C. J. Jeffery, Moonlighting proteins, Trends Biochem. Sci, vol.24, pp.8-11, 1999.

J. Piatigorsky and G. J. Wistow, Enzyme/crystallins: gene sharing as an evolutionary strategy, Cell, vol.57, pp.197-199, 1989.

K. Volz, The functional duality of iron regulatory protein 1, Curr. Opin. Struct. Biol, vol.18, pp.106-111, 2008.

C. J. Jeffery, An introduction to protein moonlighting, Biochem. Soc. Trans, vol.42, pp.1679-1683, 2014.

P. Ostrovsky-de-spicer and S. Maloy, PutA protein, a membrane-associated flavin dehydrogenase, acts as a redox-dependent transcriptional regulator, Proc. Natl. Acad. Sci. U.S.A, vol.90, pp.4295-4298, 1993.

C. J. Jeffery, Protein moonlighting: what is it, and why is it important?, Philos. Trans. R. Soc. Lond., B, Biol. Sci, vol.373, 2018.

V. Amblee and C. J. Jeffery, Physical features of intracellular proteins that moonlight on the cell surface, PLoS ONE, vol.10, p.130575, 2015.

B. D. Berkovits and C. Mayr, Alternative 3 UTRs act as scaffolds to regulate membrane protein localization, Nature, vol.522, pp.363-367, 2015.

C. Mayr, Evolution and biological roles of alternative 3 UTRs, Trends Cell Biol, vol.26, pp.227-237, 2016.

C. Mayr, Regulation by 3 -untranslated regions, Annu. Rev. Genet, vol.51, pp.171-194, 2017.

D. R. Soto-pantoja, S. Kaur, and D. D. Roberts, CD47 signaling pathways controlling cellular differentiation and responses to stress, Crit. Rev. Biochem. Mol. Biol, vol.50, pp.212-230, 2015.

W. Ma and C. Mayr, A Membraneless organelle associated with the endoplasmic reticulum enables 3 UTR-mediated protein-protein interactions, Cell, vol.175, pp.1492-1506, 2018.

S. Lee and C. Mayr, Gain of additional BIRC3 protein functions through 3 -UTR-mediated protein complex formation, Mol. Cell, vol.74, pp.701-712, 2019.

C. E. Chapple, B. Robisson, L. Spinelli, C. Guien, E. Becker et al., Extreme multifunctional proteins identified from a human protein interaction network, Nat. Commun, vol.6, p.7412, 2015.
URL : https://hal.archives-ouvertes.fr/hal-01407399

J. R. Perkins, I. Diboun, B. H. Dessailly, J. G. Lees, and C. Orengo, Transient protein-protein interactions: structural, functional, and network properties, Structure, vol.18, pp.1233-1243, 2010.

K. Van-roey, T. J. Gibson, and N. E. Davey, Motif switches: decision-making in cell regulation, Curr. Opin. Struct. Biol, vol.22, pp.378-385, 2012.

C. Mayr, What are 3 UTRs doing?, Cold Spring Harb Perspect Biol, vol.11, p.34728, 2019.

D. M. Ribeiro, G. Briere, B. Bely, L. Spinelli, and C. Brun, MoonDB 2.0: an updated database of extreme multifunctional and moonlighting proteins, Nucleic Acids Res, vol.47, pp.398-402, 2019.
URL : https://hal.archives-ouvertes.fr/hal-01907669

B. Aranda, H. Blankenburg, S. Kerrien, F. S. Brinkman, A. Ceol et al., PSICQUIC and PSISCORE: accessing and scoring molecular interactions, Nat. Methods, vol.8, pp.528-529, 2011.

E. Becker, B. Robisson, C. E. Chapple, A. Guénoche, and C. Brun, Multifunctional proteins revealed by overlapping clustering in protein interaction network, Bioinformatics, vol.28, pp.84-90, 2012.
URL : https://hal.archives-ouvertes.fr/hal-00877694

C. E. Chapple, C. Herrmann, and C. Brun, PrOnto database: GO term functional dissimilarity inferred from biological data, Front. Genet, vol.6, 0200.
URL : https://hal.archives-ouvertes.fr/hal-01408050

, Expansion of the Gene Ontology knowledgebase and resources, The Gene Ontology Consortium, vol.45, pp.331-338, 2017.

, UniProt: the universal protein knowledgebase, The UniProt Consortium, vol.45, pp.158-169, 2017.

R. J. Kinsella, A. Kähäri, S. Haider, J. Zamora, G. Proctor et al., Ensembl BioMarts: a hub for data retrieval across taxonomic space, Database, p.30, 2011.

S. Müller, L. Rycak, F. Afonso-grunz, P. Winter, A. M. Zawada et al., APADB: a database for alternative polyadenylation and microRNA regulation events, Database, p.76, 2014.

A. J. Gruber, R. Schmidt, A. R. Gruber, G. Martin, S. Ghosh et al., A comprehensive analysis of 3 end sequencing data sets reveals novel polyadenylation signals and the repressive role of heterogeneous ribonucleoprotein C on cleavage and polyadenylation, Genome Res, vol.26, pp.1145-1159, 2016.

E. Dassi, A. Re, S. Leo, T. Tebaldi, L. Pasini et al., AURA 2: Empowering discovery of post-transcriptional networks, Translation (Austin), vol.2, 2014.

M. Uhlén, L. Fagerberg, B. M. Hallström, C. Lindskog, P. Oksvold et al., ) Tissue-based map of the human proteome, p.1260419, 2015.

A. R. Quinlan and I. M. Hall, BEDTools: a flexible suite of utilities for comparing genomic features, Bioinformatics, vol.26, pp.841-842, 2010.

L. Fu, B. Niu, Z. Zhu, S. Wu, and W. Li, CD-HIT: accelerated for clustering the next-generation sequencing data, Bioinformatics, vol.28, pp.3150-3152, 2012.

P. J. Thul, L. Åkesson, M. Wiking, D. Mahdessian, A. Geladaki et al., A subcellular map of the human proteome, p.3321, 2017.

J. Reimand, T. Arak, P. Adler, L. Kolberg, S. Reisberg et al., Profiler-a web server for functional interpretation of gene lists (2016 update), Nucleic Acids Res, vol.44, pp.83-89, 2016.

S. Lianoglou, V. Garg, J. L. Yang, C. S. Leslie, and C. Mayr, Ubiquitously transcribed genes use alternative polyadenylation to achieve tissue-specific expression, Genes Dev, vol.27, pp.2380-2396, 2013.

P. Mendik, L. Dobronyi, F. Hári, C. Kerepesi, L. Maia-moço et al., Translocatome: a novel resource for the analysis of protein translocation between cellular organelles, Nucleic Acids Res, vol.47, pp.495-505, 2019.

A. Zanzoni, L. Spinelli, D. M. Ribeiro, G. G. Tartaglia, and C. Brun, Post-transcriptional regulatory patterns revealed by protein-RNA interactions, Sci. Rep, vol.9, p.4302, 2019.
URL : https://hal.archives-ouvertes.fr/hal-02070124

G. Von-heijne, Membrane-protein topology, Nat. Rev. Mol. Cell Biol, vol.7, pp.909-918, 2006.

R. Zimmermann, S. Eyrisch, M. Ahmad, and V. Helms, Protein translocation across the ER membrane, Biochim. Biophys. Acta, vol.1808, pp.912-924, 2011.

M. Bernhofer, T. Goldberg, S. Wolf, M. Ahmed, J. Zaugg et al., NLSdb-major update for database of nuclear localization signals and nuclear export signals, Nucleic Acids Res, vol.46, pp.503-508, 2018.

C. Chen, S. Zabad, H. Liu, W. Wang, and C. Jeffery, MoonProt 2.0: an expansion and update of the moonlighting proteins database, Nucleic Acids Res, vol.46, pp.640-644, 2018.

A. Díaz-ramos, A. Roig-borrellas, A. García-melero, and R. López-alemany, ?-Enolase, a multifunctional protein: its role on pathophysiological situations, J. Biomed. Biotechnol, p.156795, 2012.

O. J. Pettersson, L. Aagaard, D. Andrejeva, R. Thomsen, T. G. Jensen et al., DDX6 regulates sequestered nuclear CUG-expanded DMPK-mRNA in dystrophia myotonica type 1, Nucleic Acids Res, vol.42, pp.7186-7200, 2014.

C. A. Maxwell, J. Mccarthy, and E. Turley, Cell-surface and mitotic-spindle RHAMM: moonlighting or dual oncogenic functions?, J. Cell. Sci, vol.121, pp.925-932, 2008.

S. Sharma, S. J. Bartholdson, A. C. Couch, K. Yusa, and G. J. Wright, Genome-scale identification of cellular pathways required for cell surface recognition, Genome Res, vol.28, pp.1372-1382, 2018.

G. Sriram, J. A. Martinez, E. R. Mccabe, J. C. Liao, and K. M. Dipple, Single-gene disorders: what role could moonlighting enzymes play?, Am. J. Hum. Genet, vol.76, pp.911-924, 2005.

M. W. Hentze, A. Castello, T. Schwarzl, and T. Preiss, A brave new world of RNA-binding proteins, Nat. Rev. Mol. Cell Biol, vol.19, pp.327-341, 2018.

S. Gerstberger, M. Hafner, and T. Tuschl, A census of human RNA-binding proteins, Nat. Rev. Genet, vol.15, pp.829-845, 2014.

D. M. Ribeiro, A. Zanzoni, A. Cipriano, R. Delli-ponti, L. Spinelli et al., Protein complex scaffolding predicted as a prevalent function of long non-coding RNAs, Nucleic Acids Res, vol.46, pp.917-928, 2018.
URL : https://hal.archives-ouvertes.fr/hal-01644177

J. Cioni, M. Koppers, and C. E. Holt, Molecular control of local translation in axon development and maintenance, Curr. Opin. Neurobiol, vol.51, pp.86-94, 2018.

A. A. Schmitz, E. E. Govek, B. Böttner, and L. Van-aelst, Rho GTPases: signaling, migration, and invasion, Exp. Cell Res, vol.261, pp.1-12, 2000.

R. S. Sankhala, R. K. Lokareddy, S. Begum, R. A. Pumroy, R. E. Gillilan et al., Three-dimensional context rather than NLS amino acid sequence determines importin ? subtype specificity for RCC1, Nat. Commun, vol.8, p.979, 2017.

A. Zanzoni, D. M. Ribeiro, and C. Brun, Understanding protein multifunctionality: from short linear motifs to cellular functions, Cell. Mol. Life Sci, vol.76, pp.4407-4412, 2019.
URL : https://hal.archives-ouvertes.fr/hal-02279538

A. Shiber, K. Döring, U. Friedrich, K. Klann, D. Merker et al., Cotranslational assembly of protein complexes in eukaryotes revealed by ribosome profiling, Nature, vol.561, pp.268-272, 2018.

C. Mayr, Protein complexes assemble as they are being made, Nature, vol.561, pp.186-187, 2018.

M. Frechin, L. Enkler, E. Tetaud, D. Laporte, B. Senger et al., Expression of nuclear and mitochondrial genes encoding ATP synthase is synchronized by disassembly of a multisynthetase complex, Mol. Cell, vol.56, pp.763-776, 2014.
URL : https://hal.archives-ouvertes.fr/hal-02370180