Search Results

Overview

Uniprot IDP61221
Protein NameATP-binding cassette sub-family E member 1
Gene NameABCE1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
181 DQIPKAAKGTVGSIL
27 KCRQECKKSCPVVRM
478 ALALCLGKPADVYLI
512 KRFILHAKKTAFVVE
513 RFILHAKKTAFVVEH

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)

Protein Sequence

10 MADKLTRIAI 20 VNHDKCKPKK 30 CRQECKKSCP 40 VVRMGKLCIE 50 VTPQSKIAWI 60 SETLCIGCGI 70 CIKKCPFGAL 80 SIVNLPSNLE 90 KETTHRYCAN 100 AFKLHRLPIP 110 RPGEVLGLVG 120 TNGIGKSTAL 130 KILAGKQKPN 140 LGKYDDPPDW 150 QEILTYFRGS 160 ELQNYFTKIL 170 EDDLKAIIKP 180 QYVDQIPKAA 190 KGTVGSILDR 200 KDETKTQAIV 210 CQQLDLTHLK 220 ERNVEDLSGG 230 ELQRFACAVV 240 CIQKADIFMF 250 DEPSSYLDVK 260 QRLKAAITIR 270 SLINPDRYII 280 VVEHDLSVLD 290 YLSDFICCLY 300 GVPSAYGVVT 310 MPFSVREGIN 320 IFLDGYVPTE 330 NLRFRDASLV 340 FKVAETANEE 350 EVKKMCMYKY 360 PGMKKKMGEF 370 ELAIVAGEFT 380 DSEIMVMLGE 390 NGTGKTTFIR 400 MLAGRLKPDE 410 GGEVPVLNVS 420 YKPQKISPKS 430 TGSVRQLLHE 440 KIRDAYTHPQ 450 FVTDVMKPLQ 460 IENIIDQEVQ 470 TLSGGELQRV 480 ALALCLGKPA 490 DVYLIDEPSA 500 YLDSEQRLMA 510 ARVVKRFILH 520 AKKTAFVVEH 530 DFIMATYLAD 540 RVIVFDGVPS 550 KNTVANSPQT 560 LLAGMNKFLS 570 QLEITFRRDP 580 NNYRPRINKL 590 NSIKDVEQKK SGNYFFLDD

Gene Ontology

Classification GO ID Description
Cellular Component GO:0016020 membrane
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0022626 cytosolic ribosome
Cellular Component GO:0005759 mitochondrial matrix
Cellular Component GO:0005739 mitochondrion
Molecular Function GO:0051539 4 iron, 4 sulfur cluster binding
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0016887 ATP hydrolysis activity
Molecular Function GO:0043273 CTPase activity
Molecular Function GO:0060698 endoribonuclease inhibitor activity
Molecular Function GO:0003924 GTPase activity
Molecular Function GO:0005506 iron ion binding
Molecular Function GO:0017111 ribonucleoside triphosphate phosphatase activity
Molecular Function GO:0043024 ribosomal small subunit binding
Biological Process GO:0060702 negative regulation of endoribonuclease activity
Biological Process GO:0006417 regulation of translation
Biological Process GO:0072344 rescue of stalled cytosolic ribosome
Biological Process GO:0032790 ribosome disassembly
Biological Process GO:0006413 translational initiation
Biological Process GO:0006415 translational termination

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[3] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[4] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[5] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.