| Predicate | Object |
|---|---|
| rdf:type | |
| biopax3:comment |
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. FUNCTION: Isoform Mu17 together with obscurin in skeletal muscle may provide a molecular link between the sarcoplasmic reticulum and myofibrils. SUBUNIT: 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. 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 (Probable). SUBCELLULAR LOCATION: Isoform Mu19: Sarcoplasmic reticulum (Probable). SUBCELLULAR LOCATION: Isoform Mu20: Sarcoplasmic reticulum (Probable). ALTERNATIVE PRODUCTS: Event=Alternative promoter usage, Alternative splicing; Named isoforms=21; Name=Er1; Synonyms=1, 2.1; IsoId=P16157-1; Sequence=Displayed; Note=Major erythrocyte-specific isoform. Produced by alternative promoter usage; Name=Er2; Synonyms=2, 2.2; IsoId=P16157-4; Sequence=VSP_018442; Note=Predominant form of minor erythrocyte-specific isoforms. Produced by alternative splicing of isoform Er1; Name=Er3; Synonyms=3; IsoId=P16157-5; Sequence=VSP_018449; Note=Produced by alternative splicing of isoform Er1; Name=Er4; Synonyms=4; IsoId=P16157-6; Sequence=VSP_018442, VSP_018449; Note=Produced by alternative splicing of isoform Er1; Name=Er5; Synonyms=5; IsoId=P16157-3; Sequence=VSP_000266; Note=Produced by alternative splicing of isoform Er1; Name=Er6; Synonyms=6; IsoId=P16157-7; Sequence=VSP_018442, VSP_000266; Note=Produced by alternative splicing of isoform Er1; Name=Er7; Synonyms=7; IsoId=P16157-8; Sequence=VSP_018447; Note=Produced by alternative splicing of isoform Er1; Name=Er8; Synonyms=8; IsoId=P16157-9; Sequence=VSP_018442, VSP_018447; Name=Er9; Synonyms=9; IsoId=P16157-10; Sequence=VSP_018445; Note=Produced by alternative splicing of isoform Er1; Name=Er10; Synonyms=10; IsoId=P16157-11; Sequence=VSP_018442, VSP_018445; Note=Produced by alternative splicing of isoform Er1; Name=Er11; Synonyms=11; IsoId=P16157-12; Sequence=VSP_018450; Note=Produced by alternative splicing of isoform Er1; Name=Er12; Synonyms=12; IsoId=P16157-13; Sequence=VSP_018442, VSP_018450; Note=Produced by alternative splicing of isoform Er1; Name=Er13; Synonyms=13; IsoId=P16157-14; Sequence=VSP_018451; Note=Produced by alternative splicing of isoform Er1; Name=Er14; Synonyms=14; IsoId=P16157-15; Sequence=VSP_018442, VSP_018451; Note=Produced by alternative splicing of isoform Er1; Name=Er15; Synonyms=15; IsoId=P16157-16; Sequence=VSP_018448; Note=Produced by alternative splicing of isoform Er1; Name=Er16; IsoId=P16157-2; Sequence=VSP_000264, VSP_000265; Note=Produced by alternative splicing of isoform Er1; Name=Mu17; Synonyms=ank1.5, muscle-specific 1; IsoId=P16157-17; Sequence=VSP_018440, VSP_018443, VSP_000266; Note=Produced by alternative promoter usage; Name=Mu18; Synonyms=ank1.6, muscle-specific 2; IsoId=P16157-18; Sequence=VSP_018440, VSP_018443, VSP_018448; Note=Produced by alternative splicing of isoform Mu17; Name=Mu19; Synonyms=muscle-specific 3; IsoId=P16157-19; Sequence=VSP_018440, VSP_018443, VSP_018445; Note=Produced by alternative splicing of isoform Mu17; Name=Mu20; Synonyms=muscle-specific 4; IsoId=P16157-20; Sequence=VSP_018440, VSP_018444, VSP_018446; Note=Produced by alternative splicing of isoform Mu17; Name=Br21; IsoId=P16157-21; Sequence=VSP_018439, VSP_018441, VSP_018449; Note=No experimental confirmation available. Produced by alternative splicing of isoform Er1; TISSUE SPECIFICITY: Isoform Mu17, isoform Mu18, isoform Mu19 and isoform Mu20 are expressed in skeletal muscle. Isoform Br21 is expressed in brain. DOMAIN: The 55 kDa regulatory domain is involved in regulating binding of SPTB/spectrin (beta chain) and SLC4A1/erythrocyte membrane protein band 3. DOMAIN: The ANK repeat region forms a spiral around a large central cavity and is involved in binding of ion transporters. DOMAIN: The tandem configuration of the two ZU5 and the UPA domains forms a structural supramodule termed ZZU. ZU5-1 mediates interaction with beta-spectrin, and the ZU5-1/UPA interface is required for ankyrin's function other than binding to spectrin (By similarity). 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. DISEASE: Defects in ANK1 are a cause of spherocytosis type 1 (SPH1) [MIM:182900]; also called hereditary spherocytosis type 1 (HS1). Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. Inheritance can be autosomal dominant or recessive. SIMILARITY: Contains 23 ANK repeats. SIMILARITY: Contains 1 death domain. SIMILARITY: Contains 2 ZU5 domains. SEQUENCE CAUTION: Sequence=AAB47805.1; Type=Erroneous gene model prediction; WEB RESOURCE: Name=Wikipedia; Note=Ankyrin entry; URL="http://en.wikipedia.org/wiki/Ankyrin"; GENE SYNONYMS:ANK1 ANK. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.,
SEQUENCE 1881 AA; 206265 MW; 49466F6F915019EC CRC64;
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| biopax3:xref |
urn:biopax:RelationshipXref:HGNC_HGNC:492,
urn:biopax:RelationshipXref:NCBI GENE_286,
urn:biopax:RelationshipXref:REFSEQ_NP_000028,
urn:biopax:RelationshipXref:REFSEQ_NP_001135918,
urn:biopax:RelationshipXref:REFSEQ_NP_065208,
urn:biopax:RelationshipXref:REFSEQ_NP_065209,
urn:biopax:RelationshipXref:REFSEQ_NP_065210,
urn:biopax:UnificationXref:UNIPROT_A6NJ23,
urn:biopax:UnificationXref:UNIPROT_O43400,
urn:biopax:UnificationXref:UNIPROT_P16157,
urn:biopax:UnificationXref:UNIPROT_Q13768,
urn:biopax:UnificationXref:UNIPROT_Q59FP2,
urn:biopax:UnificationXref:UNIPROT_Q8N604,
urn:biopax:UnificationXref:UNIPROT_Q99407
|
| biopax3:displayName |
ANK1_HUMAN
|
| biopax3:name |
ANK-1,
ANK1,
Ankyrin-R,
Erythrocyte ankyrin
|
| biopax3:entityFeature |
urn:biopax:ModificationFeature:ANK1_HUMAN_1,
urn:biopax:ModificationFeature:ANK1_HUMAN_10,
urn:biopax:ModificationFeature:ANK1_HUMAN_11,
urn:biopax:ModificationFeature:ANK1_HUMAN_12,
urn:biopax:ModificationFeature:ANK1_HUMAN_13,
urn:biopax:ModificationFeature:ANK1_HUMAN_14,
urn:biopax:ModificationFeature:ANK1_HUMAN_2,
urn:biopax:ModificationFeature:ANK1_HUMAN_3,
urn:biopax:ModificationFeature:ANK1_HUMAN_4,
urn:biopax:ModificationFeature:ANK1_HUMAN_5,
urn:biopax:ModificationFeature:ANK1_HUMAN_6,
urn:biopax:ModificationFeature:ANK1_HUMAN_7,
urn:biopax:ModificationFeature:ANK1_HUMAN_8,
urn:biopax:ModificationFeature:ANK1_HUMAN_9
|
| biopax3:organism | |
| biopax3:sequence |
MPYSVGFREADAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYGTKGKVRLPALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETKTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYDAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHVRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKVNAKAKDDQTPLHCAARIGHTNMVKLLLENNANPNLATTAGHTPLHIAAREGHVETVLALLEKEASQACMTKKGFTPLHVAAKYGKVRVAELLLERDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQVEVARSLLQYGGSANAESVQGVTPLHLAAQEGHAEMVALLLSKQANGNLGNKSGLTPLHLVAQEGHVPVADVLIKHGVMVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSDGTTPLAIAKRLGYISVTDVLKVVTDETSFVLVSDKHRMSFPETVDEILDVSEDEGEELISFKAERRDSRDVDEEKELLDFVPKLDQVVESPAIPRIPCAMPETVVIRSEEQEQASKEYDEDSLIPSSPATETSDNISPVASPVHTGFLVSFMVDARGGSMRGSRHNGLRVVIPPRTCAAPTRITCRLVKPQKLSTPPPLAEEEGLASRIIALGPTGAQFLSPVIVEIPHFASHGRGDRELVVLRSENGSVWKEHRSRYGESYLDQILNGMDEELGSLEELEKKRVCRIITTDFPLYFVIMSRLCQDYDTIGPEGGSLKSKLVPLVQATFPENAVTKRVKLALQAQPVPDELVTKLLGNQATFSPIVTVEPRRRKFHRPIGLRIPLPPSWTDNPRDSGEGDTTSLRLLCSVIGGTDQAQWEDITGTTKLVYANECANFTTNVSARFWLSDCPRTAEAVNFATLLYKELTAVPYMAKFVIFAKMNDPREGRLRCYCMTDDKVDKTLEQHENFVEVARSRDIEVLEGMSLFAELSGNLVPVKKAAQQRSFHFQSFRENRLAMPVKVRDSSREPGGSLSFLRKAMKYEDTQHILCHLNITMPPCAKGSGAEDRRRTPTPLALRYSILSESTPGSLSGTEQAEMKMAVISEHLGLSWAELARELQFSVEDINRIRVENPNSLLEQSVALLNLWVIREGQNANMENLYTALQSIDRGEIVNMLEGSGRQSRNLKPDRRHTDRDYSLSPSQMNGYSSLQDELLSPASLGCALSSPLRADQYWNEVAVLDAIPLAATEHDTMLEMSDMQVWSAGLTPSLVTAEDSSLECSKAEDSDATGHEWKLEGALSEEPRGPELGSLELVEDDTVDSDATNGLIDLLEQEEGQRSEEKLPGSKRQDDATGAGQDSENEVSLVSGHQRGQARITHSPTVSQVTERSQDRLQDWDADGSIVSYLQDAAQGSWQEEVTQGPHSFQGTSTMTEGLEPGGSQEYEKVLVSVSEHTWTEQPEAESSQADRDRRQQGQEEQVQEAKNTFTQVVQGNEFQNIPGEQVTEEQFTDEQGNIVTKKIIRKVVRQIDLSSADAAQEHEEVTVEGPLEDPSELEVDIDYFMKHSKDHTSTPNP
|
| biopax3:standardName |
Ankyrin-1
|