Q02357 · ANK1_MOUSE
- ProteinAnkyrin-1
- GeneAnk1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1862 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Component of the ankyrin-1 complex, a multiprotein complex involved in the stability and shape of the erythrocyte membrane. 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.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | A band | |
Cellular Component | ankyrin-1 complex | |
Cellular Component | axolemma | |
Cellular Component | cortical cytoskeleton | |
Cellular Component | M band | |
Cellular Component | membrane | |
Cellular Component | neuron projection | |
Cellular Component | plasma membrane | |
Cellular Component | postsynaptic membrane | |
Cellular Component | sarcolemma | |
Cellular Component | sarcoplasmic reticulum | |
Cellular Component | spectrin-associated cytoskeleton | |
Cellular Component | Z disc | |
Molecular Function | cytoskeletal anchor activity | |
Molecular Function | spectrin binding | |
Molecular Function | transmembrane transporter binding | |
Biological Process | erythrocyte development | |
Biological Process | inorganic cation transmembrane transport | |
Biological Process | multicellular organismal-level iron ion homeostasis | |
Biological Process | porphyrin-containing compound biosynthetic process | |
Biological Process | positive regulation of organelle organization | |
Biological Process | protein localization to plasma membrane | |
Biological Process | signal transduction |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAnkyrin-1
- Short namesANK-1
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ02357
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Isoform Er1
Note: Probably the other erythrocyte (Er) isoforms, are located near the surface of erythrocytic plasma membrane.
Isoform Mu7
Isoform Mu8
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000066884 | 1-1862 | Ankyrin-1 | |||
Sequence: MGFCKADAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYGTKGKVRLPALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAKRLGYISVTDVLKVVTDETSVVLVSDKHRMSYPETVDEILDVSEDEGDELVGSKAERRDSRDVGEEKELLDFVPKLDQVVESPAIPRIPCVTPETVVIRSEDQEQASKEYDEDSLIPSSPATETSDNISPVASPVHTGFLVSFMVDARGGSMRGSRHNGLRVVIPPRTCAAPTRITCRLVKPQKLNTPPPLAEEEGLASRIIALGPTGAQFLSPVIVEIPHFASHGRGDRELVVLRSENGSVWKEHKSRYGESYLDQILNGMDEELGSLEELEKKRVCRIITTDFPLYFVIMSRLCQDYDTIGPEGGSLRSKLVPLVQATFPENAVTKKVKLALQAQPVPDELVTKLLGNQATFSPIVTVEPRRRKFHRPIGLRIPLPPSWTDNPRDSGEGDTTSLRLLCSVIGGTDQAQWEDITGTTKLIYANECANFTTNVSARFWLSDCPRTAEAVHFATLLYKELTAVPYMAKFVIFAKMNDAREGRLRCYCMTDDKVDKTLEQHENFVEVARSRDIEVLEGMPLFAELSGNLVPVKKAAQQRSFHFQSFRENRLAIPVKVRDSSREPGGFLSFLRKTMKYEDTQHILCHLNITMPPCTKGSGAEDRRRTLTPLTLRYSILSESRLGFTSDTDRVEMRMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIVNMLEGSGRQSRNLKPERRHGDREYSLSPSQVNGYSSLQDELLSPASLQYALPSPLCADQYWNEVTVIDAIPLAATEHDTMLEMSDMQVWSAGLTPSLVTAEDSSLECSKAEDSDAIPEWKLEGAHSEDTQGPELGSQDLVEDDTVDSDATNGLADLLGQEEGQRSEKKRQEVSGTEQDTETEVSLVSGQQRVHARITDSPSVRQVLDRSQARTLDWDKQGSTAVHPQEATQSSWQEEVTQGPHSFQRRITTIQGPEPGALQEYEQVLVSTREHVQRGPPETGSPKAGKEPSLWAPESAFSQEVQGDELQNIPGEQVTEEQFTDEQGNIVTKKIIRKVVRQVDSSGAIDTQQHEEVELRGSGLQPDLIEGRKGAQIVKRASLKRGKQ | ||||||
Modified residue | 55 | In isoform Q02357-7; Phosphoserine | ||||
Sequence: K | ||||||
Modified residue | 55 | In isoform Q02357-8; Phosphoserine | ||||
Sequence: K | ||||||
Modified residue | 101 | (3S)-3-hydroxyasparagine; by HIF1AN; partial | ||||
Sequence: N | ||||||
Modified residue | 229 | (3S)-3-hydroxyasparagine; by HIF1AN | ||||
Sequence: N | ||||||
Modified residue | 425 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 427 | (3S)-3-hydroxyasparagine; by HIF1AN | ||||
Sequence: N | ||||||
Modified residue | 460 | (3S)-3-hydroxyasparagine; by HIF1AN | ||||
Sequence: N | ||||||
Modified residue | 625 | (3S)-3-hydroxyasparagine; by HIF1AN | ||||
Sequence: N | ||||||
Modified residue | 658 | (3S)-3-hydroxyasparagine; by HIF1AN | ||||
Sequence: N | ||||||
Modified residue | 691 | (3S)-3-hydroxyaspartate; by HIF1AN | ||||
Sequence: D | ||||||
Modified residue | 724 | (3S)-3-hydroxyasparagine; by HIF1AN | ||||
Sequence: N | ||||||
Modified residue | 755 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 757 | (3S)-3-hydroxyasparagine; by HIF1AN | ||||
Sequence: N | ||||||
Modified residue | 777 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 813 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 830 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 852 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 862 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 957 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1069 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 1078 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1374 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1376 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1386 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1388 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1396 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1424 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1473 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1482 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1519 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1529 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1612 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1660 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1675 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1685 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Regulated by phosphorylation.
Acylated by palmitic acid group(s).
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.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Component of the ankyrin-1 complex in the erythrocyte, composed of ANK1, RHCE, RHAG, SLC4A1, EPB42, GYPA, GYPB and AQP1. Interacts with a number of integral membrane proteins and cytoskeletal proteins. Interacts (via N-terminus) with SPTB/spectrin (beta chain). Also interacts with TTN/titin. Isoform Mu17 interacts with OBSCN isoform 3/obscurin. Interacts with HIF1AN. Interacts (via ANK 1-5 repeats) with RHCE; this interaction mediates the primary membrane attachment site for ANK1. Interacts (via ANK 1-2 repeats) with AQP1 (via the N-terminal). Interacts (via ANK 1-13 repeats) with EPB42. Interacts directly with SLC4A1 (via the cytoplasmic domain); this interaction is mediated by the SLC4A1 Band 3-II and Band 3-III dimers.
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, repeat, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-827 | 89 kDa domain | ||||
Sequence: MGFCKADAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYGTKGKVRLPALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAKRLGYISVTDVLKVVTDETSVVLVSDKHRMSYPETVDEILDVSEDEGDELVGSKAER | ||||||
Repeat | 40-69 | ANK 1 | ||||
Sequence: NGLNGLHLASKEGHVKMVVELLHKEIILET | ||||||
Repeat | 73-102 | ANK 2 | ||||
Sequence: KGNTALHIAALAGQDEVVRELVNYGANVNA | ||||||
Repeat | 106-135 | ANK 3 | ||||
Sequence: KGFTPLYMAAQENHLEVVKFLLENGANQNV | ||||||
Repeat | 139-168 | ANK 4 | ||||
Sequence: DGFTPLAVALQQGHENVVAHLINYGTKGKV | ||||||
Repeat | 170-197 | ANK 5 | ||||
Sequence: LPALHIAARNDDTRTAAVLLQNDPNPDV | ||||||
Repeat | 201-230 | ANK 6 | ||||
Sequence: TGFTPLHIAAHYENLNVAQLLLNRGASVNF | ||||||
Repeat | 234-263 | ANK 7 | ||||
Sequence: NGITPLHIASRRGNVIMVRLLLDRGAQIET | ||||||
Repeat | 267-296 | ANK 8 | ||||
Sequence: DELTPLHCAARNGHVRISEILLDHGAPIQA | ||||||
Repeat | 300-329 | ANK 9 | ||||
Sequence: NGLSPIHMAAQGDHLDCVRLLLQYNAEIDD | ||||||
Repeat | 333-362 | ANK 10 | ||||
Sequence: DHLTPLHVAAHCGHHRVAKVLLDKGAKPNS | ||||||
Repeat | 366-395 | ANK 11 | ||||
Sequence: NGFTPLHIACKKNHIRVMELLLKTGASIDA | ||||||
Repeat | 399-428 | ANK 12 | ||||
Sequence: SGLTPLHVASFMGHLPIVKNLLQRGASPNV | ||||||
Repeat | 432-461 | ANK 13 | ||||
Sequence: KVETPLHMAARAGHTEVAKYLLQNKAKANA | ||||||
Repeat | 465-494 | ANK 14 | ||||
Sequence: DDQTPLHCAARIGHTGMVKLLLENGASPNL | ||||||
Repeat | 498-527 | ANK 15 | ||||
Sequence: AGHTPLHTAAREGHVDTALALLEKEASQAC | ||||||
Repeat | 531-560 | ANK 16 | ||||
Sequence: KGFTPLHVAAKYGKVRLAELLLEHDAHPNA | ||||||
Repeat | 564-593 | ANK 17 | ||||
Sequence: NGLTPLHVAVHHNNLDIVKLLLPRGGSPHS | ||||||
Repeat | 597-626 | ANK 18 | ||||
Sequence: NGYTPLHIAAKQNQIEVARSLLQYGGSANA | ||||||
Repeat | 630-659 | ANK 19 | ||||
Sequence: QGVTPLHLAAQEGHTEMVALLLSKQANGNL | ||||||
Repeat | 663-692 | ANK 20 | ||||
Sequence: SGLTPLHLVSQEGHVPVADVLIKHGVTVDA | ||||||
Repeat | 696-725 | ANK 21 | ||||
Sequence: MGYTPLHVASHYGNIKLVKFLLQHQADVNA | ||||||
Repeat | 729-758 | ANK 22 | ||||
Sequence: LGYSPLHQAAQQGHTDIVTLLLKNGASPNE | ||||||
Repeat | 762-791 | ANK 23 | ||||
Sequence: NGTTPLAIAKRLGYISVTDVLKVVTDETSV | ||||||
Region | 812-834 | Disordered | ||||
Sequence: VSEDEGDELVGSKAERRDSRDVG | ||||||
Compositional bias | 817-834 | Basic and acidic residues | ||||
Sequence: GDELVGSKAERRDSRDVG | ||||||
Region | 872-900 | Disordered | ||||
Sequence: DQEQASKEYDEDSLIPSSPATETSDNISP | ||||||
Domain | 909-1064 | ZU5 1 | ||||
Sequence: FLVSFMVDARGGSMRGSRHNGLRVVIPPRTCAAPTRITCRLVKPQKLNTPPPLAEEEGLASRIIALGPTGAQFLSPVIVEIPHFASHGRGDRELVVLRSENGSVWKEHKSRYGESYLDQILNGMDEELGSLEELEKKRVCRIITTDFPLYFVIMSR | ||||||
Domain | 1066-1212 | ZU5 2 | ||||
Sequence: CQDYDTIGPEGGSLRSKLVPLVQATFPENAVTKKVKLALQAQPVPDELVTKLLGNQATFSPIVTVEPRRRKFHRPIGLRIPLPPSWTDNPRDSGEGDTTSLRLLCSVIGGTDQAQWEDITGTTKLIYANECANFTTNVSARFWLSDC | ||||||
Region | 1197-1331 | UPA domain | ||||
Sequence: ANFTTNVSARFWLSDCPRTAEAVHFATLLYKELTAVPYMAKFVIFAKMNDAREGRLRCYCMTDDKVDKTLEQHENFVEVARSRDIEVLEGMPLFAELSGNLVPVKKAAQQRSFHFQSFRENRLAIPVKVRDSSRE | ||||||
Region | 1387-1862 | 55 kDa regulatory domain | ||||
Sequence: ESRLGFTSDTDRVEMRMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIVNMLEGSGRQSRNLKPERRHGDREYSLSPSQVNGYSSLQDELLSPASLQYALPSPLCADQYWNEVTVIDAIPLAATEHDTMLEMSDMQVWSAGLTPSLVTAEDSSLECSKAEDSDAIPEWKLEGAHSEDTQGPELGSQDLVEDDTVDSDATNGLADLLGQEEGQRSEKKRQEVSGTEQDTETEVSLVSGQQRVHARITDSPSVRQVLDRSQARTLDWDKQGSTAVHPQEATQSSWQEEVTQGPHSFQRRITTIQGPEPGALQEYEQVLVSTREHVQRGPPETGSPKAGKEPSLWAPESAFSQEVQGDELQNIPGEQVTEEQFTDEQGNIVTKKIIRKVVRQVDSSGAIDTQQHEEVELRGSGLQPDLIEGRKGAQIVKRASLKRGKQ | ||||||
Domain | 1399-1483 | Death | ||||
Sequence: VEMRMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIVNMLEGSG | ||||||
Region | 1481-1506 | Disordered | ||||
Sequence: GSGRQSRNLKPERRHGDREYSLSPSQ | ||||||
Compositional bias | 1486-1500 | Basic and acidic residues | ||||
Sequence: SRNLKPERRHGDREY | ||||||
Region | 1598-1720 | Disordered | ||||
Sequence: EGAHSEDTQGPELGSQDLVEDDTVDSDATNGLADLLGQEEGQRSEKKRQEVSGTEQDTETEVSLVSGQQRVHARITDSPSVRQVLDRSQARTLDWDKQGSTAVHPQEATQSSWQEEVTQGPHS | ||||||
Compositional bias | 1636-1652 | Basic and acidic residues | ||||
Sequence: EEGQRSEKKRQEVSGTE | ||||||
Compositional bias | 1653-1684 | Polar residues | ||||
Sequence: QDTETEVSLVSGQQRVHARITDSPSVRQVLDR | ||||||
Compositional bias | 1699-1720 | Polar residues | ||||
Sequence: AVHPQEATQSSWQEEVTQGPHS | ||||||
Region | 1744-1767 | Disordered | ||||
Sequence: VSTREHVQRGPPETGSPKAGKEPS |
Domain
The 55 kDa regulatory domain is involved in regulating binding of SPTB/spectrin (beta chain) and SLC4A1/erythrocyte membrane protein band 3.
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).
The ANK repeat region forms a spiral around a large central cavity and is involved in binding of ion transporters. Adopts a T-shaped arrangement, in the ankyrin-1 complex, in which ANK 1-5 repeats are orthogonal to ANK 6-24 repeats, with the peptide binding groove of ANK 1-5 repeats oriented toward the membrane. The rearrangement of the ANK 1-5 repeats orients the canonical protein binding groove to directly face the membrane, to interact the membrane-embedded targets RHCE and AQP1.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 8 isoforms produced by Alternative promoter usage & Alternative splicing.
Q02357-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- NameEr1
- NoteProduced by alternative promoter usage.
- Length1,862
- Mass (Da)204,227
- Last updated2006-05-16 v2
- ChecksumB5F3EBB447C3485D
Q02357-2
- NameBr2
- SynonymsCb14/11
- NoteProduced by alternative splicing of isoform Er1.
- Differences from canonical
- 1-5: MGFCK → MAERPRRSGSDPA
- 817-817: G → GTAHISIMG
- 1636-1665: Missing
Q02357-3
- NameEr3
- SynonymsEr18
- NoteIncomplete sequence. Produced by alternative splicing of isoform Er1.
- Differences from canonical
- 1832-1862: ELRGSGLQPDLIEGRKGAQIVKRASLKRGKQ → IVEGPLADPGDLEADIESFMKLTKDHTSTPKP
Q02357-4
- NameBr4
- SynonymsCb12
- NoteIncomplete sequence. Produced by alternative splicing of isoform Er1.
- Differences from canonical
- 1831-1831: V → VIVEGPLADPGDLEADIESFMKLTKV
Q02357-5
- Name5
- NoteProduced by alternative splicing of isoform Er1.
- Differences from canonical
- 1-4: MGFC → MAQAAKQLKKIKDIEAQALQEQKEKEESNRKRRNRSRDRKK
- 1510-1664: Missing
Q02357-6
- Name6
- NoteProduced by alternative splicing of isoform Er1.
Q02357-7
- NameMu7
- SynonymsskAnk1
- NoteProduced by alternative promoter usage.
- Differences from canonical
- 1-1707: Missing
- 1708-1780: SSWQEEVTQGPHSFQRRITTIQGPEPGALQEYEQVLVSTREHVQRGPPETGSPKAGKEPSLWAPESAFSQEVQ → MWTFITQLLVTLVLLGFFLVSCQNVMHIVKGSLCFVLKHIHQELDKELGESEGLSDDEETISTRVVRRRVFLK
Q02357-8
- NameMu8
- NoteProduced by alternative splicing of isoform Mu7.
- Differences from canonical
- 1-1707: Missing
- 1708-1780: SSWQEEVTQGPHSFQRRITTIQGPEPGALQEYEQVLVSTREHVQRGPPETGSPKAGKEPSLWAPESAFSQEVQ → MWTFITQLLVTLVLLGFFLVSCQNVMHIVKGSLCFVLKHIHQELDKELGESEGLSDDEETISTRVVRRRVFLK
- 1832-1862: ELRGSGLQPDLIEGRKGAQIVKRASLKRGKQ → IVEGPLADPGDLEADIESFMKLTKDHTSTPKP
Computationally mapped potential isoform sequences
There are 12 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0R4J1N7 | A0A0R4J1N7_MOUSE | Ank1 | 1907 | ||
G5E8J2 | G5E8J2_MOUSE | Ank1 | 1848 | ||
B7ZW98 | B7ZW98_MOUSE | Ank1 | 1852 | ||
G8JL84 | G8JL84_MOUSE | Ank1 | 1863 | ||
D3YTV8 | D3YTV8_MOUSE | Ank1 | 1878 | ||
D3Z5M4 | D3Z5M4_MOUSE | Ank1 | 1883 | ||
F7D1P5 | F7D1P5_MOUSE | Ank1 | 1098 | ||
Q0VGY9 | Q0VGY9_MOUSE | Ank1 | 1887 | ||
D6RJ51 | D6RJ51_MOUSE | Ank1 | 572 | ||
G3UXF4 | G3UXF4_MOUSE | Ank1 | 109 | ||
G3UY11 | G3UY11_MOUSE | Ank1 | 1057 | ||
E9QNT8 | E9QNT8_MOUSE | Ank1 | 1862 |
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_018454 | 1-4 | in isoform 5 and isoform 6 | |||
Sequence: MGFC → MAQAAKQLKKIKDIEAQALQEQKEKEESNRKRRNRSRDRKK | ||||||
Alternative sequence | VSP_018453 | 1-5 | in isoform Br2 | |||
Sequence: MGFCK → MAERPRRSGSDPA | ||||||
Alternative sequence | VSP_018452 | 1-1707 | in isoform Mu7 and isoform Mu8 | |||
Sequence: Missing | ||||||
Sequence conflict | 507 | in Ref. 3; BAE34375 | ||||
Sequence: A → T | ||||||
Sequence conflict | 678 | in Ref. 1; AAA37236 | ||||
Sequence: P → L | ||||||
Alternative sequence | VSP_018455 | 817 | in isoform Br2 and isoform 6 | |||
Sequence: G → GTAHISIMG | ||||||
Compositional bias | 817-834 | Basic and acidic residues | ||||
Sequence: GDELVGSKAERRDSRDVG | ||||||
Sequence conflict | 818 | in Ref. 3; BAE34375 | ||||
Sequence: D → G | ||||||
Sequence conflict | 1098 | in Ref. 2; CAA48801 | ||||
Sequence: K → N | ||||||
Sequence conflict | 1481 | in Ref. 2; CAA48801 | ||||
Sequence: G → V | ||||||
Compositional bias | 1486-1500 | Basic and acidic residues | ||||
Sequence: SRNLKPERRHGDREY | ||||||
Alternative sequence | VSP_018456 | 1510-1664 | in isoform 5 | |||
Sequence: Missing | ||||||
Sequence conflict | 1541 | in Ref. 3; BAE27815/BAE28015 | ||||
Sequence: T → A | ||||||
Compositional bias | 1636-1652 | Basic and acidic residues | ||||
Sequence: EEGQRSEKKRQEVSGTE | ||||||
Alternative sequence | VSP_018457 | 1636-1665 | in isoform Br2 | |||
Sequence: Missing | ||||||
Sequence conflict | 1644 | in Ref. 3; BAE28015 | ||||
Sequence: K → R | ||||||
Compositional bias | 1653-1684 | Polar residues | ||||
Sequence: QDTETEVSLVSGQQRVHARITDSPSVRQVLDR | ||||||
Compositional bias | 1699-1720 | Polar residues | ||||
Sequence: AVHPQEATQSSWQEEVTQGPHS | ||||||
Alternative sequence | VSP_018458 | 1708-1780 | in isoform Mu7 and isoform Mu8 | |||
Sequence: SSWQEEVTQGPHSFQRRITTIQGPEPGALQEYEQVLVSTREHVQRGPPETGSPKAGKEPSLWAPESAFSQEVQ → MWTFITQLLVTLVLLGFFLVSCQNVMHIVKGSLCFVLKHIHQELDKELGESEGLSDDEETISTRVVRRRVFLK | ||||||
Alternative sequence | VSP_018459 | 1831 | in isoform Br4 | |||
Sequence: V → VIVEGPLADPGDLEADIESFMKLTKV | ||||||
Alternative sequence | VSP_018460 | 1832-1862 | in isoform Er3 and isoform Mu8 | |||
Sequence: ELRGSGLQPDLIEGRKGAQIVKRASLKRGKQ → IVEGPLADPGDLEADIESFMKLTKDHTSTPKP |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M84756 EMBL· GenBank· DDBJ | AAA37236.1 EMBL· GenBank· DDBJ | mRNA | ||
X69063 EMBL· GenBank· DDBJ | CAA48801.1 EMBL· GenBank· DDBJ | mRNA | ||
X69064 EMBL· GenBank· DDBJ | CAA48802.1 EMBL· GenBank· DDBJ | mRNA | ||
U73972 EMBL· GenBank· DDBJ | AAC24156.1 EMBL· GenBank· DDBJ | mRNA | ||
AK134267 EMBL· GenBank· DDBJ | BAE22074.1 EMBL· GenBank· DDBJ | mRNA | ||
AK147278 EMBL· GenBank· DDBJ | BAE27815.1 EMBL· GenBank· DDBJ | mRNA | ||
AK147597 EMBL· GenBank· DDBJ | BAE28015.1 EMBL· GenBank· DDBJ | mRNA | ||
AK158131 EMBL· GenBank· DDBJ | BAE34375.1 EMBL· GenBank· DDBJ | mRNA | ||
BC061219 EMBL· GenBank· DDBJ | AAH61219.1 EMBL· GenBank· DDBJ | mRNA | ||
U76758 EMBL· GenBank· DDBJ | AAB37323.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U76758 EMBL· GenBank· DDBJ | AAB37324.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U76758 EMBL· GenBank· DDBJ | AAB37325.1 EMBL· GenBank· DDBJ | Genomic DNA |