UniProtKB - Q12532 (RQC2_YEAST)
Ribosome quality control complex subunit 2
RQC2
Functioni
As part of the ribosome quality control complex (RQC), a ribosome-associated complex, mediates the extraction of incompletely synthesized nascent chains from stalled ribosomes as well as their ubiquitin-mediated proteasomal degradation. Thereby, frees ribosomes from the stalled translation complex and prevents the accumulation of nascent polypeptide chains that are potentially toxic for the cell (PubMed:23178123).
RQC2 is responsible for selective recognition of stalled 60S subunits by recognizing an exposed, nascent chain-conjugated tRNA moiety (PubMed:25349383).
RQC2 is important for the stable association of the E3 ubiquitin-protein ligase RKR1/LTN1 to the complex (PubMed:23479637).
RQC2 is also able to recruit alanine- and threonine-charged tRNA to the A site and directs the elongation of stalled nascent chains independently of mRNA or 40S subunits, leading to non-templated C-terminal Ala and Thr extensions (CAT tails) (PubMed:25554787, PubMed:32934225).
CAT tails induce a HSF1-dependent heat shock response (PubMed:25554787).
CAT tails also promote the RKR1/LTN1-mediated ubiquitination of incompletely synthesized nascent polypeptides and their subsequent proteasomal degradation (PubMed:32934225).
6 PublicationsMiscellaneous
GO - Molecular functioni
- mRNA binding Source: SGD
- ribosomal large subunit binding Source: SGD
- tRNA binding Source: SGD
GO - Biological processi
- CAT tailing Source: UniProtKB
- peptide biosynthetic process Source: SGD
- rescue of stalled ribosome Source: SGD
- ribosome-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
Keywordsi
Biological process | Protein biosynthesis |
Names & Taxonomyi
Protein namesi | Recommended name: Ribosome quality control complex subunit 21 PublicationAlternative name(s): Translation-associated element 21 Publication |
Gene namesi | Ordered Locus Names:YPL009C ORF Names:YP8132.04C |
Organismi | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Taxonomic identifieri | 559292 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › |
Proteomesi |
|
Organism-specific databases
SGDi | S000005930, RQC2 |
VEuPathDBi | FungiDB:YPL009C |
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm 1 Publication
Other locations
- cytoplasm Source: SGD
- cytoplasmic stress granule Source: SGD
- RQC complex Source: UniProtKB
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 9 | D → A: Abolishes CAT tail synthesis and heat shock response, but still binds to 60S ribosomal subunits and supports LTN1-dependent ubiquitination of nascent chains; when associated with A-98 and A-99. 1 Publication | 1 | |
Mutagenesisi | 88 | R → S: No effect on protein abundance. Decreased CAT tail synthesis. No effect on ribosome-associated ubiquitin-dependent protein catabolic process. 1 Publication | 1 | |
Mutagenesisi | 98 | D → A: Abolishes CAT tail synthesis and heat shock response, but still binds to 60S ribosomal subunits and supports LTN1-dependent ubiquitination of nascent chains; when associated with A-9 and A-99. 1 Publication | 1 | |
Mutagenesisi | 98 | D → Y: No effect on protein abundance. Loss of CAT tail synthesis. Loss of ribosome-associated ubiquitin-dependent protein catabolic process. 1 Publication | 1 | |
Mutagenesisi | 99 | R → A: Abolishes CAT tail synthesis and heat shock response, but still binds to 60S ribosomal subunits and supports LTN1-dependent ubiquitination of nascent chains; when associated with A-9 and A-98. 1 Publication | 1 | |
Mutagenesisi | 534 | K → G: No effect on protein abundance. Decreased CAT tail synthesis. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000244627 | 1 – 1038 | Ribosome quality control complex subunit 2Add BLAST | 1038 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 797 | PhosphoserineCombined sources | 1 |
Keywords - PTMi
PhosphoproteinProteomic databases
MaxQBi | Q12532 |
PaxDbi | Q12532 |
PRIDEi | Q12532 |
PTM databases
iPTMneti | Q12532 |
Interactioni
Subunit structurei
Component of the ribosome quality control complex (RQC), composed of the E3 ubiquitin ligase RKR1/LTN1, RQC1 and RQC2, as well as CDC48 and its ubiquitin-binding cofactors associated with the 60S ribosomal subunit (PubMed:23178123, PubMed:23479637, PubMed:25349383). RQC2 binds to the 40S-binding surface of tRNAs (PubMed:25554787).
4 PublicationsProtein-protein interaction databases
BioGRIDi | 36168, 198 interactors |
ComplexPortali | CPX-3265, Ribosome quality control complex |
DIPi | DIP-6570N |
IntActi | Q12532, 21 interactors |
MINTi | Q12532 |
STRINGi | 4932.YPL009C |
Miscellaneous databases
RNActi | Q12532, protein |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 459 – 499 | DisorderedSequence analysisAdd BLAST | 41 | |
Regioni | 708 – 824 | DisorderedSequence analysisAdd BLAST | 117 | |
Regioni | 877 – 898 | DisorderedSequence analysisAdd BLAST | 22 |
Coiled coil
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Coiled coili | 350 – 383 | Sequence analysisAdd BLAST | 34 | |
Coiled coili | 713 – 768 | Sequence analysisAdd BLAST | 56 | |
Coiled coili | 830 – 912 | Sequence analysisAdd BLAST | 83 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 482 – 499 | Basic and acidic residuesSequence analysisAdd BLAST | 18 | |
Compositional biasi | 714 – 760 | Acidic residuesSequence analysisAdd BLAST | 47 | |
Compositional biasi | 777 – 798 | Basic and acidic residuesSequence analysisAdd BLAST | 22 | |
Compositional biasi | 799 – 821 | Polar residuesSequence analysisAdd BLAST | 23 |
Sequence similaritiesi
Keywords - Domaini
Coiled coilPhylogenomic databases
eggNOGi | KOG2030, Eukaryota |
GeneTreei | ENSGT00390000018516 |
HOGENOMi | CLU_003612_1_1_1 |
InParanoidi | Q12532 |
OMAi | WVNADQV |
Family and domain databases
InterProi | View protein in InterPro IPR021846, NFACT-C IPR008532, NFACT_RNA-bd |
Pfami | View protein in Pfam PF11923, NFACT-C, 1 hit PF05670, NFACT-R_1, 1 hit |
i Sequence
Sequence statusi: Complete.
10 20 30 40 50
MKQRISALDL LLLARELKQD LEGYRLSNIY NIADSSKQFL LKFNKPDSKL
60 70 80 90 100
NVVVDCGLRI YLTEFSRPIP PTPSGFVVKL RKHLKAKRLT ALKQVDQDRI
110 120 130 140 150
LVLQFADGHF YLVLEFFSAG NVILLDENRR IMALQRVVLE HENKVGQIYE
160 170 180 190 200
MFDESLFTTN NESADESIEK NRKAEYTSEL VNEWIKAVQA KYESDITVIK
210 220 230 240 250
QLNIQGKEGA KKKKVKVPSI HKLLLSKVPH LSSDLLSKNL KVFNIDPSES
260 270 280 290 300
CLNLLEETDS LAELLNSTQL EYNQLLTTTD RKGYILAKRN ENYISEKDTA
310 320 330 340 350
DLEFIYDTFH PFKPYINGGD TDSSCIIEVE GPYNRTLDKF FSTIESSKYA
360 370 380 390 400
LRIQNQESQA QKKIDDARAE NDRKIQALLD VQELNERKGH LIIENAPLIE
410 420 430 440 450
EVKLAVQGLI DQQMDWNTIE KLIKSEQKKG NRIAQLLNLP LNLKQNKISV
460 470 480 490 500
KLDLSSKELN TSSDEDNESE GNTTDSSSDS DSEDMESSKE RSTKSMKRKS
510 520 530 540 550
NEKINVTIDL GLSAYANATE YFNIKKTSAQ KQKKVEKNVG KAMKNIEVKI
560 570 580 590 600
DQQLKKKLKD SHSVLKKIRT PYFFEKYSWF ISSEGFLVMM GKSPAETDQI
610 620 630 640 650
YSKYIEDDDI YMSNSFNSHV WIKNPEKTEV PPNTLMQAGI LCMSSSEAWS
660 670 680 690 700
KKISSSPWWC FAKNVSKFDG SDNSILPEGA FRLKNENDQN HLPPAQLVMG
710 720 730 740 750
FGFLWKVKTS GNEDNGDDDE EEEEEEEEEE EEEEEEEEEE EEEKEEEEKE
760 770 780 790 800
EEQQQDEDDS NEVNGLEKGG DSNDSTKNNS FEHDNLEKDI EKHCTISSDT
810 820 830 840 850
DSDSGNAKAK NDNSSTQRIL DEPGVPISLI ENINSNVRGK RGKLKKIQKK
860 870 880 890 900
YADQDETERL LRLEALGTLK GIEKQQQRKK EEIMKREVRE DRKNKREKQR
910 920 930 940 950
RLQALKFTKK EKARVNYDKH KSELKPSLDK GDVVDDIIPV FAPWPALLKY
960 970 980 990 1000
KYKVKIQPGS AKKTKTLTEI LHYFKSRPLD GSSTDNEMDW PQEHEMIKGL
1010 1020 1030
KEQDLVLLLC VDKLKVTIAG QKSTKNGGNS SKKGKKKR
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U33335 Genomic DNA Translation: AAB68096.1 Z48483 Genomic DNA Translation: CAA88377.1 Z71255 Genomic DNA Translation: CAA95032.1 BK006949 Genomic DNA Translation: DAA11419.1 |
PIRi | S52522 |
RefSeqi | NP_015316.1, NM_001183823.1 |
Genome annotation databases
EnsemblFungii | YPL009C_mRNA; YPL009C; YPL009C |
GeneIDi | 856098 |
KEGGi | sce:YPL009C |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U33335 Genomic DNA Translation: AAB68096.1 Z48483 Genomic DNA Translation: CAA88377.1 Z71255 Genomic DNA Translation: CAA95032.1 BK006949 Genomic DNA Translation: DAA11419.1 |
PIRi | S52522 |
RefSeqi | NP_015316.1, NM_001183823.1 |
3D structure databases
SMRi | Q12532 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 36168, 198 interactors |
ComplexPortali | CPX-3265, Ribosome quality control complex |
DIPi | DIP-6570N |
IntActi | Q12532, 21 interactors |
MINTi | Q12532 |
STRINGi | 4932.YPL009C |
PTM databases
iPTMneti | Q12532 |
Proteomic databases
MaxQBi | Q12532 |
PaxDbi | Q12532 |
PRIDEi | Q12532 |
Genome annotation databases
EnsemblFungii | YPL009C_mRNA; YPL009C; YPL009C |
GeneIDi | 856098 |
KEGGi | sce:YPL009C |
Organism-specific databases
SGDi | S000005930, RQC2 |
VEuPathDBi | FungiDB:YPL009C |
Phylogenomic databases
eggNOGi | KOG2030, Eukaryota |
GeneTreei | ENSGT00390000018516 |
HOGENOMi | CLU_003612_1_1_1 |
InParanoidi | Q12532 |
OMAi | WVNADQV |
Miscellaneous databases
PROi | PR:Q12532 |
RNActi | Q12532, protein |
Family and domain databases
InterProi | View protein in InterPro IPR021846, NFACT-C IPR008532, NFACT_RNA-bd |
Pfami | View protein in Pfam PF11923, NFACT-C, 1 hit PF05670, NFACT-R_1, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | RQC2_YEAST | |
Accessioni | Q12532Primary (citable) accession number: Q12532 Secondary accession number(s): D6W403 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | June 27, 2006 |
Last sequence update: | November 1, 1996 | |
Last modified: | February 23, 2022 | |
This is version 154 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- Yeast
Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD - Yeast chromosome XVI
Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names - SIMILARITY comments
Index of protein domains and families