PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 23757730-7 2013 Serine 11 of AnxA2 was identified as the target residue of this phosphorylation switch because a phosphomimicking mutation at this site prevents complex formation with S100A10 and, in contrast to wild-type or S11A-AnxA2, is unable to restore cAMP-dependent VWF secretion in AnxA2-depleted cells. Serine 0-6 annexin A2 Homo sapiens 13-18 12962548-0 2003 Nuclear annexin II negatively regulates growth of LNCaP cells and substitution of ser 11 and 25 to glu prevents nucleo-cytoplasmic shuttling of annexin II. Serine 82-85 annexin A2 Homo sapiens 144-154 12962548-12 2003 By site-specific substitution of glutamic acid in the place of serines 11 and 25 in the N-terminus, we show that simultaneous phosphorylation of both serines 11 and 25, but not either one alone, prevents nuclear localization of annexin II. Serine 150-157 annexin A2 Homo sapiens 228-238 12962548-13 2003 CONCLUSION: Our data show that nuclear annexin II is phosphorylated in a cell cycle-dependent manner and that substitution of serines 11 and 25 inhibit nuclear entry of annexin II. Serine 126-133 annexin A2 Homo sapiens 39-49 12962548-13 2003 CONCLUSION: Our data show that nuclear annexin II is phosphorylated in a cell cycle-dependent manner and that substitution of serines 11 and 25 inhibit nuclear entry of annexin II. Serine 126-133 annexin A2 Homo sapiens 169-179 8898866-3 1996 The annexin II-p11 interaction is mediated through the unique N-terminal domain of annexin II and is inhibited by protein kinase C phosphorylation of a serine residue in annexin II. Serine 152-158 annexin A2 Homo sapiens 4-14 8898866-4 1996 To map this regulatory serine phosphorylation site we developed a baculovirus-mediated expression system for wild-type annexin II and for a series of annexin II mutants which contained substitutions in one or more serine residues present in the N-terminal domain. Serine 23-29 annexin A2 Homo sapiens 119-129 8898866-4 1996 To map this regulatory serine phosphorylation site we developed a baculovirus-mediated expression system for wild-type annexin II and for a series of annexin II mutants which contained substitutions in one or more serine residues present in the N-terminal domain. Serine 23-29 annexin A2 Homo sapiens 150-160 8898866-6 1996 However, significant differences in phosphate incorporation were observed when the individual serine mutants were subjected to phosphorylation by protein kinase C. A comparison of the phosphorylation patterns obtained identified Ser-II as the protein kinase C site responsible for regulating the annexin II-p11 interaction. Serine 94-100 annexin A2 Homo sapiens 296-306 8898866-7 1996 Ser-II lies within the sequence mediating p11 binding, i.e. amino-acid residues 1 to 14 of annexin II, and phosphorylation at this site most likely leads to a direct spatial interference with p11 binding. Serine 0-3 annexin A2 Homo sapiens 91-101 2951248-0 1986 Functionally distinct serine phosphorylation sites of p36, the cellular substrate of retroviral protein kinase; differential inhibition of reassociation with p11. Serine 22-28 annexin A2 Homo sapiens 54-57 2951248-7 1986 Phosphorylation of p36 is serine specific. Serine 26-32 annexin A2 Homo sapiens 19-22 28867585-6 2017 Thus, Ser phosphorylation of AnxA2 is involved in the recruitment and docking of secretory granules, the regulation of its association with S100A10, and sequestration of perinuclear, translationally inactive mRNP complexes. Serine 6-9 annexin A2 Homo sapiens 29-34 2463166-8 1988 In contrast, protein kinase C (PKC)-dependent serine and tyrosine phosphorylations were stimulated maximally by low level occupancy of PDGF binding sites, and phosphorylation of p36 required high occupancy. Serine 46-52 annexin A2 Homo sapiens 178-181 2948507-2 1986 While Lipocortin-I is phosphorylated on threonine residues, Lipocortin-II and Lipocortin-85 are phosphorylated on serine residues. Serine 114-120 annexin A2 Homo sapiens 60-73 2948507-3 1986 The substoichiometric phosphorylation of Lipocortin-85 appears to preclude the potential regulation of this protein by protein kinase C. The phosphorylation of Lipocortin-I on threonine residues and Lipocortin-II on serine residues suggests these proteins may be regulated by distinct phosphorylation-dephosphorylation reactions. Serine 216-222 annexin A2 Homo sapiens 199-212 2946941-2 1986 These have been used to examine the sites and extent of serine and tyrosine phosphorylation of p36 in human cells treated with epidermal growth factor and platelet-derived growth factor and in human cells transformed with viruses whose oncogenes encode protein-tyrosine kinases. Serine 56-62 annexin A2 Homo sapiens 95-98 30959964-7 2019 We demonstrate that ANXA2 via its reactive Cys-8 residue, binds to PTEN and that the co-expression of PTEN and ANXA2, but not ANXA2 Cys-8-Ala mutant, inhibits AKT phosphorylation on Ser 473. Serine 182-185 annexin A2 Homo sapiens 20-25 30959964-7 2019 We demonstrate that ANXA2 via its reactive Cys-8 residue, binds to PTEN and that the co-expression of PTEN and ANXA2, but not ANXA2 Cys-8-Ala mutant, inhibits AKT phosphorylation on Ser 473. Serine 182-185 annexin A2 Homo sapiens 111-116 30959964-7 2019 We demonstrate that ANXA2 via its reactive Cys-8 residue, binds to PTEN and that the co-expression of PTEN and ANXA2, but not ANXA2 Cys-8-Ala mutant, inhibits AKT phosphorylation on Ser 473. Serine 182-185 annexin A2 Homo sapiens 111-116 30771901-5 2019 Upon ET-1 stimulation, serine phosphorylation of annexin A2 increased, while there is no change in tyrosine phosphorylation of annexin A2. Serine 23-29 annexin A2 Homo sapiens 49-59 23757730-7 2013 Serine 11 of AnxA2 was identified as the target residue of this phosphorylation switch because a phosphomimicking mutation at this site prevents complex formation with S100A10 and, in contrast to wild-type or S11A-AnxA2, is unable to restore cAMP-dependent VWF secretion in AnxA2-depleted cells. Serine 0-6 annexin A2 Homo sapiens 214-219 23757730-7 2013 Serine 11 of AnxA2 was identified as the target residue of this phosphorylation switch because a phosphomimicking mutation at this site prevents complex formation with S100A10 and, in contrast to wild-type or S11A-AnxA2, is unable to restore cAMP-dependent VWF secretion in AnxA2-depleted cells. Serine 0-6 annexin A2 Homo sapiens 214-219 18412141-1 2008 We have previously elucidated that Epstein-Barr-virus-encoded latent membrane protein 1 (LMP1) can increase the serine phosphorylation level of annexin A2 by activating the protein kinase C (PKC) signaling pathway and that LMP1 induces the nuclear entry of annexin A2 in an energy- and temperature-dependent manner. Serine 112-118 annexin A2 Homo sapiens 144-154 18412141-5 2008 By site-specific substitution of glutamic acid in the place of serine 11 and 25 in the N-terminus, we show that serine 25 phosphorylation of annexin A2 was associated with the nuclear entry of annexin A2, DNA synthesis and cell proliferation, whereas serine 11 has no obvious influence. Serine 112-118 annexin A2 Homo sapiens 141-151 18412141-5 2008 By site-specific substitution of glutamic acid in the place of serine 11 and 25 in the N-terminus, we show that serine 25 phosphorylation of annexin A2 was associated with the nuclear entry of annexin A2, DNA synthesis and cell proliferation, whereas serine 11 has no obvious influence. Serine 112-118 annexin A2 Homo sapiens 193-203 18412141-5 2008 By site-specific substitution of glutamic acid in the place of serine 11 and 25 in the N-terminus, we show that serine 25 phosphorylation of annexin A2 was associated with the nuclear entry of annexin A2, DNA synthesis and cell proliferation, whereas serine 11 has no obvious influence. Serine 112-118 annexin A2 Homo sapiens 141-151 18412141-5 2008 By site-specific substitution of glutamic acid in the place of serine 11 and 25 in the N-terminus, we show that serine 25 phosphorylation of annexin A2 was associated with the nuclear entry of annexin A2, DNA synthesis and cell proliferation, whereas serine 11 has no obvious influence. Serine 112-118 annexin A2 Homo sapiens 193-203 18412141-8 2008 Serine 25 phosphorylation of annexin A2 is shown to be associated with its nuclear entry, DNA synthesis, and cell proliferation. Serine 0-6 annexin A2 Homo sapiens 29-39 18412141-2 2008 Here, we further confirm that LMP1 increases the serine phosphorylation level of annexin A2 by activating the phosphoinositide-specific phospholipase C (PI-PLC)-PKC alpha/PKC beta pathway, mainly through the activation of the PKCbeta pathway. Serine 49-55 annexin A2 Homo sapiens 81-91 18412141-5 2008 By site-specific substitution of glutamic acid in the place of serine 11 and 25 in the N-terminus, we show that serine 25 phosphorylation of annexin A2 was associated with the nuclear entry of annexin A2, DNA synthesis and cell proliferation, whereas serine 11 has no obvious influence. Serine 63-69 annexin A2 Homo sapiens 141-151 18065419-3 2008 In vitro activity assays and membrane binding measurements by surface plasmon resonance analysis showed that a heterotetramer (A2t) of p11 and annexin A2, but not p11 or annexin A2 alone, directly binds cPLA(2)alpha via Ser(727), which keeps the enzyme from binding the membrane and catalyzing the phospholipid hydrolysis. Serine 220-223 annexin A2 Homo sapiens 143-153 16989986-5 2007 Treatment of LMP1-expressing cells with the PKC inhibitor myr-psiPKC resulted in annexin A2 being present almost exclusively at cell surface, instead of within the nucleus, suggesting that the nuclear entry of annexin A2 was associated with serine phosphorylation mediated by PKC. Serine 241-247 annexin A2 Homo sapiens 210-220