VID28/YIL017C Protein Information Help

Standard Name Vid28p
Systematic Name Yil017cp
Alias Gid5p 1 , Yil017wp
ORF Classification Verified
Description GID Complex subunit, serves as adaptor for regulatory subunit Vid24p; protein involved in proteasome-dependent catabolite degradation of fructose-1,6-bisphosphatase (FBPase); localized to the nucleus and the cytoplasm (1, 2, 3, 4)
Name Description Vacuolar Import and Degradation
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 921
Molecular Weight (Da) 105,490
Isoelectric Point (pI) 5.76

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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 Vid28p (InterPro)
Physical Interactions There are 26 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI000013B37D | P40547
MIPS: YIL017C
NCBI: 398364481 | 599982 | 731784 | NP_012247.3
GenBank/EMBL/DDBJ: DAA08528.1 | Z46881
Amino Acid Sequence (or in FASTA format)
 
       1  MTVAYSLENL KKISNSLVGD QLAKVDYFLA PKCQIFQCLL SIEQSDGVEL
      51  KNAKLDLLYT LLHLEPQQRD IVGTYYFDIV SAIYKSMSLA SSFTKNNSST
     101  NYKYIKLLNL CAGVYPNCGF PDLQYLQNGF IQLVNHKFLR SKCKIDEVVT
     151  IIELLKLFLL VDEKNCSDFN KSKFMEEERE VTETSHYQDF KMAESLEHII
     201  VKISSKYLDQ ISLKYIVRLK VSRPASPSSV KNDPFDNKGV DCTRAIPKKI
     251  NISNMYDSSL LSLALLLYLR YHYMIPGDRK LRNDATFKMF VLGLLKSNDV
     301  NIRCVALKFL LQPYFTEDKK WEDTRTLEKI LPYLVKSFNY DPLPWWFDPF
     351  DMLDSLIVLY NEITPMNNPV LTTLAHTNVI FCILSRFAQC LSLPQHNEAT
     401  LKTTTKFIKI CASFAASDEK YRLLLLNDTL LLNHLEYGLE SHITLIQDFI
     451  SLKDEIKETT TESHSMCLPP IYDHDFVAAW LLLLKSFSRS VSALRTTLKR
     501  NKIAQLLLQI LSKTYTLTKE CYFAGQDFMK PEIMIMGITL GSICNFVVEF
     551  SNLQSFMLRN GIIDIIEKML TDPLFNSKKA WDDNEDERRI ALQGIPVHEV
     601  KANSLWVLRH LMYNCQNEEK FQLLAKIPMN LILDFINDPC WAVQAQCFQL
     651  LRNLTCNSRK IVNILLEKFK DVEYKIDPQT GNKISIGSTY LFEFLAKKMR
     701  LLNPLDTQQK KAMEGILYII VNLAAVNENK KQLVIEQDEI LNIMSEILVE
     751  TTTDSSSNGN DSNLKLACLW VLNNLLWNSS VSHYTQYAIE NGLEPGHSPS
     801  DSENPQSTVT IGYNESVAGG YSRGKYYDEP DGDDSSSNAN DDEDDDNDEG
     851  DDEGDEFVRT PAAKGSTSNV QVTRATVERC RKLVEVGLYD LVRKNITDES
     901  LSVREKARTL LYHMDLLLKV K*

external links for Vid28p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily YPL+
Ashbya (AGD) BOND GPMdb (Mass Spec.) YeastGFP
YGOB BioPIXIE MIPS YeastRC Public Image Repository
YOGY CYC2008 (complexes) Pfam domains

Complexome YeastRC Structure Prediction (Seattle)

DIP


GeneMANIA

References cited on this page View Complete Literature Guide for Vid28p
1) Regelmann J, et al.  (2003) Catabolite degradation of fructose-1,6-bisphosphatase in the yeast Saccharomyces cerevisiae: a genome-wide screen identifies eight novel GID genes and indicates the existence of two degradation pathways. Mol Biol Cell 14(4):1652-63
2) Huh WK, et al.  (2003) Global analysis of protein localization in budding yeast. Nature 425(6959):686-91
3) Hung GC, et al.  (2004) Degradation of the gluconeogenic enzymes fructose-1,6-bisphosphatase and malate dehydrogenase is mediated by distinct proteolytic pathways and signaling events. J Biol Chem 279(47):49138-50
4) Menssen R, et al.  (2012) Exploring the topology of the Gid complex, the E3 ubiquitin ligase involved in catabolite-induced degradation of gluconeogenic enzymes. J Biol Chem 287(30):25602-14