| IED ID | IndEnz0002007639 |
| Enzyme Type ID | protease007639 |
| Protein Name |
Ankyrin-1 ANK-1 Ankyrin-R Erythrocyte ankyrin |
| Gene Name | ANK1 ANK |
| 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 | MPYSVGFREADAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYGTKGKVRLPALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETKTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYDAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHVRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKVNAKAKDDQTPLHCAARIGHTNMVKLLLENNANPNLATTAGHTPLHIAAREGHVETVLALLEKEASQACMTKKGFTPLHVAAKYGKVRVAELLLERDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQVEVARSLLQYGGSANAESVQGVTPLHLAAQEGHAEMVALLLSKQANGNLGNKSGLTPLHLVAQEGHVPVADVLIKHGVMVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSDGTTPLAIAKRLGYISVTDVLKVVTDETSFVLVSDKHRMSFPETVDEILDVSEDEGEELISFKAERRDSRDVDEEKELLDFVPKLDQVVESPAIPRIPCAMPETVVIRSEEQEQASKEYDEDSLIPSSPATETSDNISPVASPVHTGFLVSFMVDARGGSMRGSRHNGLRVVIPPRTCAAPTRITCRLVKPQKLSTPPPLAEEEGLASRIIALGPTGAQFLSPVIVEIPHFASHGRGDRELVVLRSENGSVWKEHRSRYGESYLDQILNGMDEELGSLEELEKKRVCRIITTDFPLYFVIMSRLCQDYDTIGPEGGSLKSKLVPLVQATFPENAVTKRVKLALQAQPVPDELVTKLLGNQATFSPIVTVEPRRRKFHRPIGLRIPLPPSWTDNPRDSGEGDTTSLRLLCSVIGGTDQAQWEDITGTTKLVYANECANFTTNVSARFWLSDCPRTAEAVNFATLLYKELTAVPYMAKFVIFAKMNDPREGRLRCYCMTDDKVDKTLEQHENFVEVARSRDIEVLEGMSLFAELSGNLVPVKKAAQQRSFHFQSFRENRLAMPVKVRDSSREPGGSLSFLRKAMKYEDTQHILCHLNITMPPCAKGSGAEDRRRTPTPLALRYSILSESTPGSLSGTEQAEMKMAVISEHLGLSWAELARELQFSVEDINRIRVENPNSLLEQSVALLNLWVIREGQNANMENLYTALQSIDRGEIVNMLEGSGRQSRNLKPDRRHTDRDYSLSPSQMNGYSSLQDELLSPASLGCALSSPLRADQYWNEVAVLDAIPLAATEHDTMLEMSDMQVWSAGLTPSLVTAEDSSLECSKAEDSDATGHEWKLEGALSEEPRGPELGSLELVEDDTVDSDATNGLIDLLEQEEGQRSEEKLPGSKRQDDATGAGQDSENEVSLVSGHQRGQARITHSPTVSQVTERSQDRLQDWDADGSIVSYLQDAAQGSWQEEVTQGPHSFQGTSTMTEGLEPGGSQEYEKVLVSVSEHTWTEQPEAESSQADRDRRQQGQEEQVQEAKNTFTQVVQGNEFQNIPGEQVTEEQFTDEQGNIVTKKIIRKVVRQIDLSSADAAQEHEEVTVEGPLEDPSELEVDIDYFMKHSKDHTSTPNP |
| Enzyme Length | 1881 |
| Uniprot Accession Number | P16157 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: 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. {ECO:0000269|PubMed:12456646}.; FUNCTION: [Isoform Mu17]: Together with obscurin in skeletal muscle may provide a molecular link between the sarcoplasmic reticulum and myofibrils. {ECO:0000269|PubMed:12527750}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (17); Beta strand (28); Chain (1); Compositional bias (6); Domain (3); Erroneous gene model prediction (1); Helix (41); Modified residue (34); Mutagenesis (4); Natural variant (19); Region (9); Repeat (23); Sequence conflict (5); Turn (3) |
| Keywords | 3D-structure;ANK repeat;Alternative promoter usage;Alternative splicing;Cytoplasm;Cytoskeleton;Direct protein sequencing;Disease variant;Elliptocytosis;Hereditary hemolytic anemia;Hydroxylation;Lipoprotein;Membrane;Phosphoprotein;Reference proteome;Repeat;Sarcoplasmic reticulum |
| Interact With | Q5VST9-3; P50402; P54849; Q14802-3; Q8IXM6; Q5VST9-3; Q8N0V3; Q5QGT7; Q8IWU4; P0DN84; Q969S6 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Isoform Er1]: Cytoplasm, cytoskeleton. Note=Probably the other erythrocyte (Er) isoforms, are located near the surface of erythrocytic plasma membrane.; SUBCELLULAR LOCATION: [Isoform Mu17]: Membrane. Cytoplasm, myofibril, sarcomere, M line. Note=Colocalizes with OBSCN isoform 3/obscurin at the M line in differentiated skeletal muscle cells.; SUBCELLULAR LOCATION: [Isoform Mu18]: Sarcoplasmic reticulum {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform Mu19]: Sarcoplasmic reticulum {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform Mu20]: Sarcoplasmic reticulum {ECO:0000305}. |
| Modified Residue | MOD_RES 105; /note="(3S)-3-hydroxyasparagine; by HIF1AN; partial"; /evidence="ECO:0000269|PubMed:21177872"; MOD_RES 233; /note="(3S)-3-hydroxyasparagine; by HIF1AN; partial"; /evidence="ECO:0000269|PubMed:21177872"; MOD_RES 429; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 431; /note="(3S)-3-hydroxyasparagine; by HIF1AN; partial"; /evidence="ECO:0000269|PubMed:21177872"; MOD_RES 464; /note="(3S)-3-hydroxyasparagine; by HIF1AN; partial"; /evidence="ECO:0000269|PubMed:21177872"; MOD_RES 629; /note="(3S)-3-hydroxyasparagine; by HIF1AN; partial"; /evidence="ECO:0000269|PubMed:21177872"; MOD_RES 662; /note="(3S)-3-hydroxyasparagine; by HIF1AN; partial"; /evidence="ECO:0000269|PubMed:21177872"; MOD_RES 695; /note="(3S)-3-hydroxyaspartate; by HIF1AN; partial"; /evidence="ECO:0000269|PubMed:21177872"; MOD_RES 728; /note="(3S)-3-hydroxyasparagine; by HIF1AN; partial"; /evidence="ECO:0000269|PubMed:21177872"; MOD_RES 759; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 761; /note="(3S)-3-hydroxyasparagine; by HIF1AN; partial"; /evidence="ECO:0000269|PubMed:21177872"; MOD_RES 781; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"; MOD_RES 817; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:24275569"; MOD_RES 834; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:24275569"; MOD_RES 856; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"; MOD_RES 961; /note="Phosphothreonine"; /evidence="ECO:0000250|UniProtKB:Q02357"; MOD_RES 1073; /note="Phosphotyrosine"; /evidence="ECO:0000250|UniProtKB:Q02357"; MOD_RES 1082; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q02357"; MOD_RES 1378; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 1380; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 1390; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q02357"; MOD_RES 1392; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q02357"; MOD_RES 1396; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 1400; /note="Phosphothreonine"; /evidence="ECO:0000250|UniProtKB:Q02357"; MOD_RES 1428; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:24275569"; MOD_RES 1486; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 1523; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:24275569"; MOD_RES 1533; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:24275569"; MOD_RES 1617; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q02357"; MOD_RES 1666; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 1671; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 1686; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 1690; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 1696; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163" |
| Post Translational Modification | PTM: Regulated by phosphorylation.; PTM: Palmitoylated.; PTM: Hydroxylated by HIF1AN at several asparagine and 1 aspartate residue within ANK repeat region. Hydroxylation seems to increase the conformational stability of this region and may also modulate protein-protein interactions mediated by the ANK repeat region. {ECO:0000269|PubMed:21177872}.; PTM: (Microbial infection) Probably cleaved by P.falciparum SERA6; the cleavage probably causes the disruption of the actin cytoskeleton and the rupture of the erythrocyte cell membrane releasing the merozoites. {ECO:0000269|PubMed:29459732}. |
| Signal Peptide | |
| Structure 3D | NMR spectroscopy (1); X-ray crystallography (7) |
| Cross Reference PDB | 1N11; 2YQF; 2YVI; 3F59; 3KBT; 3KBU; 3UD1; 3UD2; |
| Mapped Pubmed ID | 10052452; 10679020; 10761932; 10903204; 11035033; 11167760; 11172815; 11222639; 11285137; 11306556; 11427698; 11449000; 11461920; 11470829; 11689559; 11703931; 11724816; 11726511; 11748249; 12388752; 12721290; 12925712; 14654841; 14742712; 15632110; 15728195; 15878873; 16525039; 16597699; 16633337; 16723730; 16904324; 16940185; 16962094; 17223356; 17253781; 17274799; 17760859; 17927562; 18086915; 18182008; 18809720; 19015319; 19109418; 19110015; 19112491; 19141864; 19164740; 19296914; 19631211; 19758564; 20101027; 20427317; 20637885; 21219331; 22013193; 22094269; 23839779; 24119662; 24806965; 25277244; 25416956; 25436559; 7691276; 8001155; 8128252; 8253837; 8636227; 8703812; 8991093; 9067504; 9150144; 9151675; 9244307; 9278538; 9288971; 9323141; 9371782; 9380700; 9382863; 9405360; 9490716; 9671725; 9751720; 9804856; 9837910; 9990005; |
| Motif | |
| Gene Encoded By | |
| Mass | 206,265 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |