CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002256
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Eukaryotic peptide chain release factor GTP-binding subunit 
Protein Synonyms/Alias
 ERF-3; ERF3; ERF2; G1 to S phase transition protein 1; Omnipotent suppressor protein 2; PSI no more protein 2; Polypeptide release factor 3; Translation release factor 3 
Gene Name
 SUP35 
Gene Synonyms/Alias
 GST1; PNM2; SAL3; SUF12; SUP2; YDR172W; YD9395.05 
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
400AKTQGVNKMVVVVNKubiquitination[1]
417DPTVNWSKERYDQCVubiquitination[1]
679GTTIAIGKIVKIAE*acetylation[2]
679GTTIAIGKIVKIAE*ubiquitination[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]
 [2] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919
Functional Description
 Involved in translation termination. Stimulates the activity of ERF1. Binds guanine nucleotides. Recruited by polyadenylate-binding protein PAB1 to poly(A)-tails of mRNAs. Interaction with PAB1 is also required for regulation of normal mRNA decay through translation termination-coupled poly(A) shortening. 
Sequence Annotation
 NP_BIND 267 274 GTP (By similarity).
 NP_BIND 344 348 GTP (By similarity).
 NP_BIND 406 409 GTP (By similarity).
 REGION 1 239 Interaction with PAB1.
 REGION 5 135 Prion domain (PrD).
 REGION 139 249 Charged.
 MOD_RES 571 571 Phosphoserine.  
Keyword
 3D-structure; Amyloid; Complete proteome; Cytoplasm; GTP-binding; Nucleotide-binding; Phosphoprotein; Prion; Protein biosynthesis; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 685 AA 
Protein Sequence
MSDSNQGNNQ QNYQQYSQNG NQQQGNNRYQ GYQAYNAQAQ PAGGYYQNYQ GYSGYQQGGY 60
QQYNPDAGYQ QQYNPQGGYQ QYNPQGGYQQ QFNPQGGRGN YKNFNYNNNL QGYQAGFQPQ 120
SQGMSLNDFQ KQQKQAAPKP KKTLKLVSSS GIKLANATKK VGTKPAESDK KEEEKSAETK 180
EPTKEPTKVE EPVKKEEKPV QTEEKTEEKS ELPKVEDLKI SESTHNTNNA NVTSADALIK 240
EQEEEVDDEV VNDMFGGKDH VSLIFMGHVD AGKSTMGGNL LYLTGSVDKR TIEKYEREAK 300
DAGRQGWYLS WVMDTNKEER NDGKTIEVGK AYFETEKRRY TILDAPGHKM YVSEMIGGAS 360
QADVGVLVIS ARKGEYETGF ERGGQTREHA LLAKTQGVNK MVVVVNKMDD PTVNWSKERY 420
DQCVSNVSNF LRAIGYNIKT DVVFMPVSGY SGANLKDHVD PKECPWYTGP TLLEYLDTMN 480
HVDRHINAPF MLPIAAKMKD LGTIVEGKIE SGHIKKGQST LLMPNKTAVE IQNIYNETEN 540
EVDMAMCGEQ VKLRIKGVEE EDISPGFVLT SPKNPIKSVT KFVAQIAIVE LKSIIAAGFS 600
CVMHVHTAIE EVHIVKLLHK LEKGTNRKSK KPPAFAKKGM KVIAVLETEA PVCVETYQDY 660
PQLGRFTLRD QGTTIAIGKI VKIAE 685 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0018444; C:translation release factor complex; IDA:SGD.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; IEA:InterPro.
 GO:0003747; F:translation release factor activity; IDA:SGD.
 GO:0006184; P:GTP catabolic process; IEA:GOC.
 GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IPI:SGD. 
Interpro
 IPR000795; EF_GTP-bd_dom.
 IPR027417; P-loop_NTPase.
 IPR009001; Transl_elong_EF1A/Init_IF2_C.
 IPR004161; Transl_elong_EFTu/EF1A_2.
 IPR004160; Transl_elong_EFTu/EF1A_C.
 IPR009000; Transl_elong_init/rib_B-barrel.
 IPR003285; Yeast_ERF. 
Pfam
 PF00009; GTP_EFTU
 PF03144; GTP_EFTU_D2
 PF03143; GTP_EFTU_D3 
SMART
  
PROSITE
 PS00301; EFACTOR_GTP 
PRINTS
 PR00315; ELONGATNFCT.
 PR01343; YEASTERF.