autophagy receptors to the mitochondrial outer membrane and initiates mitophagy (PubMed:29861391).MISCELLANEOUS The ABC transporter domains seem not to be functional.SIMILARITY Belongs to the ABC transporter superfamily. ABCE family.ONLINE INFORMATION Database for mutations in ABC proteins
crossReference
databaseName UniProt
dbId 49436
description
  • recommendedName: ATP-binding cassette sub-family E member 1 ecNumber evidence="7"3.6.5.- alternativeName: 2'-5'-oligoadenylate-binding protein alternativeName: HuHP68 alternativeName: RNase L inhibitor alternativeName: Ribonuclease 4 inhibitor shortName: RNS4I
displayName UniProt:P61221 ABCE1
geneName
  • ABCE1
  • RLI
  • RNASEL1
  • RNASELI
  • RNS4I
  • OK/SW-cl.40
identifier P61221
isSequenceChanged false
keyword
  • 3D-structure
  • 4Fe-4S
  • ATP-binding
  • Chaperone
  • Cytoplasm
  • Host-virus interaction
  • Hydrolase
  • Iron
  • Iron-sulfur
  • Isopeptide bond
  • Metal-binding
  • Mitochondrion
  • Nucleotide-binding
  • Phosphoprotein
  • Proteomics identification
  • Reference proteome
  • Repeat
  • Translation regulation
  • Ubl conjugation
modified [InstanceEdit:9939033] Weiser, Joel, 2025-02-21
moleculeType Protein
name
  • ABCE1
otherIdentifier
  • 11743804_at
  • 11747858_a_at
  • 11747859_s_at
  • 11747860_x_at
  • 11752588_s_at
  • 16971139
  • 201872_PM_s_at
  • 201872_s_at
  • 201873_PM_s_at
  • 201873_s_at
  • 2448887
  • 2448888
  • 2448889
  • 2448890
  • 2448891
  • 2448892
  • 2448893
  • 2448894
  • 2746025
  • 2746026
  • 2746027
  • 2746028
  • 2746029
  • 2746030
  • 2746031
  • 2746033
  • 2746034
  • 2746036
  • 2746037
  • 2746038
  • 2746040
  • 2746041
  • 2746042
  • 2746043
  • 2746044
  • 2746046
  • 2746047
  • 2746048
  • 2746049
  • 2746050
  • 2746054
  • 2746055
  • 2746056
  • 2746057
  • 2746058
  • 2746059
  • 3041566
  • 3041568
  • 3041569
  • 39355_at
  • 6059
  • 8097647
  • A_23_P41380
  • GE60020
  • GO:0000166
  • GO:0003924
  • GO:0005506
  • GO:0005515
  • GO:0005524
  • GO:0005737
  • GO:0005739
  • GO:0005759
  • GO:0005829
  • GO:0005840
  • GO:0006412
  • GO:0006413
  • GO:0006415
  • GO:0006417
  • GO:0016020
  • GO:0016787
  • GO:0016887
  • GO:0017111
  • GO:0022626
  • GO:0030163
  • GO:0032790
  • GO:0043024
  • GO:0043273
  • GO:0046872
  • GO:0051536
  • GO:0051539
  • GO:0060255
  • GO:0060698
  • GO:0060702
  • GO:0071569
  • GO:0072344
  • GO:0098772
  • GO:0140708
  • GO:1990116
  • HMNXSV003036012
  • Hs.12013.0.A1_3p_a_at
  • ILMN_1676846
  • ILMN_2330267
  • PH_hs_0001128
  • TC04000709.hg
  • X74987_s_at
  • g4506558_3p_a_at
physicalEntity
referenceDatabase [ReferenceDatabase:2] UniProt
referenceGene
referenceTranscript
schemaClass ReferenceGeneProduct
secondaryIdentifier
  • ABCE1_HUMAN
  • O88793
  • Q13181
  • Q13864
  • Q6NR76
  • Q96AL0
  • Q96B10
  • Q99K66
sequenceLength 599
species [Species:48887] Homo sapiens
stId uniprot:P61221
url http://purl.uniprot.org/uniprot/P61221
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