| IED ID | IndEnz0002008252 |
| Enzyme Type ID | protease008252 |
| Protein Name |
26S proteasome regulatory subunit 7 homolog Protein CIM5 Tat-binding homolog 3 |
| Gene Name | RPT1 CIM5 YTA3 YKL145W |
| 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 | MPPKEDWEKYKAPLEDDDKKPDDDKIVPLTEGDIQVLKSYGAAPYAAKLKQTENDLKDIEARIKEKAGVKESDTGLAPSHLWDIMGDRQRLGEEHPLQVARCTKIIKGNGESDETTTDNNNSGNSNSNSNQQSTDADEDDEDAKYVINLKQIAKFVVGLGERVSPTDIEEGMRVGVDRSKYNIELPLPPRIDPSVTMMTVEEKPDVTYSDVGGCKDQIEKLREVVELPLLSPERFATLGIDPPKGILLYGPPGTGKTLCARAVANRTDATFIRVIGSELVQKYVGEGARMVRELFEMARTKKACIIFFDEIDAVGGARFDDGAGGDNEVQRTMLELITQLDGFDPRGNIKVMFATNRPNTLDPALLRPGRIDRKVEFSLPDLEGRANIFRIHSKSMSVERGIRWELISRLCPNSTGAELRSVCTEAGMFAIRARRKVATEKDFLKAVDKVISGYKKFSSTSRYMQYN |
| Enzyme Length | 467 |
| Uniprot Accession Number | P33299 |
| 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 250..257; /note=ATP; /evidence=ECO:0000255 |
| Features | Chain (1); Compositional bias (1); Modified residue (2); Nucleotide binding (1); Region (2) |
| Keywords | 3D-structure;ATP-binding;Cytoplasm;Nucleotide-binding;Nucleus;Phosphoprotein;Proteasome;Reference proteome |
| Interact With | P48510; P38348; P22141; P32628; P38764; P43588; P53196; P40327; P33298; P53549; P33297; Q01939; P19812 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000269|PubMed:14562095}. |
| Modified Residue | MOD_RES 164; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:18407956; MOD_RES 231; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:18407956 |
| Post Translational Modification | PTM: The N-terminus is blocked. |
| Signal Peptide | |
| Structure 3D | Electron microscopy (27); X-ray crystallography (3) |
| Cross Reference PDB | 3JCO; 3JCP; 3VLF; 4A3V; 4CR2; 4CR3; 4CR4; 4JPO; 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 | 10397772; 10417703; 10503546; 10559920; 10664589; 10675611; 11742986; 11805328; 11805826; 11805837; 12200147; 12827207; 14690591; 14759368; 15135049; 15571806; 15572408; 15601860; 15699485; 15905137; 16118187; 16284124; 16429126; 16517940; 16554755; 16712842; 16735578; 16922378; 17082762; 17183369; 17499717; 17803938; 18191224; 18467557; 18515799; 19013276; 19217412; 19412160; 19446322; 19446323; 19516331; 19682071; 19843524; 20008553; 20074027; 20351217; 20800707; 20850176; 21139140; 21211719; 21321079; 21389348; 21427232; 21685082; 21931558; 22037170; 22086954; 22334676; 22349505; 22350874; 22350895; 22460800; 22474342; 22493437; 23202731; 23644457; 23672618; 23770819; 23825181; 23980094; 24038880; 24598877; 24706844; 24855027; 24857655; 25079602; 25083872; 25311859; 25333764; 26130806; 26182356; 26208326; 26262643; 26327695; 26354769; 26365526; 26449534; 26642761; 26929360; 27677933; 28106073; 28115689; 30067984; 30309908; 30792173; 7805829; 8631913; 9342402; 9430676; 9490418; 9584156; 9724628; 9741626; 9799224; |
| Motif | |
| Gene Encoded By | |
| Mass | 51,983 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 5.6.1.5; |