PTTG1_BOVIN
ID PTTG1_BOVIN Reviewed; 202 AA.
AC Q3SZY3;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Securin;
DE AltName: Full=Pituitary tumor-transforming gene 1 protein;
GN Name=PTTG1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulatory protein, which plays a central role in chromosome
CC stability, in the p53/TP53 pathway, and DNA repair. Probably acts by
CC blocking the action of key proteins. During the mitosis, it blocks
CC Separase/ESPL1 function, preventing the proteolysis of the cohesin
CC complex and the subsequent segregation of the chromosomes. At the onset
CC of anaphase, it is ubiquitinated, conducting to its destruction and to
CC the liberation of ESPL1. Its function is however not limited to a
CC blocking activity, since it is required to activate ESPL1. Negatively
CC regulates the transcriptional activity and related apoptosis activity
CC of TP53. The negative regulation of TP53 may explain the strong
CC transforming capability of the protein when it is overexpressed. May
CC also play a role in DNA repair via its interaction with Ku, possibly by
CC connecting DNA damage-response pathways with sister chromatid
CC separation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with RPS10 and DNAJA1 (By similarity). Interacts
CC with the caspase-like ESPL1, and prevents its protease activity
CC probably by covering its active site. Interacts with TP53 and blocks
CC its activity probably by blocking its binding to DNA. Interacts with
CC the Ku 70 kDa subunit of ds-DNA kinase. Interacts with PTTG1IP (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- DOMAIN: The N-terminal destruction box (D-box) acts as a recognition
CC signal for degradation via the ubiquitin-proteasome pathway.
CC {ECO:0000250}.
CC -!- DOMAIN: The TEK-boxes are required for 'Lys-11'-linked ubiquitination
CC and facilitate the transfer of the first ubiquitin and ubiquitin chain
CC nucleation. TEK-boxes may direct a catalytically competent orientation
CC of the UBE2C/UBCH10-ubiquitin thioester with the acceptor lysine
CC residue (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated at Ser-165 by CDK1 during mitosis. {ECO:0000250}.
CC -!- PTM: Phosphorylated in vitro by ds-DNA kinase. {ECO:0000250}.
CC -!- PTM: Ubiquitinated through 'Lys-11' linkage of ubiquitin moieties by
CC the anaphase promoting complex (APC) at the onset of anaphase,
CC conducting to its degradation. 'Lys-11'-linked ubiquitination is
CC mediated by the E2 ligase UBE2C/UBCH10 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the securin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC102656; AAI02657.1; -; mRNA.
DR EMBL; BC111142; AAI11143.1; -; mRNA.
DR RefSeq; NP_001029482.1; NM_001034310.2.
DR RefSeq; XP_003582518.1; XM_003582470.4.
DR RefSeq; XP_003582519.1; XM_003582471.3.
DR RefSeq; XP_003582520.1; XM_003582472.2.
DR RefSeq; XP_003586385.1; XM_003586337.4.
DR RefSeq; XP_003586386.1; XM_003586338.3.
DR RefSeq; XP_003586387.1; XM_003586339.2.
DR RefSeq; XP_010796369.1; XM_010798067.1.
DR RefSeq; XP_010805873.1; XM_010807571.1.
DR AlphaFoldDB; Q3SZY3; -.
DR STRING; 9913.ENSBTAP00000016162; -.
DR PaxDb; Q3SZY3; -.
DR PRIDE; Q3SZY3; -.
DR GeneID; 508043; -.
DR KEGG; bta:508043; -.
DR CTD; 9232; -.
DR eggNOG; ENOG502S2GG; Eukaryota.
DR HOGENOM; CLU_1363209_0_0_1; -.
DR InParanoid; Q3SZY3; -.
DR OrthoDB; 1296347at2759; -.
DR TreeFam; TF330797; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051276; P:chromosome organization; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0045143; P:homologous chromosome segregation; IBA:GO_Central.
DR GO; GO:2000816; P:negative regulation of mitotic sister chromatid separation; IBA:GO_Central.
DR InterPro; IPR006940; Securin_separation_inhibitor.
DR PANTHER; PTHR10418; PTHR10418; 1.
DR Pfam; PF04856; Securin; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Chromosome partition; Cytoplasm; DNA damage;
KW DNA repair; Mitosis; Nucleus; Phosphoprotein; Proto-oncogene;
KW Reference proteome; Repeat; SH3-binding; Ubl conjugation.
FT CHAIN 1..202
FT /note="Securin"
FT /id="PRO_0000240609"
FT REGION 36..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 61..64
FT /note="D-box"
FT MOTIF 71..73
FT /note="TEK-box 1"
FT MOTIF 94..96
FT /note="TEK-box 2"
FT MOTIF 163..173
FT /note="SH3-binding"
FT MOD_RES 165
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:O95997"
SQ SEQUENCE 202 AA; 22132 MW; 86851B710BE2DE58 CRC64;
MSTLIYVDKE NGEPGIHVAP KDGLKLGSVP SVKALDGRSQ VSTPHVGKMF DAPPALPKTA
RKALGTVNRA TEKSVKTNGP LKQKQTTFST KKITEKTVKA KSSVPASDDT YPEIEKFFPF
NPLDFENFDL PEEHQIARLP LSGVPLMILD EERELEQLLH VGPPSPLKMP PLLWESNLLQ
SPSSILSTLD VELPPVCCDL DI
