CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011242
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase listerin 
Protein Synonyms/Alias
 RING domain mutant killed by rtf1 deletion protein 1 
Gene Name
 RKR1 
Gene Synonyms/Alias
 LTN1; YMR247C; YM9408.09C; YM9920.01C 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
1219EYELRIQKQTGSDVDubiquitination[1]
Reference
 [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301] 
Functional Description
 E3 ubiquitin-protein ligase involved in protein quality control by mediating ubiquitination and subsequent degradation of proteins derived from mRNAs lacking stop codons (non-stop proteins). Associates with ribosomes and ubiquitinates nascent non-stop proteins to signal their proteasomal degradation. Ubiquitination of non-stop proteins may be triggered by their stalling in ribosomes on translation through the poly(A) tail. May indirectly play a role in chromatin and transcription. 
Sequence Annotation
 ZN_FING 1508 1555 RING-type.  
Keyword
 Complete proteome; Ligase; Metal-binding; Nucleus; Reference proteome; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1562 AA 
Protein Sequence
MSFGGINTFQ QYNTDLGLGH NGVRISLNYF DGLPDPSLLN SLYSNELKLI FKSLLKRDET 60
TKEKALMDLS NLISDFNQNE YFFNDIFLLC WSQIYAKLII SDYKVIRLQS HQITIMLVKS 120
LRKKISKFLK DFIPLILLGT CELDYSVSKP SLNELTECFN KDPAKINALW AVFQEQLLNL 180
VKEIVVNENE DTISDERYSS KEESEFRYHR VIASAVLLLI KLFVHNKDVS ERNSSSLKVI 240
LSDESIWKLL NLKNGQNTNA YETVLRLIDV LYTRGYMPSH KNIMKLAVKK LLKSLTHITS 300
KNILKVCPVL PSILNLLATL DDYEDGTIWS YDKSSKEKVL KFLSVSRTSP SPGFFNAVFA 360
LYSSTKRHSF LDYYLEWLPF WQKSVQRLNE KGFSARNSAE VLNEFWTNFL KFAEDSSEER 420
VKKMVESEIF NSLSCGKSLS EYTKLNQTLS GVFPPDKWER EIEDYFTSDE DIRKIKVSFE 480
KNLFALLVTS PNNESAISRL FDFFVQLIET DPSNVFNKYD GVYDALNYFL DSDMIFLNGK 540
IGKFINEIPT LVQESTYQNF AGIMAQYSNS KFFKMNTDAI TSLEDFFIVA LSFNLPKTII 600
LATMNELDND IYQQLMKSDS LELELYIEDF MKNYKFDDSG EIFKGNNKFL NQRTITTLYR 660
SAVANGQVEQ FCAVLSKLDE TFFSTLLLNT DFLSCALYEV SEDTNEKLFK LSLQLAKGNS 720
EIANKLAQVI LQHAQVYFSP GAKEKYVTHA VELINGCNDT SQIFFPANAI EVFARYMPAI 780
DYRSSLVSSL STNTHLLLTD DKPINLKNMQ KLIRYALFLD ALLDALPERV NNHIVAFITV 840
VSELVTDYNC LSEEPNDLYY DFGHTFFKHG KVNLNFSDIV GNVIQPANGG DAMLTFDIAE 900
SNSVYFFYYS RVLYKVLLNS IDTVSSTTLN GLLASVESFV TKTVRDQKST DKDYLLCAIL 960
LLMFNRSNSK DEITKLRTLL ASQLIGIREV ELVDQEFKSL ALLNNLLDIP QADKQFVPIA 1020
PQRLNMIFRS ILKWLDSDLA YEPSFSTVRL LLLDFFTKLM RFEGVRDMGI TAFELSERLL 1080
ADSLSMCQID DTLYLLELRS SCLNLYETLS QGVSKNGEEI SEYGDEIQEN LIELMFLNFN 1140
QERNNQVSTL FYQKLYKVIS SMELKKLESQ YKRIFEVVLN DKDIGSNINQ SRLLTTLLGS 1200
LVVKTQQDII IEYELRIQKQ TGSDVDGSAS DNDVNSKFKL PQKLLQKVTD EVPKEYLEYE 1260
NKNSFIKYLW YWHLILMYFK DTSYNMRQIF IEQLKEAGLI NRMFDFITDQ IDLRDTEFWK 1320
QVDTKEISEY NIVGNNFSPY KEDIFEECKK LLGHTLYQLF NNVGCLTSIW WLNIKDRTLQ 1380
NDIEKFVSEF ISPILIKNEF DDINSKMDRL TSNDDALTIK LNNITNEVKA SYLIDDQKLE 1440
ISFKLPKNYP LTNIQVNGVS RVGISEQKWK QWIMSTQHVI TGMNGSVLDS LELFTKNVHL 1500
QFSGFEECAI CYSILHAVDR KLPSKTCPTC KNKFHGACLY KWFRSSGNNT CPLCRSEIPF 1560
RR 1562 
Gene Ontology
 GO:0005634; C:nucleus; IDA:SGD.
 GO:0043022; F:ribosome binding; IDA:SGD.
 GO:0004842; F:ubiquitin-protein ligase activity; IDA:SGD.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0016568; P:chromatin modification; IGI:SGD.
 GO:0006348; P:chromatin silencing at telomere; IMP:SGD.
 GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:SGD. 
Interpro
 IPR016024; ARM-type_fold.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF13639; zf-RING_2 
SMART
 SM00184; RING 
PROSITE
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS