IED Industry Enzyme Database

Detail Information for IndEnz0002018761
IED ID IndEnz0002018761
Enzyme Type ID protease018761
Protein Name Alpha-adducin
Erythrocyte adducin subunit alpha
Gene Name ADD1 ADDA
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 MNGDSRAAVVTSPPPTTAPHKERYFDRVDENNPEYLRERNMAPDLRQDFNMMEQKKRVSMILQSPAFCEELESMIQEQFKKGKNPTGLLALQQIADFMTTNVPNVYPAAPQGGMAALNMSLGMVTPVNDLRGSDSIAYDKGEKLLRCKLAAFYRLADLFGWSQLIYNHITTRVNSEQEHFLIVPFGLLYSEVTASSLVKINLQGDIVDRGSTNLGVNQAGFTLHSAIYAARPDVKCVVHIHTPAGAAVSAMKCGLLPISPEALSLGEVAYHDYHGILVDEEEKVLIQKNLGPKSKVLILRNHGLVSVGESVEEAFYYIHNLVVACEIQVRTLASAGGPDNLVLLNPEKYKAKSRSPGSPVGEGTGSPPKWQIGEQEFEALMRMLDNLGYRTGYPYRYPALREKSKKYSDVEVPASVTGYSFASDGDSGTCSPLRHSFQKQQREKTRWLNSGRGDEASEEGQNGSSPKSKTKWTKEDGHRTSTSAVPNLFVPLNTNPKEVQEMRNKIREQNLQDIKTAGPQSQVLCGVVMDRSLVQGELVTASKAIIEKEYQPHVIVSTTGPNPFTTLTDRELEEYRREVERKQKGSEENLDEAREQKEKSPPDQPAVPHPPPSTPIKLEEDLVPEPTTGDDSDAATFKPTLPDLSPDEPSEALGFPMLEKEEEAHRPPSPTEAPTEASPEPAPDPAPVAEEAAPSAVEEGAAADPGSDGSPGKSPSKKKKKFRTPSFLKKSKKKSDS
Enzyme Length 737
Uniprot Accession Number P35611
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 (6); Chain (1); Compositional bias (6); Erroneous gene model prediction (1); Modified residue (30); Mutagenesis (2); Natural variant (6); Region (4); Sequence conflict (1)
Keywords Acetylation;Actin-binding;Alternative splicing;Calmodulin-binding;Cell membrane;Cytoplasm;Cytoskeleton;Direct protein sequencing;Membrane;Phosphoprotein;Reference proteome
Interact With A0A140G945; Q13153; Q9NP66
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein; Cytoplasmic side.
Modified Residue MOD_RES 1; /note="N-acetylmethionine"; /evidence="ECO:0007744|PubMed:19413330"; MOD_RES 12; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"; MOD_RES 59; /note="Phosphoserine; by PKA"; /evidence="ECO:0000269|PubMed:8810272, ECO:0007744|PubMed:24275569"; MOD_RES 64; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:24275569"; MOD_RES 331; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:18669648"; MOD_RES 334; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648"; MOD_RES 353; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 355; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 358; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"; MOD_RES 366; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 408; /note="Phosphoserine; by PKA"; /evidence="ECO:0000269|PubMed:8810272"; MOD_RES 427; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q9QYC0"; MOD_RES 429; /note="Phosphothreonine"; /evidence="ECO:0000250|UniProtKB:Q9QYC0"; MOD_RES 431; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"; MOD_RES 436; /note="Phosphoserine; by PKA"; /evidence="ECO:0000269|PubMed:8810272, ECO:0007744|PubMed:18669648"; MOD_RES 445; /note="Phosphothreonine; by ROCK2"; /evidence="ECO:0000269|PubMed:10209029"; MOD_RES 464; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q9QYC0"; MOD_RES 465; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"; MOD_RES 480; /note="Phosphothreonine; by ROCK2"; /evidence="ECO:0000269|PubMed:10209029"; MOD_RES 481; /note="Phosphoserine; by PKA"; /evidence="ECO:0000269|PubMed:8810272"; MOD_RES 586; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q9QYC0"; MOD_RES 600; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q9QYC0"; MOD_RES 613; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q9QYC0"; MOD_RES 614; /note="Phosphothreonine"; /evidence="ECO:0000250|UniProtKB:Q9QYC0"; MOD_RES 678; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:24275569"; MOD_RES 707; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"; MOD_RES 710; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:21406692"; MOD_RES 714; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21406692"; MOD_RES 716; /note="Phosphoserine; by PKC"; /evidence="ECO:0000269|PubMed:8810272, ECO:0007744|PubMed:24275569"; MOD_RES 726; /note="Phosphoserine; by PKA and PKC"; /evidence="ECO:0000269|PubMed:8810272"
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10429360; 10823823; 10912755; 10912756; 10912758; 11110979; 11116113; 11283377; 11447495; 11518842; 11528213; 11711521; 11728946; 11775124; 11847182; 11882573; 11918733; 11918988; 11926892; 12052841; 12082592; 12107246; 12172317; 12195118; 12195119; 12394950; 12427140; 12623934; 12697976; 12743105; 12885793; 12951058; 13679477; 14508192; 14530292; 14553962; 14643575; 15039125; 15055253; 15059531; 15097233; 15110895; 15187197; 15326084; 15378162; 15493144; 15554870; 15608390; 15611095; 15716695; 15773232; 15824464; 15834281; 15910744; 16043664; 16080807; 16100725; 16116087; 16266470; 16289097; 16314886; 16392768; 16420563; 16450155; 16497648; 16531798; 16539657; 16612256; 16615274; 16702981; 16724011; 16970091; 17003363; 17051589; 17082469; 17083073; 17189961; 17215849; 17267840; 17301826; 17341583; 17452507; 17472579; 17765140; 17825147; 17921817; 17984662; 18003973; 18347014; 18393230; 18398333; 18413308; 18458162; 18475162; 18513389; 18524856; 18591455; 18657677; 18660489; 18667944; 18679149; 18787518; 18800139; 18847512; 18977990; 19057513; 19103106; 19131662; 19145769; 19145770; 19148102; 19166692; 19199261; 19238444; 19242491; 19243623; 19247266; 19263529; 19274077; 19367725; 19443911; 19463016; 19479237; 19559392; 19567882; 19574959; 19620885; 19729965; 19779330; 19779464; 19838659; 19913121; 19960031; 20145305; 20160191; 20237496; 20473689; 20536507; 20565774; 20577119; 20628086; 20667857; 20711500; 20810786; 20838486; 20877298; 20927398; 20929695; 21194526; 21228790; 21339657; 21364877; 21736685; 21851590; 21900206; 22117679; 22163289; 22197999; 22272309; 22307086; 22476228; 22677360; 22810272; 23284854; 23509723; 23540412; 23691048; 23863317; 23902751; 23985264; 24379415; 24606918; 24711455; 24718403; 25262176; 25344630; 25567773; 25609649; 25816007; 26042478; 26279304; 26496610; 26638075; 27340988; 27349000; 28040068; 28686109; 28982183; 29028685; 29049185; 29925526; 30062972; 30552709; 31548578; 31943323; 32237935; 32971583; 7615546; 9495254; 9607391; 9679146;
Motif
Gene Encoded By
Mass 80,955
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda