Detail Information for IndEnz0002001657
IED ID IndEnz0002001657
Enzyme Type ID protease001657
Protein Name Securin
Cell untimely torn protein 2
Protein Cut2
Gene Name cut2 SPBC14C8.01c SPBC1815.02c
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota Taphrinomycotina Schizosaccharomycetes Schizosaccharomycetales Schizosaccharomycetaceae Schizosaccharomyces Schizosaccharomyces pombe (Fission yeast) Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Enzyme Sequence MLPRTMFSYGKENAFPVTPISNRNGTKGAGSKRAPLGSTKQSNAPSSVTVPRTVLGGKSTNISKFISAPSTKKMSPMDISMDSPTILEPNSQGISRSAVQERSKRLSASPRRSSLTDTPLPNELEEDIEYMPPPVHLDPIQSLGFDDVAIDCETLDPWPSMQNKATSVTIRNTPASDFHVYKEFSDDDPIQFPLLSVDGDSPLTEKDTNLTTPATLKASDQQRKVLEKPSVSKQSSSRTRLSTVYRTKLASGKSIPRPLSHKLTRPRVTASGNSRRRPLSRSIHSLSSSRIDFSSLDTGLL
Enzyme Length 301
Uniprot Accession Number P21135
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Regulatory protein, which plays a central role in chromosome stability. Probably acts by blocking the action of key proteins. During the mitosis, it blocks separase/cut1 function, preventing the proteolysis of the cohesin complex and the subsequent segregation of the chromosomes. At the onset of anaphase, it is ubiquitinated, conducting to its destruction and to the liberation of cut1. {ECO:0000269|PubMed:8632802, ECO:0000269|PubMed:9312055}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Compositional bias (3); Motif (2); Mutagenesis (2); Region (3); Repeat (2)
Keywords Cell cycle;Cell division;Chromosome partition;Cytoplasm;Mitosis;Nucleus;Reference proteome;Repeat;Ubl conjugation
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
Modified Residue
Post Translational Modification PTM: Ubiquitinated by the anaphase promoting complex (APC) at the onset of anaphase, conducting to its degradation. {ECO:0000269|PubMed:9312055}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 12553909; 15161942; 15329725; 16453724; 16483313; 17178839; 20473289; 21712547; 22645648; 23697806; 24763107; 26527280; 26882497; 29996109; 30072439; 30726745; 8978688; 9635190;
Motif MOTIF 33..36; /note=D-box 1; MOTIF 52..55; /note=D-box 2
Gene Encoded By
Mass 32,854
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda