Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Securin  

UniProtKB / Swiss-Prot ID :  PTTG1_HUMAN

Gene Name (Synonyms) : 
PTTG1, EAP1, PTTG, TUTR1  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. Nucleus. 

Protein 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. 

Protein Sequence MATLIYVDKENGEPGTRVVAKDGLKLGSGPSIKALDGRSQVSTPRFGKTFDAPPALPKATRKALGTVNRA...
Predicted Secondary Structure CCEEEEEECCCCCCCCEECCCCCEEECCCCCEEEECCCCCCCCCCCCCCCCCCCCCCHHHHHHHHHHHHH...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MATLIY
---CCEEEE
15.89UniProtKB
Link-
9Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)IYVDKENGE
EEEECCCCC
42.93HPRD
Link-
9Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)IYVDKENGE
EEEECCCCC
42.93Phosphositeplus
Link-
16PhosphothreonineGEPGTRVVA
CCCCCEECC
30.88Phosphositeplus
Link-
28PhosphoserineLKLGSGPSI
EEECCCCCE
58.95Phosphositeplus
Link-
48Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PRFGKTFDA
CCCCCCCCC
43.22Phosphositeplus
Link-
101Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TVKAKSSVP
HHHCCCCCC
37.23Phosphositeplus
Link-
111PhosphotyrosineSDDAYPEIE
CCCCCCHHH
14.37Phosphositeplus
Link-
165PhosphoserineLGPPSPVKM
CCCCCCCCC
45.52HPRD
Link-
165PhosphoserineLGPPSPVKM
CCCCCCCCC
45.52Phosphositeplus
Link-
165PhosphoserineLGPPSPVKM
CCCCCCCCC
45.52SysPTM
Link-
165Phosphoserine (CDK1)LGPPSPVKM
CCCCCCCCC
45.52HPRD
Link-
165Phosphoserine (CDK1)LGPPSPVKM
CCCCCCCCC
45.52PhosphoELM
Link-
165Phosphoserine; by CDK1.LGPPSPVKM
CCCCCCCCC
45.52UniProtKB
Link-
181PhosphoserineNLLQSPSSI
CCCCCCHHH
27.07HPRD
Link-
183PhosphoserineLQSPSSILS
CCCCHHHHH
34.95Phosphositeplus
Link-
184PhosphoserineQSPSSILST
CCCHHHHHH
30.82HPRD
Link-
184PhosphoserineQSPSSILST
CCCHHHHHH
30.82Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
KU70_HUMANin vitro
in vivo
HPRD:04998HPRD11238996
P53_HUMANin vitro
in vivo
HPRD:04998HPRD12355087
DNJA1_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:04998HPRD9915854
CDC20_HUMANin vitro
in vivo
HPRD:04998HPRD11553328
RS10_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:04998HPRD9915854
PTTG_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:04998HPRD10781616
CDC27_HUMANENSP00000344936STRING
UB2D1_HUMANENSP00000344936STRING
CDC23_HUMANENSP00000344936STRING
INS_HUMANENSP00000344936STRING
INS_HUMANENSP00000344936STRING
ESPL1_HUMANENSP00000344936STRING
ANC5_HUMANENSP00000344936STRING
P53_HUMANENSP00000344936STRING
BUB1B_HUMANENSP00000344936STRING
PLK1_HUMANENSP00000344936STRING
IGF1B_HUMANENSP00000344936STRING
UB2E1_HUMANENSP00000344936STRING
CDC2_HUMANENSP00000344936STRING
CDC20_HUMANENSP00000344936STRING
APC10_HUMANENSP00000344936STRING
AURKB_HUMANENSP00000344936STRING
ANC2_HUMANENSP00000344936STRING
VEGFA_HUMANENSP00000344936STRING
ANC4_HUMANENSP00000344936STRING
STK6_HUMANENSP00000344936STRING
PTTG_HUMANENSP00000344936STRING
ANC1_HUMANENSP00000344936STRING
APC11_HUMANENSP00000344936STRING
APC7_HUMANENSP00000344936STRING
CDC16_HUMANENSP00000344936STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Cell cycle regulated expression and phosphorylation of hpttg proto-oncogene product.";
Ramos-Morales F., Dominguez A., Romero F., Luna R., Multon M.-C.,Pintor-Toro J.A., Tortolero M.;
Oncogene 19:403-409(2000).
Cited for: PHOSPHORYLATION AT SER-165, AND MUTAGENESIS OF SER-165.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures