| IED ID | IndEnz0002018759 |
| Enzyme Type ID | protease018759 |
| Protein Name |
Gamma-adducin Adducin-like protein 70 |
| Gene Name | ADD3 ADDL |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MSSDASQGVITTPPPPSMPHKERYFDRINENDPEYIRERNMSPDLRQDFNMMEQRKRVTQILQSPAFREDLECLIQEQMKKGHNPTGLLALQQIADYIMANSFSGFSSPPLSLGMVTPINDLPGADTSSYVKGEKLTRCKLASLYRLVDLFGWAHLANTYISVRISKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDQGSTNLKIDHTGFSPHAAIYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESLLLGDVAYYDYQGSLEEQEERIQLQKVLGPSCKVLVLRNHGVVALGETLEEAFHYIFNVQLACEIQVQALAGAGGVDNLHVLDFQKYKAFTYTVAASGGGGVNMGSHQKWKVGEIEFEGLMRTLDNLGYRTGYAYRHPLIREKPRHKSDVEIPATVTAFSFEDDTVPLSPLKYMAQRQQREKTRWLNSPNTYMKVNVPEESRNGETSPRTKITWMKAEDSSKVSGGTPIKIEDPNQFVPLNTNPNEVLEKRNKIREQNRYDLKTAGPQSQLLAGIVVDKPPSTMQFEDDDHGPPAPPNPFSHLTEGELEEYKRTIERKQQGLEDAEQELLSDDASSVSQIQSQTQSPQNVPEKLEENHELFSKSFISMEVPVMVVNGKDDMHDVEDELAKRVSRLSTSTTIENIEITIKSPEKIEEVLSPEGSPSKSPSKKKKKFRTPSFLKKNKKKEKVEA |
| Enzyme Length | 706 |
| Uniprot Accession Number | Q9UEY8 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Membrane-cytoskeleton-associated protein that promotes the assembly of the spectrin-actin network. Plays a role in actin filament capping (PubMed:23836506). Binds to calmodulin. {ECO:0000269|PubMed:23836506}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (1); Chain (1); Compositional bias (2); Cross-link (1); Initiator methionine (1); Modified residue (15); Natural variant (1); Region (6); Sequence conflict (7) |
| Keywords | Acetylation;Actin-binding;Alternative splicing;Calmodulin-binding;Cell membrane;Cytoplasm;Cytoskeleton;Disease variant;Isopeptide bond;Membrane;Phosphoprotein;Reference proteome;Ubl conjugation |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein; Cytoplasmic side. |
| Modified Residue | MOD_RES 2; /note="N-acetylserine"; /evidence="ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231"; MOD_RES 42; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"; MOD_RES 64; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"; MOD_RES 402; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:19690332"; MOD_RES 414; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q9QYB5"; MOD_RES 423; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332"; MOD_RES 442; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"; MOD_RES 461; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 585; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q9QYB5"; MOD_RES 590; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q9QYB5"; MOD_RES 673; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"; MOD_RES 677; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"; MOD_RES 679; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q9QYB5"; MOD_RES 681; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"; MOD_RES 683; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163" |
| Post Translational Modification | PTM: Sumoylated. {ECO:0000269|PubMed:15561718}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11784792; 12951058; 15716695; 15834281; 15963851; 16385451; 17500595; 17916560; 18347014; 1840603; 18475162; 18667944; 18787518; 18847512; 19463016; 19913121; 20233848; 20379614; 20628086; 20711500; 20810786; 21119010; 21164023; 21851590; 22665057; 23275563; 23752268; 23764002; 23814265; 23872602; 23902751; 24104524; 25277244; 25285724; 25609649; 25668492; 26496610; 26638075; 27278019; 28033648; 28486133; 28902846; 29508064; 29685956; 29768408; 31871319; 31958485; 32237935; 32315284; 33172155; 7615546; |
| Motif | |
| Gene Encoded By | |
| Mass | 79,155 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |