IED Industry Enzyme Database

Detail Information for IndEnz0002016637
IED ID IndEnz0002016637
Enzyme Type ID protease016637
Protein Name Alpha-adducin
Erythrocyte adducin subunit alpha
Gene Name Add1
Organism Mus musculus (Mouse)
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 Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse)
Enzyme Sequence MNGDTRAAVVTSPPPTTAPHKERYFDRVDENNPEYLRERNMAPDLRQDFNMMEQKKRVSMILQSPAFCEELESMIQEQFKKGKNPTGLLALQQIADFMTASVPNVYPAAPQGGMAALNMSLGMVTPVNDLRGSDSIAYDKGEKLLRCKLAAFYRLADLFGWSQLIYNHITTRVNSEQEHFLIVPFGLLYSEVTASSLVKVNLQGDIVDRGSTNLGVNQAGFTLHSAVYAARPDAKCIVHIHTPAGAAVSAMKCGLLPISPEALSLGDVAYHDYHGILVDEEEKILIQKNLGPKSKVLILRNHGLVSVGESVEEAFYYIHNLVVACEIQVRTLASAGGPDNLVLLDPGKYKAKSRSPGTPAGEGSGSPPKWQIGEQEFEALMRMLDNLGYRTGYPYRYPALRERSKKYSDVEVPASVTGHSFASDGDSGTCSPLRHSFQKQQREKTRWLHSGRGDDASEEGQNGSSPKSKTKWTKEDGHRTSTSAVPNLFVPLNTNPKEVQEMRNKIREQNLQDIKTAGPQSQVLCGVMMDRSLVQGELVTASKAIIEKEYQPHVIVSTTGPNPFNTLTDRELEEYRREVERKQKGSEENLDETREQKEKSPPDQSAVPNTPPSTPVKLEEDLPQEPTSRDDSDATTFKPTPPDLSPDEPSEALAFPAVEEEAHASPDPTQPPAEADPEPASAPTPGAEEVASPATEEGSPMDPGSDGSPGKSPSKKKKKFRTPSFLKKSKKKSDS
Enzyme Length 735
Uniprot Accession Number Q9QYC0
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. Binds to calmodulin.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Alternative sequence (2); Chain (1); Compositional bias (3); Modified residue (37); Region (4); Sequence conflict (1)
Keywords Acetylation;Actin-binding;Alternative splicing;Calmodulin-binding;Cell membrane;Cytoplasm;Cytoskeleton;Membrane;Phosphoprotein;Reference proteome
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein; Cytoplasmic side.
Modified Residue MOD_RES 1; /note="N-acetylmethionine"; /evidence="ECO:0000250|UniProtKB:P35611"; MOD_RES 12; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P35611"; MOD_RES 59; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 64; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P35611"; MOD_RES 331; /note="Phosphothreonine"; /evidence="ECO:0000250|UniProtKB:P35611"; MOD_RES 334; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P35611"; MOD_RES 353; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P35611"; MOD_RES 355; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 358; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 364; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 366; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 408; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 427; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 429; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 431; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 436; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 445; /note="Phosphothreonine; by ROCK2"; /evidence="ECO:0000250|UniProtKB:P35611"; MOD_RES 464; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 465; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 480; /note="Phosphothreonine; by ROCK2"; /evidence="ECO:0000250|UniProtKB:P35611"; MOD_RES 481; /note="Phosphoserine; by PKA"; /evidence="ECO:0000250|UniProtKB:P35611"; MOD_RES 586; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:16452087, ECO:0007744|PubMed:21183079"; MOD_RES 600; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 605; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 610; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:15345747, ECO:0007744|PubMed:21183079"; MOD_RES 613; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 614; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 705; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P35611"; MOD_RES 708; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P35611"; MOD_RES 712; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P35611"; MOD_RES 714; /note="Phosphoserine; by PKC"; /evidence="ECO:0000250|UniProtKB:P35611"; MOD_RES 724; /note="Phosphoserine; by PKA and PKC"; /evidence="ECO:0000250|UniProtKB:P35611"; MOD_RES Q9QYC0-2:600; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES Q9QYC0-2:605; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES Q9QYC0-2:610; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES Q9QYC0-2:613; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES Q9QYC0-2:614; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:21183079"
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10485892; 11110696; 11152656; 11940593; 12904583; 14610273; 15163540; 16512683; 16602821; 16615898; 16635246; 17074803; 17244351; 17967808; 1864459; 18723693; 18799693; 19501643; 19900187; 20696915; 21267068; 21677750; 22147703; 22163289; 22926980; 23055939; 24803591; 25978380; 27068466; 27565344; 28701737; 28982183; 29032200; 33771994; 7919654; 7959767;
Motif
Gene Encoded By
Mass 80,647
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda