| IED ID | IndEnz0002010716 |
| Enzyme Type ID | protease010716 |
| Protein Name |
Proteasome subunit beta type-5 EC 3.4.25.1 Macropain subunit PRE2 Multicatalytic endopeptidase complex subunit PRE2 Proteasome component PRE2 Proteinase YSCE subunit PRE2 |
| Gene Name | PRE2 DOA3 PRG1 YPR103W P8283.10 |
| 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 | MQAIADSFSVPNRLVKELQYDNEQNLESDFVTGASQFQRLAPSLTVPPIASPQQFLRAHTDDSRNPDCKIKIAHGTTTLAFRFQGGIIVAVDSRATAGNWVASQTVKKVIEINPFLLGTMAGGAADCQFWETWLGSQCRLHELREKERISVAAASKILSNLVYQYKGAGLSMGTMICGYTRKEGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDSNYKWDLSVEDALYLGKRSILAAAHRDAYSGGSVNLYHVTEDGWIYHGNHDVGELFWKVKEEEGSFNNVIG |
| Enzyme Length | 287 |
| Uniprot Accession Number | P30656 |
| Absorption | |
| Active Site | ACT_SITE 76; /note=Nucleophile; /evidence=ECO:0000269|PubMed:9087403 |
| Activity Regulation | |
| Binding Site | BINDING 124; /note=Bortezomib; via amide nitrogen |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cleavage of peptide bonds with very broad specificity.; EC=3.4.25.1; |
| DNA Binding | |
| EC Number | 3.4.25.1 |
| Enzyme Function | FUNCTION: The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity. This unit is responsible of the chymotrypsin-like activity of the proteasome and is one of the principal target of the proteasome inhibitor bortezomib.; FUNCTION: This subunit is necessary for chymotryptic activity and degradation of ubiquitinated proteins. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (14); Binding site (1); Chain (1); Erroneous initiation (1); Helix (5); Mutagenesis (1); Propeptide (1); Sequence conflict (1); Turn (3) |
| Keywords | 3D-structure;Cytoplasm;Direct protein sequencing;Hydrolase;Nucleus;Protease;Proteasome;Reference proteome;Threonine protease;Zymogen |
| Interact With | P43583; P22141; P21242; P30657; P40302; P40303; P23724; P23638; P21243 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. Nucleus. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | Electron microscopy (26); X-ray crystallography (285) |
| Cross Reference PDB | 1FNT; 1G0U; 1G65; 1JD2; 1RYP; 1Z7Q; 2F16; 2FAK; 2GPL; 2ZCY; 3BDM; 3D29; 3DY3; 3DY4; 3E47; 3GPJ; 3GPT; 3GPW; 3HYE; 3JCO; 3JCP; 3MG0; 3MG4; 3MG6; 3MG7; 3MG8; 3NZJ; 3NZW; 3NZX; 3OEU; 3OEV; 3OKJ; 3SDI; 3SDK; 3SHJ; 3TDD; 3UN4; 3UN8; 3WXR; 4CR2; 4CR3; 4CR4; 4EU2; 4FZC; 4FZG; 4G4S; 4GK7; 4HNP; 4HRC; 4HRD; 4INR; 4INT; 4INU; 4J70; 4JSQ; 4JSU; 4JT0; 4LQI; 4LTC; 4NNN; 4NNW; 4NO1; 4NO6; 4NO8; 4NO9; 4Q1S; 4QBY; 4QLQ; 4QLS; 4QLT; 4QLU; 4QLV; 4QUX; 4QUY; 4QV0; 4QV1; 4QV3; 4QV4; 4QV5; 4QV6; 4QV7; 4QV8; 4QV9; 4QVL; 4QVM; 4QVN; 4QVP; 4QVQ; 4QVV; 4QVW; 4QVY; 4QW0; 4QW1; 4QW3; 4QW4; 4QW5; 4QW6; 4QW7; 4QWF; 4QWG; 4QWI; 4QWJ; 4QWK; 4QWL; 4QWR; 4QWS; 4QWU; 4QWX; 4QXJ; 4QZ0; 4QZ1; 4QZ2; 4QZ3; 4QZ4; 4QZ5; 4QZ6; 4QZ7; 4QZW; 4QZX; 4QZZ; 4R00; 4R02; 4R17; 4R18; 4RUR; 4V7O; 4X6Z; 4Y69; 4Y6A; 4Y6V; 4Y6Z; 4Y70; 4Y74; 4Y75; 4Y77; 4Y78; 4Y7W; 4Y7X; 4Y7Y; 4Y80; 4Y81; 4Y82; 4Y84; 4Y8G; 4Y8H; 4Y8I; 4Y8J; 4Y8K; 4Y8L; 4Y8M; 4Y8N; 4Y8O; 4Y8P; 4Y8Q; 4Y8R; 4Y8S; 4Y8T; 4Y8U; 4Y9Y; 4Y9Z; 4YA0; 4YA1; 4YA2; 4YA3; 4YA4; 4YA5; 4YA7; 4YA9; 4Z1L; 5A5B; 5AHJ; 5BOU; 5BXL; 5BXN; 5CGF; 5CGG; 5CGH; 5CGI; 5CZ4; 5CZ5; 5CZ6; 5CZ7; 5CZ8; 5CZ9; 5CZA; 5D0S; 5D0T; 5D0V; 5D0W; 5D0X; 5D0Z; 5DKI; 5DKJ; 5FG7; 5FG9; 5FGA; 5FGD; 5FGE; 5FGF; 5FGG; 5FGH; 5FGI; 5FHS; 5JHR; 5JHS; 5L52; 5L54; 5L55; 5L5A; 5L5B; 5L5D; 5L5E; 5L5F; 5L5H; 5L5I; 5L5J; 5L5O; 5L5P; 5L5Q; 5L5R; 5L5S; 5L5T; 5L5U; 5L5V; 5L5W; 5L5X; 5L5Y; 5L5Z; 5L60; 5L61; 5L62; 5L63; 5L64; 5L65; 5L66; 5L67; 5L68; 5L69; 5L6A; 5L6B; 5L6C; 5LAI; 5LAJ; 5LTT; 5M2B; 5MP9; 5MPA; 5MPB; 5MPC; 5NIF; 5WVI; 5WVK; 6EF3; 6FVT; 6FVU; 6FVV; 6FVW; 6FVX; 6FVY; 6G7F; 6G8M; 6G8N; 6GOP; 6H39; 6HTB; 6HTC; 6HTD; 6HTP; 6HTR; 6HUB; 6HUC; 6HUQ; 6HUU; 6HUV; 6HV3; 6HV4; 6HV5; 6HV7; 6HVA; 6HVR; 6HVS; 6HVT; 6HVU; 6HVV; 6HVW; 6HVX; 6HVY; 6HW0; 6HW3; 6HW4; 6HW5; 6HW6; 6HW7; 6HW8; 6HW9; 6HWA; 6HWB; 6HWC; 6HWD; 6HWE; 6HWF; 6J2C; 6J2N; 6J2Q; 6J2X; 6J30; 6ZOU; 6ZP6; 6ZP8; 7LS5; 7LS6; |
| Mapped Pubmed ID | 10069815; 10393174; 10452902; 10500111; 10872471; 11283351; 11493007; 11545745; 11595789; 11805328; 11805826; 11805837; 12940990; 1321727; 14690591; 14759368; 15178333; 15375696; 15571806; 15905137; 15916965; 16284124; 16429126; 16507144; 16537370; 16554755; 16607018; 16713559; 16861887; 16922378; 17227853; 17911112; 18353967; 18401409; 18482702; 18927584; 18928262; 19029916; 19073890; 19162040; 19214209; 19359491; 19536198; 19641493; 19678642; 19679091; 20632995; 20715286; 20875739; 21139140; 21154547; 21211719; 21427232; 21543789; 21685082; 21878652; 21936842; 21946808; 21966278; 22105886; 22229461; 22311637; 22341445; 22350874; 22350895; 22822185; 22870914; 22930756; 23091006; 23105001; 23320547; 23508107; 23540790; 23545414; 23547757; 23593271; 23697803; 24285701; 24396728; 24403024; 24563465; 24586798; 24706844; 24930969; 24979800; 25006746; 25038530; 25072887; 25087721; 25143386; 25244435; 25311859; 25332237; 25333764; 25549323; 25581903; 25599643; 25609009; 25812915; 25973989; 26020686; 26050527; 26130806; 26242779; 26262643; 26365526; 26471124; 26491016; 26563572; 26627836; 26670610; 26929360; 26964885; 27438186; 27677933; 27709817; 27789522; 28098422; 28106073; 28115689; 28733623; 29654304; 30029468; 30067984; 30165344; 30309908; 30365892; 30657666; 30792173; 33452852; 33846632; 8050580; 8134345; 8808631; 8861011; 8943015; 9312134; 9748229; 9770515; |
| Motif | |
| Gene Encoded By | |
| Mass | 31,637 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |