PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10932246-2 2000 To address the energetic and structural basis for WW domain recognition of phosphoserine (P.Ser)/phosphothreonine (P. Thr)- proline containing proteins, we report the energetic and structural analysis of a Pin1-phosphopeptide complex. Proline 124-131 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 206-210 11090625-2 2000 The pSer/Thr-Pro moiety in peptides exists in the two completely distinct cis and trans conformations whose conversion is catalyzed specifically by the essential prolyl isomerase Pin1. Proline 13-16 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 179-183 10932246-3 2000 The X-ray crystal structure of Pin1 bound to a doubly phosphorylated peptide (Tyr-P.Ser-Pro-Thr-P.Ser-Pro-Ser) representing a heptad repeat of the RNA polymerase II large subunit"s C-terminal domain (CTD), reveals the residues involved in the recognition of a single P.Ser side chain, the rings of two prolines, and the backbone of the CTD peptide. Proline 88-91 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 31-35 10932246-3 2000 The X-ray crystal structure of Pin1 bound to a doubly phosphorylated peptide (Tyr-P.Ser-Pro-Thr-P.Ser-Pro-Ser) representing a heptad repeat of the RNA polymerase II large subunit"s C-terminal domain (CTD), reveals the residues involved in the recognition of a single P.Ser side chain, the rings of two prolines, and the backbone of the CTD peptide. Proline 302-310 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 31-35 33807199-1 2021 Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) specifically binds and isomerizes the phosphorylated serine/threonine-proline (pSer/Thr-Pro) motif, which leads to changes in protein conformation and function. Proline 132-139 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-54 10939594-0 2000 Phosphorylation-dependent proline isomerization catalyzed by Pin1 is essential for tumor cell survival and entry into mitosis. Proline 26-33 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 61-65 10939594-3 2000 Pin1 recognizes phosphorylated serine-proline or threonine-proline peptide-bonds in test substrates up to 1300-fold better than in the respective unphosphorylated peptides. Proline 38-45 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 10939594-3 2000 Pin1 recognizes phosphorylated serine-proline or threonine-proline peptide-bonds in test substrates up to 1300-fold better than in the respective unphosphorylated peptides. Proline 59-66 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 11212339-8 1999 In contrast to other prolyl isomerases (peptidyl-prolyl isomerases, PPlases), Pin1 has an extremely high degree of substrate specificity, specifically isomerizing phosphorylated Ser/Thr-Pro bonds. Proline 186-189 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 78-82 11212339-12 1999 Thus, we have proposed a novel signaling regulatory mechanism, where protein phosphorylation creates binding sites for Pin1, which can then latch on to and isomerize the phosphorylated Ser/Thr-Pro peptide bond. Proline 193-196 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 119-123 9200606-4 1997 Pin1 displays a preference for an acidic residue N-terminal to the isomerized proline bond due to interaction of this acidic side chain with a basic cluster. Proline 78-85 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 10740817-3 2000 Pin1 is a phosphorylation-dependent prolyl isomerase that specifically isomerizes the phosphorylated serine/threonine-proline bond. Proline 118-125 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 9395400-3 1997 Pin1 is here shown to be a phosphorylation-dependent PPIase that specifically recognizes the phosphoserine-proline or phosphothreonine-proline bonds present in mitotic phosphoproteins. Proline 107-114 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 9395400-3 1997 Pin1 is here shown to be a phosphorylation-dependent PPIase that specifically recognizes the phosphoserine-proline or phosphothreonine-proline bonds present in mitotic phosphoproteins. Proline 135-142 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 9395400-4 1997 Both Pin1 and MPM-2 selected similar phosphorylated serine-proline-containing peptides, providing the basis for the specific interaction between Pin1 and MPM-2 antigens. Proline 59-66 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 5-9 9395400-4 1997 Both Pin1 and MPM-2 selected similar phosphorylated serine-proline-containing peptides, providing the basis for the specific interaction between Pin1 and MPM-2 antigens. Proline 59-66 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 145-149 9395400-5 1997 Pin1 preferentially isomerized proline residues preceded by phosphorylated serine or threonine with up to 1300-fold selectivity compared with unphosphorylated peptides. Proline 31-38 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 9395400-6 1997 Pin1 may thus regulate mitotic progression by catalyzing sequence-specific and phosphorylation-dependent proline isomerization. Proline 105-112 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 33807199-1 2021 Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) specifically binds and isomerizes the phosphorylated serine/threonine-proline (pSer/Thr-Pro) motif, which leads to changes in protein conformation and function. Proline 132-139 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 56-60 33917542-8 2021 It prefers the cis configuration of the serine-proline motif within its substrate and regulates Pin1, different from other phosphatases. Proline 47-54 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 96-100 34175703-2 2021 Excessive exposure to cobalt or inactivation of the unique proline isomerase Pin1 contributes to age-dependent neurodegeneration. Proline 59-66 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 77-81 22670809-8 2012 We determined the structures of Pin1 bound with two substrate isosteres that mimic peptides containing pSer/Thr-Pro motifs in cis or trans conformations. Proline 112-115 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 32-36 22670809-10 2012 Building on this result, we identified a specific case in which Pin1 differentially affects the rate of dephosphorylation catalyzed by two phosphatases (Scp1 and Ssu72) that target the same serine residue in the CTD heptad repeat but have different preferences for the isomerization state of the adjacent proline residue. Proline 305-312 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 64-68 34499020-5 2021 Pin1 is an attractive target for cancer therapy due to its over-expression and/or activation in various types of cancer and the disorder of Proline directed phosphorylation. Proline 140-147 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 34388391-2 2021 Unique proline isomerase Pin1 regulates multiple cancer pathways, but its role in the TME and cancer immunotherapy is unknown. Proline 7-14 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 25-29 35357776-1 2022 Pin1 catalyzes the cis-trans isomerization of pThr-Pro or pSer-Pro amide bonds of different proteins involved in several physio/pathological processes. Proline 51-54 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 33083964-1 2021 The peptidyl-prolyl isomerase Pin1 is a unique enzyme catalyzing the isomerization of the peptide bond between phosphorylated serine-proline or threonine-proline motifs in proteins, thereby regulating a wide spectrum of protein functions, including folding, intracellular signaling, transcription, cell cycle progression, and apoptosis. Proline 133-140 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 30-34 33083964-1 2021 The peptidyl-prolyl isomerase Pin1 is a unique enzyme catalyzing the isomerization of the peptide bond between phosphorylated serine-proline or threonine-proline motifs in proteins, thereby regulating a wide spectrum of protein functions, including folding, intracellular signaling, transcription, cell cycle progression, and apoptosis. Proline 154-161 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 30-34 33537091-1 2021 Pin1 belongs to the peptidyl-prolyl cis-trans isomerases (PPIases) superfamily and catalyzes the cis-trans conversion of proline in target substrates to modulate diverse cellular functions including cell cycle progression, cell motility, and apoptosis. Proline 121-128 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 33463409-1 2021 The parvulin PIN1 (peptidyl-prolyl cis-trans isomerase NIMA-interacting 1), is the only enzyme capable of isomerizing prolines of phospho-Serine/Threonine-Proline motifs. Proline 118-126 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 13-17 33463409-1 2021 The parvulin PIN1 (peptidyl-prolyl cis-trans isomerase NIMA-interacting 1), is the only enzyme capable of isomerizing prolines of phospho-Serine/Threonine-Proline motifs. Proline 118-126 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 19-73 33463409-1 2021 The parvulin PIN1 (peptidyl-prolyl cis-trans isomerase NIMA-interacting 1), is the only enzyme capable of isomerizing prolines of phospho-Serine/Threonine-Proline motifs. Proline 155-162 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 13-17 33463409-1 2021 The parvulin PIN1 (peptidyl-prolyl cis-trans isomerase NIMA-interacting 1), is the only enzyme capable of isomerizing prolines of phospho-Serine/Threonine-Proline motifs. Proline 155-162 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 19-73 32703934-2 2020 PIN1, belonging to peptidyl-prolyl cis-trans isomerase family, uniquely catalyzes the structural transformation of phosphorylated Ser/Thr-Pro motif. Proline 138-141 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 33409256-4 2020 Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1, Pin1 changes the conformation of a subset of proteins phosphorylated on Ser/Thr that precedes proline (Pro). Proline 150-157 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-54 33409256-4 2020 Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1, Pin1 changes the conformation of a subset of proteins phosphorylated on Ser/Thr that precedes proline (Pro). Proline 150-157 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 56-60 33409256-4 2020 Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1, Pin1 changes the conformation of a subset of proteins phosphorylated on Ser/Thr that precedes proline (Pro). Proline 159-162 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-54 33409256-4 2020 Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1, Pin1 changes the conformation of a subset of proteins phosphorylated on Ser/Thr that precedes proline (Pro). Proline 159-162 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 56-60 32428517-4 2020 Pin1 is able to recognize phosphorylated serine/threonine-proline motifs and regulates the structural conformation, stability and function of its substrates. Proline 58-65 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 32621833-2 2020 Peptidyl-prolyl isomerase (Pin1) is a unique peptidyl-prolyl cis/trans isomerase that interacts with phosphorylated serine or threonine of a target protein and isomerizes the adjacent proline residue. Proline 184-191 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 27-31 32296699-1 2020 Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) is an evolutionally conserved and unique enzyme that specifically catalyzes the cis-trans isomerization of phosphorylated serine/threonine-proline (pSer/Thr-Pro) motif and, subsequently, induces the conformational change of its substrates. Proline 201-208 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-54 32500074-3 2020 The peptidyl-prolyl cis/trans isomerase Pin1 binds to phosphorylated serine or threonine residues preceding proline and regulates the biological functions of its substrates. Proline 108-115 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 40-44 32426354-4 2020 Pin1, a key PPIase in the cell, recognizes a phosphorylated Ser/Thr-Pro motif to catalyze peptidyl-prolyl isomerization in proteins. Proline 68-71 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 32300594-2 2020 Following signaling events that mediate phosphorylation of MYC at Serine 62, PIN1 establishes structurally distinct pools of MYC through its trans-cis and cis-trans isomerization activity at Proline 63. Proline 191-198 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 77-81 32266261-1 2020 Pin1 is a peptidyl-prolyl cis-trans isomerase that specifically binds to a phosphorylated serine or threonine residue preceding a proline (pSer/Thr-Pro) motif and catalyzes the cis-trans isomerization of proline imidic peptide bond, resulting in conformational change of its substrates. Proline 130-137 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 32266261-1 2020 Pin1 is a peptidyl-prolyl cis-trans isomerase that specifically binds to a phosphorylated serine or threonine residue preceding a proline (pSer/Thr-Pro) motif and catalyzes the cis-trans isomerization of proline imidic peptide bond, resulting in conformational change of its substrates. Proline 204-211 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 32256312-7 2020 Therefore, proline-directed phosphorylation of the N-terminus of PSD-95, Pin1 association, and peptidyl-prolyl cis-trans isomerization may all play a role in excitatory synaptic function and synapse development. Proline 11-18 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 73-77 32258027-1 2020 Peptidyl-prolyl isomerase (PIN1) specifically binds and isomerizes the phosphorylated serine/threonine-proline (pSer/Thr-Pro) motif, which results in the alteration of protein structure, function, and stability. Proline 103-110 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 27-31 32296699-1 2020 Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) is an evolutionally conserved and unique enzyme that specifically catalyzes the cis-trans isomerization of phosphorylated serine/threonine-proline (pSer/Thr-Pro) motif and, subsequently, induces the conformational change of its substrates. Proline 201-208 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 56-60 30684192-1 2019 Peptidyl-prolyl cis/trans isomerase NIMA-interacting 1 (PIN1) induces conformational and functional changes to numerous key signaling molecules following proline-directed phosphorylation and its deregulation contributes to disease, particularly cancer. Proline 154-161 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-54 31026381-3 2019 A central common signaling mechanism in cancer is proline-directed phosphorylation, which is further regulated by the unique proline isomerase Pin1. Proline 50-57 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 143-147 31026381-3 2019 A central common signaling mechanism in cancer is proline-directed phosphorylation, which is further regulated by the unique proline isomerase Pin1. Proline 125-132 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 143-147 30684192-1 2019 Peptidyl-prolyl cis/trans isomerase NIMA-interacting 1 (PIN1) induces conformational and functional changes to numerous key signaling molecules following proline-directed phosphorylation and its deregulation contributes to disease, particularly cancer. Proline 154-161 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 56-60 30697729-1 2019 Peptidyl-prolyl cis-trans isomerase, NIMA-interacting 1 (PIN1) is a peptidyl-prolyl isomerase that binds phospho-Ser/Thr-Pro motifs in proteins and catalyzes the cis-trans isomerization of proline peptide bonds. Proline 121-124 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-55 30697729-1 2019 Peptidyl-prolyl cis-trans isomerase, NIMA-interacting 1 (PIN1) is a peptidyl-prolyl isomerase that binds phospho-Ser/Thr-Pro motifs in proteins and catalyzes the cis-trans isomerization of proline peptide bonds. Proline 121-124 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 57-61 30697729-1 2019 Peptidyl-prolyl cis-trans isomerase, NIMA-interacting 1 (PIN1) is a peptidyl-prolyl isomerase that binds phospho-Ser/Thr-Pro motifs in proteins and catalyzes the cis-trans isomerization of proline peptide bonds. Proline 189-196 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-55 30697729-1 2019 Peptidyl-prolyl cis-trans isomerase, NIMA-interacting 1 (PIN1) is a peptidyl-prolyl isomerase that binds phospho-Ser/Thr-Pro motifs in proteins and catalyzes the cis-trans isomerization of proline peptide bonds. Proline 189-196 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 57-61 30723410-1 2018 PIN1 is a member of a family of peptidylprolyl isomerases that bind phosphoproteins and catalyze the rapid cis-trans isomerization of proline peptidyl bonds, resulting in an alteration of protein structure, function, and stability. Proline 134-141 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 30316783-4 2018 Proline-directed phosphorylation of MCM3 at S112 and T722 are crucial for the interaction with Pin1. Proline 0-7 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 95-99 30534074-3 2018 PIN1 specifically binds the phosphorylated serine or threonine residue preceding a proline (pSer/Thr-Pro) motif of its target proteins and catalyzes the cis/trans isomerization on the pSer/Thr-Pro peptide bonds. Proline 83-90 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 30158600-1 2018 Pin1 is the only known peptidyl-prolyl cis-trans isomerase (PPIase) that specifically recognizes and isomerizes the phosphorylated Serine/Threonine-Proline (pSer/Thr-Pro) motif. Proline 148-155 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 30460195-1 2018 Pin1 belongs to the family of the peptidyl-prolyl cis-trans isomerase (PPIase), which is a class of enzymes that catalyze the cis/trans isomerization of the Proline residue. Proline 157-164 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 30460195-2 2018 Pin1 is unique and only catalyzes the phosphorylated Serine/Threonine-Proline (S/T-P) motifs of a subset of proteins. Proline 70-77 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 30314361-2 2018 The most extensively studied PPIase family member is protein interacting with never in mitosis A1 (PIN1), which isomerizes phosphorylated serine/threonine-proline bonds. Proline 155-162 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 99-103 30314361-4 2018 Many proteins are targets of proline-directed phosphorylation and thus PIN1-mediated isomerization of proline bonds represents an important step in the regulation of a variety of cellular mechanisms. Proline 29-36 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 71-75 30314361-4 2018 Many proteins are targets of proline-directed phosphorylation and thus PIN1-mediated isomerization of proline bonds represents an important step in the regulation of a variety of cellular mechanisms. Proline 102-109 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 71-75 27863418-1 2016 PIN1, which belongs to a family of prolyl isomerases, specifically binds to phosphorylated Ser/Thr-pro motifs to catalytically regulate the post-phosphorylation conformation of its substrates. Proline 35-38 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 27800612-1 2017 Pin1 is a peptidyl prolyl cis-trans isomerase that specifically binds to the phosphoserine-proline or phosphothreonine-proline motifs of several proteins. Proline 91-98 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 27800612-1 2017 Pin1 is a peptidyl prolyl cis-trans isomerase that specifically binds to the phosphoserine-proline or phosphothreonine-proline motifs of several proteins. Proline 119-126 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 28481868-5 2017 PIN1 also catalyses the isomerization of proline 205 of BRD4 and induces its conformational change, which promotes its interaction with CDK9 and increases BRD4"s transcriptional activity. Proline 41-48 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 27834957-2 2017 PIN1 exerts its action by inducing conformational and functional changes on key cellular proteins, following proline-directed phosphorylation. Proline 109-116 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 30149861-2 2018 In humans, peptidyl-prolyl isomerase cis-trans isomerase NIMA interacting 1 (Pin1) is responsible for mediating fast conversion between cis- and trans-conformations of serine/threonine-proline (S/T-P) motifs in a large number of cellular pathways, many of which are involved in normal development as well as progression of several cancers and diseases. Proline 185-192 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 11-75 30149861-2 2018 In humans, peptidyl-prolyl isomerase cis-trans isomerase NIMA interacting 1 (Pin1) is responsible for mediating fast conversion between cis- and trans-conformations of serine/threonine-proline (S/T-P) motifs in a large number of cellular pathways, many of which are involved in normal development as well as progression of several cancers and diseases. Proline 185-192 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 77-81 29118189-1 2017 PIN1 is a peptidyl-prolyl isomerase that catalyzes the cis/trans isomerization of peptide bonds between proline and phosphorylated serine/threonine residues. Proline 104-111 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 28184937-1 2017 The Pin1 protein (or peptidyl-prolyl cis/trans isomerase) specifically catalyzes the cis/trans isomerization of phosphorylated serine/threonine-proline (Ser/Thr-Pro) bonds and plays an important role in many cellular events through the effects of conformational change in the function of c-Jun, its biological substrate. Proline 144-151 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 4-8 28184937-1 2017 The Pin1 protein (or peptidyl-prolyl cis/trans isomerase) specifically catalyzes the cis/trans isomerization of phosphorylated serine/threonine-proline (Ser/Thr-Pro) bonds and plays an important role in many cellular events through the effects of conformational change in the function of c-Jun, its biological substrate. Proline 161-164 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 4-8 28184937-4 2017 Since phosphorylation of proteins on Ser/Thr-Pro is a key regulatory mechanism in the control of cell proliferation and transformation, Pin1 has become an attractive molecule in cancer research. Proline 45-48 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 136-140 26655473-1 2015 Hierarchic phosphorylation and concomitant Pin1-mediated proline isomerization of the oncoprotein c-Myc controls its cellular stability and activity. Proline 57-64 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 43-47 28018099-1 2016 PIN1 is a peptidyl-prolyl cis/trans isomerase that binds and catalyses isomerization of the specific motif comprising a phosphorylated serine or threonine residue preceding a proline (pSer/Thr-Pro) in proteins. Proline 175-182 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 28018099-1 2016 PIN1 is a peptidyl-prolyl cis/trans isomerase that binds and catalyses isomerization of the specific motif comprising a phosphorylated serine or threonine residue preceding a proline (pSer/Thr-Pro) in proteins. Proline 193-196 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 28018099-2 2016 PIN1 can therefore induce conformational and functional changes of its interacting proteins that are regulated by proline-directed serine/threonine phosphorylation. Proline 114-121 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 27572155-4 2016 Since Pin1 is overexpressed and/or activated in various types of cancers, and the dysregulation of proline-directed phosphorylation contributes to tumorigenesis, Pin1 represents an attractive target for cancer therapy. Proline 99-106 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 162-166 27790836-9 2016 These studies provide novel insights regarding the complexity of interactions between Pin1 and activated IRAK1, and more broadly suggest that phosphorylation of neighboring Ser/Thr-Pro motifs in proteins might provide competitive advantage at cellular concentrations for engaging with Pin1. Proline 181-184 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 86-90 27790836-9 2016 These studies provide novel insights regarding the complexity of interactions between Pin1 and activated IRAK1, and more broadly suggest that phosphorylation of neighboring Ser/Thr-Pro motifs in proteins might provide competitive advantage at cellular concentrations for engaging with Pin1. Proline 181-184 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 285-289 27499097-1 2016 Phosphorylation of proteins on serine/threonine residues that precede proline (pSer/Thr-Pro) is specifically catalyzed by the peptidyl-prolyl cis-trans isomerase PIN1. Proline 70-77 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 162-166 27499442-7 2016 Pin1 binds promiscuously to phospho-Ser/Thr-Pro motifs, however, disparate structural and dynamic responses have been reported upon binding different ligands. Proline 44-47 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 26996940-3 2016 Of those phosphorylation sites, 17 precede a proline, making them potential recognition sites for the peptidyl-prolyl isomerase Pin1. Proline 45-52 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 128-132 26996941-6 2016 We find that phosphorylated (p-) SER235-PRO, but not pTHR231-PRO, is exclusively catalyzed by full-length Pin1 and isolated PPIase domain. Proline 40-43 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 106-110 27889995-4 2016 Pin1 is the only proline isomerase that specifically recognizes certain Pro-directed Ser/Thr phosphorylation motifs. Proline 17-24 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 26508545-1 2015 Pin1 is a peptidyl prolyl isomerase that specifically catalyzes cis-trans isomerization of phosphorylated Thr/Ser-Pro peptide bonds in substrate proteins and peptides. Proline 114-117 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 26508545-3 2015 We designed and synthesized a novel series of Pin1 inhibitors based on a glutamic acid or aspartic acid scaffold bearing an aromatic moiety to provide a hydrophobic surface and a cyclic aliphatic amine moiety with affinity for the proline-binding site of Pin1. Proline 231-238 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 46-50 26332362-4 2015 Due to this inherent characteristic, these phosphatases respond differently to enzymes that catalyze the isomerization of proline, like Ess1/Pin1. Proline 122-129 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 141-145 26236013-0 2015 Pin1-Induced Proline Isomerization in Cytosolic p53 Mediates BAX Activation and Apoptosis. Proline 13-20 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 26406962-3 2015 The WW domain of human Pin1 can recognize the phosphoserine/phosphothreonine-proline (pS/pT-P) motifs, while its PPIase domain catalyzes the cis/trans isomerization of prolyl bonds to regulate the cell cycle. Proline 77-84 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 23-27 25766872-3 2015 SCOPE OF REVIEW: We have evaluated interactions between Pin1 and the regulatory kinome and proline-dependent phosphoproteome taking into consideration findings from targeted studies as well as data that has emerged from systematic phosphoproteomic workflows and from curated protein interaction databases. Proline 91-98 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 56-60 25280783-1 2015 The prolyl isomerase Pin1, which isomerizes the p-Ser/Thr-Pro peptide bonds and effects conformational and functional changes of the bound proteins, has been identified as a regulator of phosphorylation signaling in several diseases including cancer. Proline 58-61 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 21-25 25849135-3 2015 By using mechanism-based screening, here we find that all-trans retinoic acid (ATRA)--a therapy for acute promyelocytic leukemia (APL) that is considered the first example of targeted therapy in cancer, but whose drug target remains elusive--inhibits and degrades active Pin1 selectively in cancer cells by directly binding to the substrate phosphate- and proline-binding pockets in the Pin1 active site. Proline 356-363 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 271-275 25849135-3 2015 By using mechanism-based screening, here we find that all-trans retinoic acid (ATRA)--a therapy for acute promyelocytic leukemia (APL) that is considered the first example of targeted therapy in cancer, but whose drug target remains elusive--inhibits and degrades active Pin1 selectively in cancer cells by directly binding to the substrate phosphate- and proline-binding pockets in the Pin1 active site. Proline 356-363 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 387-391 25818297-1 2015 Proline-directed phosphorylation is regulated by the prolyl isomerase Pin1, which plays a fundamental role in driving breast cancer stem-like cells (BCSCs). Proline 0-7 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 70-74 25831499-12 2015 Pin1 acts via isomerization of proline side chains at phosphorylated PDPK motifs, thereby affecting substrate conformation and activity. Proline 31-38 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 25576397-1 2015 The unique proline isomerase Pin1 is pivotal for protecting against age-dependent neurodegeneration in Alzheimer"s disease (AD), with its inhibition providing a molecular link between tangle and plaque pathologies. Proline 11-18 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 29-33 25702031-0 2015 Dynamical role of phosphorylation on serine/threonine-proline Pin1 substrates from constant force molecular dynamics simulations. Proline 54-61 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 62-66 25588053-6 2015 Our data suggest that proline-directed phosphorylation regulates Rta by licensing binding to Pin1. Proline 22-29 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 93-97 25197063-4 2014 We identify a proline-directed phosphorylation motif, at serines 861/864 upstream of these sites, which is a substrate for the peptidylprolyl cis/trans isomerase, Pin1, as well as the ERK1/2 kinases. Proline 14-21 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 163-167 26133706-3 2015 PIN1 specifically binds phosphorylated serine or threonine residues immediately preceding proline (pSer/Thr-Pro) and then regulates protein functions, including catalytic activity, phosphorylation status, protein interactions, subcellular location, and protein stability, by promoting cis/trans isomerization of the peptide bond. Proline 90-97 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 26133706-3 2015 PIN1 specifically binds phosphorylated serine or threonine residues immediately preceding proline (pSer/Thr-Pro) and then regulates protein functions, including catalytic activity, phosphorylation status, protein interactions, subcellular location, and protein stability, by promoting cis/trans isomerization of the peptide bond. Proline 108-111 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 25100325-1 2014 Pin1 peptidyl-prolyl isomerase (PPIase) catalyzes specifically the pSer/pThr-Pro motif. Proline 76-80 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 25091930-3 2014 The potency of the carboxylate series is now further improved through structure-based optimization of ligand-protein interactions in the proline binding site which exploits the H-bond interactions necessary for Pin1 catalytic function. Proline 137-144 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 211-215 25124924-2 2014 Protein interacting with never in mitosis A1 (Pin1), which is overexpressed in many types of cancer, isomerizes specific phosphorylated Ser/Thr-Pro bonds in many substrate proteins, including glycolytic enzyme, protein kinases, protein phosphatases, methyltransferase, lipid kinase, ubiquitin E3 ligase, DNA endonuclease, RNA polymerase, and transcription activators and regulators. Proline 0-3 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 46-50 25120724-1 2014 Peptidyl-prolylcis-trans isomerase NIMA-interacting 1 (encoded by the PIN1 gene) regulates the conformation of proline-directed phosphorylation sites and is important in the etiology of cancer. Proline 111-118 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 70-74 25059768-1 2014 Pin1 is an enzyme that specifically catalyzes the cis-trans isomerization of proline amide bonds in peptides that contain a phosphorylated threonine or serine residue in the position preceding proline. Proline 77-84 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 25059768-1 2014 Pin1 is an enzyme that specifically catalyzes the cis-trans isomerization of proline amide bonds in peptides that contain a phosphorylated threonine or serine residue in the position preceding proline. Proline 193-200 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 22549912-1 2013 Pin1 is a unique regulator that catalyzes the conversion of a specific phospho-Ser/Thr-Pro-containing motif in target proteins. Proline 87-90 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 23839950-0 2014 Modulating the folding stability and ligand binding affinity of Pin1 WW domain by proline ring puckering. Proline 82-89 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 64-68 23994618-5 2013 PIN1 is a peptidyl-prolyl isomerase enzyme belonging to the parvulin family, which specifically recognizes phosphorylated Ser/Thr-Pro containing substrates. Proline 130-133 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 23994618-6 2013 Through protein-protein interaction assays, we showed that the Pro-directed Ser/Thr-Pro motif at Thr-93 in the KLF10 N-terminal region is essential for the interaction between KLF10 and PIN1. Proline 63-66 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 186-190 24840168-3 2014 Pin1 is a cis-trans isomerase of peptidyl-prolyl(omega-) bonds of phosphorylated-Ser/Thr-Pro motifs and has been implicated in many diseases. Proline 89-92 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 24982848-1 2014 The peptidyl-prolyl cis/trans isomerase Pin1 acts as a molecular timer in proline-directed Ser/Thr kinase signaling and shapes cellular responses based on recognition of phosphorylation marks and implementing conformational changes in its substrates. Proline 74-81 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 40-44 24534472-1 2014 Pin1 is a unique enzyme that changes the shape of target proteins by acting on specific amino acids that have been phosphorylated: serine or threonine residues that precede proline. Proline 173-180 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 24534472-2 2014 Pin1 catalyzes the flip between two distinct orientations, called cis and trans, around the proline bond. Proline 92-99 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 25485500-8 2014 Moreover, our studies confirm that the subsequently trans/cis proline isomerization of (T/S)P motif by the Pin1 prolyl-isomerase, could modulate the E3-ligase interaction, and that the (T/S)pPtransPPxY motif represent the best conformer for the ItchWW-(T/S)PPPxY motif recognition. Proline 62-69 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 107-111 24267382-5 2014 Pin1 specifically binds to a phosphopeptide corresponding to the L3 loop of Sp140-PHD and catalyzes cis-trans isomerization of a pThr-Pro bond. Proline 134-137 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 23887939-4 2013 Unrestricted proline isomerisation can be inhibited by adjacent serine phosphorylation and requires a prolyl isomerise, Pin1. Proline 13-20 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 120-124 23887939-5 2013 Pin1 therefore determines the functional outcome of proline-directed kinases acting on the GR, as cis/trans isomers are distinct pools with different interacting proteins. Proline 52-59 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 23708493-2 2013 Nanog is phosphorylated at multiple Ser/Thr-Pro motifs, which promotes the interaction between Nanog and the prolyl isomerase Pin1, leading to Nanog stabilization by suppressing its ubiquitination. Proline 44-47 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 126-130 23280577-1 2013 Pin1 is a unique enzyme that can isomerize specific phospho-Ser/Thr-Pro peptide bonds, inducing a conformational change in the target protein. Proline 68-71 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 23157676-1 2013 Proline-directed protein phosphorylation (pSer/Thr-Pro), a central signaling mechanism in diverse cellular processes in physiology and disease, has been proposed to be subject to further cis-trans conformational regulation by the unique prolyl isomerase Pin1. Proline 0-7 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 254-258 22789442-7 2012 A systematic mutation analysis of all 17 Ser/Thr-Pro-motifs in Nur77 revealed that Pin1 enhances protein stability of Nur77 in an isomerase-dependent manner by acting on phosphorylated Nur77 involving protein kinase CK2-mediated phosphorylation of the Ser(152)-Pro(153) motif in Nur77. Proline 49-52 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 83-87 23362255-6 2013 We reported previously that dephosphorylation of Tau at Cdk5-mediated sites was enhanced by Pin1, a peptidyl-prolyl isomerase that stimulates dephosphorylation at proline-directed sites by protein phosphatase 2A. Proline 163-170 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 92-96 23221557-1 2013 Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein is known as a regulator which recognizes phosphorylated Ser/Thr-Pro motifs and increases the rate of cis and trans amide isomer interconversion, thereby altering the conformation of its substrates. Proline 134-137 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-54 23221557-1 2013 Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) protein is known as a regulator which recognizes phosphorylated Ser/Thr-Pro motifs and increases the rate of cis and trans amide isomer interconversion, thereby altering the conformation of its substrates. Proline 134-137 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 56-60 23025283-6 2012 The common structural and electrostatic characteristics of Pin1 substrates, which contain a phosphorylated serine/threonine-proline motif, suggest that very rapid binding kinetics are a general feature of Pin1 interactions with other substrates. Proline 124-131 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 59-63 23025283-6 2012 The common structural and electrostatic characteristics of Pin1 substrates, which contain a phosphorylated serine/threonine-proline motif, suggest that very rapid binding kinetics are a general feature of Pin1 interactions with other substrates. Proline 124-131 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 205-209 22789442-7 2012 A systematic mutation analysis of all 17 Ser/Thr-Pro-motifs in Nur77 revealed that Pin1 enhances protein stability of Nur77 in an isomerase-dependent manner by acting on phosphorylated Nur77 involving protein kinase CK2-mediated phosphorylation of the Ser(152)-Pro(153) motif in Nur77. Proline 261-264 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 83-87 22580604-6 2013 In addition, Pin1 recognizes four phosphorylated Ser/Thr-Pro motifs in RUNX3 via its WW domain. Proline 57-60 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 13-17 23333752-1 2013 PIN1, a peptidyl-prolyl-isomerase, binds a specific motif comprising a phosphorylated serine or threonine preceding a proline (p-Ser/Thr-Pro) residue in proteins. Proline 118-125 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 23407864-2 2013 Furthermore, there is a mounting body of evidence implicating Pin1 in the emergence of pathological phenotypes in neurodegeneration and cancer through the isomerization of a wide variety of substrates at peptidyl-prolyl bonds where the residue preceding proline is a phosphorylated serine or threonine residue (i.e., pS/T-P motifs). Proline 254-261 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 62-66 23030417-2 2012 Pin1 represents an enzyme that specifically catalyzes the isomerization of peptide bonds between phosphorylated threonine or serine residues and proline. Proline 145-152 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 22976962-5 2012 Our results clearly indicate that the isomerase Pin1 interacts favorably with pSer/pThr-Pro residues in Tau, but does not bind non-phosphorylated Tau or phospho-Tyr residues in Tau films. Proline 88-91 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 48-52 21660049-9 2012 These results provide novel insights that, following stress-induced phosphorylation of Thr in the Thr-Pro motif of JNK1, JNK1 associates with Pin1 and undergoes conformational changes to promote the binding of JNK1 to its substrates, resulting in cellular responses from extracellular signals. Proline 102-105 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 142-146 22002310-1 2012 Pin1 regulates a subset of phosphoproteins by isomerizing phospho-Ser/Thr-Pro motifs via a "post-phosphorylation" mechanism. Proline 74-77 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 22002310-3 2012 There are at least three phospho-Ser-Pro motifs on TR3 that bind to Pin1. Proline 37-40 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 68-72 22318721-4 2012 The regulation by Pin1 requires both the catalytic activity of the isomerase and the presence of a Pro immediately following the phosphorylated Thr of the turn motif phosphorylation site, one of two C-terminal sites that is phosphorylated during the maturation of PKC isozymes. Proline 99-102 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 18-22 22235112-4 2012 In this assay, fusion proteins of Tau and Pin1 (peptidyl-prolyl cis-trans-isomerase 1) carrying complementary fragments of a luciferase protein serve as a sensor of altered protein-protein interaction between Tau and Pin1, a critical regulator of Tau dephosphorylation at several disease-associated proline-directed phosphorylation sites. Proline 299-306 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 42-46 22235112-4 2012 In this assay, fusion proteins of Tau and Pin1 (peptidyl-prolyl cis-trans-isomerase 1) carrying complementary fragments of a luciferase protein serve as a sensor of altered protein-protein interaction between Tau and Pin1, a critical regulator of Tau dephosphorylation at several disease-associated proline-directed phosphorylation sites. Proline 299-306 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 48-85 22235112-4 2012 In this assay, fusion proteins of Tau and Pin1 (peptidyl-prolyl cis-trans-isomerase 1) carrying complementary fragments of a luciferase protein serve as a sensor of altered protein-protein interaction between Tau and Pin1, a critical regulator of Tau dephosphorylation at several disease-associated proline-directed phosphorylation sites. Proline 299-306 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 217-221 21967280-2 2011 Human Pin1 is central to many of these cell signaling pathways in normal and aberrant subcellular processes, catalyzing cis-trans isomerization of the peptide omega-bond in phosphorylated serine/threonine-proline motifs in many proteins. Proline 205-212 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 6-10 22900083-3 2012 TbPin1 was identified as a novel class of Pin1-type parvulins from Trypanosoma brucei, containing a unique PPIase domain, which can catalyze the isomerization of phosphorylated Ser/Thr-Pro peptide bond. Proline 185-188 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 2-6 21980916-8 2011 Three additional reduced amides, with Thr replacing Ser and l- or d-pipecolate (Pip) replacing Pro, were slightly weaker inhibitors of Pin1. Proline 95-98 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 135-139 22848287-1 2011 Peptidyl-prolyl isomerase Pin1 specifically catalyzes the cis/trans-isomerization of proline in the target sequence of phosphorylated Ser/Thr-Pro in over 50 critical regulatory proteins. Proline 85-92 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 26-30 22848287-1 2011 Peptidyl-prolyl isomerase Pin1 specifically catalyzes the cis/trans-isomerization of proline in the target sequence of phosphorylated Ser/Thr-Pro in over 50 critical regulatory proteins. Proline 142-145 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 26-30 21764651-1 2011 Pin1 specifically recognizes and catalyzes the cis-trans isomerization of phosphorylated-Ser/Thr-Pro bonds, which modulate the stability, localization, and function of numerous Pin1 targets involved in tumor progression. Proline 97-100 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 21764651-1 2011 Pin1 specifically recognizes and catalyzes the cis-trans isomerization of phosphorylated-Ser/Thr-Pro bonds, which modulate the stability, localization, and function of numerous Pin1 targets involved in tumor progression. Proline 97-100 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 177-181 21746900-1 2011 Pin1 is a modular enzyme that accelerates the cis-trans isomerization of phosphorylated-Ser/Thr-Pro (pS/T-P) motifs found in numerous signaling proteins regulating cell growth and neuronal survival. Proline 96-99 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 21714498-1 2011 Pin1 is a prolyl isomerase that recognizes phosphorylated Ser/Thr-Pro sites, and phosphatase inhibitor-2 (I-2) is phosphorylated during mitosis at a PSpTP site that is expected to be a Pin1 substrate. Proline 66-69 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 21852138-1 2011 Pin1 is a highly conserved enzyme that only isomerizes specific phosphorylated Ser/Thr-Pro bonds in certain proteins, thereby inducing conformational changes. Proline 87-90 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 21947912-1 2011 The phosphorylation-specific peptidyl-prolyl isomerase Pin1 catalyzes the isomerization of the peptide bond preceding a proline residue between cis and trans isomers. Proline 120-127 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 55-59 21947912-7 2011 Specific (13)C labeling at the Pin1-targeted proline residue provided multiple reporters sensitive to individual isomer binding and on-enzyme catalysis. Proline 45-52 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 31-35 21682951-2 2011 Pin1 (peptidyl-prolyl cis-trans isomerase) is the only enzyme known that can isomerise specific Ser/Thr-Pro peptide bonds after phosphorylation and regulate their conformational changes with high efficiency. Proline 104-107 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 20932746-2 2010 Pin1 isomerizes bonds linking phospho-serine/threonine moieties to proline enabling it to play a key role in proline-directed kinase signalling. Proline 67-74 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 21219594-1 2011 BACKGROUND: Peptidyl-prolyl cis/trans isomerase (Pin1), encoded by PIN1 gene with locus in chromosome 19p13, is an enzyme that catalytically induces conformational changes in proteins after phosphorylation on serine or threonine residues preceding proline (pSer/Thr-Pro motifs); in this way, it has an influence on protein interactions and intracellular localizations of proteins. Proline 248-255 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 49-53 21219594-1 2011 BACKGROUND: Peptidyl-prolyl cis/trans isomerase (Pin1), encoded by PIN1 gene with locus in chromosome 19p13, is an enzyme that catalytically induces conformational changes in proteins after phosphorylation on serine or threonine residues preceding proline (pSer/Thr-Pro motifs); in this way, it has an influence on protein interactions and intracellular localizations of proteins. Proline 248-255 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 67-71 21219594-1 2011 BACKGROUND: Peptidyl-prolyl cis/trans isomerase (Pin1), encoded by PIN1 gene with locus in chromosome 19p13, is an enzyme that catalytically induces conformational changes in proteins after phosphorylation on serine or threonine residues preceding proline (pSer/Thr-Pro motifs); in this way, it has an influence on protein interactions and intracellular localizations of proteins. Proline 266-269 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 49-53 21219594-1 2011 BACKGROUND: Peptidyl-prolyl cis/trans isomerase (Pin1), encoded by PIN1 gene with locus in chromosome 19p13, is an enzyme that catalytically induces conformational changes in proteins after phosphorylation on serine or threonine residues preceding proline (pSer/Thr-Pro motifs); in this way, it has an influence on protein interactions and intracellular localizations of proteins. Proline 266-269 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 67-71 20932746-2 2010 Pin1 isomerizes bonds linking phospho-serine/threonine moieties to proline enabling it to play a key role in proline-directed kinase signalling. Proline 109-116 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 20529865-2 2010 Here, we show that the uncoating process requires the interaction of the capsid (CA) protein with the peptidyl-prolyl isomerase Pin1 that specifically recognizes the phosphorylated serine/threonine residue followed by proline. Proline 218-225 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 128-132 20682773-0 2010 Prolyl isomerase Pin1 regulates transcription factor LSF (TFCP2) by facilitating dephosphorylation at two serine-proline motifs. Proline 113-120 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 17-21 20529865-6 2010 Glutathione S-transferase pulldown assays demonstrated a direct interaction between Pin1 and the HIV-1 core via the Ser(16)-Pro(17) motif. Proline 124-127 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 84-88 20179103-5 2010 However, only active Mek2 could bind Pin1, acting as a scaffold to bridge Pin1 and BPGAP1 in a manner that involves the release of an autoinhibited proline-rich motif, 186-PPLP-189, proximal to the RhoGAP domain. Proline 148-155 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 37-41 20207139-2 2010 The initial loss in potency of carboxylate analogs was likely due to weaker charge-charge interactions in the putative phosphate binding pocket and was subsequently recovered by structure-based optimization of ligand-protein interactions in the proline binding site, leading to the discovery of a sub-micromolar non-phosphate small molecular Pin1 inhibitor. Proline 245-252 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 342-346 20179103-6 2010 This allows the non-canonical 186-PPLP-189 and 256-DDYGD-260 motifs of the proline-rich region and RhoGAP domain of BPGAP1 to become accessible to concerted binding by the WW and PPI domains of Pin1, respectively. Proline 75-82 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 194-198 19890497-1 2009 Pin1 specifically catalyzes the cis/trans isomerization of phospho-Ser/Thr-Pro bonds and plays an important role in many cellular events through the effects of conformational change on the function of its biological substrates, including cell division cycle 25 C (Cdc25C), c-Jun and p53. Proline 75-78 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 20009523-3 2010 The phospho-Ser/Thr-Pro specific prolyl-isomerase Pin1 is overexpressed in many different cancers, including NSCLC, and may possibly be used as a target for cancer therapy. Proline 20-23 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 50-54 19940183-6 2009 In cortical neurons, Pin1 modulates the topographic phosphorylation of the proline-directed Ser/Thr residues within the tail domain of NF proteins by inhibiting the dephosphorylation by PP2A. Proline 75-82 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 21-25 20179161-3 2010 The phosphorylation of proteins on the serine or threonine residues that immediately precede proline (pSer/Thr-Pro) is specifically catalyzed by the prolyl isomerase Pin1 and is a key signaling mechanism in cell proliferation and transformation. Proline 93-100 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 166-170 20214639-1 2010 The peptidyl prolyl isomerase (Pin1) that catalyzes the isomerization of peptide bonds involving proline and phosphorylated serine/threonine/tyrosine and alters the conformation and differential folding has been implicated in the regulation and function of phosphorylated proteins including mitotic and cell cycle proteins viz. Proline 97-104 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 31-35 19996102-0 2010 Proline cis/trans-isomerase Pin1 regulates peroxisome proliferator-activated receptor gamma activity through the direct binding to the activation function-1 domain. Proline 0-7 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 28-32 19920136-6 2010 Pin1, a peptidyl-prolyl cis/trans isomerase, recognizes phosphorylated serine/threonine-proline motifs. Proline 88-95 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 20110589-1 2010 Pin1 [Protein Interacting with NIMA (never in mitosis A)] is a peptidyl prolyl cis-trans isomerase that isomerizes phospho-Serine/Threonine-Proline [p(S/T)-P] motifs of its target proteins. Proline 140-147 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 19597489-2 2009 Because of its activity to switch the conformation of peptidyl-proline bonds in polypeptide chains, Pin1 operates as a binary switch, often in fate-determining pathways. Proline 63-70 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 100-104 19439498-11 2009 Finally, Pin1 binding was mapped to two threonine-proline motifs (Thr(8) and Thr(11)) that are not present in any of the other human cytosolic sulfotransferases. Proline 50-57 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 9-13 19288014-2 2009 The conformation and function of phosphorylated Ser/Thr-Pro motifs are further regulated by the prolyl isomerase Pin1. Proline 56-59 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 113-117 19168580-1 2009 Phosphorylation of proteins on serine or threonine residues that immediately precede proline (pSer/Thr-Pro) is specifically catalyzed by the peptidyl-prolyl cis-trans isomerase Pin1 and is a central signaling mechanism in cell proliferation and transformation. Proline 85-92 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 177-181 19291099-1 2009 Pin1 plays a key role in various biological cellular processes via the recognition of phosphorylated Ser/Thr-Proline motifs. Proline 109-116 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 19592546-1 2009 Phosphorylation of proteins on serine or threonine residues preceding proline is a major regulatory mechanism in cell proliferation and transformation, which is catalyzed specifically by Pin1, a peptidylprolyl isomerase. Proline 70-77 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 187-191 17906639-5 2007 Accordingly, tumor-associated mutations at Pin1-binding residues within the p53 proline-rich domain hamper acetylation of p53 by p300. Proline 80-87 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 43-47 18473735-3 2008 Specifically, Pin1 controls the conversion of peptidyl proline bond conversion from cis to trans, only when the preceding serine or threonine is phosphorylated. Proline 55-62 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 14-18 18062707-2 2008 Pin1 is a peptide prolyl cis/trans isomerase conserved among eukaryotes that specifically reacts with proteins phosphorylated at Ser/Thr-Pro sites. Proline 137-140 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 18357725-1 2008 Pin1 is a phosphorylation-dependent peptidyl-prolyl cis/trans isomerase, which specifically catalyzes the amide bond isomerization of phosphoserine-proline or phosphothreonine-proline in mitotic phosphoproteins. Proline 148-155 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 18359295-7 2008 By point mutating each individual Ser/Thr-Pro motif in c-Myb as well as by using deletion mutants we show that S528 in the EVES-motif was the docking site for Pin1. Proline 42-45 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 159-163 17383430-0 2007 Pin1 interacts with a specific serine-proline motif of hepatitis B virus X-protein to enhance hepatocarcinogenesis. Proline 38-45 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 17626162-4 2007 Although localization of kinases and phosphatases is certainly implicated, another possibility involves Pin1 modulation of phosphorylation of the proline-directed serine/threonine residues. Proline 146-153 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 104-108 17626162-5 2007 Pin1, a prolyl isomerase, selectively binds to phosphorylated proline-directed serine/threonine residues in target proteins and isomerizes cis isomers to more stable trans configurations. Proline 62-69 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 17626162-9 2007 Thus, isomerization of lys-ser-pro repeat residues that are abundant in NF-H tail domains by Pin1 can regulate NF-H phosphorylation, which suggests that Pin1 inhibition may be an attractive therapeutic target to reduce pathological accumulations of p-NF-H. Proline 31-34 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 93-97 17626162-9 2007 Thus, isomerization of lys-ser-pro repeat residues that are abundant in NF-H tail domains by Pin1 can regulate NF-H phosphorylation, which suggests that Pin1 inhibition may be an attractive therapeutic target to reduce pathological accumulations of p-NF-H. Proline 31-34 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 153-157 17383430-2 2007 Hepatitis B virus (HBV) is the most common etiologic agent in HCC, and its encoded X-protein (HBx) is oncogenic and possesses a serine-proline motif that may bind Pin1. Proline 135-142 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 163-167 17383430-7 2007 RESULTS: We showed preferential Pin1 overexpression in HBV-related tumors and confirmed the interaction between Pin1 and HBx at the specific serine-proline motif. Proline 148-155 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 112-116 17355867-2 2007 Pin1 recognizes phospho-Ser/Thr-Pro motifs in cell-signaling proteins, and is both a cancer and an Alzheimer"s disease target. Proline 32-35 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 16841372-1 2006 The phospho-Ser/Thr-Pro specific prolyl-isomerase PIN1 is over-expressed in more than 50% of hepatocellular carcinomas (HCCs). Proline 20-23 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 50-54 17002312-2 2006 The peptidyl prolyl cis/trans isomerase Pin1 specifically catalyzes the conformational transition of phosphorylated Ser/Thr-Pro motifs. Proline 124-127 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 40-44 17241154-6 2007 Phosphorylated APP is a Pin1 substrate, which binds to its phosphor-Thr668-Pro motif. Proline 75-78 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 24-28 21176462-1 2006 BACKGROUND: The conformation of a subset of phosphorylated serines or threonines preceding proline motifs is regulated by the prolyl isomerase Pin1. Proline 91-98 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 143-147 16945100-3 2006 Pin-1, one of the peptidyl-prolyl isomerases (PPIase), catalyzes the isomerization of the peptide bond between pSer/Thr-Pro in proteins, thereby regulating their biological functions which include protein assembly, folding, intracellular transport, intracellular signaling, transcription, cell cycle progression and apoptosis. Proline 120-123 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-5 16865248-1 2006 The prolyl isomerase Pin1, which specifically catalyzes conformational changes in certain proline-directed phosphorylation sites, is thought to be a critical catalyst for multiple oncogenic pathways. Proline 90-97 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 21-25 16706410-2 2006 The molecules studied are models for the phospho-Ser/Thr-Pro substrate for Pin-1, a peptidyl-prolyl isomerase (PPIase) involved in cell division. Proline 57-60 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 75-80 16818231-5 2006 Furthermore, in the context of Cdc4alpha and cyclin E, mutational data suggest that Pin1 isomerizes a noncanonical proline-proline bond, with the possibility that Cdc4alpha may serve as a cofactor for altering the specificity of Pin1. Proline 123-130 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 84-88 16652378-2 2006 Recent studies indicate that certain pSer/Thr-Pro motifs in native proteins exist in two completely distinct conformations, cis and trans, whose conversion is markedly slowed down upon phosphorylation, but specifically catalyzed by the peptidyl-prolyl cis/trans isomerase Pin1. Proline 46-49 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 272-276 16847925-1 2006 BACKGROUND AND OBJECTIVES: Peptidyl prolyl cis-trans isomerase (Pin1) isomerizes only phosphorylated serine or threonine residues preceding proline in certain proteins and affects the protein function. Proline 140-147 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 64-68 16818231-5 2006 Furthermore, in the context of Cdc4alpha and cyclin E, mutational data suggest that Pin1 isomerizes a noncanonical proline-proline bond, with the possibility that Cdc4alpha may serve as a cofactor for altering the specificity of Pin1. Proline 115-122 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 84-88 16706410-3 2006 Pin-1 requires phosphorylation of a Ser or Thr residue adjacent to a Pro residue in the substrate and catalyzes cis-trans isomerization about the proline amide bond. Proline 69-72 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-5 16123044-6 2005 In this regard, it has been recently observed that the prolyl isomerase Pin1 can interact with proteins phosphorylated on serine or threonine residues that precede prolines (pS/T-P), such as the transcription factors p53 and c-Jun, thereby controlling their activity by promoting the cis-trans isomerization of these pS/T-P bonds. Proline 164-172 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 72-76 15964795-0 2005 Mutations in proline 82 of p53 impair its activation by Pin1 and Chk2 in response to DNA damage. Proline 13-20 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 56-60 15964795-6 2005 These physical and functional interactions are regulated by Pin1 through cis-trans isomerization of proline 82. Proline 100-107 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 60-64 15701524-5 2005 In addition, site-directed mutagenesis indicated that the interaction of Pin1 with p54nrb was mediated by three threonine residues located in the proline-rich carboxy-terminal extremity of the protein. Proline 146-153 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 73-77 15867923-2 2005 By catalysing cis-trans interconversion of certain motifs containing phosphorylated serine or threonine residues followed by a proline residue (pSer/Thr-Pro), Pin1 can have profound effects on phosphorylation signalling. Proline 127-134 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 159-163 15867923-2 2005 By catalysing cis-trans interconversion of certain motifs containing phosphorylated serine or threonine residues followed by a proline residue (pSer/Thr-Pro), Pin1 can have profound effects on phosphorylation signalling. Proline 153-156 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 159-163 15474361-1 2004 The peptidyl-prolyl cis-trans isomerase (PPIase) Pin1 modulates the activity of a range of target proteins involved in the cell cycle, transcription, translation, endocytosis, and apoptosis by facilitating dephosphorylation of phosphorylated serine or threonine residue preceding a proline (p-Ser/Thr-Pro) motifs catalyzed by phosphatases specific for the trans conformations. Proline 282-289 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 49-53 15615648-7 2005 Pin1 binds to tau phosphorylated specifically on the Thr231-Pro site and probably catalyzes cis/trans isomerization of pSer/Thr-Pro motif(s), thereby inducing conformational changes in tau. Proline 60-63 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 15893113-2 2005 Pin1 controls the ready (low energy change) equilibrium between the cis and trans distinctive folding configurations differentially at a proline residue: this amino acid residue in proteins is unique in bending sharply its peptide chain (to 90 degrees change): in the cis rather than trans orientation with respect to the peptide bond to residue X "upstream" linked as XCONHR. Proline 137-144 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 15082314-3 2004 Pin1 is a highly conserved enzyme that isomerizes only the phosphorylated Ser/Thr-Pro bonds in certain proteins, thereby inducing conformational changes. Proline 82-85 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 15171797-2 2004 Pin1 isomerizes the peptide bond of specific phosphorylated serine or threonine residues preceding proline in several proteins involved in various cellular events including mitosis, transcription, differentiation and DNA damage response. Proline 99-106 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 15111319-2 2004 Interestingly, the pSer/Thr-Pro motifs in proteins exist in two distinct cis and trans conformations, whose conversion rate is normally reduced on phosphorylation, but is catalyzed specifically by the prolyl isomerase Pin1. Proline 28-31 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 218-222 14681225-5 2004 By using the peptidylprolyl isomerase, Pin1, as a probe for proline-directed phosphorylation, we show that ERK1/2-dependent phosphorylation of Bim(EL) occurs at (S/T)P motifs. Proline 60-67 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 39-43 12631385-1 2003 The prolyl isomerase Pin1 specifically isomerizes certain phosphorylated Ser/Thr-Pro bonds and thereby regulates various cellular processes. Proline 81-84 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 21-25 12571275-2 2003 The phosphorylated Ser/Thr-Pro motifs in a certain subset of phosphoproteins are isomerized specifically by the peptidyl-prolyl cis-trans isomerase Pin1. Proline 27-30 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 148-152 12686540-4 2003 Pin1 is able to bind phospho-Ser/Thr-Pro-containing sequences at two different sites that compete for the same substrate. Proline 37-40 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 12388558-3 2002 The Ser(P)/Thr-Pro moiety exists in the two distinct cis and trans conformations and their conversion is catalyzed specifically by the prolyl isomerase Pin1. Proline 15-18 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 152-156 11787050-2 2002 The prolyl isomerase Pin1 plays an important role in cell cycle regulation through its specific interaction with proteins that are phosphorylated at Ser/Thr-Pro motifs. Proline 157-160 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 21-25 12397361-3 2002 Here we report that DNA damage specifically induces p53 phosphorylation on Ser/Thr-Pro motifs, which facilitates its interaction with Pin1, a member of peptidyl-prolyl isomerase. Proline 83-86 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 134-138 11988841-4 2002 Pin1 and its homologues are known to target the proline residue carboxyl terminal to the phosphorylated threonine or serine residue of mitotic phosphoproteins, such as Bcl2. Proline 48-55 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 0-4 11978535-3 2002 Recent identification of the novel prolyl isomerase Pin1 that specifically isomerizes only the phosphorylated Ser/Thr-Pro bonds in certain proteins led us to propose a new signaling mechanism, whereby prolyl isomerization catalytically induces conformational changes in proteins following phosphorylation to regulate protein function. Proline 118-121 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 52-56 11774038-9 2001 Since the region in Bcl-2 containing serine 70 and serine 87 represents a proline-rich loop that has been associated with autorepression of its antiapoptotic activity, the discovery of Pin1 interactions with phosphorylated Bcl-2 raises the possibility that Pin1 alters the conformation of Bcl-2 and thereby modulates its function in cells arrested with antimicrotubule drugs. Proline 74-81 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 185-189 11533658-1 2001 Phosphorylation on a serine or threonine residue preceding proline (Ser/Thr-Pro) is a key regulatory mechanism, and the conformation of certain phosphorylated Ser/Thr-Pro bonds is regulated specifically by the prolyl isomerase Pin1. Proline 76-79 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 227-231 11013245-0 2001 p13(SUC1) and the WW domain of PIN1 bind to the same phosphothreonine-proline epitope. Proline 70-77 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 31-35 11432833-2 2001 The conformation of a subset of phosphorylated Ser/Thr-Pro motifs is regulated by the prolyl isomerase Pin1. Proline 55-58 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 103-107 11356192-4 2001 The NFAT-Pin1 interaction is mediated through the WW domain of Pin1 and the serine-proline-rich domains of NFAT. Proline 83-90 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 9-13 11389853-3 2001 We show that Pin1 catalytically generates a conformational change on the mitotic phosphatase Cdc25, as assayed by limited protease digestion, differential reactivity to a phosphoserine-proline-directed monoclonal antibody (MPM-2), and by changes in Cdc25 enzymatic activity. Proline 185-192 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 13-17 11162102-9 2001 Two of these residues are conserved and have been shown to interact with the proline residue of the substrate in hPin1. Proline 77-84 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 113-118 11326318-9 2001 Since the region in Bcl-2 containing serine 70 and serine 87 represents a proline-rich loop that has been associated with autorepression of its antiapoptotic activity, the discovery of Pin1 interactions with phosphorylated Bcl-2 raises the possibility that Pin1 alters the conformation of Bcl-2 and thereby modulates its function in cells arrested with antimicrotubule drugs. Proline 74-81 peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens 185-189