PTTG1
entrez
9232
canonical
uniprot
O95997
canonical
ensembl
ENSG00000164611
resolver
ensp
ENSP00000344936
resolver
ensp
ENSP00000377536
resolver
ensp
ENSP00000430642
resolver
ensp
ENSP00000592313
resolver
ensp
ENSP00000592319
resolver
ensp
ENSP00000592320
resolver
ensp
ENSP00000592322
resolver
ensp
ENSP00000592323
resolver
enst
ENST00000352433
resolver
enst
ENST00000393964
resolver
enst
ENST00000520452
resolver
enst
ENST00000922254
resolver
enst
ENST00000922260
resolver
enst
ENST00000922261
resolver
enst
ENST00000922263
resolver
enst
ENST00000922264
resolver
genesymbol
PTTG1
resolver
genesymbol_syn
EAP1
resolver
genesymbol_syn
PTTG
resolver
genesymbol_syn
TUTR1
resolver
hgnc
HGNC:9690
resolver
uniprot
Q6IAL9
resolver
uniprot_entry
PTTG1_HUMAN
resolver
uniprot_entry
Q6IAL9_HUMAN
resolver
amino_acid_sequence
MATLIYVDKENGEPGTRVVAKDGLKLGSGPSIKALDGRSQVSTPRFGKTFDAPPALPKATRKALGTVNRATEKSVKTKGPLKQKQPSFSAKKMTEKTVKAKSSVPASDDAYPEIEKFFPFNPLDFESFDLPEEHQIAHLPLSGVPLMILDEERELEKLFQLGPPSPVKMPSPPWESNLLQSPSSILSTLDVELPPVCCDIDI
uniprot
proteins
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}.
uniprot
proteins
mass_dalton
22024
uniprot
proteins
mutagenesis
MUTAGEN 61; /note="R->A: Abolishes ubiquitination and subsequent degradation; when associated with A-64."; /evidence="ECO:0000269|PubMed:10411507"; MUTAGEN 64; /note="L->A: Abolishes ubiquitination and subsequent degradation; when associated with A-61."; /evidence="ECO:0000269|PubMed:10411507"; MUTAGEN 163; /note="P->A: Strongly reduces transforming capability; when associated with L-170; A-172 and L-173."; /evidence="ECO:0000269|PubMed:9892021"; MUTAGEN 165; /note="S->A: Abolishes phosphorylation."; /evidence="ECO:0000269|PubMed:10656688"; MUTAGEN 170..173; /note="PSPP->LSAL: Strongly reduces transforming capability; when associated with A-163."; /evidence="ECO:0000269|PubMed:9892021
uniprot
proteins
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}.
uniprot
proteins
protein_family
Securin family
uniprot
proteins
pubmed
10022450
uniprot
proteins
pubmed
10393434
uniprot
proteins
pubmed
10411507
uniprot
proteins
pubmed
10580151
uniprot
proteins
pubmed
10656688
uniprot
proteins
pubmed
10781616
uniprot
proteins
pubmed
11158059
uniprot
proteins
pubmed
11238996
uniprot
proteins
pubmed
11371342
uniprot
proteins
pubmed
12355087
uniprot
proteins
pubmed
18485873
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
9811450
uniprot
proteins
pubmed
9892021
uniprot
proteins
sequence_length
202
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
uniprot
proteins