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Overview

Uniprot IDO60524
Protein NameRibosome quality control complex subunit NEMF
Gene NameNEMF
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
1037 LNSFMHSKEATAREK
795 QPQRSIQKLASKEES
828 RREMKKKKLPSDSGD

Function

Key component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates the extraction of incompletely synthesized nascent chains from stalled ribosomes as well as their ubiquitin-mediated proteasomal degradation (PubMed:25578875, PubMed:32726578, PubMed:33406423, PubMed:33909987). Thereby, frees 60S subunit ribosomes from the stalled translation complex and prevents the accumulation of nascent polypeptide chains that are potentially toxic for the cell (PubMed:25578875, PubMed:33406423, PubMed:33909987). Within the RQC complex, NEMF specifically binds stalled 60S ribosomal subunits by recognizing an exposed, nascent chain-conjugated tRNA moiety and promotes the recruitment of LTN1 to stalled 60S subunits (PubMed:25578875). Following binding to stalled 60S ribosomal subunits, NEMF mediates CAT tailing by recruiting alanine-charged tRNA to the A-site and directing the elongation of stalled nascent chains independently of mRNA or 40S subunits, leading to non-templated C-terminal alanine extensions (CAT tails) (PubMed:33406423, PubMed:33909987). Mainly recruits alanine-charged tRNAs, but can also other amino acid-charged tRNAs (PubMed:33406423, PubMed:33909987). CAT tailing is required to promote ubiquitination of stalled nascent chains by different E3 ubiquitin-protein ligases (PubMed:33909987). In the canonical RQC pathway (RQC-L), CAT tailing facilitates LTN1-dependent ubiquitination by exposing lysine residues that would otherwise remain buried in the ribosomal exit tunnel (By similarity). In the alternative RQC pathway (RQC-C) CAT tailing creates an C-degron mainly composed of alanine that is recognized by the CRL2(KLHDC10) and RCHY1/PIRH2 E3 ligases, leading to ubiquitination and degradation of stalled nascent chains (PubMed:33909987). NEMF may also indirectly play a role in nuclear export (PubMed:16103875)

Protein Sequence

10 MKSRFSTIDL 20 RAVLAELNAS 30 LLGMRVNNVY 40 DVDNKTYLIR 50 LQKPDFKATL 60 LLESGIRIHT 70 TEFEWPKNMM 80 PSSFAMKCRK 90 HLKSRRLVSA 100 KQLGVDRIVD 110 FQFGSDEAAY 120 HLIIELYDRG 130 NIVLTDYEYV 140 ILNILRFRTD 150 EADDVKFAVR 160 ERYPLDHARA 170 AEPLLTLERL 180 TEIVASAPKG 190 ELLKRVLNPL 200 LPYGPALIEH 210 CLLENGFSGN 220 VKVDEKLETK 230 DIEKVLVSLQ 240 KAEDYMKTTS 250 NFSGKGYIIQ 260 KREIKPSLEA 270 DKPVEDILTY 280 EEFHPFLFSQ 290 HSQCPYIEFE 300 SFDKAVDEFY 310 SKIEGQKIDL 320 KALQQEKQAL 330 KKLDNVRKDH 340 ENRLEALQQA 350 QEIDKLKGEL 360 IEMNLQIVDR 370 AIQVVRSALA 380 NQIDWTEIGL 390 IVKEAQAQGD 400 PVASAIKELK 410 LQTNHVTMLL 420 RNPYLLSEEE 430 DDDVDGDVNV 440 EKNETEPPKG 450 KKKKQKNKQL 460 QKPQKNKPLL 470 VDVDLSLSAY 480 ANAKKYYDHK 490 RYAAKKTQKT 500 VEAAEKAFKS 510 AEKKTKQTLK 520 EVQTVTSIQK 530 ARKVYWFEKF 540 LWFISSENYL 550 IIGGRDQQQN 560 EIIVKRYLTP 570 GDIYVHADLH 580 GATSCVIKNP 590 TGEPIPPRTL 600 TEAGTMALCY 610 SAAWDARVIT 620 SAWWVYHHQV 630 SKTAPTGEYL 640 TTGSFMIRGK 650 KNFLPPSYLM 660 MGFSFLFKVD 670 ESCVWRHQGE 680 RKVRVQDEDM 690 ETLASCTSEL 700 ISEEMEQLDG 710 GDTSSDEDKE 720 EHETPVEVEL 730 MTQVDQEDIT 740 LQSGRDELNE 750 ELIQEESSED 760 EGEYEEVRKD 770 QDSVGEMKDE 780 GEETLNYPDT 790 TIDLSHLQPQ 800 RSIQKLASKE 810 ESSNSSDSKS 820 QSRRHLSAKE 830 RREMKKKKLP 840 SDSGDLEALE 850 GKDKEKESTV 860 HIETHQNTSK 870 NVAAVQPMKR 880 GQKSKMKKMK 890 EKYKDQDEED 900 RELIMKLLGS 910 AGSNKEEKGK 920 KGKKGKTKDE 930 PVKKQPQKPR 940 GGQRVSDNIK 950 KETPFLEVIT 960 HELQDFAVDD 970 PHDDKEEQDL 980 DQQGNEENLF 990 DSLTGQPHPE 1000 DVLLFAIPIC 1010 APYTTMTNYK 1020 YKVKLTPGVQ 1030 KKGKAAKTAL 1040 NSFMHSKEAT 1050 AREKDLFRSV 1060 KDTDLSRNIP 1070 GKVKVSAPNL LNVKRK

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005829 cytosol
Cellular Component GO:0022626 cytosolic ribosome
Cellular Component GO:0005634 nucleus
Cellular Component GO:1990112 RQC complex
Molecular Function GO:1904678 alpha-aminoacyl-tRNA binding
Molecular Function GO:0043023 ribosomal large subunit binding
Molecular Function GO:0000049 tRNA binding
Biological Process GO:0140708 CAT tailing
Biological Process GO:0051168 nuclear export
Biological Process GO:0065003 protein-containing complex assembly
Biological Process GO:0072344 rescue of stalled cytosolic ribosome
Biological Process GO:1990116 ribosome-associated ubiquitin-dependent protein catabolic process

Reference

[1] 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.