Detail Information for IndEnz0002010765
IED ID IndEnz0002010765
Enzyme Type ID protease010765
Protein Name 26S proteasome regulatory subunit 6A
Tat-binding protein homolog 1
TBP-1
Gene Name RPT5 YTA1 YOR117W O3258 YOR3258W
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 MATLEELDAQTLPGDDELDQEILNLSTQELQTRAKLLDNEIRIFRSELQRLSHENNVMLEKIKDNKEKIKNNRQLPYLVANVVEVMDMNEIEDKENSESTTQGGNVNLDNTAVGKAAVVKTSSRQTVFLPMVGLVDPDKLKPNDLVGVNKDSYLILDTLPSEFDSRVKAMEVDEKPTETYSDVGGLDKQIEELVEAIVLPMKRADKFKDMGIRAPKGALMYGPPGTGKTLLARACAAQTNATFLKLAAPQLVQMYIGEGAKLVRDAFALAKEKAPTIIFIDELDAIGTKRFDSEKSGDREVQRTMLELLNQLDGFSSDDRVKVLAATNRVDVLDPALLRSGRLDRKIEFPLPSEDSRAQILQIHSRKMTTDDDINWQELARSTDEFNGAQLKAVTVEAGMIALRNGQSSVKHEDFVEGISEVQARKSKSVSFYA
Enzyme Length 434
Uniprot Accession Number P33297
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity). {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding NP_BIND 222..229; /note=ATP; /evidence=ECO:0000255
Features Beta strand (1); Chain (1); Helix (4); Initiator methionine (1); Modified residue (2); Nucleotide binding (1); Turn (1)
Keywords 3D-structure;ATP-binding;Acetylation;Cytoplasm;Direct protein sequencing;Nucleotide-binding;Nucleus;Phosphoprotein;Proteasome;Reference proteome
Interact With P38348; P40555; P38764; P38886; P53196; P33299; P33298; P53549
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
Modified Residue MOD_RES 2; /note="N-acetylalanine"; /evidence="ECO:0000269|PubMed:12504901, ECO:0007744|PubMed:22814378"; MOD_RES 180; /note="Phosphotyrosine"; /evidence="ECO:0007744|PubMed:19779198"
Post Translational Modification PTM: N-acetylated by NAT1. {ECO:0000269|PubMed:12504901}.
Signal Peptide
Structure 3D Electron microscopy (27); X-ray crystallography (2)
Cross Reference PDB 3JCO; 3JCP; 3WHK; 3WHL; 4CR2; 4CR3; 4CR4; 5A5B; 5MP9; 5MPA; 5MPB; 5MPC; 5WVI; 5WVK; 6EF0; 6EF1; 6EF2; 6EF3; 6FVT; 6FVU; 6FVV; 6FVW; 6FVX; 6FVY; 6J2C; 6J2N; 6J2Q; 6J2X; 6J30;
Mapped Pubmed ID 10363642; 10417703; 10503546; 10559920; 10664589; 10688190; 11283351; 11595789; 11742986; 11805826; 11805837; 11964484; 15135049; 15263065; 15571806; 15905137; 16284124; 16429126; 16554755; 16725216; 16922378; 17227853; 17499717; 17803938; 18467557; 18719252; 18757749; 19013276; 19198063; 19412160; 19446322; 19446323; 19516331; 19536198; 19843524; 20020052; 20074027; 20800707; 21139140; 21211719; 21389348; 21685082; 21734642; 21878651; 21931558; 22037170; 22086954; 22350874; 22350895; 22493437; 23202731; 23617410; 23644457; 23672618; 23770819; 23965995; 23995839; 24013205; 24598877; 24685148; 24706844; 25083872; 25333764; 26130806; 26182356; 26208326; 26262643; 26327695; 26365526; 26449534; 26929360; 27302526; 27677933; 28106073; 28115689; 30067984; 30309908; 30792173; 31289129; 9342402; 9584156; 9724628; 9741626; 9790993;
Motif
Gene Encoded By
Mass 48,256
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 5.6.1.5;