Detail Information for IndEnz0002008065
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;