RKR1/YMR247C Protein Information Help

Standard Name Rkr1p 1
Systematic Name Ymr247cp
Alias Ltn1p 2
ORF Classification Verified
Description RING domain E3 ubiquitin ligase; involved in ubiquitin-mediated degradation of non-stop proteins; component of ribosome-bound RQC (ribosome quality control) complex required for degradation of polypeptides arising from stalled translation; degrades products of mRNAs lacking a termination codon regardless of a poly(A) tail; functional connections to chromatin modification; homolog of mouse Listerin, mutations in which reported to cause neurodegeneration (1, 2, 3, 4, 5)
Name Description RING domain mutant Killed by rtf1 deletion 1
Experimental Data
Molecules/cell 222 6
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 1,562
Molecular Weight (Da) 180,184
Isoelectric Point (pI) 5.24

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Post-translational Modifications PhosphoGRID | PhosphoPep Database
Domains/motifs See the graphical view and list of proteins that share domains/motifs in common with Rkr1p (InterPro)
Physical Interactions There are 10 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI000013B92C | Q04781
MIPS: YMR247C
NCBI: 2497203 | 6323904 | 732925 | 736313 | NP_013975.1 | NM_001182755.1
GenBank/EMBL/DDBJ: CAA88574.1 | CAA88657.1 | DAA10148.1 | Z48639 | Z48756
External Classifications EC: 6.3.2.- [Acid-Amino-Acid Ligases (Peptide Synthases)]
Amino Acid Sequence (or in FASTA format)
       1  MSFGGINTFQ QYNTDLGLGH NGVRISLNYF DGLPDPSLLN SLYSNELKLI
      51  FKSLLKRDET TKEKALMDLS NLISDFNQNE YFFNDIFLLC WSQIYAKLII
     101  SDYKVIRLQS HQITIMLVKS LRKKISKFLK DFIPLILLGT CELDYSVSKP
     151  SLNELTECFN KDPAKINALW AVFQEQLLNL VKEIVVNENE DTISDERYSS
     201  KEESEFRYHR VIASAVLLLI KLFVHNKDVS ERNSSSLKVI LSDESIWKLL
     251  NLKNGQNTNA YETVLRLIDV LYTRGYMPSH KNIMKLAVKK LLKSLTHITS
     301  KNILKVCPVL PSILNLLATL DDYEDGTIWS YDKSSKEKVL KFLSVSRTSP
     351  SPGFFNAVFA LYSSTKRHSF LDYYLEWLPF WQKSVQRLNE KGFSARNSAE
     401  VLNEFWTNFL KFAEDSSEER VKKMVESEIF NSLSCGKSLS EYTKLNQTLS
     451  GVFPPDKWER EIEDYFTSDE DIRKIKVSFE KNLFALLVTS PNNESAISRL
     501  FDFFVQLIET DPSNVFNKYD GVYDALNYFL DSDMIFLNGK IGKFINEIPT
     551  LVQESTYQNF AGIMAQYSNS KFFKMNTDAI TSLEDFFIVA LSFNLPKTII
     601  LATMNELDND IYQQLMKSDS LELELYIEDF MKNYKFDDSG EIFKGNNKFL
     651  NQRTITTLYR SAVANGQVEQ FCAVLSKLDE TFFSTLLLNT DFLSCALYEV
     701  SEDTNEKLFK LSLQLAKGNS EIANKLAQVI LQHAQVYFSP GAKEKYVTHA
     751  VELINGCNDT SQIFFPANAI EVFARYMPAI DYRSSLVSSL STNTHLLLTD
     801  DKPINLKNMQ KLIRYALFLD ALLDALPERV NNHIVAFITV VSELVTDYNC
     851  LSEEPNDLYY DFGHTFFKHG KVNLNFSDIV GNVIQPANGG DAMLTFDIAE
     901  SNSVYFFYYS RVLYKVLLNS IDTVSSTTLN GLLASVESFV TKTVRDQKST
     951  DKDYLLCAIL LLMFNRSNSK DEITKLRTLL ASQLIGIREV ELVDQEFKSL
    1001  ALLNNLLDIP QADKQFVPIA PQRLNMIFRS ILKWLDSDLA YEPSFSTVRL
    1051  LLLDFFTKLM RFEGVRDMGI TAFELSERLL ADSLSMCQID DTLYLLELRS
    1101  SCLNLYETLS QGVSKNGEEI SEYGDEIQEN LIELMFLNFN QERNNQVSTL
    1151  FYQKLYKVIS SMELKKLESQ YKRIFEVVLN DKDIGSNINQ SRLLTTLLGS
    1201  LVVKTQQDII IEYELRIQKQ TGSDVDGSAS DNDVNSKFKL PQKLLQKVTD
    1251  EVPKEYLEYE NKNSFIKYLW YWHLILMYFK DTSYNMRQIF IEQLKEAGLI
    1301  NRMFDFITDQ IDLRDTEFWK QVDTKEISEY NIVGNNFSPY KEDIFEECKK
    1351  LLGHTLYQLF NNVGCLTSIW WLNIKDRTLQ NDIEKFVSEF ISPILIKNEF
    1401  DDINSKMDRL TSNDDALTIK LNNITNEVKA SYLIDDQKLE ISFKLPKNYP
    1451  LTNIQVNGVS RVGISEQKWK QWIMSTQHVI TGMNGSVLDS LELFTKNVHL
    1501  QFSGFEECAI CYSILHAVDR KLPSKTCPTC KNKFHGACLY KWFRSSGNNT
    1551  CPLCRSEIPF RR*                                        

external links for Rkr1p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily LoQate
Ashbya (AGD) BOND GPMdb (Mass Spec.) YPL+
Aspergillus (AspGD) CYC2008 (complexes) MIPS YeastGFP
Candida (CGD) Complexome Pfam domains
YGOB GeneMANIA YeastRC Structure Prediction (Seattle)
YOGY IMP

References cited on this page View Complete Literature Guide for Rkr1p
1) Braun MA, et al.  (2007) Identification of Rkr1, a nuclear RING domain protein with functional connections to chromatin modification in Saccharomyces cerevisiae. Mol Cell Biol 27(8):2800-11
2) Bengtson MH and Joazeiro CA  (2010) Role of a ribosome-associated E3 ubiquitin ligase in protein quality control. Nature 467(7314):470-3
3) Fleischer TC, et al.  (2006) Systematic identification and functional screens of uncharacterized proteins associated with eukaryotic ribosomal complexes. Genes Dev 20(10):1294-307
4) Brandman O, et al.  (2012) A ribosome-bound quality control complex triggers degradation of nascent peptides and signals translation stress. Cell 151(5):1042-54
5) Matsuda R, et al.  (2014) Protein quality control systems associated with no-go and nonstop mRNA surveillance in yeast. Genes Cells 19(1):1-12
6) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41