IED ID | IndEnz0002008065 |
Enzyme Type ID | protease008065 |
Protein Name |
26S proteasome subunit RPT4 26S protease subunit SUG2 Proteasomal cap subunit |
Gene Name | RPT4 CRL13 PCS1 SUG2 YOR259C |
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 | MSEEQDPLLAGLGETSGDNHTQQSHEQQPEQPQETEEHHEEEPSRVDPEQEAHNKALNQFKRKLLEHRRYDDQLKQRRQNIRDLEKLYDKTENDIKALQSIGQLIGEVMKELSEEKYIVKASSGPRYIVGVRNSVDRSKLKKGVRVTLDITTLTIMRILPRETDPLVYNMTSFEQGEITFDGIGGLTEQIRELREVIELPLKNPEIFQRVGIKPPKGVLLYGPPGTGKTLLAKAVAATIGANFIFSPASGIVDKYIGESARIIREMFAYAKEHEPCIIFMDEVDAIGGRRFSEGTSADREIQRTLMELLTQMDGFDNLGQTKIIMATNRPDTLDPALLRPGRLDRKVEIPLPNEAGRLEIFKIHTAKVKKTGEFDFEAAVKMSDGFNGADIRNCATEAGFFAIRDDRDHINPDDLMKAVRKVAEVKKLEGTIEYQKL |
Enzyme Length | 437 |
Uniprot Accession Number | P53549 |
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 | Chain (1); Compositional bias (2); Initiator methionine (1); Modified residue (1); Nucleotide binding (1); Region (1); Sequence conflict (2) |
Keywords | 3D-structure;ATP-binding;Acetylation;Direct protein sequencing;Nucleotide-binding;Proteasome;Reference proteome |
Interact With | P43588; P33299; P33298; P33297; Q01939 |
Induction | |
Subcellular Location | |
Modified Residue | MOD_RES 2; /note=N-acetylserine; /evidence=ECO:0000269|PubMed:12504901 |
Post Translational Modification | PTM: N-acetylated by NAT1. {ECO:0000269|PubMed:12504901}. |
Signal Peptide | |
Structure 3D | Electron microscopy (27) |
Cross Reference PDB | 3JCO; 3JCP; 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 | 10350051; 10417703; 10419517; 10519004; 10559920; 10664589; 10688190; 11152478; 11283351; 11389845; 11410533; 11418596; 11590019; 11595789; 11742986; 11805826; 11805837; 11964465; 11964484; 12399382; 14967150; 15135049; 15571806; 15843385; 15905137; 16284124; 16429126; 16517940; 16554755; 16763564; 16837462; 16922378; 17150417; 17499717; 18174173; 18374642; 18467557; 18604275; 19013276; 19412160; 19446322; 19446323; 19516331; 19536198; 19841731; 19843524; 20074027; 20508643; 20519439; 21139140; 21209940; 21211719; 21266254; 21389348; 21685082; 21931558; 22037170; 22086954; 22311637; 22350874; 22350895; 22474342; 22491889; 22493437; 23105001; 23202731; 23209158; 23644457; 23672618; 23770819; 24013205; 24243762; 24327750; 24598877; 24706844; 25333764; 25926993; 26130806; 26182356; 26208326; 26262643; 26365526; 26449534; 26929360; 27677933; 28106073; 28115689; 30067984; 30309908; 30792173; 3294103; 3294104; 8962070; 8973309; 9342402; 9584156; 9724628; 9741626; |
Motif | |
Gene Encoded By | |
Mass | 49,408 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 5.6.1.5; |