| IED ID | IndEnz0002010404 |
| Enzyme Type ID | protease010404 |
| Protein Name |
Securin Esp1-associated protein Pituitary tumor-transforming gene 1 protein Tumor-transforming protein 1 hPTTG |
| Gene Name | PTTG1 EAP1 PTTG TUTR1 |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MATLIYVDKENGEPGTRVVAKDGLKLGSGPSIKALDGRSQVSTPRFGKTFDAPPALPKATRKALGTVNRATEKSVKTKGPLKQKQPSFSAKKMTEKTVKAKSSVPASDDAYPEIEKFFPFNPLDFESFDLPEEHQIAHLPLSGVPLMILDEERELEKLFQLGPPSPVKMPSPPWESNLLQSPSSILSTLDVELPPVCCDIDI |
| Enzyme Length | 202 |
| Uniprot Accession Number | O95997 |
| 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, in the p53/TP53 pathway, and DNA repair. Probably acts by blocking the action of key proteins. During the mitosis, it blocks Separase/ESPL1 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 ESPL1. Its function is however not limited to a blocking activity, since it is required to activate ESPL1. Negatively regulates the transcriptional activity and related apoptosis activity of TP53. The negative regulation of TP53 may explain the strong transforming capability of the protein when it is overexpressed. May also play a role in DNA repair via its interaction with Ku, possibly by connecting DNA damage-response pathways with sister chromatid separation. {ECO:0000269|PubMed:10411507, ECO:0000269|PubMed:11238996, ECO:0000269|PubMed:11371342, ECO:0000269|PubMed:12355087}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Initiator methionine (1); Modified residue (2); Motif (4); Mutagenesis (5); Region (1) |
| Keywords | 3D-structure;Acetylation;Cell cycle;Cell division;Chromosome partition;Cytoplasm;DNA damage;DNA repair;Mitosis;Nucleus;Phosphoprotein;Proto-oncogene;Reference proteome;Repeat;SH3-binding;Ubl conjugation |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. Nucleus. |
| Modified Residue | MOD_RES 2; /note=N-acetylalanine; /evidence=ECO:0007744|PubMed:22814378; MOD_RES 165; /note=Phosphoserine; by CDK1; /evidence=ECO:0000269|PubMed:10656688 |
| Post Translational Modification | PTM: Phosphorylated at Ser-165 by CDK1 during mitosis. {ECO:0000269|PubMed:10656688}.; PTM: Phosphorylated in vitro by ds-DNA kinase. {ECO:0000269|PubMed:10656688}.; PTM: Ubiquitinated through 'Lys-11' linkage of ubiquitin moieties by the anaphase promoting complex (APC) at the onset of anaphase, conducting to its degradation. 'Lys-11'-linked ubiquitination is mediated by the E2 ligase UBE2C/UBCH10. {ECO:0000269|PubMed:10411507, ECO:0000269|PubMed:18485873}. |
| Signal Peptide | |
| Structure 3D | Electron microscopy (2) |
| Cross Reference PDB | 7NJ0; 7NJ1; |
| Mapped Pubmed ID | 10733526; 11081627; 12070128; 12194817; 12213878; 12324572; 12403781; 12444553; 12446569; 12554778; 12590639; 12727994; 12958169; 12960092; 14671639; 14709851; 14966902; 15024062; 15178645; 15281346; 15514942; 15591026; 15649325; 15678131; 15769981; 15846392; 15880121; 15897900; 16205121; 16292982; 16394085; 16413484; 16685397; 16705156; 16705313; 16799481; 16809406; 16820881; 16926250; 17071631; 17210994; 17297475; 17353909; 17383977; 17507465; 17652795; 17854787; 17962814; 18047793; 18217976; 18245958; 18339849; 18384692; 18426563; 18522889; 18550719; 18594525; 18620995; 18663361; 18753362; 18984771; 19000457; 19008095; 19053469; 19117984; 19302955; 19351864; 19407503; 19477929; 19539243; 19690544; 19837943; 19840458; 19958546; 20106827; 20116377; 20198633; 20360068; 20406982; 20452981; 20621061; 20628624; 20650808; 20677014; 20953187; 20962850; 20978326; 21068098; 21069851; 21099350; 21126432; 21129230; 21176344; 21181309; 21272169; 21336306; 21439054; 21757741; 21839581; 21858218; 21937724; 22002306; 22081074; 22209758; 22260438; 22475756; 22511756; 22522436; 22783570; 22789011; 22805307; 22819078; 22994714; 23051594; 23128677; 23164239; 23267136; 23404407; 23416975; 23489647; 23523951; 23527717; 23671127; 23677169; 23755904; 23798554; 23850618; 23867215; 24051510; 24176776; 24238056; 24377512; 24594688; 24627133; 24754453; 24781523; 24816985; 24853182; 24879625; 24908230; 25549700; 25627474; 25739119; 25814554; 25816405; 25871022; 25874498; 25908389; 26264222; 26320179; 26445238; 26496610; 26578364; 26710612; 26824458; 26894859; 26900962; 26984614; 27756608; 27766744; 27787230; 27829547; 27893422; 28219049; 28242412; 28504713; 28658604; 29218429; 29288516; 29432944; 29575197; 29622689; 29649138; 29803224; 29989583; 30154144; 30506545; 30519761; 30582202; 30590814; 30607824; 30853662; 30961403; 31278532; 31385458; 31521689; 31641007; 32163388; 32216239; 32277958; 32314536; 32322060; 32519672; 32549754; 32725378; 33173433; 33243736; 33498448; 33624604; 33743960; 33881746; 34290405; 34539658; 34728029; |
| Motif | MOTIF 61..64; /note=D-box; MOTIF 71..73; /note=TEK-box 1; MOTIF 94..96; /note=TEK-box 2; MOTIF 163..173; /note=SH3-binding |
| Gene Encoded By | |
| Mass | 22,024 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |