Table 4.

Identified interaction partners for agnoprotein.

PyV	Interaction partner	Functional implication	Interacting domain partner	Interacting domain agnoprotein	Reference
BKPyV	α-SNAP	Interference secretion	Not determined	N-terminus	(Johannessen et al., 2011)
	PCNA	Inhibition DNA synthesis			our unpublished results
	p50a	Unknown	Unknown	Unknown	(Rinaldo et al., 1998)
	p75	Unknown	Unknown	Unknown	(Rinaldo et al., 1998)
	p100	Unknown	Unknown	Unknown	(Rinaldo et al., 1998)
JCPyV	FEZ1	Facilitates viral release	Coiled-coil domain	Not determined	(Suzuki et al., 2005)
	HP1α	Nuclear egress virions	Not determined	N-terminus	(Okada et al., 2005)
	Ku70	Aberrant DNA repair	Not determined	N-terminus	(Darbinyan et al., 2004)
	Tumor suppressor p53	Dysregulation cell cycle	Not determined	N-terminus (aa 1–36)	(Darbinyan et al., 2002)
	p52a	Unknown	Unknown	Unknown	(Endo et al., 2003)
	p103	Unknown	Unknown	Unknown	(Endo et al., 2003)
	p112	Unknown	Unknown	Unknown	(Endo et al., 2003)
	p158	Unknown	Unknown	Unknown	(Endo et al., 2003)
	HIV-1 Tat	Inhibition HIV-1 gene expression	Residues 1–50	Residues 18–54	(Kaniowska et al., 2006)
	Tubulin	Unknown	Unknown	Unknown	(Endo et al., 2003, Suzuki et al., 2005)
	YB-1	Altered gene expression	C-terminal half	Residues 18–36	(Safak et al., 2002)
	LT-ag	Repression viral transcription and DNA replication	Central domain	N-terminus	(Safak et al., 2001)
	st-ag	Disrupt PP2A:st-ag interaction?	C-terminus	N-terminus	(Sariyer et al., 2008)
	PP2A	Dephosphorylation of agnoprotein	Not determined	Residues 18–36	(Sariyer et al., 2008)

^aJCPyV binds tubulin which has an estimated molecular mass of 54 kD. The p50 and p52 proteins known to interact with, respectively, BKPyV and JCPyV agnoprotein may therefore represent tubulin.