Detail Information for IndEnz0002011024
IED ID IndEnz0002011024
Enzyme Type ID protease011024
Protein Name Ubiquitin-like-specific protease 2
EC 3.4.22.-
Gene Name ULP2 SMT4 YIL031W
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 MSARKRKFNSLKPLDTLNSSRASSPRSSASLPPKRYNTFRKDPKIVDHLNNASTKDFLPVLSMNSESKRQIELSDNDVDNNDEGEGVNSGCSDQDFEPLQSSPLKRHSSLKSTSNGLLFQMSNNLGNGSPEPAVASTSPNGSIISTKLNLNGQFSCVDSKTLRIYRHKAPCIMTFVSDHNHPKFSLYFQQSVIYNSQVNLLDDVELIILDKKNSFMAIILKDLKKVKMILDVNNSSININTNILIWSTASSASNKKIKSIKRFLLMSYSSSIKVEILDHKEQILERLKHLIHPISSSSPSLNMERAINSTKNAFDSLRLKKTKLSTNDDESPQIHTHFLSNKPHGLQSLTKRTRIASLGKKEHSISVPKSNISPSDFYNTNGTETLQSHAVSQLRRSNRFKDVSDPANSNSNSEFDDATTEFETPELFKPSLCYKFNDGSSYTITNQDFKCLFNKDWVNDSILDFFTKFYIESSIEKSIIKREQVHLMSSFFYTKLISNPADYYSNVKKWVNNTDLFSKKYVVIPINISYHWFSCIITNLDAILDFHQNKDKNDAINSDEISINNPLVNILTFDSLRQTHSREIDPIKEFLISYALDKYSIQLDKTQIKMKTCPVPQQPNMSDCGVHVILNIRKFFENPVETIDVWKNSKIKSKHFTAKMINKYFDKNERNSARKNLRHTLKLLQLNYISYLKKENLYEEVMQMEEKKSTNINNNENYDDDDEEIQIIENIDQSSKDNNAQLTSEPPCSRSSSISTTEREPTELHNSVVRQPTGEIITDNEDPVRAASPETASVSPPIRHNILKSSSPFISESANETEQEEFTSPYFGRPSLKTRAKQFEGVSSPIKNDQALSSTHDIMMPSPKPKRIYPSKKIPQLSSHVQSLSTDSMERQSSPNNTNIVISDTEQDSRLGVNSESKNTSGIVNRDDSDVNLIGSSLPNVAEKNHDNTQESNGNNDSLGKILQNVDKELNEKLVDIDDVAFSSPTRGIPRTSATSKGSNAQLLSNYGDENNQSQDSVWDEGRDNPILLEDEDP
Enzyme Length 1034
Uniprot Accession Number P40537
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.22.-
Enzyme Function FUNCTION: Insertion mutation in SMT4 confers temperature and benomyl sensitivity; high copy suppressor of a temperature sensitive mutation in MIF2.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (8); Chain (1); Compositional bias (7); Helix (18); Modified residue (4); Region (6); Turn (2)
Keywords 3D-structure;Hydrolase;Phosphoprotein;Protease;Reference proteome;Thiol protease
Interact With
Induction
Subcellular Location
Modified Residue MOD_RES 788; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:18407956; MOD_RES 903; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:18407956; MOD_RES 983; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:19779198; MOD_RES 984; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:19779198
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (2)
Cross Reference PDB 5LNB; 5V1A;
Mapped Pubmed ID 10094048; 10713161; 10713162; 10905345; 11283351; 11333221; 11595179; 12086615; 12429940; 12654900; 14574415; 14607092; 15023545; 15137939; 15703941; 15795314; 15808504; 16429126; 16501610; 17031663; 17234788; 17499995; 17664284; 17668044; 17724121; 17768054; 18196960; 18296067; 19008217; 19107407; 19107421; 19107423; 19162180; 19225149; 19536198; 19823017; 19887903; 21059884; 21222284; 21483811; 21892772; 22025676; 22350877; 23175280; 23403034; 23550137; 23712011; 23812602; 24498309; 25302077; 25434491; 25833950; 25946564; 26598615; 26837752; 26921322; 27585592; 27839712; 28487408; 29903909; 30575729; 31313851; 31747400; 34081091;
Motif
Gene Encoded By
Mass 116,883
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.4.22.B67;