Detail Information for IndEnz0002010063
IED ID IndEnz0002010063
Enzyme Type ID protease010063
Protein Name 26S proteasome regulatory subunit RPN3
Gene Name RPN3 SUN2 YER021W
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Enzyme Sequence MASTAVMMDVDSSGVNDLHHSEKKYAEEDQVQELLKVLNEISKTTLTLDPRYIWRSLKDLSSLRNQELLNAETLCFTVNVLYPDSSSFKKNLLKFITSNHKSSVPGSAELRNSYPASFYSVNTEKKTIEVTAEINCFMHLLVQLFLWDSKELEQLVEFNRKVVIPNLLCYYNLRSLNLINAKLWFYIYLSHETLARSSEEINSDNQNIILRSTMMKFLKIASLKHDNETKAMLINLILRDFLNNGEVDSASDFISKLEYPHTDVSSSLEARYFFYLSKINAIQLDYSTANEYIIAAIRKAPHNSKSLGFLQQSNKLHCCIQLLMGDIPELSFFHQSNMQKSLLPYYHLTKAVKLGDLKKFTSTITKYKQLLLKDDTYQLCVRLRSNVIKTGIRIISLTYKKISLRDICLKLNLDSEQTVEYMVSRAIRDGVIEAKINHEDGFIETTELLNIYDSEDPQQVFDERIKFANQLHDEYLVSMRYPEDKKTQQNEKSENGENDDDTLDGDLMDDMSDISDLDDLGFL
Enzyme Length 523
Uniprot Accession Number P40016
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (5); Chain (1); Compositional bias (2); Domain (1); Helix (19); Initiator methionine (1); Modified residue (2); Region (1); Sequence conflict (2); Turn (2)
Keywords 3D-structure;Acetylation;Direct protein sequencing;Phosphoprotein;Proteasome;Reference proteome
Interact With Q12250; Q06103
Induction
Subcellular Location
Modified Residue MOD_RES 2; /note=N-acetylalanine; /evidence=ECO:0000269|PubMed:12504901; MOD_RES 454; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:18407956
Post Translational Modification PTM: N-acetylated by NAT1. {ECO:0000269|PubMed:12504901}.
Signal Peptide
Structure 3D Electron microscopy (25)
Cross Reference PDB 3J47; 3JCK; 3JCO; 3JCP; 4CR2; 4CR3; 4CR4; 5A5B; 5MPB; 5MPC; 5MPD; 5MPE; 5WVI; 5WVK; 6FVT; 6FVU; 6FVV; 6FVW; 6FVX; 6FVY; 6J2C; 6J2N; 6J2Q; 6J2X; 6J30;
Mapped Pubmed ID 10323869; 10490625; 10508607; 10664589; 10688190; 11283351; 11742986; 11805826; 11805837; 12827207; 12853471; 14687415; 14759368; 15571806; 15611133; 15905137; 16284124; 16429126; 16554755; 16869714; 16922378; 17499717; 18467557; 18719252; 19446322; 19446323; 19536198; 19683491; 20800707; 21139140; 21543789; 21619884; 21685082; 21966278; 22140548; 22195964; 22237024; 22350874; 22350895; 22956996; 23202731; 23545414; 23643786; 23672618; 23770819; 23911091; 23934994; 24040173; 24412063; 24598877; 24681338; 24706844; 25333764; 26130806; 26182356; 26262643; 26327695; 26365526; 26451487; 26642761; 26744777; 26929360; 27677933; 28106073; 28115689; 30067984; 30792173; 3141402; 8882582; 8982460; 9427841; 9584156; 9697412; 9741626;
Motif
Gene Encoded By
Mass 60,393
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda