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Database Commons - ANIA

ANIA

Citations: 6

z-index 0.28

Short name ANIA
Full name ANnotation and Integrated Analysis of the 14-3-3 interactome
Description The dimeric 14-3-3 proteins dock onto pairs of phosphorylated Ser and Thr residues on hundreds of proteins, and thereby regulate many events in mammalian cells. ANnotation and Integrated Analysis of the 14-3-3 interactome, which integrates multiple data sets on 14-3-3-binding phosphoproteins.
URL https://ania-1433.lifesci.dundee.ac.uk/prediction/webserver/index.py
Year founded 2012
Last update & version NA    v1.0
Availability Free to all users
University/Institution hosted University of Dundee
Address Dundee DD1 5EH, Scotland, UK
City Scotland
Province/State
Country/Region United Kingdom
Contact name Carol MacKintosh
Contact email c.mackintosh@dundee.ac.uk
Data type(s)
Major organism(s)
Keyword(s)
  • 14-3-3 protein
  • human kimono
Publication(s)
  • ANIA: ANnotation and Integrated Analysis of the 14-3-3 interactome. [PMID: 24501395]

    Michele Tinti, Fábio Madeira, Gavuthami Murugesan, Gerta Hoxhaj, Rachel Toth, Carol Mackintosh
    Database : the journal of biological databases and curation 2014:2014
    6 Citations (Google Scholar as of 2016-03-28)

    Abstract: The dimeric 14-3-3 proteins dock onto pairs of phosphorylated Ser and Thr residues on hundreds of proteins, and thereby regulate many events in mammalian cells. To facilitate global analyses of these interactions, we developed a web resource named ANIA: ANnotation and Integrated Analysis of the 14-3-3 interactome, which integrates multiple data sets on 14-3-3-binding phosphoproteins. ANIA also pinpoints candidate 14-3-3-binding phosphosites using predictor algorithms, assisted by our recent discovery that the human 14-3-3-interactome is highly enriched in 2R-ohnologues. 2R-ohnologues are proteins in families of two to four, generated by two rounds of whole genome duplication at the origin of the vertebrate animals. ANIA identifies candidate 'lynchpins', which are 14-3-3-binding phosphosites that are conserved across members of a given 2R-ohnologue protein family. Other features of ANIA include a link to the catalogue of somatic mutations in cancer database to find cancer polymorphisms that map to 14-3-3-binding phosphosites, which would be expected to interfere with 14-3-3 interactions. We used ANIA to map known and candidate 14-3-3-binding enzymes within the 2R-ohnologue complement of the human kinome. Our projections indicate that 14-3-3s dock onto many more human kinases than has been realized. Guided by ANIA, PAK4, 6 and 7 (p21-activated kinases 4, 6 and 7) were experimentally validated as a 2R-ohnologue family of 14-3-3-binding phosphoproteins. PAK4 binding to 14-3-3 is stimulated by phorbol ester, and involves the 'lynchpin' site phosphoSer99 and a major contribution from Ser181. In contrast, PAK6 and PAK7 display strong phorbol ester-independent binding to 14-3-3, with Ser113 critical for the interaction with PAK6. These data point to differential 14-3-3 regulation of PAKs in control of cell morphology. Database URL: https://ania-1433.lifesci.dundee.ac.uk/prediction/webserver/index.py.

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Tags

Interaction and Network Protein
Homo sapiens
14-3-3 protein human kimono

Record metadata

  • Created on: 2015-06-20
  • Curated by:
    • Mengwei Li [2016-03-31]
    • Mengwei Li [2016-03-28]
    • Mengwei Li [2015-11-24]
    • Mengwei Li [2015-06-26]
Stats