DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study. The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study. Structure (London, England : 1993) 2013 imex curation Francis DM., Kumar GS., Koveal D., Tortajada A., Page R., Peti W. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Francis DM., Kumar GS., Koveal D., Tortajada A., Page R., Peti W. DIP original experiment: DIP-255731X Structure (London, England : 1993) 2013 IMEx The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study. The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study. The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study. Structure (London, England : 1993) 2013 imex curation Francis DM., Kumar GS., Koveal D., Tortajada A., Page R., Peti W. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Francis DM., Kumar GS., Koveal D., Tortajada A., Page R., Peti W. DIP original experiment: DIP-255724X Structure (London, England : 1993) 2013 IMEx The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study. The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study. The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study. Structure (London, England : 1993) 2013 imex curation Francis DM., Kumar GS., Koveal D., Tortajada A., Page R., Peti W. Only protein-protein interactions in vitro In vitro saxs x ray scattering saxs predetermined predetermined participant predetermined Francis DM., Kumar GS., Koveal D., Tortajada A., Page R., Peti W. DIP original experiment: DIP-255726X Structure (London, England : 1993) 2013 IMEx The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study. The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study. The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study. Structure (London, England : 1993) 2013 imex curation Francis DM., Kumar GS., Koveal D., Tortajada A., Page R., Peti W. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Francis DM., Kumar GS., Koveal D., Tortajada A., Page R., Peti W. DIP original experiment: DIP-255725X Structure (London, England : 1993) 2013 IMEx The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study. The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study. The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study. Structure (London, England : 1993) 2013 imex curation Francis DM., Kumar GS., Koveal D., Tortajada A., Page R., Peti W. Only protein-protein interactions in vitro In vitro saxs x ray scattering saxs predetermined predetermined participant predetermined Francis DM., Kumar GS., Koveal D., Tortajada A., Page R., Peti W. DIP original experiment: DIP-255727X Structure (London, England : 1993) 2013 IMEx The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study. The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study. The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study. Structure (London, England : 1993) 2013 imex curation Francis DM., Kumar GS., Koveal D., Tortajada A., Page R., Peti W. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Francis DM., Kumar GS., Koveal D., Tortajada A., Page R., Peti W. DIP original experiment: DIP-255721X Structure (London, England : 1993) 2013 IMEx The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study. The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study. The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study. Structure (London, England : 1993) 2013 imex curation Francis DM., Kumar GS., Koveal D., Tortajada A., Page R., Peti W. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Francis DM., Kumar GS., Koveal D., Tortajada A., Page R., Peti W. DIP original experiment: DIP-255720X Structure (London, England : 1993) 2013 IMEx The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study. The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study. The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study. Structure (London, England : 1993) 2013 imex curation Francis DM., Kumar GS., Koveal D., Tortajada A., Page R., Peti W. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Francis DM., Kumar GS., Koveal D., Tortajada A., Page R., Peti W. DIP original experiment: DIP-255722X Structure (London, England : 1993) 2013 IMEx The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study. The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study. The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study. Structure (London, England : 1993) 2013 imex curation Francis DM., Kumar GS., Koveal D., Tortajada A., Page R., Peti W. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Francis DM., Kumar GS., Koveal D., Tortajada A., Page R., Peti W. DIP original experiment: DIP-255723X Structure (London, England : 1993) 2013 IMEx The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study. The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study. The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study. Structure (London, England : 1993) 2013 imex curation Francis DM., Kumar GS., Koveal D., Tortajada A., Page R., Peti W. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Francis DM., Kumar GS., Koveal D., Tortajada A., Page R., Peti W. DIP original experiment: DIP-255728X Structure (London, England : 1993) 2013 IMEx The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study. The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study. The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study. Structure (London, England : 1993) 2013 imex curation Francis DM., Kumar GS., Koveal D., Tortajada A., Page R., Peti W. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Francis DM., Kumar GS., Koveal D., Tortajada A., Page R., Peti W. DIP original experiment: DIP-255730X Structure (London, England : 1993) 2013 IMEx The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study. The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study. The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study. Structure (London, England : 1993) 2013 imex curation Francis DM., Kumar GS., Koveal D., Tortajada A., Page R., Peti W. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Francis DM., Kumar GS., Koveal D., Tortajada A., Page R., Peti W. DIP original experiment: DIP-255729X Structure (London, England : 1993) 2013 IMEx The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study. p54830-1 Tyrosine-protein phosphatase non-receptor type 5 Ptpn5 Neural-specific protein-tyrosine phosphatase Striatum-enriched protein-tyrosine phosphatase protein protein mouse Mus musculus Mouse MCCSERLLGLPQPVEMEAPDEAEGLPSKQKEMPPPPPPSPPSEPAQKLPPQGAGSHSLTVRSSLCLFAASQFLLACGVLWLSGHGHSWLQNTTDLISSSLTVLNHLGPVAWLGSGTWGIPSLLLVSLTVSLVIVTTLVWHLLKAPPEPPAPLPPEDRRQSVSRQPSFTYSEWMEEKVEDDFLDLDAVPETPVFDCVMDIKPETDPASLTVKSMGLQERRGSNVSLTLDMCTPGCNEEGFGYLVSPREESAHEYLLSASRVLRAEELHEKALDPFLLQAEFFEIPMNFVDPKEYDIPGLVRKNRYKTILPNPHSRVRLTSPDPEDPLSSYINANYIRGYSGEEKVYIATQGPIVSTVADFWRMVWQERTPIIVMITNIEEMNEKCTEYWPEEQVVHDGVEITVQKVIHTEDYRLRLISLRRGTEERSLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPHCSPIIVHCSAGIGRTGCFIATSICCQQLRREGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHAMSLYEKQLSLQSSE DIP protein P54830-1 original sequence version: 108 q16539-1 Mitogen-activated protein kinase 14 MAPK14 CSBP CSBP1 CSBP2 CSPB1 MXI2 SAPK2A Cytokine suppressive anti-inflammatory drug-binding protein MAP kinase MXI2 MAX-interacting protein 2 Mitogen-activated protein kinase p38 alpha Stress-activated protein kinase 2a protein protein human Homo sapiens Human MSQERPTFYRQELNKTIWEVPERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVIGLLDVFTPARSLEEFNDVYLVTHLMGADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTDDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRLVGTPGAELLKKISSESARNYIQSLTQMPKMNFANVFIGANPLAVDLLEKMLVLDSDKRITAAQALAHAYFAQYHDPDDEPVADPYDQSFESRDLLIDEWKSLTYDEVISFVPPPLDQEEMES DIP protein Q16539-1 original sequence version: 169 DIP protein Q16539 original sequence version: 138 DIP protein Q16539 original sequence version: 187 q15256-1 Receptor-type tyrosine-protein phosphatase R PTPRR ECPTP PTPRQ Ch-1PTPase NC-PTPCOM1 Protein-tyrosine phosphatase PCPTP1 protein protein human Homo sapiens Human MRRAVCFPALCLLLNLHAAGCFSGNNDHFLAINQKKSGKPVFIYKHSQDIEKSLDIAPQKIYRHSYHSSSEAQVSKRHQIVNSAFPRPAYDPSLNLLAMDGQDLEVENLPIPAANVIVVTLQMDVNKLNITLLRIFRQGVAAALGLLPQQVHINRLIGKKNSIELFVSPINRKTGISDALPSEEVLRSLNINVLHQSLSQFGITEVSPEKNVLQGQHEADKIWSKEGFYAVVIFLSIFVIIVTCLMILYRLKERFQLSLRQDKEKNQEIHLSPITLQPALSEAKTVHSMVQPEQAPKVLNVVVDPQGRGAPEIKATTATSVCPSPFKMKPIGLQERRGSNVSLTLDMSSLGNIEPFVSIPTPREKVAMEYLQSASRILTRSQLRDVVASSHLLQSEFMEIPMNFVDPKEIDIPRHGTKNRYKTILPNPLSRVCLRPKNVTDSLSTYINANYIRGYSGKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEKNEKCVLYWPEKRGIYGKVEVLVISVNECDNYTIRNLVLKQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRLASQGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHHALCLYESRLSAETVQ DIP protein Q15256-1 original sequence version: 132 mapk14-ptprr-2 7 15 unspecified role unspecified role unspecified role unspecified role Region 331-347 Region 331-347 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 14 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction mapk14-ptprr-3 8 15 unspecified role unspecified role unspecified role unspecified role Region 331-347 Region 331-347 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 14 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction mapk14-ptpn5-1 12 13 unspecified role unspecified role unspecified role unspecified role Region 214-539 Region 214-539 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 14 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction mapk14-ptpn5-2 1 13 unspecified role unspecified role unspecified role unspecified role Region 244-539 Region 244-539 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Region 214-539 Region 214-539 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 14 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction mapk14-ptprr-4 3 15 unspecified role unspecified role unspecified role unspecified role Region 332-655 Region 332-655 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 14 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction mapk14-ptpn5-3 5 13 unspecified role unspecified role unspecified role unspecified role Region 214-539 Region 214-539 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 14 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction mapk14-ptpn5-4 4 13 unspecified role unspecified role unspecified role unspecified role Region 214-539 Region 214-539 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P54830-1:p.[Phe274Ala;Phe281Ala] F274A/F281A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain F A certain certain sequence position certain certain certain sequence position certain F A This feature has been corrected as a result of our quality control procedures. The original label was 'F274A/F281A'. Wed May 02 15:07:18 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe274ala,phe281ala' Tue Jun 30 20:03:49 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Phe274Ala;Phe281Ala]' P54830-1:p.[Phe281Ala;Ile307Ala] F281A/I307A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain I A certain certain sequence position certain certain certain sequence position certain F A This feature has been corrected as a result of our quality control procedures. The original label was 'F281A/I307A'. Wed May 02 18:51:34 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe281ala,ile307ala' Tue Jun 30 16:36:49 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Phe281Ala;Ile307Ala]' ecolx Escherichia coli 14 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction mapk14-ptpn5-5 9 13 unspecified role unspecified role unspecified role unspecified role Region 213-229 Region 213-229 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Region 213-256 Region 213-256 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 14 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction mapk14-ptpn5-6 6 14 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 13 unspecified role unspecified role unspecified role unspecified role Region 213-229 Region 213-229 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Region 213-256 Region 213-256 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro direct interaction direct interaction mapk14-ptprr-5 11 15 unspecified role unspecified role unspecified role unspecified role Region 361-655 Region 361-655 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Region 332-373 Region 332-373 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 14 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction mapk14-ptprr-6 10 15 unspecified role unspecified role unspecified role unspecified role Region 332-655 Region 332-655 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 14 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction mapk14-ptprr-7 2 15 unspecified role unspecified role unspecified role unspecified role Region 332-655 Region 332-655 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Region 332-373 Region 332-373 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 14 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction