SUP35/YDR172W Protein Information Help

Standard Name Sup35p
Systematic Name Ydr172wp
Alias Gst1p , Pnm2p 1 , Sal3p , Suf12p , Sup2p , Sup36p
ORF Classification Verified
Description Translation termination factor eRF3, has a role in mRNA deadenylation and decay; altered protein conformation creates the [PSI(+)] prion that alters translational fidelity and results in a nonsense suppressor phenotype (2, 3, 4, 5) Also known as: [PSI] , [PSI(+)]
Name Description SUPpressor
Gene Product eRF3
Experimental Data
Molecules/cell 78900 6
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 685
Molecular Weight (Da) 76,551
Isoelectric Point (pI) 7

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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 Sup35p (InterPro)
Physical Interactions There are 166 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI0000035CE3 | P05453
MIPS: YDR172W
NCBI: 135056 | 3712 | 398365953 | 71042047 | 71042048 | NP_010457.3
GenBank/EMBL/DDBJ: DAA12014.1 | M21129 | X07163 | Y00829 | Z46727
Amino Acid Sequence (or in FASTA format)
 
       1  MSDSNQGNNQ QNYQQYSQNG NQQQGNNRYQ GYQAYNAQAQ PAGGYYQNYQ
      51  GYSGYQQGGY QQYNPDAGYQ QQYNPQGGYQ QYNPQGGYQQ QFNPQGGRGN
     101  YKNFNYNNNL QGYQAGFQPQ SQGMSLNDFQ KQQKQAAPKP KKTLKLVSSS
     151  GIKLANATKK VGTKPAESDK KEEEKSAETK EPTKEPTKVE EPVKKEEKPV
     201  QTEEKTEEKS ELPKVEDLKI SESTHNTNNA NVTSADALIK EQEEEVDDEV
     251  VNDMFGGKDH VSLIFMGHVD AGKSTMGGNL LYLTGSVDKR TIEKYEREAK
     301  DAGRQGWYLS WVMDTNKEER NDGKTIEVGK AYFETEKRRY TILDAPGHKM
     351  YVSEMIGGAS QADVGVLVIS ARKGEYETGF ERGGQTREHA LLAKTQGVNK
     401  MVVVVNKMDD PTVNWSKERY DQCVSNVSNF LRAIGYNIKT DVVFMPVSGY
     451  SGANLKDHVD PKECPWYTGP TLLEYLDTMN HVDRHINAPF MLPIAAKMKD
     501  LGTIVEGKIE SGHIKKGQST LLMPNKTAVE IQNIYNETEN EVDMAMCGEQ
     551  VKLRIKGVEE EDISPGFVLT SPKNPIKSVT KFVAQIAIVE LKSIIAAGFS
     601  CVMHVHTAIE EVHIVKLLHK LEKGTNRKSK KPPAFAKKGM KVIAVLETEA
     651  PVCVETYQDY PQLGRFTLRD QGTTIAIGKI VKIAE*

external links for Sup35p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily YPL+
Ashbya (AGD) BOND GPMdb (Mass Spec.) YeastGFP
Candida (CGD) BioPIXIE MIPS YeastRC Public Image Repository
Candida (CandidaDB) CYC2008 (complexes) Pfam domains
YGOB Complexome YeastRC Structure Prediction (Seattle)
YOGY DIP


GeneMANIA

References cited on this page View Complete Literature Guide for Sup35p
1) Doel SM, et al.  (1994) The dominant PNM2- mutation which eliminates the psi factor of Saccharomyces cerevisiae is the result of a missense mutation in the SUP35 gene. Genetics 137(3):659-70
2) Lindquist S, et al.  (2001) Investigating protein conformation-based inheritance and disease in yeast. Philos Trans R Soc Lond B Biol Sci 356(1406):169-76
3) Derkatch IL, et al.  (2004) Effects of Q/N-rich, polyQ, and non-polyQ amyloids on the de novo formation of the [PSI+] prion in yeast and aggregation of Sup35 in vitro. Proc Natl Acad Sci U S A 101(35):12934-9
4) Salnikova AB, et al.  (2005) Nonsense suppression in yeast cells overproducing Sup35 (eRF3) is caused by its non-heritable amyloids. J Biol Chem 280(10):8808-12
5) Funakoshi Y, et al.  (2007) Mechanism of mRNA deadenylation: evidence for a molecular interplay between translation termination factor eRF3 and mRNA deadenylases. Genes Dev 21(23):3135-48
6) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41