Detail Information for IndEnz0002013231
IED ID IndEnz0002013231
Enzyme Type ID protease013231
Protein Name Ubiquitin carboxyl-terminal hydrolase 2
EC 3.4.19.12
Deubiquitinating enzyme 2
Ubiquitin thioesterase 2
Ubiquitin-specific-processing protease 2
Gene Name UBP2 YOR124C O3281 YOR3281C
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 MPNEDNELQKAIENHHNQLLNQDKENADRNGSVIEDLPLYGTSINQQSTPGDVDDGKHLLYPDIATNLPLKTSDRLLDDILCDTIFLNSTDPKVMQKGLQSRGILKESMLSYSTFRSSIRPNCLGSLTDQVVFQTKSEYDSISCPKYNKIHVFQAVIFNPSLAEQQISTFDDIVKIPIYHLKVSVKVRQELERLKKHVGVTQFHSLDHLHEYDRVDLSTFDSSDPNLLDYGIYVSDDTNKLILIEIFKPEFNSPEEHESFTADAIKKRYNAMCVKNESLDKSETPSQVDCFYTLFKIFKGPLTRKSKAEPTKTIDSGNLALNTHLNPEWLTSKYGFQASSEIDEETNEIFTEYVPPDMVDYVNDLETRKIRESFVRKCLQLIFWGQLSTSLLAPNSPLKNTKSVKGMSSLQTSFSTLPWFHLLGESRARILLNSNEQTHSPLDAEPHFINLSVSHYYTDRDIIRNYESLSSLDPENIGLYFDALTYIANRKGAYQLIAYCGKQDIIGQEALENALLMFKINPKECNISELNEATLLSIYKYETSNKSQVTSNHLTNLKNALRLLAKYTKSDKLKFYVDHEPYRALSQAYDTLSIDESVDEDIIKTAYSVKINDSPGLKLDCDRALYTIAISKRSLDLFNFLTEECPQFSNYYGPEKLDYQEALKLLQVNENASDETILKIFKQKWFDENVYEPDQFLILRAALTKISIERNSTLITNFLLTGTIDPNSLPPENWPTGINNIGNTCYLNSLLQYYFSIAPLRRYVLEYQKTVENFNDHLSNSGHIRRIGGREISRGEVERSIQFIYQLRNLFYAMVHTRERCVTPSKELAYLAFAPSNVEVEFEVEGNKVVDQTGVLSDSKKETTDDAFTTKIKDTSLIDLEMEDGLNGDVGTDANRKKNESNDAEVSENEDTTGLTSPTRVAKISSDQLENALEMGRQQDVTECIGNVLFQIESGSEPIRYDEDNEQYDLVKQLFYGTTKQSIVPLSATNKVRTKVERFLSLLINIGDHPKDIYDAFDSYFKDEYLTMEEYGDVIRTVAVTTFPTILQVQIQRVYYDRERLMPFKSIEPLPFKEVIYMDRYADTENPLLLAKKKETEEMKQKLKVMKNRQRELLSRDDSGLTRKDAFLESIKLLESDTIKKTPLKIEAANDVIKTLRNNVQNIDNELMKLYNDINSLEEKISHQFDDFKEYGYSLFSVFIHRGEASYGHYWIYIKDRNRNGIWRKYNDETISEVQEEEVFNFNEGNTATPYFLVYVKQGQEGDIEPLKRILK
Enzyme Length 1272
Uniprot Accession Number Q01476
Absorption
Active Site ACT_SITE 745; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093"; ACT_SITE 1209; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093"
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12;
DNA Binding
EC Number 3.4.19.12
Enzyme Function FUNCTION: Has an ATP-independent isopeptidase activity, cleaving at the C-terminus of the ubiquitin moiety in natural or engineered linear fusion proteins, irrespective of their size or the presence of an N-terminal extension to ubiquitin. Removes ubiquitin chains that initiate proteolysis of FZO1 and inhibit mitochondrial fusion. {ECO:0000269|PubMed:15933713, ECO:0000269|PubMed:23317502}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Compositional bias (1); Domain (1); Modified residue (1); Region (1); Sequence conflict (1)
Keywords Hydrolase;Phosphoprotein;Protease;Reference proteome;Thiol protease;Ubl conjugation pathway
Interact With Q12242
Induction
Subcellular Location
Modified Residue MOD_RES 907; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10527495; 10570463; 10900456; 10953877; 11283351; 14690591; 16429126; 16554755; 17028178; 17079730; 17240353; 17668044; 17951556; 18719252; 18793138; 19165343; 19436320; 19447341; 19489724; 19536198; 19920177; 20074044; 20542005; 21035538; 21242292; 21427232; 22493318; 23208446; 23217712; 23747013; 23828602; 23993092; 24040048; 24069405; 24746795; 24845677; 25120264; 25396681; 25484185; 25622294; 27698423; 28298493; 28607491; 7929235; 9271226;
Motif
Gene Encoded By
Mass 146,355
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda