Annotation for this protein is in progress - please check future releases for more complete information


DP00521: SecurinFASTA viewXML view

General information
DisProt:DP00521
Name:Securin
Synonym(s):PTTG1_HUMAN
Pituitary tumor-transforming gene 1 protein
hPTTG
Tumor-transforming protein 1
Esp1-associated protein
First appeared in release:Release 3.5 (12/22/2006)
UniProt:O95997
UniGene:Hs.350966
SwissProt: PTTG1_HUMAN
TrEMBL:  
NCBI (GI): 29336594
Source organism:Homo sapiens (Human)
Sequence length:202
Percent disordered:100%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MATLIYVDKE NGEPGTRVVA KDGLKLGSGP SIKALDGRSQ VSTPRFGKTF DAPPALPKAT - 60
RKALGTVNRA TEKSVKTKGP LKQKQPSFSA KKMTEKTVKA KSSVPASDDA YPEIEKFFPF - 120
NPLDFESFDL PEEHQIAHLP LSGVPLMILD EERELEKLFQ LGPPSPVKMP SPPWESNLLQ - 180
SPSSILSTLD VELPPVCCDI DI



Functional narrative    

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.

Region 1: 1-202

Map of ordered and disordered regions







Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.


Region 1
Type:Disordered
Name: 
Location:1 - 202
Length:202
Region sequence:

MATLIYVDKENGEPGTRVVAKDGLKLGSGPSIKALDGRSQVSTPRFGKTFDAPPALPKAT
RKALGTVNRATEKSVKTKGPLKQKQPSFSAKKMTEKTVKAKSSVPASDDAYPEIEKFFPF
NPLDFESFDLPEEHQIAHLPLSGVPLMILDEERELEKLFQLGPPSPVKMPSPPWESNLLQ
SPSSILSTLDVELPPVCCDIDI

Modification type: Monomeric
Native
PDB:  
Structural/functional type: Function arises from the disordered state
Function arises via a disorder to order transition
Functional classes: Modification site
Molecular recognition effectors
Functional subclasses: Phosphorylation
Protein-DNA binding
Apoptosis Regulation
Protein-protein binding
Detection methods:
  1. Size exclusion/gel filtration chromatography (pH: 7.2; 2-mercaptoethanol (buffer) 10 mM; KCl (buffer) 150 mM; phosphate (buffer) 25 mM; securin (sample) 100 microM; Superdex 200 HR10/30 column)

  2. Circular dichroism (CD) spectroscopy, far-UV (pH: 7.2; 1-mm pathlength; DTE (buffer) 1 mM; KCl (buffer) 150 mM; NaPi (buffer) 25 mM; protein (sample) 10 microM)

  3. Analytical ultracentrifugation (283 K; )

  4. Nuclear magnetic resonance (NMR) (293 K; pH: 7.2; 2-mercaptoethanol 10 mM; KCl 150 mM; NaP 25 mM)
References:
  1. Sanchez-Puig N, Veprintsev DB, Fersht AR. "Human full-length Securin is a natively unfolded protein." Protein Sci. 2005; 14(6): 1410-8. PubMed: 15929994
Comments:
 


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