Gene
KWMTBOMO11870 Validated by peptides from experiments
Pre Gene Modal
BGIBMGA004414
Annotation
PREDICTED:_microtubule-actin_cross-linking_factor_1?_isoforms_1/2/3/5_[Amyelois_transitella]
Full name
Plectin
+ More
Dystonin
Microtubule-actin cross-linking factor 1, isoforms 1/2/3/5
Microtubule-actin cross-linking factor 1
Periplakin
Dystonin
Microtubule-actin cross-linking factor 1, isoforms 1/2/3/5
Microtubule-actin cross-linking factor 1
Periplakin
Alternative Name
Plectin-1
Plectin-6
300 kDa intermediate filament-associated protein
IFAP300
Hemidesmosomal protein 1
230 kDa bullous pemphigoid antigen
230/240 kDa bullous pemphigoid antigen
Bullous pemphigoid antigen 1
Dystonia musculorum protein
Hemidesmosomal plaque protein
Microtubule actin cross-linking factor 2
620 kDa actin-binding protein
Actin cross-linking family protein 7
Macrophin-1
Trabeculin-alpha
Actin cross-linking family 7
190 kDa paraneoplastic pemphigus antigen
195 kDa cornified envelope precursor protein
Plectin-6
300 kDa intermediate filament-associated protein
IFAP300
Hemidesmosomal protein 1
230 kDa bullous pemphigoid antigen
230/240 kDa bullous pemphigoid antigen
Bullous pemphigoid antigen 1
Dystonia musculorum protein
Hemidesmosomal plaque protein
Microtubule actin cross-linking factor 2
620 kDa actin-binding protein
Actin cross-linking family protein 7
Macrophin-1
Trabeculin-alpha
Actin cross-linking family 7
190 kDa paraneoplastic pemphigus antigen
195 kDa cornified envelope precursor protein
Location in the cell
Cytoplasmic Reliability : 1.472 Nuclear Reliability : 1.898
Sequence
CDS
ATGTACGGCAGCGGTTTCGCCCAGGCCGAGACACTGGGCACCGGCGCCGGAACGAACGCTGGCTTAGCCTGCGACACAGAGGGTGCCGAGGCTTTGATGTCTGGGCCGGAAGCTCGGAGGCGGGTGAATCCATCCGTCGATGAGACGGGGGCAAGGTCGACCTCCATCTCCGAGTCAGAGTCGGAGGACGAGCAGGCGGGCGCAGGTGACCTACGAGTAGGTGTTTTGGAGGGCGCGACGGAGGCCGCGGATGATCGCGCTGCTGGAATGGTGACCACGGCGGACGACGCAGCAGTTTTACTCGCCAGTATAGGCGACGCGGGAACGGCAGGCACGACGGAGGCTGCGGTGCTCGATGCAGAAGCTTTGCACGCAGGTACAGGCGACGCAGGAGCAGCGAGCGCGGCGGAGGACATCAAACAAACCGAAAGCGGTCTGGACAGCGTGGAGCGGCACATCGAGGGGGAGCTGCGTCGCGTGGAGCGCGGCGTGCACCCCGCCGACGCCAAGACCGCCGCCGAGCAGATCGAGCACGACCTGCGCGCCATGGAGCTCGCGCTGCACGAGATGTTCCAGGACGCGAACGCGCTCCGGGAGGGGAGGTACCCGCAAGCCAACGAGCTGCACAGGCGCGTGCAGCAACTCCAGGAGCGCTGGGCGCTGGCCCGACAGGCGCTGGCGAGCCGGCTGGTGCCGCGGCTGGCGGGCGTGCGCATGCCCGTGCAGCACACCACCGTGCGCCGCGAGACCCGCACCGTGCTGGAGACGCGCGTGCACGATGCCGACCCGCGCTTCCACCAGCTCGCCGACGCCGCCGCCTGGTGCCGGGACAAACTGAAAAAACTTCACGAATCAGAATACGGCTCCGACCTGCCGTCGGTGCTGCACGAGCTGGACAAACACCAGCGGGAACACAAACTGATCGACCAGTTCCATTCCAAGGTTGAACAGTGCGTCCACAACCGCTCCAACTTCAACGGCGAAGAGTTGAATTTGTACAACCAGCATCTGAGTCAGTTGCAAAAGTTATACGCCGAGCTACTGTCTACTAGTACTAAGCGGATGTCGGATCTGGACGCGTTACACGACTTCCTTCAATCAGCGACGGCGGAGTTGAACTGGCTCAACGAGAAGGAACAAGTGGAGTTGTCTCGCGACTGGGCCGACCCGCACATCAACCTGCCCGCCGTGCAGCACTATTACGAGCAACTCATGTCGTCCCTTGAGAAGCGGGAGCTCCAGTTCAGCAACGTGATCGACCGCGGCGAGGCGCTCATCGCGCAGCACCACCCCGCCACCAAGACCATCGAGAGCCACCTGCAGGTGATGCAGTCTCAATGGGCATGGGTGCTCCAGCTGACCCTCTGCTTGGAGACCCACTTGAAACACACCACGCAGTACCACACCTTCTTCGAGGAGATCAAAGAGGCGGAGAAATGGATCGCAAAACGCGAGGAAGCATTAAACACGACATTCTCCCAATCGGAGTTCACCTTGGACCAGGGGGAGAGGCTCCTCAAGGGCATGCAGGACCTTCGGGAAGAGCTGAACACGCACGGAGCCGCCGTGTCGCGTCTCGTCGAGGAGGCGCAGGAAGTCAGGCCCGTCAAGCTGCGGAGGGCGCCCGTCACCAGACCCATCAGGGCTGAGACCGTATGCGCGTACAAACACGCTAATGTGGCGATCGAGAAGGGCGCGTCGCTGTCGGTGGTGGACAACTCCGGGCGCAGCCGGTGGCGCGTGCGGCTGGGCGGCGCGGGCTCCGAGGCGCAGGTGCCGGGCGCCGTGCTGGCGCTGCCGCCGCCCTGCCGCGACGCGCTCGCCGCCGCCGACGCGCTGCGGGCACAGCTCGACCGGGTCATCCACCTGTGGCAGAGGAAGCAACTCCGAATGAGACAGAACATGATTTTCGCGACCATCAAAGTTGTGAAAGGCTGGGACTTCCCTCAGTTCGTGGCGATGGGAGCAGAGCAACGTCAGGCCATCCGCCGCGCCCTTAACGAGGACGCGGAGAAGCTGCTCGCCGAGGGAGACCCCGCCGACCCGCAGCTGAGGAGGCTGCGTCGGGAGATCGATGACGTCAACAGGCTGTTTGACGAGTTCGAGCGCAGAGCCAGAGCTGAGGAGGAATCCAAAAATGCAGCTCGCATCTTCACCGAACAATCCACCCACCTGCTGGAACGGCTGGAAGTGCTTGAACGACAGCTACACGAGAGGATCGCGAGCCACATCCCGAGAGACCTGGACTCTTTAGAACACCTGGTGCTCCAGCACAAAGACTGGGAGGGAAACCTGCACGCGCTCTCCGGAGATGTCGAAGAAGCGCAGTCTACATTCAGAGGCATAGCCCTCAAGACCCCAGCAATGAAGAAGAGTCTCGACAAAGTAATGGGCAAGTGGAACGACCTGCATTCAAAGAGTCAACTGTTTGTTGAAAGATTGAAATTCGTCGAGATCGTGGTGAACAGCGTGGAGGAGAACCACCAGGTCATATCCGAGTTTGAAATCAAATTGGCGCAGTTCAGTGACCTACCGAACGACATTGAAATTCTTAAAGACATCCACGAAGACCTGCTCCGCATGCAAGTGGCGGTGAGCAAGCAACAGATCCAGGTGGACCAGATGAACGACGACGCGGAGAACTGCCGGCGGCTCGTGCACGCCTCCCGGGACGCGCTGCCGCACTCCTCGCTGCCGCGCGCCGGCAAGCACCAGGACCTCGAGCGCCTGGACAAGGAGGTGGCGCAGCTCAACGCCAGGTGGAGCAACGTCTGCACTCAGCTGGCCGAGAGGCTTCGAAGTTGCGAGGCCGCCTACCAGCTGCTGCGCAACTACAACGCGGGACTCGAGAAGGAAGCCGAGTGGATCGACGACGCATACAAGCGGCTCCAAGCGCAGCCGCCCGTCGAAGTCAGGCCCAAAGAACAGTTCGAGCCCACCAGGAATCTGCTGACAAGCGTTGTGGAGAGGACGCCAAAGATTGAGAAGGTTAACGTGGACGGCGGACGATTCATACGTGAAGCGAAGATAAACTCGTCGAGATGCCAGCGTTACACGGAGTGGCTTTGTGAGGAGGTCCACCCGTCACTGGATGTCAGGCATTTGAGGCGCCAGGCCGACCTGGACCAGGCCGAGAGGATCCGGCGATTGGGCCGAGATATCGACCCCGACAGGATCCCGGTGGGGTCCGACGCTGTGGCCCGGGAATTGGATGAGCTGAATGCGAAGTACCAGAGGTTGCTGGACATGCTTTACGAGAGATTGAGGCGAATCGCTGCTGCCAATCCCGGAGACATTGTTACATTGCGCCTTGTGGAGGCAATGGCTCCTCGTTCGGCAAGATCCTTCCGGCAGGAGTTCAATATGCAAGACACGACCACAGAGCACACGTACACCTCACAATATACCACAGAAAAATACGTGAGAACCTCACATACTACGGAACTTGACGGTGAAGCACCGGTCAGATCAATGACCAATGGCAAATTAACATCTCCTAAGTACACAACAAAGACTATAATTACGGACGAAGACAGACCTGATGTTCGAAAGCTAAAACGCGTCCACAGAATGTATGAAGGTCCCAATATCATCGAATCGAGGGGTATAGTGCATCCCGAAACCAGAGAAATATTGACAGTGGGCCAGGCGATCAGTATGAGAATACTTGACGTTCGCACAGGAAGACTCCTGTCTTCGCCCGACACGAGACAGACTATAACGATTGAACAAGCAGCCAAAGAAGGTCTTATTGACCCTAAGCTAGCTGCGAGGCTCACTGGCCCGTGTGGAATGACCGAAGACGGAAACGAAGTCACTCTATTGGAAGCCATACAGCGAGAACTCTATGACGCTGAACAAGGATTGTCTGATCCAGCAGAAAAAAGGATCAAGGTAACTGTACAGGGCGAAGGGCCCGGAACCCAAGGAATGAGTATCTCGGACGCGGTCAGTCGAGGACAAGTCGACCTTGACAAAGGTCTCTATAGATTACCCAATGGAAGTTACATTTCCATCGCCGAAGCCTATCAAAGAGGGTACCTTATATACAACGAGATTATCAAAATCAAATCGAGCGCGCTGTGTCTGTCGGACGCGATAAGTCAAGACTTAGTAGATAACAACGGTTGGATCTTGGATAGGAATTCGGGCGACAAATTCCAAATAGACGTTGCTATACAAAATGAATTAATCAACCCTAACGTTAGGGAAATTCTTGATCCTAAAAACGACACAAAAATAACTCTTTCTGAATCTATCGAGAAGAATATAATTAACACTAAACATTCTAAATACGTGCACAATGTTACAAAAGAGAAGCTTAGTTTCAAGGAAGCGGCGTATAAACGTTACATTTGTAAACCTATGACCCTTAAAGACGTTTGCGATAACAATTTGATGACTAACGATGGTAAAATATTTTCCCTATCCAACAGAGTTCCATTGAATATATTAGAAGCTATATCGGTCGGTATTCTCGACAGCGACAATGTTAAATGTGTAACAGATACAACGACAGGTCAGCTACTTACTTTATCGGAGGCGATAGGAGCCAAAATAATTCTTCCGGATAATAAGTTTAGGGATAATCTGACCGATGAGATATGTACTATACCGGAAGCAGTCGACCGCGGTCTTATTACTTCTGTTTCGCAAAGATCCATTTTCGATATTGACGGTTTCAGAGATCCGAAATCAGGTGAATTCGTATCGTTCAATGCTGCTTTAAGCAAAGGCAACTTAAAATATGTAAATGGTGAAACTTTCTTGAAAGCAGAAAGTGGGGATTTCGTCTTTCTAGAAGACTGCACTAAAGTGTCTATAGTTCGACCTGAAGTTTTAGAAATGTTCAACAGAAAGATAGGTGTTTACGAAAACGGTAAGGAACTTAGCGTTTTAGATGCTGTGTTCAAAAATATTCTTGATCCTAAATCGGGACATTTACTGGAAGCGACCACTAAAAAACCTATTCCTTTCAATAAAGCTGTAGAGATCAATATGATAACGCCCGAAGGTGCGGCACTTTTGAATTCTTTGTTAAATATCACTCTTACTTTGCAAACAGTTACTAAAACAGTTAAACGCTATGTGACGGTGACTAATACGACTTCAACTCAACGTACTGAAACTCTAATCACATTTGCTGAAGCTATTAGACGTGGACTTATCGATGAAAACACTCAGACCTTTACCGACCCAACCACGGGCACCGTGATGCCAATACAGCAAGCTTTGGACGAAGGTTTATTAGGGGTTGAAAAGAACGAACCACGTGTCGTTCACATATCCGATCGAGTAGCTAAAAAAGATTTAGTACCGGGACAAGTAGTAGAATTAAAAATAACGAAAAAGTCGTTTATTAAAGATCTACCTTCTAGTCCCGAAAGTAAGGTTGAGCGCGATAGTCGACCAGAAACATTAAAAAGCCCTGAATACACAGTTCGTGAGGTTAGTCAACCGCGTGAAAGTGTAGTCCAAGAAATTAGGACGGTTACTTCAAAATCTGTTGTCACTGAACCTTCGGTAACCTCAATGACCATTAAGAAAAACACCATTGAATTGCCGAGAGGAGGGTGGACTTTAAATGAAGCTATACATCTTAACTTTTTCGACCCTACTACGGGTATGTTCGTTATTCCTGGTACTGACAGAGTTTTAGACCTTGAAGAAGCCCTTAAATTAAACCTAATTAATCCTGAATCCGCAAAAGTCATTGACCCCAAAACTCGTAAAGAAATGCCATTAGATAAAGCACTCGAATTACGTTTAATTGATCATGTCGGTCGTTATAAATATATCACTGAAACTATTACAATGTTACAAGCAATAGAAAGTAAATATATTGTATTTATTCACCTAACTCAATCGGTGTCATCTCAAAAAGTTATAACGATTACATCGGTAGCCGGTATGCCAGATAAAATGGAAATTTCGGAAATATCAGACGTGACCACGTATCCACGTGACCTCGAAATAGAGGAACAAGTGGCTTTAGAACCAGTACAAGTAGCACCTGGGGTTATATTTGATCCTGCCACAGCTTTAGTCATATCTACTCCTTCTGGAGTTTCAGAGAATATAATAGAAGCTGCTTATAATGGTACTGTCGCTCCTGACACTGTTAAAGTCATTGAACCTCAGACTAGGAAATTCATAACATTGCAGCAAGCCATTGCTAAACGTATTATTGATAGAAAAACAGGGGATTACATAGATAACTCAGGAAATAAATTTACTCTAGCAGATGCTGCAAAAGTAGGTTTGATAGCTGTTGTAGGTGCACCTTTAGTTGCGGCTTCTAAAGTTATTCAGGTTGTAAGGAGTACTATGGTAGTTGATCCACAAACGGGAGAAAAATTACCGATGGAGGTAGCATATGAAAGGGGCTTAGTTGACCCTGATACGTATAAGCGCTATGAAGAAGAAATTAGAGATAGGACGTTAGAAAGCGACAAACCAAGAAGCGAACATACAACAAAAACAGAGACAATCACGGTTACTCAAACAACAAAGACATCACCGGAGGGAGCCGCTACTGTTACAGTGGTGGTTGACCCAAATACCGGGGAAAGATTACCACTTGATGTAGCTTATGGAAGAGGCCTAATAGATCCCGTTTCATACAAAAAATACGTATTGTCGGTTAGTGATCAAAAACCAGGTTCCATTACTTATCATGATATTAAGTCACCTAGTACTAGCAAAGTAACTTTCAGCCAAGCACCTCAGAACTTTGAGACTGAACCCATAAATATATCGAATAGTAAAACAGTTACTGTTTCACATTCGACCACAAAACCAATATCAGTAGGTGCAGCTGTTTCTGAAGGATTCATTACAGTAGAATCAATTCAAAATAGTCTATCTGCTGATAACAGGCGAGTGATAACAACACAGGCATTAGACAAAAAAGACAAGCCGCCGGAAGTAATTCAAATTATTAAAGCTAATTTAAAACCCAAATACAAAGTCGCTGCTGTTAGAGAAAACACTCCTGATATCCCGATAGAGTCTAAACCCGTTATTCTTCAAAAATTAAGAAAACGTGTAGTAACACCTATGGAAGCTCTCGAGAAAGCCTTAGTCGATAAAGATACAGCAAATATTTTAGAGTTGGTTAAAGCTTATAAAGATGAGAACGGCCTTCCTATTAATCTAAAAAAAGCGATTGATATCGGGTTAGTTGATGAAAACGACGGTAAATTAGTAGATCCAGTACATGGTGATACTTTAACGATTAAAGTAGCGATAAATAGAGGAATCTTAGACGGTGAAGGTCAAGATGAAGTTCTGATACCGCTTGCAAGAAGTTTAACTATTCCCGAAGTTCTTGAACAAGGGTTACTCGATCCAGTAACAGGTAAGATTATACATCCCGAGACAGGTAGCCTTTTGACACTTAGAGAAGCTTTAATTTGTGATATCGTAGATCCATTGTCAAGTGTATCTATAGCACCGGGAAAGAAAATAACCTTAACCGATGCTATTACCAGAAATATGATAGATGATAGTAAAAATTTAATTAAAACTAATGATGGTTCCATGGATTTATTAACCGCTGTCAACGCTCAAGTCTTCTCTGATGTCCAAGTAATTAAAAAAGATGAAACAATACCTCCTGCAGCAATGACTCTTAATGTTGCTATTAAAAAGAATTTAATAAATCCTCATACAGGGGAAATAAAACACCCACTTACTGGTGAATTAATTTCACTTACTGATGCCATTAACAGAGACTTGATTATGGCAATACCTTACCCTCAAACGTCTGATACTATTATTTTAGAGGATGCTTTAGAAAAAGGTGCTATAAATCTTAAACAGGGTGTCTTCATTAATCCAGATACTAAGGAAATACTTCCAATTGACAAAGCTTTGGAACAAGGACTATTGGCCATTAAAACGAACCCAATAGCTATGGAAACAAGCGGTGTGGTAACTACTATTACTGAAACATTTACATCGCAGCATACAATTACAACAAAAATGATTGAACTTCTCGCTGATTATGTATTAATCAATGCGAATGAAATAAAAAACACTAGAACCGGTGAAATCATGACTATAGATGAAGCTCGTCTTAAAGGTATTGTGAGAGATGAACAAACCAGTAAGGAACAGTTTATTACATCTGATACCAATATTAATTTTGAAGATGCGCTAAGTCACGGCTATATCAACATTGAAACCGGCACTTTCACTCATCCTAATACTGGCGAAACTCTATCAATACCAGATGCAGTTACTTCGGGAGTATTAACTACAGAAATTAAGCCAGATTCTAGTGAGCCTTCTCTGAAGAAAAAAGAGTTAGAAATGCTAGATCTAAATGAAGCATTTGAACTTCTGTTTGATGAAAGAACGCAAAAATTCAAGGATCCCAAATCACCTCACAAACTAATATCATTCAAAGATGCTCTTGCTAAGAAAATTATAGATCCTGAATCTGTAATATACAATGTAGAGGCTGCTAAACCAGTTACTTTACAAGAAGCTGTAAAAATAGGGCTTATTGACATCAAAACAGGACAATTAAAAGAACCTAAAACAGGTAAATTGGTAGATATAAAGAAAGCTGCAAAAATTGGGCTAGTCGCTGTGATCGCAGCTCCTGTACTCGCTGGTATGGCAGTAGTACAGGGAGCTCAAGCGGTGAAAAGTAAATTGATGCAACCAAAGCAAGACAAGGTGTTTGAGGAACCAAGTAGAATTGTGTCCGCTGATAAAGCGACTGTTGACAAGGTTACAGAGCCTAAAAAAGTAATTCAACGTAATATTGAAGTAGAACCAAAAGTGAAAGATGCTAAAGTAAGTGTTAAGGATATTCCGTCGCGGCCTAGCATATCCGAGGATCCTAAGAAAGATGTCAGTAAAGAAAAACTAAAAACGGAAATTACTCCTACAGAAAAAAGGGAAATTGAAACTGAAACTGCCGTAGCATCATCAGCGGAAAAACAGGTTATAACTTCTGCCAACCAACCATCATCAATAACTACGAAGCCTGAACATCAGATAGCTACCTCAGTGCCAAGTAAAACTAGTATCAAGCACGAAGAGCAAGTTCTTGAATCATCTAAAGTGTTAGAAAAAAATATTATTGATCTCAAAGAAGTTGTTGAAACATGTCAAAAGGTCAAATACGGTACTAAACCTGAAAATGAGAAAACGCAAATGACAGTAACCGAGAAATTAACTACAGAACATATTAAACAAGCCCCCAAGCATGACAAACCAATTTCAGGACAAGAAATGGATATAGTGAAACAAAAAGATAGTCATGAATTAAATGACGAAGATACGGCGAAACAAAATCCTGAGCAGTCAACCCCAAGAGATGAAGGAACAAGAATTACAAAAACTACAATTACAAAAACAGATCCATCCAAGTCTTCATTACAGACGACTAGCACAATAACAGCTACTAAGACATCAACTGTGACAACAATAGAGGTCACTCAAAGTGCATCTTCATACAAGATCAGTCCTGAAGATTACGAATCTGAGGTCACTATTGAAGAAATTGATAGTGAACCTTACCAATCTTCACAAGTGCTTGATAAAGAATATACTACGGATGTTTCTAAAGATCGTTATGAAATAACAACTGAAGATGTATCTCCCAAAGACATAATCAAGTCTAAACCTATTGATGAAGCTTCTATAAAACAGAAATCACCCGAAGTAGAAACAAAAATAGCTGAACCTCCCAAAATTATCGAAGTGACCGAGGGTGTTATTTTTGATCCTAAAACATCTTTGGTTATTTCAGAAGCTATTGGAGTGTCTGGAGATTTGTTAGAAGCTGTAAATAAAGGTGTCGTTCCATCTCAGAATGTTAAAGTTGTAGATCCGAAAACAGGTGTTCAGATTTCACTCCCAGAAGCTATTAAAAAAGGTGTTGTCGACGAAAAAACTGGCAAAGTGAAAGACACAACAGGGAAAAAAATTAGTTTCGCAGATGCAGCGAAGTTGGGGCTTGTAGCCGTTGTGGGTGCACCTATTTACGCAGCATCTAAAGTAATTGAAATTGTTAAAAATGCAGTCGTAGTTGATCCTAAAACTGGAGAAAAATTGCCTATAGATCAAGCTCGTCAACGCGGCTTAATTGACTCACAGGCTTATGGCAAATATGAAGAGGTTATAAAAAGTAATACTTGTCAAGATATTACTACTTCTCAGGTTACTGAATATATCAAAACAGTAGTAGTCGTCGATCCGAAATCAGGCGAAAAATTATCCATAGATGATGCTTATCAGCGTGGACTTGTTGAACCCGATGTTTATGAAGAGTACAAAAAATCTGGGCAAATTGCAAATACTGAAGGATTAGTTTCTTCAACAGAAACTAGTCCTAAAAGGGAAATTTTGCAGCCAAGTTCGATTGACGAATCTTCTTTGATTATACGACAAGGTACTATGACCGTAACTGACATCGTCAAAACGGTCATTGTAGATCCTAAAACCGGTGAACAAGTAACTTTAGAGGAAGCCCTTAACCGTGGTTTAGTTAACCAAAAGGAGTATGACACATTACAAGATACTGCCAAATCTTATAGTCCACAAAATATAGTTGTATCAAAAACTTCAGAAACAAAATCATTCCTTATTGAAGATCCTAAATCAGGTAAGAAATTGAAATTAGACGAGGCACTTGAACAAGGTATAATTGACTCTGATACTTATGAAACATATGAAGATTCTTCTAAGTCGTACGATGTCAGAGATGTATATGTTATTGATCCTAAAACAAACGAGAAGTTACTATTAGAAGACGCTTTAAAACAGGGTGTCATTGACTCTGAGAGTTACGAGAAGCTTAAAGATAATACAGATCACCAACAAGTATCACATGAAACTAAAGTTATTAAAACCATTCTCATTAAAGATCCACAAACAGGTGAAAATATGTCTTTGGAGGAATCTTTAAATAGAGGTGTTATAGATAAAGACACATATATAAAATATAACGAAGTATTAAAATCTAACAATCCTGAAGATTTGATGCTTCTGCAACGTCTTAAGGATTTTGATATAACAGTCACCGAACAGATTGTACAACACCAAGTAATAACTAAAACTACAACCAAGGCTGGAGAAATAATAACAAGTAAAAAAATTGAATATGAACCGACCATTTCTATAGAACAAAAAGTCTCCGAGTTCGAAGGTCCAATTCAGACAGTTGTTAAGGACGGTAAGACCGTATCTGCCATGTTGATTGATGCCGAACGACAACCCTTAAGGGTAATTGATGAAATAACTGAACAAAATGTAACGAAAGAGAAACCGACTCCTGTTAAACCATTATATGAAAACGTAACGCTCATCGATGCTATTGCTCAAGGTAAAGTGGAGCCTAAAATTTGTAGGATTATCATAAACGGAGTTGAATCTCCACTTACTGTTCAAGACTCTCTTGAACAGGAACAGATAAGCCGATTTGTACAGGTTGATGTACTGTCTAAAAATTGTGTAGTGTTGAAAGAGACCAAACCCACTTACTGTGTCGCTATATCTCAAAGATTAACCCCAGAAGAATTATCAGAAATGGGCGTATATGATATTGAGAAAGGTATTTTCTTAAATCCTGAAACAGGGGCTAAGATATCCTTTGAAGAGTTGGTTTATAGCTTACAAATATTCGATCCCGAGGCTATATTAGTTAAAGATTTAAGTTCTAAATCGGACGATTACATTTCATTTGATGAAGCTATCGCTAGACCTATAATTGATAAAACCACAGGTCACATGGTCAATCCGAAAACCGGTAAACGCGTGCCCTTCTTAGAATGCGTTCAATTGCGATGGATTGTAGAGAAACCTGATGATGTTTCAATAACGGAACAGGTCACAATTGAATCCGCGCTAGAACAAGGATTATATAATGCTCAGACAGGTGTAATAAAAGATGTTAATACTGGTGCCTTAGTGCCTATAGGTGAAGCGGTGCAAAAAGGCTTGATAGATCATGAGTCTTTGTTAATCACCGTACCGCGAACTAATGAATTAGTAACTCTCTCAGACGCAATAGAGCGTGGTATACTCGAAATTCACGACGGGGTTATCACTATTATTGAGACGCAAGAAATCATTGAAATATCTGTTGCTATCCAACGCGGTTTGATTACTATCATCCGACGGGCTGTTTCTATTGAAGCAATTATAAAGAGCCAAATGTATGATTCCAAAACGGGAAAAGTTAAGGATATTTTGACTGATCAATTAATTACTGTACGCGACGCGGTAGATAGGAACATAGTTCATCCAACAATATCTGAAGTAAAAGATACGGGAACCGATAAATTCCTACCATTAGGAGATGCTCTTGATGTAAAACTCGTTGATCCAATAACAGGGAAATTAAAAGACAAAAAGACTGGTAAATACATTCCATTAGACGATGCATTAAATAAAGGATTGGTTGCTACTAAATCTGTTACTTTCACTTTGTTCGATATCATCGAATTAGGTTACTATACACCTGAAAATGGACAAATTCTAAATCCGATATCGGGTAAAATTATAACACTGAAGAAAGCTATTCACGAGAAACTTGTAGATCCTACCGAGATACAAATTAAAGATGATAAGTCAGAGGCAGTTGTATCGTTCGATAAAGCTGTACAGTCTGGCCTGATAGATCTTGAACAAGGAATAATCACGTCACCAGTTATGAACCTTAAAGATGCGTGTGATAAGGGTTATCTTCTTAGCGATAAAAAACCATGGACATTACAAGAAGGTCTCGTACAAGGATTTTACGATCCTGGAACGGGTCTTTTGACAATTAATAATATTACAATGACTTTAGAAGACGCTATCAAAATTGGTAATATAAATCCAGAAGCTTTGACTGTAAGAAATGCAATAACGGGGGAAATTATTTCATTGTCAGACGCTATCAAAGTAGGAATAATTGACTCTAAAGAAGGTAGGGTTAGAGATCCGGTTCACGGGGATAAAATATCCCTTACAGATGCCGCCGAACGTGGTTTAATTGTACCCGCCAAACGAAAATTAAGTTTGCCAGAAGCAGTATTTAAGGGTTTCTACGATCCAAAAACTGGTAAATTTTCACATCCTCAAAGTAAAGAGAAAGTGCCCACTGATAGGGCAATAAGGAAACGAATGATAGATCCTCAGTCAACTTTGGTACACTTTGCTGGTAAAGTAATTCCGTTTGAATTCGCAGTAGACAGAGGTATTGTAGATAGCAGAACAGGTACTATATTTGTAGGCGATGAAAAAATTGACTTCCGTGAAGCTTTTGAAAGGGGGGTTTTAGTTGAAGTTCGTAAACCTTTATCGCTCGTTGAAGCTATTGAAAAGGGTGTTTATAATGAAATATCTGGACTGTTTATGGATCCACAAACTGGTAAAAAGTACACTCTTACTGAAGCAATTAAACTTCATTTGATCGATCCTCATTCAGTGCACATTCAAGACAATAGATTAGGTAAATGGGACAAGTTGTCATTGCCAGAGTCCTTAGAAACAGGAGTCATAGATGATCAAAGTGGTAAGATCAGAAATATAAATAATGACAATGAAGAAATTTCTTTACGCAAAGCATTTGAAATCGGTCTCCTTGTTGATAGTAAAGCACCAATAAGCTTGCAAAGAGCATTGCATCAAGGACTTTACGATGATGCGACCGGTAAATTTATTGATCCAACTAGTAATCGTAAAATTACTCTTCATGAAGCTATTAGGAGGTCAGTCATTAGTCCGAAGTATCTATGCTACTTCGACAAAAAATCTGAAAAACCTTTGTCTCTTGGCGAGTGTTGCCGTAACGAAATTATTGATAGGAGAAGTGGCAAGTTCCACGAACCAGGTTCCGATGTCCAGATACCCTTATCTGAAGCCATGAGTCTAGGATTAATCGTGGATATTGAAAGTGCTGGCTTCACTTTGTACGACACATTAGCCATGAACATGTATAACATAACAGAATTAATATTTATTCATCCGGTAACGGAACGTAAAATAACACTTAATTTAGCAATAGCTGAAGAGCTCATAAATCCTGAAACTTCCTTGGTAAAACATATACCGTCTAGCAAATATATTAAATTGACTGAAGCCATCGAAAGCGGTATAGTAGACGATGAAAACAATATTTACGTTCTACCTAACGGCAATCAAATCAATTTGTTAGATGCTAAACATCGCGGCCTTGTGGTAACGACAAAGAAAAATCTTAGCCTAGAAGAAATAATTAGAAACGGCTTATTTAGAGCGGATAACGGCAAAATCGTTGATCCATGCACAAATGAATTCATTGATATAAATAAAGCTATCGACATTGGTCTCCTCAATCCGGAACTTACAGTTGTTAAAGATAGTTTTACGAATAAATACAAACCGCTTTTATTGGCTATTCAACAAGGTGATGTTGATGTTGCAAAAGGCAGGGTACTAGATACAAAAGCAAAGAAAACATTTAGCATTGACACTGCGTTCGATAAGGGTTTGCTCGTGACTGTTATACAGCCAATTACTTCTCAAACAATATCTAGAAAATTCGTGTCAGATAGTGCGGCCTATAAACAACCCATGCTTAGGGAATTTTCTCTTGATGAAGCTATCAAGTATGAATTTATTGATCCAGAAACGGCCGTCATAAAAGATCCCCATAAGAATAAATACATTCCACTTAACCTAGCTATTACTGAAGGTATTATTGACAAAAATGCGAAGGGATCTTTCGATACTCAGAATAGGTCGCGCACGCTTTGTTTCGTTTTTGAAAACGGTTTAATTGTGTACGTAAGAGAGCCTCTTACGTTCGAACAAGCGCTCGAAAAGGGTTACCTTAACGTTAGCACCGCTCGATTTACCGATCCATCCTCCAACGAAGTGCTCACGATTAAAGACGCAACCACACTTGGGTATATTGATGCAGACACAGCGCTCATCAAAGATAATCTCAAAAAGAGGCTAACTAAACTTCCGGAAGCTTTCCGTAAGGGTTTCATGGACGCTGAAAAAGGCAATATATTAGACACTGAGACCTCAAAACTTAATACATTATCTGCTGCAATCGAAAGCGGTCTACTCATGACGCCAAAGAAGAGCTTCACCTTAATCGAAACTCTAAATTTCGGTATCTACAATCCTACTACCGGTGCCTTGAACGATCCATTCATTACTACCAGCGTTATCGATAGAAAGAGGCTTAATTTAGACGAAGCGATCCAACAAGGAATCGTTGATCCGTCAAGCACAGTTGTCAAGGAACCGGAGACCGGAAAGATATTGCCATTGGTTCAAGCTATAGAACAAAGGTTGGTTGATCCCGTTGAAGGCAGACTCACGATTGATGCAAAGAAAGGGATCAGTCTTGATTTAGTCAAAGCCCTAAAGAAGGGGTATTTGCTGCCAGCAGAAACGAGGCAAGCAGTAGAAGAGAAATATAGGCTTTGCGACGACACCCTGTCGAAATTGCTCGAATGGATCGGCAATGTTGAGGACCGATTAGCCAACCAAGAGGCAGTAAAGGAAGATATCGATGAACTACGTAACCAGATAAATACATTGAAGTCGATCAAGGATGACCTTGAGGGTCACCAGCGTCAAGTATCCGCTTGCGCAGACCAGGCCAAGCAACTCCTCGTGTCCGGAGGCGACGTGCTTGCTCCACATGAGGTATGTTAA
Protein
MYGSGFAQAETLGTGAGTNAGLACDTEGAEALMSGPEARRRVNPSVDETGARSTSISESESEDEQAGAGDLRVGVLEGATEAADDRAAGMVTTADDAAVLLASIGDAGTAGTTEAAVLDAEALHAGTGDAGAASAAEDIKQTESGLDSVERHIEGELRRVERGVHPADAKTAAEQIEHDLRAMELALHEMFQDANALREGRYPQANELHRRVQQLQERWALARQALASRLVPRLAGVRMPVQHTTVRRETRTVLETRVHDADPRFHQLADAAAWCRDKLKKLHESEYGSDLPSVLHELDKHQREHKLIDQFHSKVEQCVHNRSNFNGEELNLYNQHLSQLQKLYAELLSTSTKRMSDLDALHDFLQSATAELNWLNEKEQVELSRDWADPHINLPAVQHYYEQLMSSLEKRELQFSNVIDRGEALIAQHHPATKTIESHLQVMQSQWAWVLQLTLCLETHLKHTTQYHTFFEEIKEAEKWIAKREEALNTTFSQSEFTLDQGERLLKGMQDLREELNTHGAAVSRLVEEAQEVRPVKLRRAPVTRPIRAETVCAYKHANVAIEKGASLSVVDNSGRSRWRVRLGGAGSEAQVPGAVLALPPPCRDALAAADALRAQLDRVIHLWQRKQLRMRQNMIFATIKVVKGWDFPQFVAMGAEQRQAIRRALNEDAEKLLAEGDPADPQLRRLRREIDDVNRLFDEFERRARAEEESKNAARIFTEQSTHLLERLEVLERQLHERIASHIPRDLDSLEHLVLQHKDWEGNLHALSGDVEEAQSTFRGIALKTPAMKKSLDKVMGKWNDLHSKSQLFVERLKFVEIVVNSVEENHQVISEFEIKLAQFSDLPNDIEILKDIHEDLLRMQVAVSKQQIQVDQMNDDAENCRRLVHASRDALPHSSLPRAGKHQDLERLDKEVAQLNARWSNVCTQLAERLRSCEAAYQLLRNYNAGLEKEAEWIDDAYKRLQAQPPVEVRPKEQFEPTRNLLTSVVERTPKIEKVNVDGGRFIREAKINSSRCQRYTEWLCEEVHPSLDVRHLRRQADLDQAERIRRLGRDIDPDRIPVGSDAVARELDELNAKYQRLLDMLYERLRRIAAANPGDIVTLRLVEAMAPRSARSFRQEFNMQDTTTEHTYTSQYTTEKYVRTSHTTELDGEAPVRSMTNGKLTSPKYTTKTIITDEDRPDVRKLKRVHRMYEGPNIIESRGIVHPETREILTVGQAISMRILDVRTGRLLSSPDTRQTITIEQAAKEGLIDPKLAARLTGPCGMTEDGNEVTLLEAIQRELYDAEQGLSDPAEKRIKVTVQGEGPGTQGMSISDAVSRGQVDLDKGLYRLPNGSYISIAEAYQRGYLIYNEIIKIKSSALCLSDAISQDLVDNNGWILDRNSGDKFQIDVAIQNELINPNVREILDPKNDTKITLSESIEKNIINTKHSKYVHNVTKEKLSFKEAAYKRYICKPMTLKDVCDNNLMTNDGKIFSLSNRVPLNILEAISVGILDSDNVKCVTDTTTGQLLTLSEAIGAKIILPDNKFRDNLTDEICTIPEAVDRGLITSVSQRSIFDIDGFRDPKSGEFVSFNAALSKGNLKYVNGETFLKAESGDFVFLEDCTKVSIVRPEVLEMFNRKIGVYENGKELSVLDAVFKNILDPKSGHLLEATTKKPIPFNKAVEINMITPEGAALLNSLLNITLTLQTVTKTVKRYVTVTNTTSTQRTETLITFAEAIRRGLIDENTQTFTDPTTGTVMPIQQALDEGLLGVEKNEPRVVHISDRVAKKDLVPGQVVELKITKKSFIKDLPSSPESKVERDSRPETLKSPEYTVREVSQPRESVVQEIRTVTSKSVVTEPSVTSMTIKKNTIELPRGGWTLNEAIHLNFFDPTTGMFVIPGTDRVLDLEEALKLNLINPESAKVIDPKTRKEMPLDKALELRLIDHVGRYKYITETITMLQAIESKYIVFIHLTQSVSSQKVITITSVAGMPDKMEISEISDVTTYPRDLEIEEQVALEPVQVAPGVIFDPATALVISTPSGVSENIIEAAYNGTVAPDTVKVIEPQTRKFITLQQAIAKRIIDRKTGDYIDNSGNKFTLADAAKVGLIAVVGAPLVAASKVIQVVRSTMVVDPQTGEKLPMEVAYERGLVDPDTYKRYEEEIRDRTLESDKPRSEHTTKTETITVTQTTKTSPEGAATVTVVVDPNTGERLPLDVAYGRGLIDPVSYKKYVLSVSDQKPGSITYHDIKSPSTSKVTFSQAPQNFETEPINISNSKTVTVSHSTTKPISVGAAVSEGFITVESIQNSLSADNRRVITTQALDKKDKPPEVIQIIKANLKPKYKVAAVRENTPDIPIESKPVILQKLRKRVVTPMEALEKALVDKDTANILELVKAYKDENGLPINLKKAIDIGLVDENDGKLVDPVHGDTLTIKVAINRGILDGEGQDEVLIPLARSLTIPEVLEQGLLDPVTGKIIHPETGSLLTLREALICDIVDPLSSVSIAPGKKITLTDAITRNMIDDSKNLIKTNDGSMDLLTAVNAQVFSDVQVIKKDETIPPAAMTLNVAIKKNLINPHTGEIKHPLTGELISLTDAINRDLIMAIPYPQTSDTIILEDALEKGAINLKQGVFINPDTKEILPIDKALEQGLLAIKTNPIAMETSGVVTTITETFTSQHTITTKMIELLADYVLINANEIKNTRTGEIMTIDEARLKGIVRDEQTSKEQFITSDTNINFEDALSHGYINIETGTFTHPNTGETLSIPDAVTSGVLTTEIKPDSSEPSLKKKELEMLDLNEAFELLFDERTQKFKDPKSPHKLISFKDALAKKIIDPESVIYNVEAAKPVTLQEAVKIGLIDIKTGQLKEPKTGKLVDIKKAAKIGLVAVIAAPVLAGMAVVQGAQAVKSKLMQPKQDKVFEEPSRIVSADKATVDKVTEPKKVIQRNIEVEPKVKDAKVSVKDIPSRPSISEDPKKDVSKEKLKTEITPTEKREIETETAVASSAEKQVITSANQPSSITTKPEHQIATSVPSKTSIKHEEQVLESSKVLEKNIIDLKEVVETCQKVKYGTKPENEKTQMTVTEKLTTEHIKQAPKHDKPISGQEMDIVKQKDSHELNDEDTAKQNPEQSTPRDEGTRITKTTITKTDPSKSSLQTTSTITATKTSTVTTIEVTQSASSYKISPEDYESEVTIEEIDSEPYQSSQVLDKEYTTDVSKDRYEITTEDVSPKDIIKSKPIDEASIKQKSPEVETKIAEPPKIIEVTEGVIFDPKTSLVISEAIGVSGDLLEAVNKGVVPSQNVKVVDPKTGVQISLPEAIKKGVVDEKTGKVKDTTGKKISFADAAKLGLVAVVGAPIYAASKVIEIVKNAVVVDPKTGEKLPIDQARQRGLIDSQAYGKYEEVIKSNTCQDITTSQVTEYIKTVVVVDPKSGEKLSIDDAYQRGLVEPDVYEEYKKSGQIANTEGLVSSTETSPKREILQPSSIDESSLIIRQGTMTVTDIVKTVIVDPKTGEQVTLEEALNRGLVNQKEYDTLQDTAKSYSPQNIVVSKTSETKSFLIEDPKSGKKLKLDEALEQGIIDSDTYETYEDSSKSYDVRDVYVIDPKTNEKLLLEDALKQGVIDSESYEKLKDNTDHQQVSHETKVIKTILIKDPQTGENMSLEESLNRGVIDKDTYIKYNEVLKSNNPEDLMLLQRLKDFDITVTEQIVQHQVITKTTTKAGEIITSKKIEYEPTISIEQKVSEFEGPIQTVVKDGKTVSAMLIDAERQPLRVIDEITEQNVTKEKPTPVKPLYENVTLIDAIAQGKVEPKICRIIINGVESPLTVQDSLEQEQISRFVQVDVLSKNCVVLKETKPTYCVAISQRLTPEELSEMGVYDIEKGIFLNPETGAKISFEELVYSLQIFDPEAILVKDLSSKSDDYISFDEAIARPIIDKTTGHMVNPKTGKRVPFLECVQLRWIVEKPDDVSITEQVTIESALEQGLYNAQTGVIKDVNTGALVPIGEAVQKGLIDHESLLITVPRTNELVTLSDAIERGILEIHDGVITIIETQEIIEISVAIQRGLITIIRRAVSIEAIIKSQMYDSKTGKVKDILTDQLITVRDAVDRNIVHPTISEVKDTGTDKFLPLGDALDVKLVDPITGKLKDKKTGKYIPLDDALNKGLVATKSVTFTLFDIIELGYYTPENGQILNPISGKIITLKKAIHEKLVDPTEIQIKDDKSEAVVSFDKAVQSGLIDLEQGIITSPVMNLKDACDKGYLLSDKKPWTLQEGLVQGFYDPGTGLLTINNITMTLEDAIKIGNINPEALTVRNAITGEIISLSDAIKVGIIDSKEGRVRDPVHGDKISLTDAAERGLIVPAKRKLSLPEAVFKGFYDPKTGKFSHPQSKEKVPTDRAIRKRMIDPQSTLVHFAGKVIPFEFAVDRGIVDSRTGTIFVGDEKIDFREAFERGVLVEVRKPLSLVEAIEKGVYNEISGLFMDPQTGKKYTLTEAIKLHLIDPHSVHIQDNRLGKWDKLSLPESLETGVIDDQSGKIRNINNDNEEISLRKAFEIGLLVDSKAPISLQRALHQGLYDDATGKFIDPTSNRKITLHEAIRRSVISPKYLCYFDKKSEKPLSLGECCRNEIIDRRSGKFHEPGSDVQIPLSEAMSLGLIVDIESAGFTLYDTLAMNMYNITELIFIHPVTERKITLNLAIAEELINPETSLVKHIPSSKYIKLTEAIESGIVDDENNIYVLPNGNQINLLDAKHRGLVVTTKKNLSLEEIIRNGLFRADNGKIVDPCTNEFIDINKAIDIGLLNPELTVVKDSFTNKYKPLLLAIQQGDVDVAKGRVLDTKAKKTFSIDTAFDKGLLVTVIQPITSQTISRKFVSDSAAYKQPMLREFSLDEAIKYEFIDPETAVIKDPHKNKYIPLNLAITEGIIDKNAKGSFDTQNRSRTLCFVFENGLIVYVREPLTFEQALEKGYLNVSTARFTDPSSNEVLTIKDATTLGYIDADTALIKDNLKKRLTKLPEAFRKGFMDAEKGNILDTETSKLNTLSAAIESGLLMTPKKSFTLIETLNFGIYNPTTGALNDPFITTSVIDRKRLNLDEAIQQGIVDPSSTVVKEPETGKILPLVQAIEQRLVDPVEGRLTIDAKKGISLDLVKALKKGYLLPAETRQAVEEKYRLCDDTLSKLLEWIGNVEDRLANQEAVKEDIDELRNQINTLKSIKDDLEGHQRQVSACADQAKQLLVSGGDVLAPHEVC
Summary
Description
Interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. Could also bind muscle proteins such as actin to membrane complexes in muscle. May be involved not only in the filaments network, but also in the regulation of their dynamics. Structural component of muscle. Isoform 9 plays a major role in the maintenance of myofiber integrity.
Cytoskeletal linker protein. Acts as an integrator of intermediate filaments, actin and microtubule cytoskeleton networks. Required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. The proteins may self-aggregate to form filaments or a two-dimensional mesh. Regulates the organization and stability of the microtubule network of sensory neurons to allow axonal transport. Mediates docking of the dynein/dynactin motor complex to vesicle cargos for retrograde axonal transport through its interaction with TMEM108 and DCTN1 (By similarity).
Isoform 6: required for bundling actin filaments around the nucleus.
Cytoskeletal linker protein. Acts as an integrator of intermediate filaments, actin and microtubule cytoskeleton networks. Required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. The proteins may self-aggregate to form filaments or a two-dimensional mesh. Regulates the organization and stability of the microtubule network of sensory neurons to allow axonal transport. Mediates docking of the dynein/dynactin motor complex to vesicle cargos for retrograde axonal transport through its interaction with TMEM108 and DCTN1.
Isoform 2: F-actin-binding protein which plays a role in cross-linking actin to other cytoskeletal proteins and also binds to microtubules (PubMed:15265687, PubMed:20937854). Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex (PubMed:20937854). Acts as a positive regulator of Wnt receptor signaling pathway and is involved in the translocation of AXIN1 and its associated complex (composed of APC, CTNNB1 and GSK3B) from the cytoplasm to the cell membrane (By similarity). Has actin-regulated ATPase activity and is essential for controlling focal adhesions (FAs) assembly and dynamics (By similarity). Interaction with CAMSAP3 at the minus ends of non-centrosomal microtubules tethers microtubules minus-ends to actin filaments, regulating focal adhesion size and cell migration (PubMed:27693509). May play role in delivery of transport vesicles containing GPI-linked proteins from the trans-Golgi network through its interaction with GOLGA4 (PubMed:15265687). Plays a key role in wound healing and epidermal cell migration (By similarity). Required for efficient upward migration of bulge cells in response to wounding and this function is primarily rooted in its ability to coordinate microtubule dynamics and polarize hair follicle stem cells (By similarity).
Isoform 2: F-actin-binding protein which plays a role in cross-linking actin to other cytoskeletal proteins and also binds to microtubules (PubMed:16815997, PubMed:18854161, PubMed:21295697). Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex (By similarity). Acts as a positive regulator of Wnt receptor signaling pathway and is involved in the translocation of AXIN1 and its associated complex (composed of APC, CTNNB1 and GSK3B) from the cytoplasm to the cell membrane (PubMed:16815997). Has actin-regulated ATPase activity and is essential for controlling focal adhesions (FAs) assembly and dynamics (PubMed:18854161). Interaction with CAMSAP3 at the minus ends of non-centrosomal microtubules tethers microtubules minus-ends to actin filaments, regulating focal adhesion size and cell migration (By similarity). May play role in delivery of transport vesicles containing GPI-linked proteins from the trans-Golgi network through its interaction with GOLGA4 (By similarity). Plays a key role in wound healing and epidermal cell migration (PubMed:21295697). Required for efficient upward migration of bulge cells in response to wounding and this function is primarily rooted in its ability to coordinate microtubule dynamics and polarize hair follicle stem cells (PubMed:21295697).
F-actin-binding protein which plays a role in cross-linking actin to other cytoskeletal proteins and also binds to microtubules. Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex (By similarity). Acts as a positive regulator of Wnt receptor signaling pathway and is involved in the translocation of AXIN1 and its associated complex (composed of APC, CTNNB1 and GSK3B) from the cytoplasm to the cell membrane (By similarity). Has actin-regulated ATPase activity and is essential for controlling focal adhesions (FAs) assembly and dynamics (By similarity). Interaction with CAMSAP3 at the minus ends of non-centrosomal microtubules tethers microtubules minus-ends to actin filaments, regulating focal adhesion size and cell migration (By similarity). May play role in delivery of transport vesicles containing GPI-linked proteins from the trans-Golgi network through its interaction with GOLGA4 (By similarity). Plays a key role in wound healing and epidermal cell migration (By similarity). Required for efficient upward migration of bulge cells in response to wounding and this function is primarily rooted in its ability to coordinate microtubule dynamics and polarize hair follicle stem cells (By similarity).
Component of the cornified envelope of keratinocytes. May link the cornified envelope to desmosomes and intermediate filaments. May act as a localization signal in PKB/AKT-mediated signaling.
Cytoskeletal linker protein. Acts as an integrator of intermediate filaments, actin and microtubule cytoskeleton networks. Required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. The proteins may self-aggregate to form filaments or a two-dimensional mesh. Regulates the organization and stability of the microtubule network of sensory neurons to allow axonal transport. Mediates docking of the dynein/dynactin motor complex to vesicle cargos for retrograde axonal transport through its interaction with TMEM108 and DCTN1 (By similarity).
Isoform 6: required for bundling actin filaments around the nucleus.
Cytoskeletal linker protein. Acts as an integrator of intermediate filaments, actin and microtubule cytoskeleton networks. Required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. The proteins may self-aggregate to form filaments or a two-dimensional mesh. Regulates the organization and stability of the microtubule network of sensory neurons to allow axonal transport. Mediates docking of the dynein/dynactin motor complex to vesicle cargos for retrograde axonal transport through its interaction with TMEM108 and DCTN1.
Isoform 2: F-actin-binding protein which plays a role in cross-linking actin to other cytoskeletal proteins and also binds to microtubules (PubMed:15265687, PubMed:20937854). Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex (PubMed:20937854). Acts as a positive regulator of Wnt receptor signaling pathway and is involved in the translocation of AXIN1 and its associated complex (composed of APC, CTNNB1 and GSK3B) from the cytoplasm to the cell membrane (By similarity). Has actin-regulated ATPase activity and is essential for controlling focal adhesions (FAs) assembly and dynamics (By similarity). Interaction with CAMSAP3 at the minus ends of non-centrosomal microtubules tethers microtubules minus-ends to actin filaments, regulating focal adhesion size and cell migration (PubMed:27693509). May play role in delivery of transport vesicles containing GPI-linked proteins from the trans-Golgi network through its interaction with GOLGA4 (PubMed:15265687). Plays a key role in wound healing and epidermal cell migration (By similarity). Required for efficient upward migration of bulge cells in response to wounding and this function is primarily rooted in its ability to coordinate microtubule dynamics and polarize hair follicle stem cells (By similarity).
Isoform 2: F-actin-binding protein which plays a role in cross-linking actin to other cytoskeletal proteins and also binds to microtubules (PubMed:16815997, PubMed:18854161, PubMed:21295697). Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex (By similarity). Acts as a positive regulator of Wnt receptor signaling pathway and is involved in the translocation of AXIN1 and its associated complex (composed of APC, CTNNB1 and GSK3B) from the cytoplasm to the cell membrane (PubMed:16815997). Has actin-regulated ATPase activity and is essential for controlling focal adhesions (FAs) assembly and dynamics (PubMed:18854161). Interaction with CAMSAP3 at the minus ends of non-centrosomal microtubules tethers microtubules minus-ends to actin filaments, regulating focal adhesion size and cell migration (By similarity). May play role in delivery of transport vesicles containing GPI-linked proteins from the trans-Golgi network through its interaction with GOLGA4 (By similarity). Plays a key role in wound healing and epidermal cell migration (PubMed:21295697). Required for efficient upward migration of bulge cells in response to wounding and this function is primarily rooted in its ability to coordinate microtubule dynamics and polarize hair follicle stem cells (PubMed:21295697).
F-actin-binding protein which plays a role in cross-linking actin to other cytoskeletal proteins and also binds to microtubules. Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex (By similarity). Acts as a positive regulator of Wnt receptor signaling pathway and is involved in the translocation of AXIN1 and its associated complex (composed of APC, CTNNB1 and GSK3B) from the cytoplasm to the cell membrane (By similarity). Has actin-regulated ATPase activity and is essential for controlling focal adhesions (FAs) assembly and dynamics (By similarity). Interaction with CAMSAP3 at the minus ends of non-centrosomal microtubules tethers microtubules minus-ends to actin filaments, regulating focal adhesion size and cell migration (By similarity). May play role in delivery of transport vesicles containing GPI-linked proteins from the trans-Golgi network through its interaction with GOLGA4 (By similarity). Plays a key role in wound healing and epidermal cell migration (By similarity). Required for efficient upward migration of bulge cells in response to wounding and this function is primarily rooted in its ability to coordinate microtubule dynamics and polarize hair follicle stem cells (By similarity).
Component of the cornified envelope of keratinocytes. May link the cornified envelope to desmosomes and intermediate filaments. May act as a localization signal in PKB/AKT-mediated signaling.
Subunit
Homodimer or homotetramer (By similarity). Interacts (via actin-binding domain) with SYNE3 (PubMed:16330710). Interacts (via calponin-homology (CH) 1 domain) with VIM (via rod region) (PubMed:15128297). Interacts (via N-terminus) with DST isoform 2 (via N-terminus) (PubMed:19932097). Interacts with FER (PubMed:12200133). Interacts with TOR1A (PubMed:18827015). Interacts with ANK3 (By similarity). Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin (PubMed:21745462).
Homodimer or homotetramer (By similarity). Interacts (via actin-binding domain) with SYNE3. Interacts (via calponin-homology (CH) 1 domain) with VIM (via rod region). Interacts (via N-terminus) with DST isoform 2 (via N-terminus). Interacts with FER. Interacts with TOR1A (By similarity). Interacts with ANK3 (By similarity). Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin (By similarity).
Homodimer or homotetramer (By similarity). Interacts (via actin-binding domain) with SYNE3. Interacts (via calponin-homology (CH) 1 domain) with VIM (via rod region). Interacts (via N-terminus) with DST isoform 2 (via N-terminus). Interacts with FER. Interacts with TOR1A (By similarity). Interacts with ANK3 (PubMed:21223964). Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin (By similarity).
Homodimer or homotetramer. Interacts (via actin-binding domain) with SYNE3. Interacts (via calponin-homology (CH) 1 domain) with VIM (via rod region) (By similarity). Interacts (via N-terminus) with DST isoform 2 (via N-terminus) (PubMed:19932097). Interacts with FER. Interacts with TOR1A (PubMed:18827015). Interacts with ANK3 (PubMed:21223964). Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin (By similarity). Interacts with COL17A1 (PubMed:12482924).
Homodimer. Isoform 1 interacts (via N-terminus) with PLEC (via N-terminus). Interacts with the neuronal intermediate filament protein, PRPH. Interacts with DES. Interacts with SYNE3 (By similarity). Isoform 1 and isoform 6 can homodimerize (via N-terminus). Isoform 1 interacts (via N-terminus) with ACTN2. Isoform 1 interacts (via N-terminus) with PLEC (via N-terminus). Isoform 3 interacts (via N-terminus) with COL17A1 (via cytoplasmic region). Isoform 3 interacts (via N-terminus) with ITGB4 isoform beta-4a (via cytoplasmic region). Isoform 3 interacts (via N-terminus) with ERBIN (via C-terminus). Isoform 3 associates (via C-terminal) with KRT5-KRT14 (via rod region) intermediate filaments of keratins. Interacts with MAPRE1; probably required for targeting to the growing microtubule plus ends. Interacts with TMIGD2. Isoform 9 interacts with TMEM108 (By similarity).
Homodimer. Interacts with MAPRE1; probably required for targeting to the growing microtubule plus ends. Isoform 2 interacts (via N-terminus) with ACTN2. Isoform 2 interacts (via N-terminus) with PLEC (via N-terminus). Isoform 5 interacts (via N-terminus) with COL17A1 (via cytoplasmic region). Isoform 5 interacts (via N-terminus) with ITGB4 isoform beta-4a (via cytoplasmic region). Isoform 5 interacts (via N-terminus) with ERBIN (via C-terminus). Isoform 5 associates (via C-terminal) with KRT5-KRT14 (via rod region) intermediate filaments of keratins (By similarity). Isoform 2 and isoform 6 can homodimerize (via N-terminus). Isoform 2 interacts (via N-terminus) with PLEC (via N-terminus). Interacts with the neuronal intermediate filament protein, PRPH. Interacts with DES. Interacts with SYNE3. Isoform 1 interacts with TMEM108 (PubMed:17287360).
Isoform 2: Interacts with MAPRE1, CLASP1, CLASP2, AXIN1 and LRP6 (By similarity). Isoform 2: Found in a complex composed of MACF1, APC, AXIN1, CTNNB1 and GSK3B (By similarity). Isoform 2: Interacts with GOLGA4 (PubMed:15265687). Isoform 2: Interacts with CAMSAP3 (PubMed:27693509, PubMed:27802168).
Isoform 2: Interacts with AXIN1, LRP6 and GOLGA4 (By similarity). Isoform 2: Found in a complex composed of MACF1, APC, AXIN1, CTNNB1 and GSK3B (By similarity). Isoform 2: Interacts with MAPRE1, CLASP1 AND CLASP2 (PubMed:18854161). Isoform 2: Interacts with CAMSAP3.
Interacts with MAPRE1, CLASP1, CLASP2 and GOLGA4 (By similarity). Interacts with AXIN1 and LRP6 (PubMed:16815997). Found in a complex composed of MACF1, APC; AXIN1, CTNNB1 and GSK3B (PubMed:16815997). Interacts with CAMSAP3 (By similarity).
Homodimer or a heterodimer with EVPL. Interacts with PPHLN1 and VIM. Binds to the PH domain of AKT1. Interacts with FCGR1A.
Homodimer or a heterodimer with EVPL. Interacts with PPHLN1 and VIM. Binds to the PH domain of AKT1. Interacts with FCGR1A (By similarity).
Homodimer or homotetramer (By similarity). Interacts (via actin-binding domain) with SYNE3. Interacts (via calponin-homology (CH) 1 domain) with VIM (via rod region). Interacts (via N-terminus) with DST isoform 2 (via N-terminus). Interacts with FER. Interacts with TOR1A (By similarity). Interacts with ANK3 (By similarity). Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin (By similarity).
Homodimer or homotetramer (By similarity). Interacts (via actin-binding domain) with SYNE3. Interacts (via calponin-homology (CH) 1 domain) with VIM (via rod region). Interacts (via N-terminus) with DST isoform 2 (via N-terminus). Interacts with FER. Interacts with TOR1A (By similarity). Interacts with ANK3 (PubMed:21223964). Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin (By similarity).
Homodimer or homotetramer. Interacts (via actin-binding domain) with SYNE3. Interacts (via calponin-homology (CH) 1 domain) with VIM (via rod region) (By similarity). Interacts (via N-terminus) with DST isoform 2 (via N-terminus) (PubMed:19932097). Interacts with FER. Interacts with TOR1A (PubMed:18827015). Interacts with ANK3 (PubMed:21223964). Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin (By similarity). Interacts with COL17A1 (PubMed:12482924).
Homodimer. Isoform 1 interacts (via N-terminus) with PLEC (via N-terminus). Interacts with the neuronal intermediate filament protein, PRPH. Interacts with DES. Interacts with SYNE3 (By similarity). Isoform 1 and isoform 6 can homodimerize (via N-terminus). Isoform 1 interacts (via N-terminus) with ACTN2. Isoform 1 interacts (via N-terminus) with PLEC (via N-terminus). Isoform 3 interacts (via N-terminus) with COL17A1 (via cytoplasmic region). Isoform 3 interacts (via N-terminus) with ITGB4 isoform beta-4a (via cytoplasmic region). Isoform 3 interacts (via N-terminus) with ERBIN (via C-terminus). Isoform 3 associates (via C-terminal) with KRT5-KRT14 (via rod region) intermediate filaments of keratins. Interacts with MAPRE1; probably required for targeting to the growing microtubule plus ends. Interacts with TMIGD2. Isoform 9 interacts with TMEM108 (By similarity).
Homodimer. Interacts with MAPRE1; probably required for targeting to the growing microtubule plus ends. Isoform 2 interacts (via N-terminus) with ACTN2. Isoform 2 interacts (via N-terminus) with PLEC (via N-terminus). Isoform 5 interacts (via N-terminus) with COL17A1 (via cytoplasmic region). Isoform 5 interacts (via N-terminus) with ITGB4 isoform beta-4a (via cytoplasmic region). Isoform 5 interacts (via N-terminus) with ERBIN (via C-terminus). Isoform 5 associates (via C-terminal) with KRT5-KRT14 (via rod region) intermediate filaments of keratins (By similarity). Isoform 2 and isoform 6 can homodimerize (via N-terminus). Isoform 2 interacts (via N-terminus) with PLEC (via N-terminus). Interacts with the neuronal intermediate filament protein, PRPH. Interacts with DES. Interacts with SYNE3. Isoform 1 interacts with TMEM108 (PubMed:17287360).
Isoform 2: Interacts with MAPRE1, CLASP1, CLASP2, AXIN1 and LRP6 (By similarity). Isoform 2: Found in a complex composed of MACF1, APC, AXIN1, CTNNB1 and GSK3B (By similarity). Isoform 2: Interacts with GOLGA4 (PubMed:15265687). Isoform 2: Interacts with CAMSAP3 (PubMed:27693509, PubMed:27802168).
Isoform 2: Interacts with AXIN1, LRP6 and GOLGA4 (By similarity). Isoform 2: Found in a complex composed of MACF1, APC, AXIN1, CTNNB1 and GSK3B (By similarity). Isoform 2: Interacts with MAPRE1, CLASP1 AND CLASP2 (PubMed:18854161). Isoform 2: Interacts with CAMSAP3.
Interacts with MAPRE1, CLASP1, CLASP2 and GOLGA4 (By similarity). Interacts with AXIN1 and LRP6 (PubMed:16815997). Found in a complex composed of MACF1, APC; AXIN1, CTNNB1 and GSK3B (PubMed:16815997). Interacts with CAMSAP3 (By similarity).
Homodimer or a heterodimer with EVPL. Interacts with PPHLN1 and VIM. Binds to the PH domain of AKT1. Interacts with FCGR1A.
Homodimer or a heterodimer with EVPL. Interacts with PPHLN1 and VIM. Binds to the PH domain of AKT1. Interacts with FCGR1A (By similarity).
Similarity
Belongs to the plakin or cytolinker family.
Keywords
3D-structure
Acetylation
Actin-binding
Alternative splicing
Cell junction
Coiled coil
Complete proteome
Cytoplasm
Cytoskeleton
Direct protein sequencing
Methylation
Phosphoprotein
Reference proteome
Repeat
SH3 domain
Disease mutation
Epidermolysis bullosa
Limb-girdle muscular dystrophy
Polymorphism
Alternative promoter usage
Calcium
Cell adhesion
Cell membrane
Cell projection
Endoplasmic reticulum
Intermediate filament
Isopeptide bond
Lipoprotein
Membrane
Metal-binding
Microtubule
Muscle protein
Neurodegeneration
Neuropathy
Nucleus
Palmitate
Transmembrane
Ubl conjugation
Myristate
Golgi apparatus
Leucine-rich repeat
Wnt signaling pathway
Keratinization
Mitochondrion
Feature
chain Plectin
splice variant In isoform PLEC-1H.
sequence variant In dbSNP:rs200335928.
splice variant In isoform PLEC-1H.
sequence variant In dbSNP:rs200335928.
Uniprot
Pubmed
14672974
19468303
10556294
16141072
12200133
16330710
+ More
15592455 16452087 17947660 17114649 17208939 17242355 18827015 18630941 19144319 19131326 21183079 19932097 21745462 23806337 24129315 15128297 10873583 8626512 2050743 8633055 9177781 16641100 21223964 22673903 8698233 16421571 12482924 17081983 17525332 18220336 19367720 18691976 18669648 19413330 19369195 19690332 19608861 21109228 20665883 20068231 21269460 21263134 21406692 23186163 24275569 25944712 17397861 12791251 8894687 11159198 11851880 14675180 25712130 26477546 25556389 27234031 1717441 8345227 11751855 14702039 14574404 8575775 10428034 1712022 15489334 9872452 12168954 2461961 2090522 8010969 8752219 10637308 8621649 11375975 14581450 12802069 19403692 20164846 22522446 22113475 22419821 19632184 11514586 7670468 16289082 16797530 17161423 9971739 7736575 10357897 14576348 17287360 18638474 20209123 10529403 10559237 11845288 16710414 10574462 9455484 15265687 16076900 20937854 27693509 27802168 16959974 10601340 8954775 15345747 16815997 18854161 21295697 15057822 9412476 9521878 10051401 15616553 9628581 12244133 15229321 15226441
15592455 16452087 17947660 17114649 17208939 17242355 18827015 18630941 19144319 19131326 21183079 19932097 21745462 23806337 24129315 15128297 10873583 8626512 2050743 8633055 9177781 16641100 21223964 22673903 8698233 16421571 12482924 17081983 17525332 18220336 19367720 18691976 18669648 19413330 19369195 19690332 19608861 21109228 20665883 20068231 21269460 21263134 21406692 23186163 24275569 25944712 17397861 12791251 8894687 11159198 11851880 14675180 25712130 26477546 25556389 27234031 1717441 8345227 11751855 14702039 14574404 8575775 10428034 1712022 15489334 9872452 12168954 2461961 2090522 8010969 8752219 10637308 8621649 11375975 14581450 12802069 19403692 20164846 22522446 22113475 22419821 19632184 11514586 7670468 16289082 16797530 17161423 9971739 7736575 10357897 14576348 17287360 18638474 20209123 10529403 10559237 11845288 16710414 10574462 9455484 15265687 16076900 20937854 27693509 27802168 16959974 10601340 8954775 15345747 16815997 18854161 21295697 15057822 9412476 9521878 10051401 15616553 9628581 12244133 15229321 15226441
EMBL
AY480033
AY480038
AY480043
AC110211
AF188006
AF188007
+ More
AF188008 AF188009 AF188010 AF188011 AF188012 AF188013 AF188014 AF188015 AF188016 AF188017 AF188018 AF188019 AF188020 AF188021 AF188022 AF188023 AK017743 AF260753 X59601 U96274 U96275 U96276 Z54367 U53204 U63610 U63609 X97053 AY480044 AY480045 AY480046 AY480047 AY480048 AY480049 AY480050 AY480051 AC109322 M69225 L11690 AF400226 AF400227 AK055189 AK094883 AK096713 AK295864 AL049215 AL096710 AL590005 AL137008 AL512422 AL512448 AL590037 KF458172 U31850 U31851 AF165191 AY032900 AY032901 M63618 BC016991 AB018271 M22942 X58677 U04850 AF396877 AF396878 AF396879 AC123072 AC124386 AC127433 U22452 U25158 DQ023311 DQ463750 AK051626 AK037206 AF115383 AB085694 AAK83384.1 AB029290 AF141968 AF317696 AF325341 AF325333 AF325334 AF325335 AF325336 AF325339 AF325340 AF325330 AF325331 AF325332 AL137853 AL355477 AL365277 AL442071 AL356055 AB033077 AB007934 AF150755 DQ067088 AL606932 AL606918 U67203 U67204 U67205 AC114512 AC131172 AF001691 AF013717 AF041004 AF040999 AF041000 AF041002 AF041003 AC027687 CH471112 BC114620 AB011140 AF126834 AF116523 AF116519 AF116520 AF116521 AF116522 AK014700 AF013715
AF188008 AF188009 AF188010 AF188011 AF188012 AF188013 AF188014 AF188015 AF188016 AF188017 AF188018 AF188019 AF188020 AF188021 AF188022 AF188023 AK017743 AF260753 X59601 U96274 U96275 U96276 Z54367 U53204 U63610 U63609 X97053 AY480044 AY480045 AY480046 AY480047 AY480048 AY480049 AY480050 AY480051 AC109322 M69225 L11690 AF400226 AF400227 AK055189 AK094883 AK096713 AK295864 AL049215 AL096710 AL590005 AL137008 AL512422 AL512448 AL590037 KF458172 U31850 U31851 AF165191 AY032900 AY032901 M63618 BC016991 AB018271 M22942 X58677 U04850 AF396877 AF396878 AF396879 AC123072 AC124386 AC127433 U22452 U25158 DQ023311 DQ463750 AK051626 AK037206 AF115383 AB085694 AAK83384.1 AB029290 AF141968 AF317696 AF325341 AF325333 AF325334 AF325335 AF325336 AF325339 AF325340 AF325330 AF325331 AF325332 AL137853 AL355477 AL365277 AL442071 AL356055 AB033077 AB007934 AF150755 DQ067088 AL606932 AL606918 U67203 U67204 U67205 AC114512 AC131172 AF001691 AF013717 AF041004 AF040999 AF041000 AF041002 AF041003 AC027687 CH471112 BC114620 AB011140 AF126834 AF116523 AF116519 AF116520 AF116521 AF116522 AK014700 AF013715
Proteomes
Pfam
Interpro
IPR001715
CH-domain
+ More
IPR018159 Spectrin/alpha-actinin
IPR036872 CH_dom_sf
IPR036388 WH-like_DNA-bd_sf
IPR001452 SH3_domain
IPR035915 Plakin_repeat_sf
IPR005326 S10_plectin_N
IPR041573 Desmoplakin_Spectrin-like
IPR001589 Actinin_actin-bd_CS
IPR001101 Plectin_repeat
IPR041615 Desmoplakin_SH3
IPR030269 Plectin
IPR036534 GAR_dom_sf
IPR018247 EF_Hand_1_Ca_BS
IPR003108 GAR_dom
IPR002017 Spectrin_repeat
IPR029926 Dystonin-like
IPR002048 EF_hand_dom
IPR011992 EF-hand-dom_pair
IPR018159 Spectrin/alpha-actinin
IPR036872 CH_dom_sf
IPR036388 WH-like_DNA-bd_sf
IPR001452 SH3_domain
IPR035915 Plakin_repeat_sf
IPR005326 S10_plectin_N
IPR041573 Desmoplakin_Spectrin-like
IPR001589 Actinin_actin-bd_CS
IPR001101 Plectin_repeat
IPR041615 Desmoplakin_SH3
IPR030269 Plectin
IPR036534 GAR_dom_sf
IPR018247 EF_Hand_1_Ca_BS
IPR003108 GAR_dom
IPR002017 Spectrin_repeat
IPR029926 Dystonin-like
IPR002048 EF_hand_dom
IPR011992 EF-hand-dom_pair
Gene 3D
ProteinModelPortal
PDB
3PDY
E-value=3.90096e-35,
Score=381
Ontologies
GO
GO:0031581
GO:0047485
GO:0042383
GO:0048471
GO:0005903
GO:0008092
GO:0016020
GO:0009925
GO:0042060
GO:0043292
GO:0016528
GO:0005925
GO:0005829
GO:0008307
GO:0003779
GO:0005737
GO:0030506
GO:0007584
GO:0045111
GO:0005198
GO:0030056
GO:0016324
GO:0045104
GO:0005200
GO:0005856
GO:0030496
GO:0007010
GO:0043034
GO:0030855
GO:0007565
GO:0045296
GO:0070062
GO:0003723
GO:0005886
GO:0015629
GO:0008022
GO:0015630
GO:1904115
GO:0042803
GO:0031122
GO:0000226
GO:0005509
GO:0009611
GO:0030424
GO:0008017
GO:0031673
GO:0005882
GO:0005635
GO:0005938
GO:0005789
GO:0030011
GO:0008090
GO:0005604
GO:0016021
GO:0030018
GO:0048870
GO:0031252
GO:0005178
GO:0035371
GO:0007229
GO:0005634
GO:0031410
GO:0051010
GO:0007155
GO:0060053
GO:0097038
GO:0009898
GO:0007409
GO:0014069
GO:0031110
GO:0001725
GO:0046907
GO:0014704
GO:0045773
GO:0005874
GO:0030177
GO:0032587
GO:0032886
GO:0051015
GO:0051011
GO:0043001
GO:0051893
GO:0016887
GO:0016055
GO:0030334
GO:0005794
GO:0010632
GO:0008104
GO:0007163
GO:0001707
GO:0006620
GO:0070268
GO:0009612
GO:0030057
GO:0005739
GO:0001533
GO:0019897
GO:0031424
GO:0005515
GO:0006470
GO:0008138
GO:0004890
GO:0005216
GO:0043564
GO:0006418
GO:0003824
PANTHER
Topology
Subcellular location
Cytoplasm
Cytoskeleton
Cell junction
Hemidesmosome
Stress fiber Associates with intermediate filaments, actin and microtubule cytoskeletons. Localizes to actin stress fibers and to actin-rich ruffling at the cortex of cells (By similarity). Associated at the growing distal tip of microtubules. With evidence from 6 publications.
Cell projection Associates with intermediate filaments, actin and microtubule cytoskeletons. Localizes to actin stress fibers and to actin-rich ruffling at the cortex of cells (By similarity). Associated at the growing distal tip of microtubules. With evidence from 6 publications.
Axon Associates with intermediate filaments, actin and microtubule cytoskeletons. Localizes to actin stress fibers and to actin-rich ruffling at the cortex of cells (By similarity). Associated at the growing distal tip of microtubules. With evidence from 6 publications.
Myofibril Localizes to microtubules and actin microfilaments throughout the cytoplasm and at focal contact attachments at the plasma membrane. With evidence from 5 publications.
Sarcomere Localizes to microtubules and actin microfilaments throughout the cytoplasm and at focal contact attachments at the plasma membrane. With evidence from 5 publications.
Z line Localizes to microtubules and actin microfilaments throughout the cytoplasm and at focal contact attachments at the plasma membrane. With evidence from 5 publications.
H zone Localizes to microtubules and actin microfilaments throughout the cytoplasm and at focal contact attachments at the plasma membrane. With evidence from 5 publications.
Nucleus Localizes to actin and intermediate filaments cytoskeletons. Localizes to central actin stress fibers around the nucleus and is excluded form focal contact sites in myoblast cells. Translocates to the nucleus (By similarity). Associates with actin cytoskeleton in sensory neurons. With evidence from 6 publications.
Nucleus envelope Localizes to actin and intermediate filaments cytoskeletons. Localizes to central actin stress fibers around the nucleus and is excluded form focal contact sites in myoblast cells. Translocates to the nucleus (By similarity). Associates with actin cytoskeleton in sensory neurons. With evidence from 6 publications.
Membrane Localizes to actin and intermediate filaments cytoskeletons. Localizes to central actin stress fibers around the nucleus and is excluded form focal contact sites in myoblast cells. Translocates to the nucleus (By similarity). Associates with actin cytoskeleton in sensory neurons. With evidence from 6 publications.
Endoplasmic reticulum membrane Localizes to actin and intermediate filaments cytoskeletons. Localizes to central actin stress fibers around the nucleus and is excluded form focal contact sites in myoblast cells. Translocates to the nucleus (By similarity). Associates with actin cytoskeleton in sensory neurons. With evidence from 6 publications.
Cell cortex
Cell membrane
Sarcolemma
Golgi apparatus The phosphorylated form is found in the cytoplasm while the non-phosphorylated form associates with the microtubules (By similarity). Localizes to the tips of microtubules (PubMed:27693509). Associated with the minus-end of microtubules via interaction with CAMSAP3 (PubMed:27693509). APC controls its localization to the cell membrane which is critical for its function in microtubule stabilization (PubMed:20937854). With evidence from 14 publications.
Ruffle membrane The phosphorylated form is found in the cytoplasm while the non-phosphorylated form associates with the microtubules (By similarity). Localizes to the tips of microtubules (PubMed:27693509). Associated with the minus-end of microtubules via interaction with CAMSAP3 (PubMed:27693509). APC controls its localization to the cell membrane which is critical for its function in microtubule stabilization (PubMed:20937854). With evidence from 14 publications.
Desmosome
Mitochondrion
Cytoskeleton
Cell junction
Hemidesmosome
Stress fiber Associates with intermediate filaments, actin and microtubule cytoskeletons. Localizes to actin stress fibers and to actin-rich ruffling at the cortex of cells (By similarity). Associated at the growing distal tip of microtubules. With evidence from 6 publications.
Cell projection Associates with intermediate filaments, actin and microtubule cytoskeletons. Localizes to actin stress fibers and to actin-rich ruffling at the cortex of cells (By similarity). Associated at the growing distal tip of microtubules. With evidence from 6 publications.
Axon Associates with intermediate filaments, actin and microtubule cytoskeletons. Localizes to actin stress fibers and to actin-rich ruffling at the cortex of cells (By similarity). Associated at the growing distal tip of microtubules. With evidence from 6 publications.
Myofibril Localizes to microtubules and actin microfilaments throughout the cytoplasm and at focal contact attachments at the plasma membrane. With evidence from 5 publications.
Sarcomere Localizes to microtubules and actin microfilaments throughout the cytoplasm and at focal contact attachments at the plasma membrane. With evidence from 5 publications.
Z line Localizes to microtubules and actin microfilaments throughout the cytoplasm and at focal contact attachments at the plasma membrane. With evidence from 5 publications.
H zone Localizes to microtubules and actin microfilaments throughout the cytoplasm and at focal contact attachments at the plasma membrane. With evidence from 5 publications.
Nucleus Localizes to actin and intermediate filaments cytoskeletons. Localizes to central actin stress fibers around the nucleus and is excluded form focal contact sites in myoblast cells. Translocates to the nucleus (By similarity). Associates with actin cytoskeleton in sensory neurons. With evidence from 6 publications.
Nucleus envelope Localizes to actin and intermediate filaments cytoskeletons. Localizes to central actin stress fibers around the nucleus and is excluded form focal contact sites in myoblast cells. Translocates to the nucleus (By similarity). Associates with actin cytoskeleton in sensory neurons. With evidence from 6 publications.
Membrane Localizes to actin and intermediate filaments cytoskeletons. Localizes to central actin stress fibers around the nucleus and is excluded form focal contact sites in myoblast cells. Translocates to the nucleus (By similarity). Associates with actin cytoskeleton in sensory neurons. With evidence from 6 publications.
Endoplasmic reticulum membrane Localizes to actin and intermediate filaments cytoskeletons. Localizes to central actin stress fibers around the nucleus and is excluded form focal contact sites in myoblast cells. Translocates to the nucleus (By similarity). Associates with actin cytoskeleton in sensory neurons. With evidence from 6 publications.
Cell cortex
Cell membrane
Sarcolemma
Golgi apparatus The phosphorylated form is found in the cytoplasm while the non-phosphorylated form associates with the microtubules (By similarity). Localizes to the tips of microtubules (PubMed:27693509). Associated with the minus-end of microtubules via interaction with CAMSAP3 (PubMed:27693509). APC controls its localization to the cell membrane which is critical for its function in microtubule stabilization (PubMed:20937854). With evidence from 14 publications.
Ruffle membrane The phosphorylated form is found in the cytoplasm while the non-phosphorylated form associates with the microtubules (By similarity). Localizes to the tips of microtubules (PubMed:27693509). Associated with the minus-end of microtubules via interaction with CAMSAP3 (PubMed:27693509). APC controls its localization to the cell membrane which is critical for its function in microtubule stabilization (PubMed:20937854). With evidence from 14 publications.
Desmosome
Mitochondrion
Length:
5219
Number of predicted TMHs:
0
Exp number of AAs in TMHs:
0.0818299999999999
Exp number, first 60 AAs:
0.00062
Total prob of N-in:
0.00008
outside
1 - 5219
Population Genetic Test Statistics
Pi
200.397032
Theta
167.134799
Tajima's D
0.312063
CLR
0.573396
CSRT
0.458777061146943
Interpretation
Uncertain
