Q02357 · ANK1_MOUSE

  • Protein
    Ankyrin-1
  • Gene
    Ank1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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 annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular ComponentA band
Cellular Componentankyrin-1 complex
Cellular Componentaxolemma
Cellular Componentcortical cytoskeleton
Cellular ComponentM band
Cellular Componentmembrane
Cellular Componentneuron projection
Cellular Componentplasma membrane
Cellular Componentpostsynaptic membrane
Cellular Componentsarcolemma
Cellular Componentsarcoplasmic reticulum
Cellular Componentspectrin-associated cytoskeleton
Cellular ComponentZ disc
Molecular Functioncytoskeletal anchor activity
Molecular Functionspectrin binding
Molecular Functiontransmembrane transporter binding
Biological Processerythrocyte development
Biological Processinorganic cation transmembrane transport
Biological Processmulticellular organismal-level iron ion homeostasis
Biological Processporphyrin-containing compound biosynthetic process
Biological Processpositive regulation of organelle organization
Biological Processprotein localization to plasma membrane
Biological Processsignal transduction

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Ankyrin-1
  • Short names
    ANK-1
  • Alternative names
    • Erythrocyte ankyrin

Gene names

    • Name
      Ank1
    • Synonyms
      Ank-1

Organism names

  • Taxonomic identifier
  • Strain
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q02357
  • Secondary accessions
    • P70440
    • P97446
    • P97941
    • Q3TZ35
    • Q3UH42

Proteomes

Organism-specific databases

Subcellular Location

Isoform Er1

Note: Probably the other erythrocyte (Er) isoforms, are located near the surface of erythrocytic plasma membrane.

Isoform Mu7

Membrane

Isoform Mu8

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00000668841-1862Ankyrin-1
Modified residue55In isoform Q02357-7; Phosphoserine
Modified residue55In isoform Q02357-8; Phosphoserine
Modified residue101(3S)-3-hydroxyasparagine; by HIF1AN; partial
Modified residue229(3S)-3-hydroxyasparagine; by HIF1AN
Modified residue425Phosphoserine
Modified residue427(3S)-3-hydroxyasparagine; by HIF1AN
Modified residue460(3S)-3-hydroxyasparagine; by HIF1AN
Modified residue625(3S)-3-hydroxyasparagine; by HIF1AN
Modified residue658(3S)-3-hydroxyasparagine; by HIF1AN
Modified residue691(3S)-3-hydroxyaspartate; by HIF1AN
Modified residue724(3S)-3-hydroxyasparagine; by HIF1AN
Modified residue755Phosphoserine
Modified residue757(3S)-3-hydroxyasparagine; by HIF1AN
Modified residue777Phosphoserine
Modified residue813Phosphoserine
Modified residue830Phosphoserine
Modified residue852Phosphoserine
Modified residue862Phosphothreonine
Modified residue957Phosphothreonine
Modified residue1069Phosphotyrosine
Modified residue1078Phosphoserine
Modified residue1374Phosphothreonine
Modified residue1376Phosphothreonine
Modified residue1386Phosphoserine
Modified residue1388Phosphoserine
Modified residue1396Phosphothreonine
Modified residue1424Phosphoserine
Modified residue1473Phosphoserine
Modified residue1482Phosphoserine
Modified residue1519Phosphoserine
Modified residue1529Phosphoserine
Modified residue1612Phosphoserine
Modified residue1660Phosphoserine
Modified residue1675Phosphoserine
Modified residue1685Phosphoserine

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

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.

TypeIDPosition(s)Description
Region1-82789 kDa domain
Repeat40-69ANK 1
Repeat73-102ANK 2
Repeat106-135ANK 3
Repeat139-168ANK 4
Repeat170-197ANK 5
Repeat201-230ANK 6
Repeat234-263ANK 7
Repeat267-296ANK 8
Repeat300-329ANK 9
Repeat333-362ANK 10
Repeat366-395ANK 11
Repeat399-428ANK 12
Repeat432-461ANK 13
Repeat465-494ANK 14
Repeat498-527ANK 15
Repeat531-560ANK 16
Repeat564-593ANK 17
Repeat597-626ANK 18
Repeat630-659ANK 19
Repeat663-692ANK 20
Repeat696-725ANK 21
Repeat729-758ANK 22
Repeat762-791ANK 23
Region812-834Disordered
Compositional bias817-834Basic and acidic residues
Region872-900Disordered
Domain909-1064ZU5 1
Domain1066-1212ZU5 2
Region1197-1331UPA domain
Region1387-186255 kDa regulatory domain
Domain1399-1483Death
Region1481-1506Disordered
Compositional bias1486-1500Basic and acidic residues
Region1598-1720Disordered
Compositional bias1636-1652Basic and acidic residues
Compositional bias1653-1684Polar residues
Compositional bias1699-1720Polar residues
Region1744-1767Disordered

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

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (8)
  • Sequence status
    Complete

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.

  • Name
    Er1
  • Note
    Produced by alternative promoter usage.
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    1,862
  • Mass (Da)
    204,227
  • Last updated
    2006-05-16 v2
  • Checksum
    B5F3EBB447C3485D
MGFCKADAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYGTKGKVRLPALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAKRLGYISVTDVLKVVTDETSVVLVSDKHRMSYPETVDEILDVSEDEGDELVGSKAERRDSRDVGEEKELLDFVPKLDQVVESPAIPRIPCVTPETVVIRSEDQEQASKEYDEDSLIPSSPATETSDNISPVASPVHTGFLVSFMVDARGGSMRGSRHNGLRVVIPPRTCAAPTRITCRLVKPQKLNTPPPLAEEEGLASRIIALGPTGAQFLSPVIVEIPHFASHGRGDRELVVLRSENGSVWKEHKSRYGESYLDQILNGMDEELGSLEELEKKRVCRIITTDFPLYFVIMSRLCQDYDTIGPEGGSLRSKLVPLVQATFPENAVTKKVKLALQAQPVPDELVTKLLGNQATFSPIVTVEPRRRKFHRPIGLRIPLPPSWTDNPRDSGEGDTTSLRLLCSVIGGTDQAQWEDITGTTKLIYANECANFTTNVSARFWLSDCPRTAEAVHFATLLYKELTAVPYMAKFVIFAKMNDAREGRLRCYCMTDDKVDKTLEQHENFVEVARSRDIEVLEGMPLFAELSGNLVPVKKAAQQRSFHFQSFRENRLAIPVKVRDSSREPGGFLSFLRKTMKYEDTQHILCHLNITMPPCTKGSGAEDRRRTLTPLTLRYSILSESRLGFTSDTDRVEMRMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIVNMLEGSGRQSRNLKPERRHGDREYSLSPSQVNGYSSLQDELLSPASLQYALPSPLCADQYWNEVTVIDAIPLAATEHDTMLEMSDMQVWSAGLTPSLVTAEDSSLECSKAEDSDAIPEWKLEGAHSEDTQGPELGSQDLVEDDTVDSDATNGLADLLGQEEGQRSEKKRQEVSGTEQDTETEVSLVSGQQRVHARITDSPSVRQVLDRSQARTLDWDKQGSTAVHPQEATQSSWQEEVTQGPHSFQRRITTIQGPEPGALQEYEQVLVSTREHVQRGPPETGSPKAGKEPSLWAPESAFSQEVQGDELQNIPGEQVTEEQFTDEQGNIVTKKIIRKVVRQVDSSGAIDTQQHEEVELRGSGLQPDLIEGRKGAQIVKRASLKRGKQ

Q02357-2

  • Name
    Br2
  • Synonyms
    Cb14/11
  • Note
    Produced by alternative splicing of isoform Er1.
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q02357-3

  • Name
    Er3
  • Synonyms
    Er18
  • Note
    Incomplete sequence. Produced by alternative splicing of isoform Er1.
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1832-1862: ELRGSGLQPDLIEGRKGAQIVKRASLKRGKQ → IVEGPLADPGDLEADIESFMKLTKDHTSTPKP

Q02357-4

  • Name
    Br4
  • Synonyms
    Cb12
  • Note
    Incomplete sequence. Produced by alternative splicing of isoform Er1.
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1831-1831: V → VIVEGPLADPGDLEADIESFMKLTKV

Q02357-5

  • Name
    5
  • Note
    Produced by alternative splicing of isoform Er1.
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1-4: MGFC → MAQAAKQLKKIKDIEAQALQEQKEKEESNRKRRNRSRDRKK
    • 1510-1664: Missing

Q02357-6

  • Name
    6
  • Note
    Produced by alternative splicing of isoform Er1.
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1-4: MGFC → MAQAAKQLKKIKDIEAQALQEQKEKEESNRKRRNRSRDRKK
    • 817-817: G → GTAHISIMG

Q02357-7

  • Name
    Mu7
  • Synonyms
    skAnk1
  • Note
    Produced by alternative promoter usage.
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1-1707: Missing
    • 1708-1780: SSWQEEVTQGPHSFQRRITTIQGPEPGALQEYEQVLVSTREHVQRGPPETGSPKAGKEPSLWAPESAFSQEVQ → MWTFITQLLVTLVLLGFFLVSCQNVMHIVKGSLCFVLKHIHQELDKELGESEGLSDDEETISTRVVRRRVFLK

Q02357-8

  • Name
    Mu8
  • Note
    Produced by alternative splicing of isoform Mu7.
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • 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

View all
EntryEntry nameGene nameLength
A0A0R4J1N7A0A0R4J1N7_MOUSEAnk11907
G5E8J2G5E8J2_MOUSEAnk11848
B7ZW98B7ZW98_MOUSEAnk11852
G8JL84G8JL84_MOUSEAnk11863
D3YTV8D3YTV8_MOUSEAnk11878
D3Z5M4D3Z5M4_MOUSEAnk11883
F7D1P5F7D1P5_MOUSEAnk11098
Q0VGY9Q0VGY9_MOUSEAnk11887
D6RJ51D6RJ51_MOUSEAnk1572
G3UXF4G3UXF4_MOUSEAnk1109
G3UY11G3UY11_MOUSEAnk11057
E9QNT8E9QNT8_MOUSEAnk11862

Features

Showing features for alternative sequence, sequence conflict, compositional bias.

TypeIDPosition(s)Description
Alternative sequenceVSP_0184541-4in isoform 5 and isoform 6
Alternative sequenceVSP_0184531-5in isoform Br2
Alternative sequenceVSP_0184521-1707in isoform Mu7 and isoform Mu8
Sequence conflict507in Ref. 3; BAE34375
Sequence conflict678in Ref. 1; AAA37236
Alternative sequenceVSP_018455817in isoform Br2 and isoform 6
Compositional bias817-834Basic and acidic residues
Sequence conflict818in Ref. 3; BAE34375
Sequence conflict1098in Ref. 2; CAA48801
Sequence conflict1481in Ref. 2; CAA48801
Compositional bias1486-1500Basic and acidic residues
Alternative sequenceVSP_0184561510-1664in isoform 5
Sequence conflict1541in Ref. 3; BAE27815/BAE28015
Compositional bias1636-1652Basic and acidic residues
Alternative sequenceVSP_0184571636-1665in isoform Br2
Sequence conflict1644in Ref. 3; BAE28015
Compositional bias1653-1684Polar residues
Compositional bias1699-1720Polar residues
Alternative sequenceVSP_0184581708-1780in isoform Mu7 and isoform Mu8
Alternative sequenceVSP_0184591831in isoform Br4
Alternative sequenceVSP_0184601832-1862in isoform Er3 and isoform Mu8

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

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