CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007310
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 ERAD-associated E3 ubiquitin-protein ligase DOA10 
Protein Synonyms/Alias
  
Gene Name
 SSM4 
Gene Synonyms/Alias
 DOA10; YIL030C; YI3299.01C; YI9905.18C 
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
83SKNIDISKPGADVKCubiquitination[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, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301
Functional Description
 E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC6 and UBC7 E2 ligases, and transfers it to substrates promoting their degradation. Mediates the degradation of a broad range of substrates, inluding endoplasmic reticulum membrane proteins (ERQC), soluble nuclear proteins and soluble cytoplasmic proteins (CytoQC). Component of the DOA10 ubiquitin ligase complex, which is part of the ERAD-C pathway responsible for the rapid degradation of membrane proteins with misfolded cytoplasmic domains. ERAD-C substrates are ubiquitinated through DOA10 in conjunction with the E2 ubiquitin-conjugating enzymes UBC6 and UBC7-CUE1. Ubiquitinated substrates are then removed to the cytosol via the action of the UFD1-NPL4-CDC48/p97 (UNC) AAA ATPase complex and targeted to the proteasome. Also recognizes the N- terminally acetylated residue of proteins as degradation signal (degron). N-terminally acetylated target proteins include MATALPHA2, TBF1, SLK19, YMR090W, HIS3, HSP104, UBP6 and ARO8. 
Sequence Annotation
 ZN_FING 31 100 RING-CH-type.  
Keyword
 Complete proteome; Endoplasmic reticulum; Ligase; Membrane; Metal-binding; Nucleus; Reference proteome; Transmembrane; Transmembrane helix; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1319 AA 
Protein Sequence
MDVDSDVNVS RLRDELHKVA NEETDTATFN DDAPSGATCR ICRGEATEDN PLFHPCKCRG 60
SIKYMHESCL LEWVASKNID ISKPGADVKC DICHYPIQFK TIYAENMPEK IPFSLLLSKS 120
ILTFFEKARL ALTIGLAAVL YIIGVPLVWN MFGKLYTMML DGSSPYPGDF LKSLIYGYDQ 180
SATPELTTRA IFYQLLQNHS FTSLQFIMIV ILHIALYFQY DMIVREDVFS KMVFHKIGPR 240
LSPKDLKSRL KERFPMMDDR MVEYLAREMR AHDENRQEQG HDRLNMPAAA ADNNNNVINP 300
RNDNVPPQDP NDHRNFENLR HVDELDHDEA TEEHENNDSD NSLPSGDDSS RILPGSSSDN 360
EEDEEAEGQQ QQQQPEEEAD YRDHIEPNPI DMWANRRAQN EFDDLIAAQQ NAINRPNAPV 420
FIPPPAQNRA GNVDQDEQDF GAAVGVPPAQ ANPDDQGQGP LVINLKLKLL NVIAYFIIAV 480
VFTAIYLAIS YLFPTFIGFG LLKIYFGIFK VILRGLCHLY YLSGAHIAYN GLTKLVPKVD 540
VAMSWISDHL IHDIIYLYNG YTENTMKHSI FIRALPALTT YLTSVSIVCA SSNLVSRGYG 600
RENGMSNPTR RLIFQILFAL KCTFKVFTLF FIELAGFPIL AGVMLDFSLF CPILASNSRM 660
LWVPSICAIW PPFSLFVYWT IGTLYMYWFA KYIGMIRKNI IRPGVLFFIR SPEDPNIKIL 720
HDSLIHPMSI QLSRLCLSMF IYAIFIVLGF GFHTRIFFPF MLKSNLLSVP EAYKPTSIIS 780
WKFNTILLTL YFTKRILESS SYVKPLLERY WKTIFKLCSR KLRLSSFILG KDTPTERGHI 840
VYRNLFYKYI AAKNAEWSNQ ELFTKPKTLE QAEELFGQVR DVHAYFVPDG VLMRVPSSDI 900
VSRNYVQTMF VPVTKDDKLL KPLDLERIKE RNKRAAGEFG YLDEQNTEYD QYYIVYVPPD 960
FRLRYMTLLG LVWLFASILM LGVTFISQAL INFVCSFGFL PVVKLLLGER NKVYVAWKEL 1020
SDISYSYLNI YYVCVGSVCL SKIAKDILHF TEGQNTLDEH AVDENEVEEV EHDIPERDIN 1080
NAPVNNINNV EEGQGIFMAI FNSIFDSMLV KYNLMVFIAI MIAVIRTMVS WVVLTDGILA 1140
CYNYLTIRVF GNSSYTIGNS KWFKYDESLL FVVWIISSMV NFGTGYKSLK LFFRNRNTSK 1200
LNFLKTMALE LFKQGFLHMV IYVLPIIILS LVFLRDVSTK QIIDISHGSR SFTLSLNESF 1260
PTWTRMQDIY FGLLIALESF TFFFQATVLF IQWFKSTVQN VKDEVYTKGR ALENLPDES 1319 
Gene Ontology
 GO:0000837; C:Doa10p ubiquitin ligase complex; IDA:SGD.
 GO:0030176; C:integral to endoplasmic reticulum membrane; IDA:SGD.
 GO:0005637; C:nuclear inner membrane; IDA:SGD.
 GO:0004842; F:ubiquitin-protein ligase activity; IDA:SGD.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0030433; P:ER-associated protein catabolic process; IMP:SGD. 
Interpro
 IPR011016; Znf_RING-CH.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF12906; RINGv 
SMART
 SM00744; RINGv 
PROSITE
 PS51292; ZF_RING_CH 
PRINTS