Pre Gene Modal
BGIBMGA013427
Annotation
PREDICTED:_LOW_QUALITY_PROTEIN:_ankyrin-2-like_[Bombyx_mori]
Full name
Ankyrin-3
+ More
Ankyrin-2
Ankyrin-1
p53-induced death domain-containing protein 1
Ankyrin-2
Ankyrin-1
p53-induced death domain-containing protein 1
Alternative Name
Ankyrin-G
Ankyrin-B
Brain ankyrin
Non-erythroid ankyrin
Ankyrin-R
Erythrocyte ankyrin
Leucine-rich repeat and death domain-containing protein
Ankyrin-B
Brain ankyrin
Non-erythroid ankyrin
Ankyrin-R
Erythrocyte ankyrin
Leucine-rich repeat and death domain-containing protein
Location in the cell
Nuclear Reliability : 3.554
Sequence
CDS
ATGCCGCCTTTGATGGAGGGCGAGGCTCTTGCTTCGAGAGTTTTAGAAATGGGACCTGTTTCTGCTAAATTCTTAGGGCCAGTTATTCTGGAGGTGCCCCATTACGCTTCACTGCGAGGCAAAGAACGAGAGATTGTGATCCTCCGTTCAGATAATGGCACTAGCTGGAGGGAGCATAATGCTGACGCTACAGATGACGTGGTTCAAGATATCCTGCACGAGACCTTAGAAATTGAAGAAGCTAATGAAGATGAGAAAGGATGGGATGCTCCGCGTCTCACCAGAATCCTGACTCACGATTTCCCGCAATACTTTGCTGTTATATCGCGCATACGTCAAGAAGTACACGCTATTGGACCTGAAGGTGGAATGGTTTCGAGTTCAGTCGTTCCACAAGTCCAAGCGGTCTTCCCTCAGGGAGCTCTGACGAAGAAGATCAAAGTTGGCCTCCAGGCTCAAATTATAGATTCTGAATTAACTGCTAAGCTACTGGGACGTGGAGTAGCGGTTTCTCCTGTGGTTACTGTCGAGCCACGCAGGAGAAAGTTCCACAAAGCAATTACTCTGAGCATGCCAGCGCCTAGACCTCATACTCAGGGCATGACAAACCAGTATAGCACATCATCTGCGCCAACGTTAAGACTTCTTTGCTCCATTTCAGGAGGAACAAACAGGGCTCACTGGGAAGACGTTACTGAAAATACACCTTTGACGTTTGTAAACGATTGTGTTTCCTTTACTACGACGGTATCGGCTAGATACTGGCTGATCGATTGTAGACACATCGAAGATGCTACGAAAATGGCTACAGAATTATATAGAGAGGCTATTCATGTACCATTTATGTCGCGTTTTGTTGTTTACGCGAAGAGATCTGACGAAAACCAAGCGCAGCTCAGGATGTTCTGTGTTACTGATGATAAAGAAGATAAAGCTTTAGAACGCATCGAACGATTTATTCAAGTTGCTAAAAGTCGCGATGTTGAGGTCCACGAAGGAAAACCAGTCTATCTGGAATTCGGTGGAAACCTCGTTCCGGTAGCTAAATCAGGAGAACAGTTGACAATACCATTCCGGGCCTTCCGAGAAAATCGCATGGCGTTCCCGGTTATGATCAAGACCCAGGATCTAGAACCGATTTGCAGATGTCAGTTCATGAGAGATCCGAAGGTGCCTAAAGGCGAACCTTCCCCCGCTCCTATTGCCGTTCTCAACATAATGGTACCTGACGAGCCGACTGATAGGACATCGCCTCTACCATCAGAAGCGGTTCCGAGACGCACTGAGGAACAAGAATTGATTTGGAGGCAGCGACTCAGTGATCCTAGGCTGGAAGATATCTGCAATCTACTGGGTAAAGATTGGGTGGCTTTAGCTTATGAATTGGGCGTGAGTGTTGCCACGGTTAATCAAATTCAAGCTAAAAGGATCACCGCACCGGAACAAGCTCAGCTTATGTTGAAACTTTGGAAGACACAATCTGGAACAAAGGCTCAAGACAATTCCTTGGAACTAGCACTCTGTCGTATAGGCAGAGATGACATAATAGCTCCGCAGTCAGACACGATAAACGAAAGACGAATCCGGCGTAACATTTACCAAGAGAGGCAAGCATCTGAAGAGATCGAAGCGTATAAAGCAGAAGAAGATAATAAGCTCAAAGAAAAACTGTACAATGAAGAAGATATACTACCGGAGCATAGAGAATCAGAACATGATCAAGATGAAGCCAAATATTCACCGGAAGAAAAATCTATTGTTGAAAAGAGTGAAATAGATAGAACGCCTTCACCAAGTGAGGAGAGCGAGGAAGATGAAGACATCAAACGAAGCGTTGCTGAAAGAAAGGAACAAATAACTAGAAAGTTAAGTTCTAGTAAAGTGCCAGCTTCAAAACAAAAGAAAGAAATTCGTGAAGAAATAATTGAAATTAAGACACAAATCAAACCGGATATCAAGAAATTCCACGACATTGAGCAACAGTCTTTAGATAAGGAACCCACATTAGAAAAGTCACGATCGAAAACATCTCCAGATAAAGTTGAAGAGGGGACAGAAGAACAGGAAGTCATTACAGAAACTATTGTTGAAGCTATCGTTGAAGAAAGAAAGGAAGAGGTAAAACCAGTAGAAAAACCTATAGAACAATTTAGGAAGTTCGATCCATCATCGCCAGCTAAGCCTACCCCTAAACATCTGCAGAGACACATGCGAAATGAATCAATGCGGTTTCCATCAGGGGACTTTTCCAATGTTGTAATAACCCCAAGAAAATCAATAACAAATGAAGCAGTAGAAAAACAAGCGATTGAAACTAAACCTCATACGGTTACAAAAGAAGAGATTTCACAGAAAGAAATTTTCACATCTAAAGTCGAAGAAAAGATGGAAGAAATTGAAAAAACGGCCAAAATCGTTAAAGAAGAGAAAGATATTGCTGAAGCTACTTTGAAAGATAAAATTAATTCATTCGAATCGAAAATGGTAAAAGAAATCAATGTTGATGTTTCAAAACCAACGATAAAACTAACTAAAGAAGCCCTAAAAAAACATACTTTGGAACAAGGACAAGGCAATGGGTATACTCAAGAGTTCGTTAGAGAGCAATCTAAGCAATTATCGAGCATGGAATCTCACGTTACACATAAAGTGACCGTCGAAACTGAGACACATATTGAGACAGTAAAATCCGTCAAAGAGACGATACAGCAATTCGATTCGAAAACAAAACTATGTGAGAAACCAAAGCATTTCCCTAAGACTATACGAACAGACTCAACCCTCGTTCAAGTATCTTCCGAGGAAGATAGCGAATTCCTTAAAAAATCGACAGATTCTGAAACAGAAACGGAATCGCAGACTACAACAGTCAAAGTGGACAAATTAGACAACAAAACTAAAGTCAAGCCCTACAGGGAATATATTGGCGCTGAAATAGATCACGAAGACAGTCCTAAAGTTAGTGACAAAGATAAAAAAGGAGATGAAGACGATAAGGATTACAAAGGTGTTGCTGTAATGAAAGATGTCTTCCTAGAAAAAATAACTACTGAAGAACCAGTACAAGTTACCGAAGAATATAAAAAGCAATCGTTGGAGGAAAGAGATGTCTCTTTAACTGATAAATCAAAGGAAAAGGTTGAGACTCAGACCTCTACAGCAAGTACTAAATCAGACCTTAGCAGACATACGAAGACAGATTCTGTAGGTTCAGATATGCAAGATTTAATAGCACAAAAAGTATCAACAGAATCACCAATCCAATCTGTCGTTGACAAAGCTGATTCTTTAGCGGATCTCCAGCACAGCACCGAGAAAGACTTCAGCTTTATTTCCCAAACTGAGTCCAAGGTATACTCAAAAGATTCTAAGCACAGAAGTGATTCATTGGATGAAGCTTCTCAGTTTTCTGATCTAGAAGATCAAATTGGCTCAAGTCCGGCGCACAGACCAGTTACTGAGAAAATAGAAGCAGGCTCAATTAAAACCGATGTGAAATCCGTTTCAAAATTGATTGAAAAGTTTGACACGTCCCCGAAAAGTCAGACCATGGAATTTTTGAAATTCGAGAGTGAGCATAGTGCCCAAGTACAGGTACCTTTAACGGAATCAGATAAGACTAAAGAGACACCAGTGATAAGTGCTAAAGCGAGACAGTTTATTGAAACTGTACCTGAGGATGATTCAGTGCAGGAATGTTTCTTTTCAAAGCGTATATATTCAGATTCGCTTGAAGATTCCGAGCATACTGATTCAAGAAGACATTCAGAAGCAGAATCACTAAAATCTGACCAATCCGATACAAAAGTTAAAGTTTCGTCATCTGAATTTGATGAAAGGGCTGAATTCGAAGAGGCGGCTGATTCTGGAAGTGGATTTGGTGACGAAAAATTTGAGGAAAGCGTTGGATTTACTTCATTTAAAATTGACCCTAAAGTGCTTGAAATTGAGAGGCAAGATTCGGAATCTGATAAAGAGTCAGACGTCGTTTTTAAGAAAATGATACCTAAGCGACATTCTAGAACTGAATCTATATCAATAACTAAGCTAAGTGATATTGGTGATATTGAAATCAAACCAAAACAAGAATTCCAAATTATTGTAACCGAAGCAGAAGAAATAGATAAATCTTTTGAAAAAGACAAGATTAGTTCGGAAGATGCGGTTACCAAGAAAACATCTTCGGAAGAAGACGTAGTCTATGAAGCAGAGCGATTGCAACAGCAAAAGACAGAAGTTGTTGCAACAACTGTAATTGAAAAGAAAATGGTTTCGGATGATGCGAAAGAGGATGTTGATTCAAAACGCCAATCAGTGACGTCAACAGAATCAGTGGGTGAACTACGTCTAGAGGAAAAGCGACCGTCAGATGCTCACAGTCTTACTGAATCTAGAGATTACACTTTTGAAGAGTCGGAGGACGATATTGCAACCCAAGGCACACATGTGGATCATTCCAAGGATATTGGGCCACATAAAATTGAAACCGAAGAAATTATACAGATTGCTGAAAAATCTGTAGAACACCCGAAACTCGCCAAACTGACTCACGGGGATTCACTTGATGACGTTGAAGGATTTCCAGAAGATCATACTGCAGATTATGTGCATAAATTACCACATATTGCAGAGATTGGATCTGTTTCTGATAAAGATATGACTATTGAATTTCTCAATAGAGAGAAACAAGAACAACTAAAACGCGTGTCTGTTCAAGAACCAGTCCCTGAAGTGATTGTTCCTTTAACTCAAGATGAAATAATTAAGGAAACAGTAACACATAAAGAAACCCCGACCGTCTTTACTTCGACCAAAACTGAAACACATTATTCTAGCACAACTAGAACAGAGCCTTTGGTCACATCTGAAATGATGAGCCAAACTAAATCATCTATAAAAGAATCTACCACAACTAAATCATTCAGAACAGAAGGGAAATTCGACGTTTCAAAGATAAGGACCGATACTTTGGGCAAATTTGATATTGGTGAACAATTGGAGGAAATGAAGGAAACCAAAAAACATATGCCGAGAGATTTACAAGAATTACCTGAAATAACGAAAGAGCAAGTCAAACCAGTTATCGATGATATTTTGCAAAAAGGTACAATTGCTGCTGTTGCACGAAGCCCAATTGTAGATAAAGACATTAAAACCATTACCAAAGAAATAGTAGAATCAGAAAAGAGATCTTACGACACGAAAGTGCCTCAGAAAGAAGAACGAAGACATTCGTGTATCAGTCCAGCTATTTCCTTAGAAAGGATTGCTGAGTCTGATGTTGAAACAGATGAAGAAGTCAGTAAATCTATTCCCATTGTTGCCCATGAGAAAACAACTGAAATTAAAACGGATATGAAAAAATCTGATTCGGCCATGAAACAAATGGCAGATAATATAGAAATTATCATTAAGCAGGCTTCGGAGGAAGTCGATATGTCATCAGAAGAACACCCTGTTGAAGTTGCAGAGCCTCAGGACATTGCTGGTCAAGTTTCTGTGGATTCAATAATTGAAGAGGCCGTAACAACCGTCGAAGGTTATTTGGAATCAGCTAAAGACAAAGAAAAAGAAATTGAAGCTAAGAAAGAAATTGTTTACGCTGAGACAAAGAAATTCGCTAAAGATAGACCGGGCCTCATTAAATCGCTTTCCAGGGATAGTGGTGAAATTGTCATAATGCCCAAAAAGAAACAAACGAGAACATTTTCAGTACAGAGTTCTCCGGAAGAAGTCGAAGAACAAATATATACAGATTCGGAATCAGACATGGACAAAGCTAAAGTTTTAGAAATAATTGAACCAATGTCTGACCTAGACGGAAAACTACCAACGTCAAGTTTCGATTCCAGGAAAATAAGAACAGATTCGCTGGATGATGCTGATGATTTCCCGGAGAAAGAGGCTGACGTCTTTGGTGAAGATTATCAATATCCTGACGACGGCATACATTCAATTATAAAGAAACCTGATACAGCTAAGTATGAGCCAAGCACAAGCTCTACAACAAAAACATCCGATGAAGAAAAATCAACTGATAAAGTGATGAAAAAGACCCACTTCGTCGATAGTCTTCTTCAGTCTGATTTAGTATCAAAATCTACAACAGAATCATCTGTAACAACGGTTATATCCACCTTGACAAAATCATCTGACGAGGAGCAAAAGTCTGTTTTGGAAGACTGTACGTCAGCTGATTTGTCTAAAATCAGTGGTGCAGATCTGGTCAAGGATCCGTCAAAAACTTCTTTCGACACAAAAGAAGATTCAAGAATCGATGAACATACAGAAGACAGGGCGACCCCAGATTTATCTAAAAAGTCTCTTGACTTAACTAAAGATTACTCTAAATCTTCAATTGACAGCAAAGATACGTCTAGAGATTTCGCCACCAACGAGCTATCGAAAGATTCAACGGTAGACCTAACAAAAGATTACTCAAAAGTATCAGTGGAAAGTGTCAAAGAATCATCGAAATCATTAGATGAAAAAACAATTTCTGAAGATCATTCTTCCTTAGATGTATCGAAAACGTTAGCTTCTGACGTTTCAGAATGCATTACAATAAGCAAAGAATTTATTGAAGAAGAGAGATCGGTATCTCGTGTTTTTAGAATATCAACAAGTTCCTCACAAGAGACATCAATAATGACAGAAAGCAAGATGTTCAGTGAATTGGATGATAAATCAATTAGTAAAGCAAAATCGGAAGTGATTGAAGTGGAAAAAGATTTATCAGAATCTATTCAGGACCAAGAACAGGAAGCGAAACGAGCACCTGATACCAGTGATGTGGCTCAAGCTAGAGCTGTCCAAGACCTACAACTAATAGAAGATATTTCTGATAAATCGACACGTGAAATAAAAGAGCTCTCAAGAACAAAGCCTGCATTAACAGAAACAAGTGGTGAAAATTTTTCAGAAGAAGTAATTAAGCCATCTTTTGAAAAAGTTAAGGCTGAAGAAATTATTTCATCCCCAGAGACGAGTCATATTATTGAAAAATCGACTAAATTAGTCACTAAGCCGTTATCAACAGTGAGTGCAGGAACTTTGACAGACGTACGGGATGAACAAGAAAAATTAAAAGATTTTATTAAGGAAGATAATGTTGAAGATTCAAAAAAACAGATCGAAGGCGAACGTACAGTATCAGCAATTGCTGATCACGTAGATGGGGAAAAAATTGCCATACAAGCGAAAATTGTTGAGGAGGAGGGAAAGAGTTCAAAAGGTGATATAAAAGAAGAAAGATTAGAGTCAGTAACATCAACTGCAGAAAAAGAAGAATCAGACGAAGTACCAGACATGAAAGAATTAAACAGAAGATGTTCTAACCTTCTCGAAGATATCTCTCAAGGGGCTTTGATTCGAATTGATACTAGCCACGTGACACACGATCTTGCATCAAAATTCTCCAAAACTCCGCCTCCCTCACCGGTGGACCTGATCCTCAAAGATAAAACCAAGTCTGAAGAATTTACTGGTGAAAAGCATGTAGGATTACAGTTAAGAGGTTCAGATTCATCATTCCTTGACACCAGCCGACAATCTCCGAGGGCTTCATCAGCTGGAGACAGCCTACTTAGCGAAACTGAAGCTCATCAGAGCGAAGTATCAAAGACGCCCTTCAAACCGATCGCCACTGGGTCTAGACCAAAATCCCCTGTTAAGCACATCGCCGAAAACATGGAGTTTGTCAATGTTGATCAACCTACTATCACTAGTGGGGCCATTGAACTCGTTGATCGTACGATTGAAAAGAGCATGGACGTAATTGACCAAATTAAGAAAGAACAACTTGCCGTGAAATTGGAAGAAATTCAAAAGTCCACATCAACCGATACGTTTTATTCTGAATCAAGGGTCGAAACATCAACGTCCTCTTCATCAGTCCATAAAACAATCGAAGGTGGAGAGCTTAAATTCCAATCCATCGACCCACAAGCTTTGATGTCAGATATGGCAGCTAAATTTAGTGTCACTGACGATACGCCTACAATTTTGACGCATAAAGAAACCGAGACTCGAAAAATATCAGGACAAGAGTTTTTCACTGAAACAAAACAAATATCTTCATCGGATGATGACTCATTGATTATTAAAACTGAAACTACTCATGAATTACACGGTCAAGAACATGAGACCAAAGAAAAAACGATTATTCGAAAAGACGGCGATCAAACTCAAACATCTCAGAAAAAGTTAGAAAAAGCTCATGAAGCCACGGCAAAGCGATCTGACATTGAAACTAAGACAGTCTTCAAAAGTACTGATGATACTGATATTATTAAAGTTGAAAGAGAATTTTCTGAACAGGGCTTGTACCATGGTAGACAAACAAAATCTGAGGAGAAAATGACCGCTTTGAAAGATGATACGGTTAAAAAAAAACACGAAGTAAAGATATCTGAGAGAGATTTGTCTCATGAACAATGGGGCAAAGAATACTTCACAGAGCCTGGAGAGCTGGAAGATATAGTAGAGGACGATGATAAGTCGAAAGTAGCATTCGTTGACTCAACTCTGAAAATTATTGAGTCTGATGAAGTAGTCTCAAGCGTCGAGGTATCAGAAAAGGGTAAAATTGTGAGTTCAACATTAGAACACCATAGAGAAGAATCTATAATTGAAAGCAAGGAGCACGATGATCTGAGTTCTGATACTTCTCACGCTCCAAGTTTCAAGAGTGAACCAGCTGACAAACATGATTCTTCTGAAGCTAGTCCAAGAAGTAAATCCAAGTCGTTTAAGAAAGATAATGAAGTTTATGAAGTAGATTTTATCAAAGAAATTAAAGTTTCCACTTCACCAGTTAAGAGTACGTTTAGTCGAACAGGAAGTCAAGATACACATTCTGAGTCTGAAATAGCACCCGATTTGCCACATGATGACAAGACTGGTGACACACCAAAAAAAGAACGACCATCAAAATCACCAATAAAATTACCACAAGAGCAGATTGAAAATCAGGTTTGGGAAGTTACAATACAGAAAGCAGATTCCTTTGAAATTGGTGACGACACACCAAAAACGCCTTTGTTCAAAACAGTTGAATCTATTAGTACTATAAATCTGGAGAGCACTACTACGGATATCAGAACTAACATTGAAACAAACACTGCAGATATAAAACTAACCAAAACTGACATGTCGCCCATCGCTTTTGAGGTATCCGAAGACATTAGCGGTATATCCAAAGACATTATGGTGAAATCAGGCGAGAGTATCGATACCGAATACATGATTAAATCATTAGAATCACACGAAGGGGAAGTATTACAGAAATCTATGGATTCGACTATGAGCGCCGAAACATTACAACCATCAGAATTTTCCACTGATTCTGCCTACCTAACCGGCACTGATCATAAAAGAGAAGAAATTAAGTTATTCAAAGAAAAGAGTCTAGAAGATATTTGCAGTAGCGGTTACGATACTGATCTCTCCTCTGCCGAGTTTCATGCAAAACTTGAGACAGAAAGAGTTGATTATGATTCTTTAATGTCTGCTCAACCACTAGCCGACTTGTCAGTTTTGGAAAAAACGATCGACGAAGTCAAGCAGTCTCTTGAAGCAGCACAAGTAGAAATCATCAGTGAAAAGAACGATGGAAGTATAAAATATAAACAGTCGCCTTCTGAATTTCAATTCAAATTATTAATTAGTCCGGACAGACCCGAAGTTATAACAGAAGAACCACATCACACAGAAGGTCACGCCGATAAAACACCAGTTATTGAAAAAACTGAAACTTTGTTAGATAGTCAGATATCAGACAGTGTTACCCAGAAAATAAGTTCCCAAGAGGAAACCACATCCGATGAAGATAAAGACACAGTCTACATTAAGGAACCAAGCCCCCCATTAGACGCTGGTGATATTTCTATTAGATCAACGGATAGTGGTCCACACTCGATTTTAGAGACTGAAAGTGAGATTGTTACGTCAGATCGTGACGGCTCTTCAAAAGGAAGTCCTGAAGTCAAACTAAGAGTCCAAAAGCATATCAAGTCTAAACTTGGTATTGTAGAAAGACGATCTGCATCGGATATTGAAGGTTGGTCTAGCTCAGGGGAAAGTCATTACCATAGCTTTGAGCATTCTGAAGGAAGACCACTGTCTTCAGATGTTGACGTTATGATGACCGCTCAAAGTGGAACCGAATTCGATACAGCGATGACAAGTCAAGATGTTTCATCACAATCCTTACGAACTTCGAGAGACTACTATACAGCAGGAAGCTCTTTAGCTTCTAGGGATAGTATGAAAAGTCTAGATTCAGATGGTTCTAGCCATGTAGCCAGTATTGACATATCAGATGCTTCAGAAACATTAGTACCTTCAGCCAATGAGCTAAAAGAAGAACTTATGGAAAGTAGTACTTACGTAGAACAATTTCTGCATGAAACCGAAAAAGATCAAACATCTAAATCCAAAGACATAAGCGACGAAGATGTCTCTGGCGAAGAAGAAGATGCTAAGCCCGGTATCTTTGAACCAATAGGAAAAATGAAAAGATCACATGAGATGCGATTTCAACCAAAAGAGATGATACCTGAAAGTTTTCAAGTTGGAAGTACGTCAGAAAGCATTGAAGTAGATGAAGATTCATCGAAAGATAAAGAATTTTCGGATACCACAATATCTAGTCAGTTTAAAACAGATGAAATCCTTTCATCGTCCATTTCAAAACTTGATATGCCTTCGTCACAATCTCAATCAGAATTGGATCTAGACGAAGTGAAAGAAGTGATAACGAAAACGATATGTCAAAAGGATGAAGCGATACCTTTTAATGTTACCAAAATTGAAAAACCTCAACGAGAATTCGCTGACGTTGACAGCGATATTATTCCAATAGGGTCCTCTGAATATGAAGCAATAGTCAAATATGGTGCTGTAACATCGGATCTAAAAAGTCCTTCACATCAAGAAACGACCATCACTAAAATGAGTATTGAAATGAATGAAAGTACACCAGGAGAGCATAAAGTAGAAGTATCAGAAGTTTGTGAGAGAAAGGAAATCAAAGATGTAAGCGTAATTCCATTTCCTAAAACAGAAATACCCACACCTAGACAGAGAGAATTTGTCGATGTCGAACAAGAAATCATACCAATAGGTTCGATACAATATGAGGAAATACTCAAATCTAAAAGTGATTCGTCGGTACCAAAAACCAAAGTTGAAAAATCTGTCATAAAAACTCCTGAGTCAGAATTAGACAGCAAACAAAGTTCAATGTCCAGTTTGAAAACGCAAGAAACACCACAAACGCCCTTATCTGCTCCTAGTCAGAGTTCTATTTCAACTGATAACGGACGAGAATATATACTAGATGATATGTATGATATTTCAGAAACTCCTGAACTAAAATCCGATGTAGTTACCGAAAGCAGTAAATCTGAATTGATGATTACAACGGAAGAGAAAACTCTATATACATACGAAAAAGATCAAGAGTCGCCCACTAGTGACGAGTTTGAAATAGTAGATAAACCAAGCGAAATGGATGAATTCGTTGTAATTGAAGAAGTCGCTAAAGAGGCCCAAGAAACTGATACAGAAGGTAAAAGTGTGCAAATCGTTGCACAGAAATATGTAAAAAGACATGATACTGAAGTGGAAGAATTACTGTCGAAAACTGCTAAAAAACAAGAAAGTACTAGTAGCGCTTCTGGGTCACTATCAGATGAGGAATTATTGCAATTTGAAATAGAACAAAAAAGGTTACAAGCGCAAGAGCTAGCTGAAATAGAAGCAGGCAAGCGTTGGATACAAATGAGATTCGAAGGCGATCCACGATACGACTATGAAAGGGTACCCTTAGAAGACATTAAAGAAGAAGAAATGACTGACTTTGATGCCAGCAGGATCGGAAGTCTGAGTTCTCAAAAGGAATCAATAGGCAGTTTCGGCAGCTTCAGAAACTCTTACGGCAGTCTTTCTGAATCGGAAATGGCATCTCGTATTAGATTTAGAGTCAGAGGAGAAAACGATGATATTTCGATCAGCTCTTTGCAGGAATTCGAAAATCTAGAAAGAGCGCTGATGGAACAGTATCAACAAAATTCTTCTTCTTCACAAGATTCTTTGAACGGTTCGCTTCCCAAACGATACATATTGAGCAGAAGTCAAGGAGATGATATTTCAATTTCAAGCTTAAAAGAATTCGAAGGATTAGAATCGGCATGCTTAGAAGCTTTAAGAGCTGAAATACTGGCAAAACAAAAAGAAGCTCTATTATTAGCCGATCCCAAAGAAGTAAGTGGGAGCTTTTTAGAAAGAGAAAAACGGTCATACAGCGGAAGCTCTGAGAGTAGTCCTCCTCAAAAAAGTGGCAGTCCTAGTCAAAAATCTGGGAGTCCATCGCAAAAAGGCGGAAGCCCTTCACAAAAAATCGGGAGCTACGGCAGTCCTTCACAAAAAATGCTGACTGATTCTGCTGCAATCAGAAAACTAATTGATCAACAAATGGCTATAGAGGCAAAACTACAGGAGCAAGTCGTTCCTAAAGTGGTGACAGTCAAGAAATTTGATGACAGGGGTGCATTTTTTGTACCTGAACCAGAAACAGAGTCAACAGAATCAAAATCATCTGATATAAATGAAGAGTGCCAAAAAACATCGACATTTATATGTGCCTCTGCGCCAAGTGACGGCTCGGCGGAATCTATCCCTGGAGACTGCGAAGAAATGATGAAGCTCCTTGACCAAGAAGAAAAATCGAAGACCTCACAGCCCGTTACTCGAACCTTCACCGACAGCGGAGTCATTGAAGTAGTCAGAACCACGACAGTGATCCAACAAAGATTCGTTGACGGAAAGAAGGTCTCCGAAACGGTCACTAGCACAGACGCAGATGTGGGAGCAAGTCCAGTTGATATACCCGCCAGAACTAGACATTACGATGAAGGAATCTTGTCGTATGGATCCGAAATGTCATCATCTATAACCTCCCAGCCGTCGGAGATGGATAGCTTGATGACCGTTATGGAAAAGCATTCCGATGGTGAAATAGTGACGGTTACAAAGCAGACAATAATAATGACGGACAAACACGAAGATTTGGAATTTTCGCGAGAGGATCCAGCCAGCGGCTCCTGGAGCGGACAGGACGAAGAGCTCAGTTCGTCTGGAAGCTTCAGTCGGGGGGCACGAGCCGATCTGATGCTTGGGAGTACGGACAGTCTTGAAGCCACCAGTTCGAACGCAACGCGAGCAACTTACAACTACGAGGTGGACACTCCAATGACCGGGAGTCTCACCTCCGGAGGGTCGAACACCATGGTGTCTTCCCTGGACACCCTGGAACCCATCACCGCCGTGCAGATGGACAGTATGGAACACCAGTCTACGAGTGAGCAGCAGTCCCACGAGTATGATGTCCAAGAACCGGATTCTGATACTGAAAGACTAGAGCTTGATAGCAAAACACCTAAAGCCAAGGAGCGAACCATAATGTTTGACAGTACTGACACTCTAAGTGCTGTGAGTGGCGATAGTTCCATCAAAGAAGCGAAAGTCGAGACGCCCGCTGCTACGTTCTATATCGGAGACACACCTATTGTTAGAGGTGGGGGACGTGAAGAGGCAGAGCCTCAGCAACCATTGTCCGAAAGCTGTCCAGCATCATTGCAACCTGTTCCTCAATCATCACCACCTGTACCTACACAAAGAAGATCCCTAACGATGATAGCCAAGGCACCGCACACAAGTCTAGAGGAAGCTGCAAAGAAATCCTAA
Protein
MPPLMEGEALASRVLEMGPVSAKFLGPVILEVPHYASLRGKEREIVILRSDNGTSWREHNADATDDVVQDILHETLEIEEANEDEKGWDAPRLTRILTHDFPQYFAVISRIRQEVHAIGPEGGMVSSSVVPQVQAVFPQGALTKKIKVGLQAQIIDSELTAKLLGRGVAVSPVVTVEPRRRKFHKAITLSMPAPRPHTQGMTNQYSTSSAPTLRLLCSISGGTNRAHWEDVTENTPLTFVNDCVSFTTTVSARYWLIDCRHIEDATKMATELYREAIHVPFMSRFVVYAKRSDENQAQLRMFCVTDDKEDKALERIERFIQVAKSRDVEVHEGKPVYLEFGGNLVPVAKSGEQLTIPFRAFRENRMAFPVMIKTQDLEPICRCQFMRDPKVPKGEPSPAPIAVLNIMVPDEPTDRTSPLPSEAVPRRTEEQELIWRQRLSDPRLEDICNLLGKDWVALAYELGVSVATVNQIQAKRITAPEQAQLMLKLWKTQSGTKAQDNSLELALCRIGRDDIIAPQSDTINERRIRRNIYQERQASEEIEAYKAEEDNKLKEKLYNEEDILPEHRESEHDQDEAKYSPEEKSIVEKSEIDRTPSPSEESEEDEDIKRSVAERKEQITRKLSSSKVPASKQKKEIREEIIEIKTQIKPDIKKFHDIEQQSLDKEPTLEKSRSKTSPDKVEEGTEEQEVITETIVEAIVEERKEEVKPVEKPIEQFRKFDPSSPAKPTPKHLQRHMRNESMRFPSGDFSNVVITPRKSITNEAVEKQAIETKPHTVTKEEISQKEIFTSKVEEKMEEIEKTAKIVKEEKDIAEATLKDKINSFESKMVKEINVDVSKPTIKLTKEALKKHTLEQGQGNGYTQEFVREQSKQLSSMESHVTHKVTVETETHIETVKSVKETIQQFDSKTKLCEKPKHFPKTIRTDSTLVQVSSEEDSEFLKKSTDSETETESQTTTVKVDKLDNKTKVKPYREYIGAEIDHEDSPKVSDKDKKGDEDDKDYKGVAVMKDVFLEKITTEEPVQVTEEYKKQSLEERDVSLTDKSKEKVETQTSTASTKSDLSRHTKTDSVGSDMQDLIAQKVSTESPIQSVVDKADSLADLQHSTEKDFSFISQTESKVYSKDSKHRSDSLDEASQFSDLEDQIGSSPAHRPVTEKIEAGSIKTDVKSVSKLIEKFDTSPKSQTMEFLKFESEHSAQVQVPLTESDKTKETPVISAKARQFIETVPEDDSVQECFFSKRIYSDSLEDSEHTDSRRHSEAESLKSDQSDTKVKVSSSEFDERAEFEEAADSGSGFGDEKFEESVGFTSFKIDPKVLEIERQDSESDKESDVVFKKMIPKRHSRTESISITKLSDIGDIEIKPKQEFQIIVTEAEEIDKSFEKDKISSEDAVTKKTSSEEDVVYEAERLQQQKTEVVATTVIEKKMVSDDAKEDVDSKRQSVTSTESVGELRLEEKRPSDAHSLTESRDYTFEESEDDIATQGTHVDHSKDIGPHKIETEEIIQIAEKSVEHPKLAKLTHGDSLDDVEGFPEDHTADYVHKLPHIAEIGSVSDKDMTIEFLNREKQEQLKRVSVQEPVPEVIVPLTQDEIIKETVTHKETPTVFTSTKTETHYSSTTRTEPLVTSEMMSQTKSSIKESTTTKSFRTEGKFDVSKIRTDTLGKFDIGEQLEEMKETKKHMPRDLQELPEITKEQVKPVIDDILQKGTIAAVARSPIVDKDIKTITKEIVESEKRSYDTKVPQKEERRHSCISPAISLERIAESDVETDEEVSKSIPIVAHEKTTEIKTDMKKSDSAMKQMADNIEIIIKQASEEVDMSSEEHPVEVAEPQDIAGQVSVDSIIEEAVTTVEGYLESAKDKEKEIEAKKEIVYAETKKFAKDRPGLIKSLSRDSGEIVIMPKKKQTRTFSVQSSPEEVEEQIYTDSESDMDKAKVLEIIEPMSDLDGKLPTSSFDSRKIRTDSLDDADDFPEKEADVFGEDYQYPDDGIHSIIKKPDTAKYEPSTSSTTKTSDEEKSTDKVMKKTHFVDSLLQSDLVSKSTTESSVTTVISTLTKSSDEEQKSVLEDCTSADLSKISGADLVKDPSKTSFDTKEDSRIDEHTEDRATPDLSKKSLDLTKDYSKSSIDSKDTSRDFATNELSKDSTVDLTKDYSKVSVESVKESSKSLDEKTISEDHSSLDVSKTLASDVSECITISKEFIEEERSVSRVFRISTSSSQETSIMTESKMFSELDDKSISKAKSEVIEVEKDLSESIQDQEQEAKRAPDTSDVAQARAVQDLQLIEDISDKSTREIKELSRTKPALTETSGENFSEEVIKPSFEKVKAEEIISSPETSHIIEKSTKLVTKPLSTVSAGTLTDVRDEQEKLKDFIKEDNVEDSKKQIEGERTVSAIADHVDGEKIAIQAKIVEEEGKSSKGDIKEERLESVTSTAEKEESDEVPDMKELNRRCSNLLEDISQGALIRIDTSHVTHDLASKFSKTPPPSPVDLILKDKTKSEEFTGEKHVGLQLRGSDSSFLDTSRQSPRASSAGDSLLSETEAHQSEVSKTPFKPIATGSRPKSPVKHIAENMEFVNVDQPTITSGAIELVDRTIEKSMDVIDQIKKEQLAVKLEEIQKSTSTDTFYSESRVETSTSSSSVHKTIEGGELKFQSIDPQALMSDMAAKFSVTDDTPTILTHKETETRKISGQEFFTETKQISSSDDDSLIIKTETTHELHGQEHETKEKTIIRKDGDQTQTSQKKLEKAHEATAKRSDIETKTVFKSTDDTDIIKVEREFSEQGLYHGRQTKSEEKMTALKDDTVKKKHEVKISERDLSHEQWGKEYFTEPGELEDIVEDDDKSKVAFVDSTLKIIESDEVVSSVEVSEKGKIVSSTLEHHREESIIESKEHDDLSSDTSHAPSFKSEPADKHDSSEASPRSKSKSFKKDNEVYEVDFIKEIKVSTSPVKSTFSRTGSQDTHSESEIAPDLPHDDKTGDTPKKERPSKSPIKLPQEQIENQVWEVTIQKADSFEIGDDTPKTPLFKTVESISTINLESTTTDIRTNIETNTADIKLTKTDMSPIAFEVSEDISGISKDIMVKSGESIDTEYMIKSLESHEGEVLQKSMDSTMSAETLQPSEFSTDSAYLTGTDHKREEIKLFKEKSLEDICSSGYDTDLSSAEFHAKLETERVDYDSLMSAQPLADLSVLEKTIDEVKQSLEAAQVEIISEKNDGSIKYKQSPSEFQFKLLISPDRPEVITEEPHHTEGHADKTPVIEKTETLLDSQISDSVTQKISSQEETTSDEDKDTVYIKEPSPPLDAGDISIRSTDSGPHSILETESEIVTSDRDGSSKGSPEVKLRVQKHIKSKLGIVERRSASDIEGWSSSGESHYHSFEHSEGRPLSSDVDVMMTAQSGTEFDTAMTSQDVSSQSLRTSRDYYTAGSSLASRDSMKSLDSDGSSHVASIDISDASETLVPSANELKEELMESSTYVEQFLHETEKDQTSKSKDISDEDVSGEEEDAKPGIFEPIGKMKRSHEMRFQPKEMIPESFQVGSTSESIEVDEDSSKDKEFSDTTISSQFKTDEILSSSISKLDMPSSQSQSELDLDEVKEVITKTICQKDEAIPFNVTKIEKPQREFADVDSDIIPIGSSEYEAIVKYGAVTSDLKSPSHQETTITKMSIEMNESTPGEHKVEVSEVCERKEIKDVSVIPFPKTEIPTPRQREFVDVEQEIIPIGSIQYEEILKSKSDSSVPKTKVEKSVIKTPESELDSKQSSMSSLKTQETPQTPLSAPSQSSISTDNGREYILDDMYDISETPELKSDVVTESSKSELMITTEEKTLYTYEKDQESPTSDEFEIVDKPSEMDEFVVIEEVAKEAQETDTEGKSVQIVAQKYVKRHDTEVEELLSKTAKKQESTSSASGSLSDEELLQFEIEQKRLQAQELAEIEAGKRWIQMRFEGDPRYDYERVPLEDIKEEEMTDFDASRIGSLSSQKESIGSFGSFRNSYGSLSESEMASRIRFRVRGENDDISISSLQEFENLERALMEQYQQNSSSSQDSLNGSLPKRYILSRSQGDDISISSLKEFEGLESACLEALRAEILAKQKEALLLADPKEVSGSFLEREKRSYSGSSESSPPQKSGSPSQKSGSPSQKGGSPSQKIGSYGSPSQKMLTDSAAIRKLIDQQMAIEAKLQEQVVPKVVTVKKFDDRGAFFVPEPETESTESKSSDINEECQKTSTFICASAPSDGSAESIPGDCEEMMKLLDQEEKSKTSQPVTRTFTDSGVIEVVRTTTVIQQRFVDGKKVSETVTSTDADVGASPVDIPARTRHYDEGILSYGSEMSSSITSQPSEMDSLMTVMEKHSDGEIVTVTKQTIIMTDKHEDLEFSREDPASGSWSGQDEELSSSGSFSRGARADLMLGSTDSLEATSSNATRATYNYEVDTPMTGSLTSGGSNTMVSSLDTLEPITAVQMDSMEHQSTSEQQSHEYDVQEPDSDTERLELDSKTPKAKERTIMFDSTDTLSAVSGDSSIKEAKVETPAATFYIGDTPIVRGGGREEAEPQQPLSESCPASLQPVPQSSPPVPTQRRSLTMIAKAPHTSLEEAAKKS
Summary
Description
Membrane-cytoskeleton linker. May participate in the maintenance/targeting of ion channels and cell adhesion molecules at the nodes of Ranvier and axonal initial segments (By similarity). In skeletal muscle, required for costamere localization of DMD and betaDAG1. Regulates KCNA1 channel activity in function of dietary Mg(2+) levels, and thereby contributes to the regulation of renal Mg(2+) reabsorption (PubMed:23903368).
Plays an essential role in the localization and membrane stabilization of ion transporters and ion channels in several cell types, including cardiomyocytes, as well as in striated muscle cells. In skeletal muscle, required for proper localization of DMD and DCTN4 and for the formation and/or stability of a special subset of microtubules associated with costameres and neuromuscular junctions. In cardiomyocytes, required for coordinate assembly of Na/Ca exchanger, SLC8A1/NCX1, Na/K ATPases ATP1A1 and ATP1A2 and inositol 1,4,5-trisphosphate (InsP3) receptors at sarcoplasmic reticulum/sarcolemma sites. Required for expression and targeting of SPTBN1 in neonatal cardiomyocytes and for the regulation of neonatal cardiomyocyte contraction rate (PubMed:12571597). In the inner segment of rod photoreceptors, required for the coordinated expression of the Na/K ATPase, Na/Ca exchanger and beta-2-spectrin (SPTBN1) (By similarity). Plays a role in endocytosis and intracellular protein transport. Associates with phosphatidylinositol 3-phosphate (PI3P)-positive organelles and binds dynactin to promote long-range motility of cells. Recruits RABGAP1L to (PI3P)-positive early endosomes, where RABGAP1L inactivates RAB22A, and promotes polarized trafficking to the leading edge of the migrating cells. Part of the ANK2/RABGAP1L complex which is required for the polarized recycling of fibronectin receptor ITGA5 ITGB1 to the plasma membrane that enables continuous directional cell migration (By similarity).
Plays an essential role in the localization and membrane stabilization of ion transporters and ion channels in several cell types, including cardiomyocytes, as well as in striated muscle cells. In skeletal muscle, required for proper localization of DMD and DCTN4 and for the formation and/or stability of a special subset of microtubules associated with costameres and neuromuscular junctions (PubMed:19109891). In cardiomyocytes, required for coordinate assembly of Na/Ca exchanger, SLC8A1/NCX1, Na/K ATPases ATP1A1 and ATP1A2 and inositol 1,4,5-trisphosphate (InsP3) receptors at sarcoplasmic reticulum/sarcolemma sites (PubMed:12571597). Required for expression and targeting of SPTBN1 in neonatal cardiomyocytes and for the regulation of neonatal cardiomyocyte contraction rate (PubMed:15262991). In the inner segment of rod photoreceptors, required for the coordinated expression of the Na/K ATPase, Na/Ca exchanger and beta-2-spectrin (SPTBN1) (PubMed:19007774). Plays a role in endocytosis and intracellular protein transport. Associates with phosphatidylinositol 3-phosphate (PI3P)-positive organelles and binds dynactin to promote long-range motility of cells. Recruits RABGAP1L to (PI3P)-positive early endosomes, where RABGAP1L inactivates RAB22A, and promotes polarized trafficking to the leading edge of the migrating cells. Part of the ANK2/RABGAP1L complex which is required for the polarized recycling of fibronectin receptor ITGA5 ITGB1 to the plasma membrane that enables continuous directional cell migration (PubMed:27718357).
In skeletal muscle, required for costamere localization of DMD and betaDAG1 (By similarity). Membrane-cytoskeleton linker. May participate in the maintenance/targeting of ion channels and cell adhesion molecules at the nodes of Ranvier and axonal initial segments. Regulates KCNA1 channel activity in function of dietary Mg(2+) levels, and thereby contributes to the regulation of renal Mg(2+) reabsorption (PubMed:23903368).
Isoform 5: May be part of a Golgi-specific membrane cytoskeleton in association with beta-spectrin.
Membrane-cytoskeleton linker. May participate in the maintenance/targeting of ion channels and cell adhesion molecules at the nodes of Ranvier and axonal initial segments. In skeletal muscle, required for costamere localization of DMD and betaDAG1 (By similarity). Regulates KCNA1 channel activity in function of dietary Mg(2+) levels, and thereby contributes to the regulation of renal Mg(2+) reabsorption (By similarity).
Attaches integral membrane proteins to cytoskeletal elements; binds to the erythrocyte membrane protein band 4.2, to Na-K ATPase, to the lymphocyte membrane protein GP85, and to the cytoskeletal proteins fodrin, tubulin, vimentin and desmin. Erythrocyte ankyrins also link spectrin (beta chain) to the cytoplasmic domain of the erythrocytes anion exchange protein; they retain most or all of these binding functions.
Isoform Mu17: Together with obscurin in skeletal muscle may provide a molecular link between the sarcoplasmic reticulum and myofibrils.
Component of the DNA damage/stress response pathway that functions downstream of p53/TP53 and can either promote cell survival or apoptosis (PubMed:10973264, PubMed:15073321, PubMed:16360037, PubMed:17159900). Associated with CRADD and the CASP2 caspase, it forms the PIDDosome a complex that activates CASP2 and triggers apoptosis (PubMed:15073321, PubMed:17159900). Associated with IKBKG and RIPK1, it enhances sumoylation and ubiquitination of IKBKG which is important for activation of the transcription factor NF-kappa-B (PubMed:16360037, PubMed:17159900).
Plays an essential role in the localization and membrane stabilization of ion transporters and ion channels in several cell types, including cardiomyocytes, as well as in striated muscle cells. In skeletal muscle, required for proper localization of DMD and DCTN4 and for the formation and/or stability of a special subset of microtubules associated with costameres and neuromuscular junctions. In cardiomyocytes, required for coordinate assembly of Na/Ca exchanger, SLC8A1/NCX1, Na/K ATPases ATP1A1 and ATP1A2 and inositol 1,4,5-trisphosphate (InsP3) receptors at sarcoplasmic reticulum/sarcolemma sites. Required for expression and targeting of SPTBN1 in neonatal cardiomyocytes and for the regulation of neonatal cardiomyocyte contraction rate (PubMed:12571597). In the inner segment of rod photoreceptors, required for the coordinated expression of the Na/K ATPase, Na/Ca exchanger and beta-2-spectrin (SPTBN1) (By similarity). Plays a role in endocytosis and intracellular protein transport. Associates with phosphatidylinositol 3-phosphate (PI3P)-positive organelles and binds dynactin to promote long-range motility of cells. Recruits RABGAP1L to (PI3P)-positive early endosomes, where RABGAP1L inactivates RAB22A, and promotes polarized trafficking to the leading edge of the migrating cells. Part of the ANK2/RABGAP1L complex which is required for the polarized recycling of fibronectin receptor ITGA5 ITGB1 to the plasma membrane that enables continuous directional cell migration (By similarity).
Plays an essential role in the localization and membrane stabilization of ion transporters and ion channels in several cell types, including cardiomyocytes, as well as in striated muscle cells. In skeletal muscle, required for proper localization of DMD and DCTN4 and for the formation and/or stability of a special subset of microtubules associated with costameres and neuromuscular junctions (PubMed:19109891). In cardiomyocytes, required for coordinate assembly of Na/Ca exchanger, SLC8A1/NCX1, Na/K ATPases ATP1A1 and ATP1A2 and inositol 1,4,5-trisphosphate (InsP3) receptors at sarcoplasmic reticulum/sarcolemma sites (PubMed:12571597). Required for expression and targeting of SPTBN1 in neonatal cardiomyocytes and for the regulation of neonatal cardiomyocyte contraction rate (PubMed:15262991). In the inner segment of rod photoreceptors, required for the coordinated expression of the Na/K ATPase, Na/Ca exchanger and beta-2-spectrin (SPTBN1) (PubMed:19007774). Plays a role in endocytosis and intracellular protein transport. Associates with phosphatidylinositol 3-phosphate (PI3P)-positive organelles and binds dynactin to promote long-range motility of cells. Recruits RABGAP1L to (PI3P)-positive early endosomes, where RABGAP1L inactivates RAB22A, and promotes polarized trafficking to the leading edge of the migrating cells. Part of the ANK2/RABGAP1L complex which is required for the polarized recycling of fibronectin receptor ITGA5 ITGB1 to the plasma membrane that enables continuous directional cell migration (PubMed:27718357).
In skeletal muscle, required for costamere localization of DMD and betaDAG1 (By similarity). Membrane-cytoskeleton linker. May participate in the maintenance/targeting of ion channels and cell adhesion molecules at the nodes of Ranvier and axonal initial segments. Regulates KCNA1 channel activity in function of dietary Mg(2+) levels, and thereby contributes to the regulation of renal Mg(2+) reabsorption (PubMed:23903368).
Isoform 5: May be part of a Golgi-specific membrane cytoskeleton in association with beta-spectrin.
Membrane-cytoskeleton linker. May participate in the maintenance/targeting of ion channels and cell adhesion molecules at the nodes of Ranvier and axonal initial segments. In skeletal muscle, required for costamere localization of DMD and betaDAG1 (By similarity). Regulates KCNA1 channel activity in function of dietary Mg(2+) levels, and thereby contributes to the regulation of renal Mg(2+) reabsorption (By similarity).
Attaches integral membrane proteins to cytoskeletal elements; binds to the erythrocyte membrane protein band 4.2, to Na-K ATPase, to the lymphocyte membrane protein GP85, and to the cytoskeletal proteins fodrin, tubulin, vimentin and desmin. Erythrocyte ankyrins also link spectrin (beta chain) to the cytoplasmic domain of the erythrocytes anion exchange protein; they retain most or all of these binding functions.
Isoform Mu17: Together with obscurin in skeletal muscle may provide a molecular link between the sarcoplasmic reticulum and myofibrils.
Component of the DNA damage/stress response pathway that functions downstream of p53/TP53 and can either promote cell survival or apoptosis (PubMed:10973264, PubMed:15073321, PubMed:16360037, PubMed:17159900). Associated with CRADD and the CASP2 caspase, it forms the PIDDosome a complex that activates CASP2 and triggers apoptosis (PubMed:15073321, PubMed:17159900). Associated with IKBKG and RIPK1, it enhances sumoylation and ubiquitination of IKBKG which is important for activation of the transcription factor NF-kappa-B (PubMed:16360037, PubMed:17159900).
Subunit
May be a constituent of a NFASC/NRCAM/ankyrin G complex. Interacts with RHBG (By similarity). Directly interacts with DMD and betaDAG1; this interaction does not interfere with DMD-binding and is required for DMD and betaDAG1 retention at costameres. Interacts (via N-terminal ANK repeats) with SCHIP1 isoform 7 (via C-terminus); this interaction is required for the localization at axon initial segments (AISs) and nodes of Ranvier (NRs). Interacts with PLEC and FLNC (By similarity). Interacts with KCNA1; this inhibits channel activity (PubMed:23903368). Interacts with SCN5A (By similarity).
Interacts with RHBG and SPTBN1 (PubMed:15262991, PubMed:15611082). Colocalizes with Na/K ATPase, Na/Ca exchanger and SPTBN1 (PubMed:19007774). Directly interacts with DMD; this interaction is necessary for DMD localization at the sarcolemma. Interacts with DCTN4; this interaction is required for DCTN4 retention at costameres. Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin (By similarity). Interacts (via death domain) with RABGAP1L (via Rab-GAP TBC domain) (PubMed:27718357).
Interacts with RHBG (By similarity). Interacts with SPTBN1 (PubMed:15262991, PubMed:19007774). Colocalizes with Na/Ca exchanger (PubMed:19007774). Interacts with Na/K ATPases ATP1A1 and ATP1A2 (PubMed:19007774, PubMed:12571597). Directly interacts with DMD; this interaction is necessary for DMD localization at the sarcolemma. Interacts with DCTN4; this interaction is required for DCTN4 retention at costameres (PubMed:19109891). Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin (PubMed:21745462). Interacts (via death domain) with RABGAP1L (via Rab-GAP TBC domain) (PubMed:27718357). Interacts with SLC8A1/NCX1 (PubMed:12571597). May interact with inositol 1,4,5-trisphosphate receptors (PubMed:12571597).
Directly interacts with DMD and betaDAG1. This interaction does not interfere with binding between DMD and betaDAG1. It is also required for DMD and betaDAG1 retention at costameres (By similarity). Interacts (via N-terminal ANK repeats) with SCHIP1 isoform 5 (via C-terminus); this interaction is required for the localization at axon initial segments (AISs) and nodes of Ranvier (NRs) (By similarity). May be a constituent of a NFASC/NRCAM/ankyrin G complex. Interacts with RHBG (PubMed:15611082). Interacts with PLEC and FLNC (PubMed:21223964). Interacts with KCNA1; this inhibits channel activity (PubMed:23903368). Interacts (via ANK repeats) with IQCJ-SCHIP1; required for IQCJ-SCHIP1 localization at axon initial segments (AIS) and nodes of Ranvier (PubMed:25950943). Interacts with SCHIP1 (PubMed:25950943). Interacts with SCN5A (PubMed:15579534).
May be a constituent of a NFASC/NRCAM/ankyrin G complex. Interacts with RHBG. Directly interacts with DMD and betaDAG1; this interaction does not interfere with DMD-binding and is required for DMD and betaDAG1 retention at costameres. Interacts (via N-terminal ANK repeats) with SCHIP1 isoform 7 (via C-terminus); this interaction is required for the localization at axon initial segments (AISs) and nodes of Ranvier (NRs) (By similarity). Interacts with PLEC and FLNC (PubMed:21223964). Isoform 7 interacts with PLEC and FLNC through its muscle-specific C-terminal sequence. Interacts with KCNA1; this inhibits channel activity (By similarity). Interacts (via ANK repeats) with IQCJ-SCHIP1; required for IQCJ-SCHIP1 localization at axon initial segments (AIS) and nodes of Ranvier (By similarity). Interacts with SCHIP1 (By similarity). Interacts with SCN5A (By similarity).
Interacts with a number of integral membrane proteins and cytoskeletal proteins. Interacts (via N-terminus) with SPTB/spectrin (beta chain). Interacts (via N-terminus ANK repeats) with SLC4A1/erythrocyte membrane protein band 3 (via cytoplasmic N-terminus). Also interacts with TTN/titin. Isoform Mu17 interacts with OBSCN isoform 3/obscurin. Interacts with HIF1AN.
Interacts with a number of integral membrane proteins and cytoskeletal proteins. Interacts (via N-terminus) with SPTB/spectrin (beta chain). Interacts (via N-terminus ANK repeats) with SLC4A1/erythrocyte membrane protein band 3 (via cytoplasmic N-terminus). Also interacts with TTN/titin. Isoform Mu17 interacts with OBSCN isoform 3/obscurin. Interacts with HIF1AN (By similarity).
Forms a complex named the PIDDosome with CASP2 and CRADD (PubMed:15073321, PubMed:16652156, PubMed:17159900, PubMed:17289572). Forms a complex with IKBKG and RIPK1 (PubMed:16360037). Interacts with FADD and MADD (PubMed:10825539).
Interacts with RHBG and SPTBN1 (PubMed:15262991, PubMed:15611082). Colocalizes with Na/K ATPase, Na/Ca exchanger and SPTBN1 (PubMed:19007774). Directly interacts with DMD; this interaction is necessary for DMD localization at the sarcolemma. Interacts with DCTN4; this interaction is required for DCTN4 retention at costameres. Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin (By similarity). Interacts (via death domain) with RABGAP1L (via Rab-GAP TBC domain) (PubMed:27718357).
Interacts with RHBG (By similarity). Interacts with SPTBN1 (PubMed:15262991, PubMed:19007774). Colocalizes with Na/Ca exchanger (PubMed:19007774). Interacts with Na/K ATPases ATP1A1 and ATP1A2 (PubMed:19007774, PubMed:12571597). Directly interacts with DMD; this interaction is necessary for DMD localization at the sarcolemma. Interacts with DCTN4; this interaction is required for DCTN4 retention at costameres (PubMed:19109891). Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin (PubMed:21745462). Interacts (via death domain) with RABGAP1L (via Rab-GAP TBC domain) (PubMed:27718357). Interacts with SLC8A1/NCX1 (PubMed:12571597). May interact with inositol 1,4,5-trisphosphate receptors (PubMed:12571597).
Directly interacts with DMD and betaDAG1. This interaction does not interfere with binding between DMD and betaDAG1. It is also required for DMD and betaDAG1 retention at costameres (By similarity). Interacts (via N-terminal ANK repeats) with SCHIP1 isoform 5 (via C-terminus); this interaction is required for the localization at axon initial segments (AISs) and nodes of Ranvier (NRs) (By similarity). May be a constituent of a NFASC/NRCAM/ankyrin G complex. Interacts with RHBG (PubMed:15611082). Interacts with PLEC and FLNC (PubMed:21223964). Interacts with KCNA1; this inhibits channel activity (PubMed:23903368). Interacts (via ANK repeats) with IQCJ-SCHIP1; required for IQCJ-SCHIP1 localization at axon initial segments (AIS) and nodes of Ranvier (PubMed:25950943). Interacts with SCHIP1 (PubMed:25950943). Interacts with SCN5A (PubMed:15579534).
May be a constituent of a NFASC/NRCAM/ankyrin G complex. Interacts with RHBG. Directly interacts with DMD and betaDAG1; this interaction does not interfere with DMD-binding and is required for DMD and betaDAG1 retention at costameres. Interacts (via N-terminal ANK repeats) with SCHIP1 isoform 7 (via C-terminus); this interaction is required for the localization at axon initial segments (AISs) and nodes of Ranvier (NRs) (By similarity). Interacts with PLEC and FLNC (PubMed:21223964). Isoform 7 interacts with PLEC and FLNC through its muscle-specific C-terminal sequence. Interacts with KCNA1; this inhibits channel activity (By similarity). Interacts (via ANK repeats) with IQCJ-SCHIP1; required for IQCJ-SCHIP1 localization at axon initial segments (AIS) and nodes of Ranvier (By similarity). Interacts with SCHIP1 (By similarity). Interacts with SCN5A (By similarity).
Interacts with a number of integral membrane proteins and cytoskeletal proteins. Interacts (via N-terminus) with SPTB/spectrin (beta chain). Interacts (via N-terminus ANK repeats) with SLC4A1/erythrocyte membrane protein band 3 (via cytoplasmic N-terminus). Also interacts with TTN/titin. Isoform Mu17 interacts with OBSCN isoform 3/obscurin. Interacts with HIF1AN.
Interacts with a number of integral membrane proteins and cytoskeletal proteins. Interacts (via N-terminus) with SPTB/spectrin (beta chain). Interacts (via N-terminus ANK repeats) with SLC4A1/erythrocyte membrane protein band 3 (via cytoplasmic N-terminus). Also interacts with TTN/titin. Isoform Mu17 interacts with OBSCN isoform 3/obscurin. Interacts with HIF1AN (By similarity).
Forms a complex named the PIDDosome with CASP2 and CRADD (PubMed:15073321, PubMed:16652156, PubMed:17159900, PubMed:17289572). Forms a complex with IKBKG and RIPK1 (PubMed:16360037). Interacts with FADD and MADD (PubMed:10825539).
Keywords
Alternative splicing
ANK repeat
Cell junction
Cell membrane
Cell projection
Complete proteome
Cytoplasm
Cytoskeleton
Lysosome
Membrane
Phosphoprotein
Postsynaptic cell membrane
Reference proteome
Repeat
Synapse
3D-structure
Disease mutation
Endocytosis
Endosome
Long QT syndrome
Mitochondrion
Polymorphism
Protein transport
Transport
Autism spectrum disorder
Golgi apparatus
Mental retardation
Alternative promoter usage
Direct protein sequencing
Elliptocytosis
Hereditary hemolytic anemia
Hydroxylation
Lipoprotein
Sarcoplasmic reticulum
Acetylation
Apoptosis
Hydrolase
Leucine-rich repeat
Nucleus
Feature
chain Ankyrin-3
splice variant In isoform 4, isoform 5 and isoform 6.
sequence variant In a breast cancer sample; somatic mutation.
splice variant In isoform 4, isoform 5 and isoform 6.
sequence variant In a breast cancer sample; somatic mutation.
EC Number
3.4.21.-
Pubmed
7615634
16141072
19468303
15489334
9060470
19109891
+ More
18550753 21183079 21223964 23903368 1830053 8253844 17974005 15815621 1833308 12571597 15262991 15611082 19007774 21269460 21406692 24275569 27718357 22411828 15178757 16959974 17940615 16452087 18034455 21745462 7836469 8666667 11230166 14702039 15164054 15579534 23186163 25950943 25966638 25307106 22865819 23390136 9744885 11796721 15953600 22673903 2137557 1689849 9235914 9430667 16421571 2141335 21177872 7665627 12444090 12527750 18088087 18669648 12456646 22310050 8640229 11102985 1386265 8486643 9628825 9024692 17242355 10825539 10973264 15073321 16360037 16652156 17159900 17289572 28397838
18550753 21183079 21223964 23903368 1830053 8253844 17974005 15815621 1833308 12571597 15262991 15611082 19007774 21269460 21406692 24275569 27718357 22411828 15178757 16959974 17940615 16452087 18034455 21745462 7836469 8666667 11230166 14702039 15164054 15579534 23186163 25950943 25966638 25307106 22865819 23390136 9744885 11796721 15953600 22673903 2137557 1689849 9235914 9430667 16421571 2141335 21177872 7665627 12444090 12527750 18088087 18669648 12456646 22310050 8640229 11102985 1386265 8486643 9628825 9024692 17242355 10825539 10973264 15073321 16360037 16652156 17159900 17289572 28397838
EMBL
L40631
L40632
AK035681
AK162007
AC100427
AC129018
+ More
AC132435 AC156836 CH466553 BC021657 U89274 U89275 X56957 X56958 Z26634 BX537758 AC004057 AC093617 AC093879 AC093900 BC125235 BC125236 M37123 AK032060 AK036018 AK044634 AK083111 AK083826 AK084070 AK166115 AC102480 AC102591 AC131744 BC043123 BC059251 AAH59251.1 BAC27676.1 BAC32012.1 BAC38764.1 BAE38580.1 BAE43385.1 U13616 U43965 AL136710 AK295661 BX537917 BX648574 AC022390 AC023904 AL359267 AL359377 AL391707 AL592430 AL607065 AF102552 AJ428573 AJ812019 AJ812021 AJ812022 AJ812023 AJ812024 X16609 M28880 U50133 U50092 U50093 U50094 U50095 U50096 U50097 U50098 U50099 U50100 U50101 U50102 U50103 U50104 U50105 U50106 U50107 U50108 U50109 U50110 U50111 U50112 U50113 U50114 U50115 U50116 U50117 U50118 U50119 U50120 U50121 U50122 U50123 U50124 U50125 U50126 U50127 U50128 U50129 U50130 U50131 U50132 AF005213 AB209418 AK223578 AC027702 AC113133 CH471080 BC030957 BC117121 BC014467 M84756 X69063 X69064 U73972 AK134267 AK147278 AK147597 AK158131 BC061219 U76758 AF229178 AF274972 AF465246 AK074893 AB208832 AB208949 AB209529 AL833849 BC014904
AC132435 AC156836 CH466553 BC021657 U89274 U89275 X56957 X56958 Z26634 BX537758 AC004057 AC093617 AC093879 AC093900 BC125235 BC125236 M37123 AK032060 AK036018 AK044634 AK083111 AK083826 AK084070 AK166115 AC102480 AC102591 AC131744 BC043123 BC059251 AAH59251.1 BAC27676.1 BAC32012.1 BAC38764.1 BAE38580.1 BAE43385.1 U13616 U43965 AL136710 AK295661 BX537917 BX648574 AC022390 AC023904 AL359267 AL359377 AL391707 AL592430 AL607065 AF102552 AJ428573 AJ812019 AJ812021 AJ812022 AJ812023 AJ812024 X16609 M28880 U50133 U50092 U50093 U50094 U50095 U50096 U50097 U50098 U50099 U50100 U50101 U50102 U50103 U50104 U50105 U50106 U50107 U50108 U50109 U50110 U50111 U50112 U50113 U50114 U50115 U50116 U50117 U50118 U50119 U50120 U50121 U50122 U50123 U50124 U50125 U50126 U50127 U50128 U50129 U50130 U50131 U50132 AF005213 AB209418 AK223578 AC027702 AC113133 CH471080 BC030957 BC117121 BC014467 M84756 X69063 X69064 U73972 AK134267 AK147278 AK147597 AK158131 BC061219 U76758 AF229178 AF274972 AF465246 AK074893 AB208832 AB208949 AB209529 AL833849 BC014904
Proteomes
Pfam
Interpro
IPR002110
Ankyrin_rpt
+ More
IPR000488 Death_domain
IPR020683 Ankyrin_rpt-contain_dom
IPR000906 ZU5_dom
IPR011029 DEATH-like_dom_sf
IPR036770 Ankyrin_rpt-contain_sf
IPR037971 Ank3_Death
IPR040745 Ankyrin_UPA
IPR032675 LRR_dom_sf
IPR003591 Leu-rich_rpt_typical-subtyp
IPR019502 Peptidase_S68_pidd
IPR001611 Leu-rich_rpt
IPR000488 Death_domain
IPR020683 Ankyrin_rpt-contain_dom
IPR000906 ZU5_dom
IPR011029 DEATH-like_dom_sf
IPR036770 Ankyrin_rpt-contain_sf
IPR037971 Ank3_Death
IPR040745 Ankyrin_UPA
IPR032675 LRR_dom_sf
IPR003591 Leu-rich_rpt_typical-subtyp
IPR019502 Peptidase_S68_pidd
IPR001611 Leu-rich_rpt
Gene 3D
PDB
4D8O
E-value=1.22065e-128,
Score=1187
Ontologies
GO
GO:0045162
GO:0045296
GO:0016323
GO:0043001
GO:0045838
GO:0030315
GO:0010960
GO:0033270
GO:0014704
GO:0090314
GO:2000651
GO:0072660
GO:0010628
GO:0005200
GO:0016328
GO:0071286
GO:0014731
GO:0033268
GO:1900827
GO:0050808
GO:0007165
GO:0005764
GO:0030018
GO:0099612
GO:0007528
GO:0042383
GO:0010765
GO:0072659
GO:0045211
GO:0030507
GO:0019228
GO:0005886
GO:0007409
GO:0034112
GO:1902260
GO:0140031
GO:0016529
GO:0043266
GO:0009986
GO:0030425
GO:0043005
GO:0030424
GO:0043194
GO:0010650
GO:0044325
GO:0045184
GO:0030674
GO:0007411
GO:0016020
GO:0031594
GO:0007009
GO:0045760
GO:0009925
GO:0045202
GO:0008092
GO:2001259
GO:0000281
GO:0071709
GO:0031672
GO:0050821
GO:0055037
GO:0043034
GO:0010881
GO:0036371
GO:0060307
GO:1901019
GO:0019901
GO:0086070
GO:0051928
GO:0034394
GO:0051597
GO:0005769
GO:0043268
GO:0055117
GO:0033365
GO:0006897
GO:0019899
GO:0086005
GO:1901021
GO:0006874
GO:0015031
GO:0036309
GO:0010882
GO:0086015
GO:0006888
GO:0070296
GO:0070972
GO:0086046
GO:0051924
GO:0002027
GO:0086066
GO:0031647
GO:0034613
GO:0005739
GO:0005829
GO:0030913
GO:0033292
GO:0086004
GO:0051279
GO:1901018
GO:0005856
GO:0086014
GO:0098907
GO:0098910
GO:0031430
GO:0045121
GO:0051117
GO:0003283
GO:0016324
GO:0086091
GO:0005737
GO:0008104
GO:0086036
GO:0015459
GO:2001257
GO:0098904
GO:0014069
GO:0060048
GO:0005887
GO:0048471
GO:0005794
GO:0007016
GO:0005783
GO:0005198
GO:0006887
GO:0005634
GO:0009898
GO:0010638
GO:0030673
GO:0007010
GO:0008093
GO:0019903
GO:0045199
GO:0015672
GO:0055072
GO:0048821
GO:0030863
GO:0006779
GO:0004175
GO:0016540
GO:0051092
GO:0006977
GO:0005123
GO:0034702
GO:0006974
GO:0006915
GO:0005225
GO:0043065
GO:0098656
GO:0042981
GO:0005654
GO:0043122
GO:0043066
GO:0006919
GO:0008625
GO:0005515
GO:0007264
GO:0006811
GO:0005220
GO:0006816
GO:0000287
GO:0006281
GO:0006259
Topology
Subcellular location
Cytoplasm
Cytoskeleton
Cell projection
Axon
Cell membrane
Sarcolemma
Cell junction
Synapse
Postsynaptic cell membrane
Lysosome
T-tubule
Membrane Expressed at the apical membrane of airway lung epithelial cells (By similarity). Localized to the plasma membrane of the inner segments of photoreceptors in retina. Colocalizes with SPTBN1 in a distinct intracellular compartment of neonatal cardiomyocytes (PubMed:19007774). In skeletal muscle, localizes to neuromuscular junctions (By similarity). Localizes with puncta at mitochondria ends. Colocalizes and cotransports on motile vesicles with RABGAP1L (By similarity). With evidence from 9 publications.
Myofibril Expressed at the apical membrane of airway lung epithelial cells (By similarity). Localized to the plasma membrane of the inner segments of photoreceptors in retina. Colocalizes with SPTBN1 in a distinct intracellular compartment of neonatal cardiomyocytes (PubMed:19007774). In skeletal muscle, localizes to neuromuscular junctions (By similarity). Localizes with puncta at mitochondria ends. Colocalizes and cotransports on motile vesicles with RABGAP1L (By similarity). With evidence from 9 publications.
Sarcomere Expressed at the apical membrane of airway lung epithelial cells (By similarity). Localized to the plasma membrane of the inner segments of photoreceptors in retina. Colocalizes with SPTBN1 in a distinct intracellular compartment of neonatal cardiomyocytes (PubMed:19007774). In skeletal muscle, localizes to neuromuscular junctions (By similarity). Localizes with puncta at mitochondria ends. Colocalizes and cotransports on motile vesicles with RABGAP1L (By similarity). With evidence from 9 publications.
M line Expressed at the apical membrane of airway lung epithelial cells (By similarity). Localized to the plasma membrane of the inner segments of photoreceptors in retina. Colocalizes with SPTBN1 in a distinct intracellular compartment of neonatal cardiomyocytes (PubMed:19007774). In skeletal muscle, localizes to neuromuscular junctions (By similarity). Localizes with puncta at mitochondria ends. Colocalizes and cotransports on motile vesicles with RABGAP1L (By similarity). With evidence from 9 publications.
Apical cell membrane Expressed at the apical membrane of airway lung epithelial cells (By similarity). Localized to the plasma membrane of the inner segments of photoreceptors in retina. Colocalizes with SPTBN1 in a distinct intracellular compartment of neonatal cardiomyocytes (PubMed:19007774). In skeletal muscle, localizes to neuromuscular junctions (By similarity). Localizes with puncta at mitochondria ends. Colocalizes and cotransports on motile vesicles with RABGAP1L (By similarity). With evidence from 9 publications.
Early endosome Expressed at the apical membrane of airway lung epithelial cells (By similarity). Localized to the plasma membrane of the inner segments of photoreceptors in retina. Colocalizes with SPTBN1 in a distinct intracellular compartment of neonatal cardiomyocytes (PubMed:19007774). In skeletal muscle, localizes to neuromuscular junctions (By similarity). Localizes with puncta at mitochondria ends. Colocalizes and cotransports on motile vesicles with RABGAP1L (By similarity). With evidence from 9 publications.
Recycling endosome Expressed at the apical membrane of airway lung epithelial cells (By similarity). Localized to the plasma membrane of the inner segments of photoreceptors in retina. Colocalizes with SPTBN1 in a distinct intracellular compartment of neonatal cardiomyocytes (PubMed:19007774). In skeletal muscle, localizes to neuromuscular junctions (By similarity). Localizes with puncta at mitochondria ends. Colocalizes and cotransports on motile vesicles with RABGAP1L (By similarity). With evidence from 9 publications.
Mitochondrion Expressed at the apical membrane of airway lung epithelial cells (By similarity). Localized to the plasma membrane of the inner segments of photoreceptors in retina. Colocalizes with SPTBN1 in a distinct intracellular compartment of neonatal cardiomyocytes (PubMed:19007774). In skeletal muscle, localizes to neuromuscular junctions (By similarity). Localizes with puncta at mitochondria ends. Colocalizes and cotransports on motile vesicles with RABGAP1L (By similarity). With evidence from 9 publications.
Z line Expressed at the apical membrane of airway lung epithelial cells (By similarity). Localized to the plasma membrane of the inner segments of photoreceptors in retina. Colocalizes with SPTBN1 in a distinct intracellular compartment of neonatal cardiomyocytes (PubMed:19007774). In skeletal muscle, localizes to neuromuscular junctions (By similarity). Localizes with puncta at mitochondria ends. Colocalizes and cotransports on motile vesicles with RABGAP1L (By similarity). With evidence from 9 publications.
Golgi apparatus
Sarcoplasmic reticulum
Nucleus Enriched in the nucleus upon DNA damage. With evidence from 12 publications.
Cytoskeleton
Cell projection
Axon
Cell membrane
Sarcolemma
Cell junction
Synapse
Postsynaptic cell membrane
Lysosome
T-tubule
Membrane Expressed at the apical membrane of airway lung epithelial cells (By similarity). Localized to the plasma membrane of the inner segments of photoreceptors in retina. Colocalizes with SPTBN1 in a distinct intracellular compartment of neonatal cardiomyocytes (PubMed:19007774). In skeletal muscle, localizes to neuromuscular junctions (By similarity). Localizes with puncta at mitochondria ends. Colocalizes and cotransports on motile vesicles with RABGAP1L (By similarity). With evidence from 9 publications.
Myofibril Expressed at the apical membrane of airway lung epithelial cells (By similarity). Localized to the plasma membrane of the inner segments of photoreceptors in retina. Colocalizes with SPTBN1 in a distinct intracellular compartment of neonatal cardiomyocytes (PubMed:19007774). In skeletal muscle, localizes to neuromuscular junctions (By similarity). Localizes with puncta at mitochondria ends. Colocalizes and cotransports on motile vesicles with RABGAP1L (By similarity). With evidence from 9 publications.
Sarcomere Expressed at the apical membrane of airway lung epithelial cells (By similarity). Localized to the plasma membrane of the inner segments of photoreceptors in retina. Colocalizes with SPTBN1 in a distinct intracellular compartment of neonatal cardiomyocytes (PubMed:19007774). In skeletal muscle, localizes to neuromuscular junctions (By similarity). Localizes with puncta at mitochondria ends. Colocalizes and cotransports on motile vesicles with RABGAP1L (By similarity). With evidence from 9 publications.
M line Expressed at the apical membrane of airway lung epithelial cells (By similarity). Localized to the plasma membrane of the inner segments of photoreceptors in retina. Colocalizes with SPTBN1 in a distinct intracellular compartment of neonatal cardiomyocytes (PubMed:19007774). In skeletal muscle, localizes to neuromuscular junctions (By similarity). Localizes with puncta at mitochondria ends. Colocalizes and cotransports on motile vesicles with RABGAP1L (By similarity). With evidence from 9 publications.
Apical cell membrane Expressed at the apical membrane of airway lung epithelial cells (By similarity). Localized to the plasma membrane of the inner segments of photoreceptors in retina. Colocalizes with SPTBN1 in a distinct intracellular compartment of neonatal cardiomyocytes (PubMed:19007774). In skeletal muscle, localizes to neuromuscular junctions (By similarity). Localizes with puncta at mitochondria ends. Colocalizes and cotransports on motile vesicles with RABGAP1L (By similarity). With evidence from 9 publications.
Early endosome Expressed at the apical membrane of airway lung epithelial cells (By similarity). Localized to the plasma membrane of the inner segments of photoreceptors in retina. Colocalizes with SPTBN1 in a distinct intracellular compartment of neonatal cardiomyocytes (PubMed:19007774). In skeletal muscle, localizes to neuromuscular junctions (By similarity). Localizes with puncta at mitochondria ends. Colocalizes and cotransports on motile vesicles with RABGAP1L (By similarity). With evidence from 9 publications.
Recycling endosome Expressed at the apical membrane of airway lung epithelial cells (By similarity). Localized to the plasma membrane of the inner segments of photoreceptors in retina. Colocalizes with SPTBN1 in a distinct intracellular compartment of neonatal cardiomyocytes (PubMed:19007774). In skeletal muscle, localizes to neuromuscular junctions (By similarity). Localizes with puncta at mitochondria ends. Colocalizes and cotransports on motile vesicles with RABGAP1L (By similarity). With evidence from 9 publications.
Mitochondrion Expressed at the apical membrane of airway lung epithelial cells (By similarity). Localized to the plasma membrane of the inner segments of photoreceptors in retina. Colocalizes with SPTBN1 in a distinct intracellular compartment of neonatal cardiomyocytes (PubMed:19007774). In skeletal muscle, localizes to neuromuscular junctions (By similarity). Localizes with puncta at mitochondria ends. Colocalizes and cotransports on motile vesicles with RABGAP1L (By similarity). With evidence from 9 publications.
Z line Expressed at the apical membrane of airway lung epithelial cells (By similarity). Localized to the plasma membrane of the inner segments of photoreceptors in retina. Colocalizes with SPTBN1 in a distinct intracellular compartment of neonatal cardiomyocytes (PubMed:19007774). In skeletal muscle, localizes to neuromuscular junctions (By similarity). Localizes with puncta at mitochondria ends. Colocalizes and cotransports on motile vesicles with RABGAP1L (By similarity). With evidence from 9 publications.
Golgi apparatus
Sarcoplasmic reticulum
Nucleus Enriched in the nucleus upon DNA damage. With evidence from 12 publications.
Length:
4582
Number of predicted TMHs:
0
Exp number of AAs in TMHs:
0.00204
Exp number, first 60 AAs:
0.00204
Total prob of N-in:
0.00011
outside
1 - 4582
Population Genetic Test Statistics
Pi
223.220211
Theta
201.085053
Tajima's D
0.208189
CLR
0.842888
CSRT
0.428828558572071
Interpretation
Uncertain
