PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 31581522-10 2019 Inhibitors of selected signaling pathways suppressed the migration and differentiation of activated HSCs by regulating specific serine phosphorylated sites on vimentin. Serine 128-134 vimentin Homo sapiens 159-167 2503376-2 1989 The in vitro phosphorylation of vimentin, the intermediate filament protein of mesenchymal cells, by kinases A and C is serine-specific and involves only the N-terminal head domain. Serine 120-126 vimentin Homo sapiens 32-40 32389644-4 2020 After cell binding to fibronectin, there was a time-dependent increase of phosphorylation of serine 39, 56 and 72 in vimentin, which was associated with vimentin filament assembly. Serine 93-99 vimentin Homo sapiens 117-125 32389644-4 2020 After cell binding to fibronectin, there was a time-dependent increase of phosphorylation of serine 39, 56 and 72 in vimentin, which was associated with vimentin filament assembly. Serine 93-99 vimentin Homo sapiens 153-161 32389644-8 2020 Compared with wild type, FLNA KD cells showed loss of phosphorylation of serine 56 and 72 in vimentin and reduced numbers and lengths of cell extensions by >4-fold. Serine 73-79 vimentin Homo sapiens 93-101 30403907-5 2019 E-cadherin was not consistently affected but vimentin was induced by low serum-containing media and was increased by serine proteases in MCF-7 and MDA-MB-231 cells in parallel with increased wound closure. Serine 117-123 vimentin Homo sapiens 45-53 30925160-0 2019 Phosphorylation of a serine/proline-rich motif in oxysterol binding protein-related protein 4L (ORP4L) regulates cholesterol and vimentin binding. Serine 21-27 vimentin Homo sapiens 129-137 30925160-9 2019 We conclude that phosphorylation of a unique serine/proline motif in the ORD induces a conformation change in ORP4L that enhances interaction with vimentin and cholesterol extraction from membranes. Serine 45-51 vimentin Homo sapiens 147-155 32328567-3 2019 Contractile activation induces vimentin phosphorylation at Ser-56 and vimentin network reorientation, facilitating contractile force transmission among and within smooth muscle cells. Serine 59-62 vimentin Homo sapiens 31-39 32328567-4 2019 p21-activated kinase 1 and polo-like kinase 1 catalyze vimentin phosphorylation at Ser-56, whereas type 1 protein phosphatase dephosphorylates vimentin at this residue. Serine 83-86 vimentin Homo sapiens 55-63 30135525-11 2018 miR-509 exposure inhibited vimentin phosphorylation at Ser-56, vimentin network reorganization, focal adhesion formation, and cell migration. Serine 55-58 vimentin Homo sapiens 27-35 29724197-15 2018 An excess amount of Nup88 in cell lysates inhibited the dephosphorylation of a serine residue (Ser83) within the vimentin N-terminal region even in the absence and presence of an exogenous phosphatase. Serine 79-85 vimentin Homo sapiens 113-121 27603133-4 2016 Furthermore, p17 was found to occupy the Plk1-binding site within the vimentin, thereby blocking Plk1 recruitment to CDK1-induced vimentin phosphorylation at Ser 56. Serine 158-161 vimentin Homo sapiens 70-78 29021254-6 2017 Moreover, phospho-deficient OGT (S20A) cells attenuated cellular O-GlcNAcylation levels and also reduced phosphorylation of Ser-71 in the cytoskeletal protein vimentin, a modification critical for severing vimentin filament during cytokinesis. Serine 124-127 vimentin Homo sapiens 159-167 27603133-4 2016 Furthermore, p17 was found to occupy the Plk1-binding site within the vimentin, thereby blocking Plk1 recruitment to CDK1-induced vimentin phosphorylation at Ser 56. Serine 158-161 vimentin Homo sapiens 130-138 27603133-5 2016 Interaction of p17 to CDK1 or vimentin interferes with CDK1-catalyzed phosphorylation of vimentin at Ser 56 and subsequently vimentin phosphorylation at Ser 82 by Plk1. Serine 101-104 vimentin Homo sapiens 30-38 27603133-5 2016 Interaction of p17 to CDK1 or vimentin interferes with CDK1-catalyzed phosphorylation of vimentin at Ser 56 and subsequently vimentin phosphorylation at Ser 82 by Plk1. Serine 101-104 vimentin Homo sapiens 89-97 27603133-5 2016 Interaction of p17 to CDK1 or vimentin interferes with CDK1-catalyzed phosphorylation of vimentin at Ser 56 and subsequently vimentin phosphorylation at Ser 82 by Plk1. Serine 101-104 vimentin Homo sapiens 89-97 27603133-5 2016 Interaction of p17 to CDK1 or vimentin interferes with CDK1-catalyzed phosphorylation of vimentin at Ser 56 and subsequently vimentin phosphorylation at Ser 82 by Plk1. Serine 153-156 vimentin Homo sapiens 30-38 27603133-5 2016 Interaction of p17 to CDK1 or vimentin interferes with CDK1-catalyzed phosphorylation of vimentin at Ser 56 and subsequently vimentin phosphorylation at Ser 82 by Plk1. Serine 153-156 vimentin Homo sapiens 89-97 27603133-5 2016 Interaction of p17 to CDK1 or vimentin interferes with CDK1-catalyzed phosphorylation of vimentin at Ser 56 and subsequently vimentin phosphorylation at Ser 82 by Plk1. Serine 153-156 vimentin Homo sapiens 89-97 27603133-6 2016 Furthermore, we have identified upstream signaling pathways and cellular factor(s) targeted by p17 and found that p17 regulates inhibitory phosphorylation of CDK1 and blocks vimentin phosphorylation at Ser 56 and Ser 82. Serine 202-205 vimentin Homo sapiens 174-182 27603133-6 2016 Furthermore, we have identified upstream signaling pathways and cellular factor(s) targeted by p17 and found that p17 regulates inhibitory phosphorylation of CDK1 and blocks vimentin phosphorylation at Ser 56 and Ser 82. Serine 213-216 vimentin Homo sapiens 174-182 22795529-0 2013 Detection of vimentin serine phosphorylation by multicolor Quenchbodies. Serine 22-28 vimentin Homo sapiens 13-21 25855378-6 2015 Consistent with its role as an intermediate filament, vimentin acted as a scaffold to recruit Slug to ERK and promote Slug phosphorylation at serine-87. Serine 142-148 vimentin Homo sapiens 54-62 24073199-6 2013 Further analysis revealed that the vimentin in the virus factories was serine-82 phosphorylated. Serine 71-77 vimentin Homo sapiens 35-43 24073199-7 2013 More importantly, EV71 VP1 protein is responsible for the activation of calmodulin-dependent protein kinase II (CaMK-II) which phosphorylated the N-terminal domain of vimentin on serine 82. Serine 179-185 vimentin Homo sapiens 167-175 22795529-2 2013 Vimentin, the most abundant intermediate filament protein, is phosphorylated at its specific serine (Ser) residues in a cell cycle dependent manner. Serine 93-99 vimentin Homo sapiens 0-8 22795529-2 2013 Vimentin, the most abundant intermediate filament protein, is phosphorylated at its specific serine (Ser) residues in a cell cycle dependent manner. Serine 101-104 vimentin Homo sapiens 0-8 22846177-5 2012 The interaction with GlcNAc-bearing polymers promoted the cell surface recruitment of vimentin followed by the phosphorylation of vimentin serine 71 and the increase in tetrameric vimentin disassembled from vimentin filaments in HeLa cells. Serine 139-145 vimentin Homo sapiens 86-94 22846177-5 2012 The interaction with GlcNAc-bearing polymers promoted the cell surface recruitment of vimentin followed by the phosphorylation of vimentin serine 71 and the increase in tetrameric vimentin disassembled from vimentin filaments in HeLa cells. Serine 139-145 vimentin Homo sapiens 130-138 22846177-5 2012 The interaction with GlcNAc-bearing polymers promoted the cell surface recruitment of vimentin followed by the phosphorylation of vimentin serine 71 and the increase in tetrameric vimentin disassembled from vimentin filaments in HeLa cells. Serine 139-145 vimentin Homo sapiens 130-138 22846177-5 2012 The interaction with GlcNAc-bearing polymers promoted the cell surface recruitment of vimentin followed by the phosphorylation of vimentin serine 71 and the increase in tetrameric vimentin disassembled from vimentin filaments in HeLa cells. Serine 139-145 vimentin Homo sapiens 130-138 22345628-6 2012 In the present study, we observed that O-GlcNAc proteins from apoptotic cells interacted with the surface vimentin of neighboring phagocytes and that this interaction induced serine 71-phosphorylation and recruitment of vimentin to the cell surface of the neighboring phagocytes. Serine 175-181 vimentin Homo sapiens 106-114 22345628-7 2012 Moreover, tetrameric vimentin that was disassembled by serine 71-phosphorylation possessed a GlcNAc-binding activity and was localized to the cell surface. Serine 55-61 vimentin Homo sapiens 21-29 22720028-4 2012 This reorganization is dose dependent and is accompanied by a change in cell shape, decreased motility and an increase in vimentin phosphorylation at serine-38. Serine 150-156 vimentin Homo sapiens 122-130 19584300-5 2009 Although the interaction between vimentin and IDE is enhanced by vimentin phosphorylation at Ser-55, the interaction between nestin and IDE is phosphorylation independent. Serine 93-96 vimentin Homo sapiens 33-41 19812368-8 2009 Cdc42 activation, p21-activated kinase 1 (PAK1) phosphorylation at Thr-423 (an indication of PAK activation), and vimentin phosphorylation at Ser-56 in response to 5-HT activation were also attenuated in smooth muscle cells producing shRNA against p47(phox). Serine 142-145 vimentin Homo sapiens 114-122 19584300-5 2009 Although the interaction between vimentin and IDE is enhanced by vimentin phosphorylation at Ser-55, the interaction between nestin and IDE is phosphorylation independent. Serine 93-96 vimentin Homo sapiens 65-73 16997882-5 2007 ACh activation also induced vimentin phosphorylation at Ser(56) as assessed by immunoblot analysis. Serine 56-59 vimentin Homo sapiens 28-36 19291697-5 2009 Specific analysis of the phosphorylation state of vimentin in macrophages showed that this protein becomes rapidly phosphorylated in both tyrosine and serine residues upon chemokine stimulation. Serine 151-157 vimentin Homo sapiens 50-58 19291697-8 2009 While WT macrophages infected with a vimentin mutant resistant to N-terminal serine phosphorylation showed a reduction in transendothelial migration, infection of PI3Kgamma-null macrophages with a vimentin mutant mimicking serine phosphorylation of N-terminal residues rescued the transendothelial migration defect. Serine 77-83 vimentin Homo sapiens 37-45 17507370-8 2007 By combining a new O-GlcNAc peptide enrichment method and beta-elimination followed by Michael addition with DTT, we also mapped the O-GlcNAc site (Ser-55) of vimentin, which showed an apparent increase of O-GlcNAcylation upon GSK-3 inhibition. Serine 148-151 vimentin Homo sapiens 159-167 16997882-10 2007 These results suggest that PAK may regulate CAS release from the vimentin intermediate filaments by mediating vimentin phosphorylation at Ser(56) and the transition of cytoskeletal vimentin to soluble vimentin. Serine 138-141 vimentin Homo sapiens 110-118 16997882-10 2007 These results suggest that PAK may regulate CAS release from the vimentin intermediate filaments by mediating vimentin phosphorylation at Ser(56) and the transition of cytoskeletal vimentin to soluble vimentin. Serine 138-141 vimentin Homo sapiens 110-118 16997882-10 2007 These results suggest that PAK may regulate CAS release from the vimentin intermediate filaments by mediating vimentin phosphorylation at Ser(56) and the transition of cytoskeletal vimentin to soluble vimentin. Serine 138-141 vimentin Homo sapiens 110-118 16990256-0 2006 Critical role of vimentin phosphorylation at Ser-56 by p21-activated kinase in vimentin cytoskeleton signaling. Serine 45-48 vimentin Homo sapiens 17-25 16140754-6 2005 Interestingly, viral DNA replication also resulted in the activation of calcium calmodulin-dependent protein kinase II (CaM kinase II) and phosphorylation of the N-terminal domain of vimentin on serine 82. Serine 195-201 vimentin Homo sapiens 183-191 16990256-0 2006 Critical role of vimentin phosphorylation at Ser-56 by p21-activated kinase in vimentin cytoskeleton signaling. Serine 45-48 vimentin Homo sapiens 79-87 16990256-5 2006 Expression of mutant S56A vimentin in cells inhibited the increase in phosphorylation at Ser-56 and in the ratios of soluble to insoluble vimentin (an index of vimentin disassembly) and the dissociation of CAS from cytoskeletal vimentin in response to 5-HT activation compared with cells expressing wild-type vimentin. Serine 89-92 vimentin Homo sapiens 26-34 16990256-9 2006 Our results suggest that vimentin phosphorylation at Ser-56 may inversely regulate PAK activation possibly via the increase in the amount of soluble CAS upon agonist stimulation of smooth muscle cells. Serine 53-56 vimentin Homo sapiens 25-33 16140754-7 2005 Immunostaining showed that vimentin within the cage was phosphorylated on serine 82. Serine 74-80 vimentin Homo sapiens 27-35 16140754-9 2005 Phosphorylation of vimentin on serine 82 may be necessary for cage formation or may simply be a consequence of activation of CaM kinase II by ASFV. Serine 31-37 vimentin Homo sapiens 19-27 15140879-7 2004 Furthermore, overexpression of PPM1F in fibroblasts caused a reduction in the CaMKII-specific phosphorylation of the known substrate vimentin(Ser-82) following induction of the endogenous CaM kinase. Serine 142-145 vimentin Homo sapiens 133-141 15766329-0 2005 Silencing of p21-activated kinase attenuates vimentin phosphorylation on Ser-56 and reorientation of the vimentin network during stimulation of smooth muscle cells by 5-hydroxytryptamine. Serine 73-76 vimentin Homo sapiens 45-53 15766329-4 2005 Stimulation of smooth muscle cells with 5-HT also induced phosphorylation of vimentin on Ser-56. Serine 89-92 vimentin Homo sapiens 77-85 15713670-7 2005 EGCG inhibited phosphorylation of vimentin at serines 50 and 55 and phosphorylation of vimentin by cyclin-dependent kinase 2 and cAMP-dependent protein kinase. Serine 46-53 vimentin Homo sapiens 34-42 10574968-4 1999 We also found that an antibody, which specifically recognizes vimentin phosphorylated at Ser-71 by Rho kinase, became immunoreactive after calyculin A treatment. Serine 89-92 vimentin Homo sapiens 62-70 12686602-4 2003 This nestin-mediated disassembly of IFs is dependent on the phosphorylation of vimentin by the maturation/M-phase-promoting factor at ser-55 in the amino-terminal head domain. Serine 134-137 vimentin Homo sapiens 79-87 12458200-2 2003 We previously demonstrated the possible existence of a protein kinase that phosphorylates at least Ser-72 on vimentin, the most widely expressed intermediate filament protein, in the cleavage furrow-specific manner. Serine 99-102 vimentin Homo sapiens 109-117 12458200-3 2003 Here we showed that vimentin-Ser-72 phosphorylation occurred specifically at the border of the Aurora-B-localized area from anaphase to telophase. Serine 29-32 vimentin Homo sapiens 20-28 12458200-4 2003 Expression of a dominant-negative mutant of Aurora-B led to a reduction of this vimentin-Ser-72 phosphorylation. Serine 89-92 vimentin Homo sapiens 80-88 12458200-6 2003 We further identified eight Aurora-B phosphorylation sites, including Ser-72 on vimentin, and then constructed the mutant vimentin in which these identified sites are changed into Ala. Serine 70-73 vimentin Homo sapiens 80-88 14762106-5 2004 Characterization of the (32)P-labeled vimentin phosphopeptides, demonstrated Ser-4, Ser-6, Ser-7, Ser-8, Ser-9, Ser-38, Ser-41, Ser-71, Ser-72, Ser-418, Ser-429, Thr-456, and Ser-457 as significant in vivo phosphorylation sites. Serine 77-80 vimentin Homo sapiens 38-46 14762106-5 2004 Characterization of the (32)P-labeled vimentin phosphopeptides, demonstrated Ser-4, Ser-6, Ser-7, Ser-8, Ser-9, Ser-38, Ser-41, Ser-71, Ser-72, Ser-418, Ser-429, Thr-456, and Ser-457 as significant in vivo phosphorylation sites. Serine 84-87 vimentin Homo sapiens 38-46 14762106-5 2004 Characterization of the (32)P-labeled vimentin phosphopeptides, demonstrated Ser-4, Ser-6, Ser-7, Ser-8, Ser-9, Ser-38, Ser-41, Ser-71, Ser-72, Ser-418, Ser-429, Thr-456, and Ser-457 as significant in vivo phosphorylation sites. Serine 84-87 vimentin Homo sapiens 38-46 14762106-5 2004 Characterization of the (32)P-labeled vimentin phosphopeptides, demonstrated Ser-4, Ser-6, Ser-7, Ser-8, Ser-9, Ser-38, Ser-41, Ser-71, Ser-72, Ser-418, Ser-429, Thr-456, and Ser-457 as significant in vivo phosphorylation sites. Serine 84-87 vimentin Homo sapiens 38-46 14762106-5 2004 Characterization of the (32)P-labeled vimentin phosphopeptides, demonstrated Ser-4, Ser-6, Ser-7, Ser-8, Ser-9, Ser-38, Ser-41, Ser-71, Ser-72, Ser-418, Ser-429, Thr-456, and Ser-457 as significant in vivo phosphorylation sites. Serine 84-87 vimentin Homo sapiens 38-46 14762106-5 2004 Characterization of the (32)P-labeled vimentin phosphopeptides, demonstrated Ser-4, Ser-6, Ser-7, Ser-8, Ser-9, Ser-38, Ser-41, Ser-71, Ser-72, Ser-418, Ser-429, Thr-456, and Ser-457 as significant in vivo phosphorylation sites. Serine 84-87 vimentin Homo sapiens 38-46 14762106-5 2004 Characterization of the (32)P-labeled vimentin phosphopeptides, demonstrated Ser-4, Ser-6, Ser-7, Ser-8, Ser-9, Ser-38, Ser-41, Ser-71, Ser-72, Ser-418, Ser-429, Thr-456, and Ser-457 as significant in vivo phosphorylation sites. Serine 84-87 vimentin Homo sapiens 38-46 14762106-5 2004 Characterization of the (32)P-labeled vimentin phosphopeptides, demonstrated Ser-4, Ser-6, Ser-7, Ser-8, Ser-9, Ser-38, Ser-41, Ser-71, Ser-72, Ser-418, Ser-429, Thr-456, and Ser-457 as significant in vivo phosphorylation sites. Serine 84-87 vimentin Homo sapiens 38-46 14762106-5 2004 Characterization of the (32)P-labeled vimentin phosphopeptides, demonstrated Ser-4, Ser-6, Ser-7, Ser-8, Ser-9, Ser-38, Ser-41, Ser-71, Ser-72, Ser-418, Ser-429, Thr-456, and Ser-457 as significant in vivo phosphorylation sites. Serine 84-87 vimentin Homo sapiens 38-46 14762106-5 2004 Characterization of the (32)P-labeled vimentin phosphopeptides, demonstrated Ser-4, Ser-6, Ser-7, Ser-8, Ser-9, Ser-38, Ser-41, Ser-71, Ser-72, Ser-418, Ser-429, Thr-456, and Ser-457 as significant in vivo phosphorylation sites. Serine 84-87 vimentin Homo sapiens 38-46 14762106-5 2004 Characterization of the (32)P-labeled vimentin phosphopeptides, demonstrated Ser-4, Ser-6, Ser-7, Ser-8, Ser-9, Ser-38, Ser-41, Ser-71, Ser-72, Ser-418, Ser-429, Thr-456, and Ser-457 as significant in vivo phosphorylation sites. Serine 84-87 vimentin Homo sapiens 38-46 14762106-5 2004 Characterization of the (32)P-labeled vimentin phosphopeptides, demonstrated Ser-4, Ser-6, Ser-7, Ser-8, Ser-9, Ser-38, Ser-41, Ser-71, Ser-72, Ser-418, Ser-429, Thr-456, and Ser-457 as significant in vivo phosphorylation sites. Serine 84-87 vimentin Homo sapiens 38-46 12761892-7 2003 We show that MAPKAP kinase-2 mainly phosphorylates vimentin at Ser-38, Ser-50, Ser-55, and Ser-82, residues all located in the head domain of the protein. Serine 63-66 vimentin Homo sapiens 51-59 12761892-7 2003 We show that MAPKAP kinase-2 mainly phosphorylates vimentin at Ser-38, Ser-50, Ser-55, and Ser-82, residues all located in the head domain of the protein. Serine 71-74 vimentin Homo sapiens 51-59 12761892-7 2003 We show that MAPKAP kinase-2 mainly phosphorylates vimentin at Ser-38, Ser-50, Ser-55, and Ser-82, residues all located in the head domain of the protein. Serine 71-74 vimentin Homo sapiens 51-59 12761892-7 2003 We show that MAPKAP kinase-2 mainly phosphorylates vimentin at Ser-38, Ser-50, Ser-55, and Ser-82, residues all located in the head domain of the protein. Serine 71-74 vimentin Homo sapiens 51-59 12761892-10 2003 Finally, a mutational analysis of each of the phosphorylated serine residues in vimentin suggested that no single serine site was primarily responsible for structure maintenance, implying that the retention of filamentous structure may be the result of the coordinated action of several phosphorylated serine sites. Serine 61-67 vimentin Homo sapiens 80-88 12761892-10 2003 Finally, a mutational analysis of each of the phosphorylated serine residues in vimentin suggested that no single serine site was primarily responsible for structure maintenance, implying that the retention of filamentous structure may be the result of the coordinated action of several phosphorylated serine sites. Serine 114-120 vimentin Homo sapiens 80-88 12761892-10 2003 Finally, a mutational analysis of each of the phosphorylated serine residues in vimentin suggested that no single serine site was primarily responsible for structure maintenance, implying that the retention of filamentous structure may be the result of the coordinated action of several phosphorylated serine sites. Serine 114-120 vimentin Homo sapiens 80-88 12483219-4 2003 We show that secretion of vimentin, which is phosphorylated at serine and threonine residues, is enhanced by the phosphatase inhibitor okadaic acid and blocked by the specific protein kinase C inhibitor GO6983. Serine 63-69 vimentin Homo sapiens 26-34 10574968-5 1999 This calyculin A-induced interphase phosphorylation of vimentin at Ser-71 was blocked by Rho kinase inhibitor or by expression of the dominant-negative Rho kinase. Serine 67-70 vimentin Homo sapiens 55-63 9794428-7 1998 Western blot analysis using an anti-phospho-serine mAb (MO82) reveals that Ser82 in the vimentin is phosphorylated specifically by Ca2+/calmodulin-dependent kinase II through sVCAM-1 activation in the IL-2 dependent T cells. Serine 44-50 vimentin Homo sapiens 88-96 7832980-2 1994 Tryptic phosphopeptide mapping by high-performance liquid chromatography followed by sequential manual Edman degradation and direct peptide sequence analysis revealed that Ser-25, Ser-38, Ser-65, and Ser-71 in the amino-terminal domain and Ser-411 in the carboxyl-terminal domain are the phosphorylation sites in vimentin phosphorylated by this kinase, indicating that autophosphorylation-dependent protein kinase is a potent and unique vimentin kinase. Serine 172-175 vimentin Homo sapiens 313-321 7832980-2 1994 Tryptic phosphopeptide mapping by high-performance liquid chromatography followed by sequential manual Edman degradation and direct peptide sequence analysis revealed that Ser-25, Ser-38, Ser-65, and Ser-71 in the amino-terminal domain and Ser-411 in the carboxyl-terminal domain are the phosphorylation sites in vimentin phosphorylated by this kinase, indicating that autophosphorylation-dependent protein kinase is a potent and unique vimentin kinase. Serine 172-175 vimentin Homo sapiens 437-445 34087674-5 2021 In detail, the serine residue of vimentin was phosphorylated at position 38 (Ser38) by calcium calmodulin-dependent protein kinase II gamma (CaMKIIgamma), and vimentin filaments reorganized into cage-like structures enwrapping PRRSV replication complex (RC) at the perinuclear location. Serine 15-21 vimentin Homo sapiens 33-41 8373419-1 1993 Synthetic peptide representing the site Ser-41 in vimentin, Leu-Gly-Ser41-Ala42-Leu-Arg44-Arg-Arg-NH2, and its analogs in which Ala-42 was replaced by various amino acids were tested as substrates for cdc2 kinase. Serine 40-43 vimentin Homo sapiens 50-58 1727439-4 1992 In addition, it was determined that the intermediate filament protein kinase activity phosphorylated both serine and threonine residues of the intermediate filament proteins, vimentin and GFAP. Serine 106-112 vimentin Homo sapiens 175-183 1850997-0 1991 Evidence that Ser-82 is a unique phosphorylation site on vimentin for Ca2(+)-calmodulin-dependent protein kinase II. Serine 14-17 vimentin Homo sapiens 57-65 1850997-2 1991 Sequential analysis of the purified phosphopeptides demonstrated that the sites are -Thr-Arg-Thr-Tyr-Ser(PO4)38-Leu-Gly-Ser-Ala- and -Val-Arg-Leu-Leu-Gln-Asp-Ser(PO4)82-Val-Asp-, which are located within the amino-terminal head domain of vimentin. Serine 101-104 vimentin Homo sapiens 238-246 1850997-2 1991 Sequential analysis of the purified phosphopeptides demonstrated that the sites are -Thr-Arg-Thr-Tyr-Ser(PO4)38-Leu-Gly-Ser-Ala- and -Val-Arg-Leu-Leu-Gln-Asp-Ser(PO4)82-Val-Asp-, which are located within the amino-terminal head domain of vimentin. Serine 120-123 vimentin Homo sapiens 238-246 1850997-2 1991 Sequential analysis of the purified phosphopeptides demonstrated that the sites are -Thr-Arg-Thr-Tyr-Ser(PO4)38-Leu-Gly-Ser-Ala- and -Val-Arg-Leu-Leu-Gln-Asp-Ser(PO4)82-Val-Asp-, which are located within the amino-terminal head domain of vimentin. Serine 120-123 vimentin Homo sapiens 238-246 2013762-5 1991 The phosphorylation of vimentin and GFAP resulting from PMA or 8-BR treatment was restricted to serine residues in the N-terminal domain of these proteins. Serine 96-102 vimentin Homo sapiens 23-31 34066419-4 2021 We discovered that RAB7A regulates AKT and PAK1, and we demonstrated that increased vimentin phosphorylation at Ser38 (Serine 38), observed upon RAB7A overexpression, is due to AKT activity. Serine 119-125 vimentin Homo sapiens 84-92