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7TW3

Cryo-EM structure of human ankyrin complex (B2P1A1) from red blood cell

Functional Information from GO Data
ChainGOidnamespacecontents
A0005452molecular_functionsolute:inorganic anion antiporter activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0006820biological_processmonoatomic anion transport
A0006821biological_processchloride transport
A0006873biological_processintracellular monoatomic ion homeostasis
A0007596biological_processblood coagulation
A0008092molecular_functioncytoskeletal protein binding
A0008509molecular_functionmonoatomic anion transmembrane transporter activity
A0009898cellular_componentcytoplasmic side of plasma membrane
A0015106molecular_functionbicarbonate transmembrane transporter activity
A0015108molecular_functionchloride transmembrane transporter activity
A0015297molecular_functionantiporter activity
A0015701biological_processbicarbonate transport
A0016020cellular_componentmembrane
A0016323cellular_componentbasolateral plasma membrane
A0017121biological_processplasma membrane phospholipid scrambling
A0030018cellular_componentZ disc
A0030492molecular_functionhemoglobin binding
A0030506molecular_functionankyrin binding
A0030863cellular_componentcortical cytoskeleton
A0035811biological_processnegative regulation of urine volume
A0036296biological_processresponse to increased oxygen levels
A0042803molecular_functionprotein homodimerization activity
A0043495molecular_functionprotein-membrane adaptor activity
A0045852biological_processpH elevation
A0048821biological_processerythrocyte development
A0051453biological_processregulation of intracellular pH
A0055085biological_processtransmembrane transport
A0070062cellular_componentextracellular exosome
A0072562cellular_componentblood microparticle
A0072659biological_processprotein localization to plasma membrane
A0140900molecular_functionchloride:bicarbonate antiporter activity
A0170014cellular_componentankyrin-1 complex
A1902476biological_processchloride transmembrane transport
A1904539biological_processnegative regulation of glycolytic process through fructose-6-phosphate
B0005452molecular_functionsolute:inorganic anion antiporter activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005886cellular_componentplasma membrane
B0006811biological_processmonoatomic ion transport
B0006820biological_processmonoatomic anion transport
B0006821biological_processchloride transport
B0006873biological_processintracellular monoatomic ion homeostasis
B0007596biological_processblood coagulation
B0008092molecular_functioncytoskeletal protein binding
B0008509molecular_functionmonoatomic anion transmembrane transporter activity
B0009898cellular_componentcytoplasmic side of plasma membrane
B0015106molecular_functionbicarbonate transmembrane transporter activity
B0015108molecular_functionchloride transmembrane transporter activity
B0015297molecular_functionantiporter activity
B0015701biological_processbicarbonate transport
B0016020cellular_componentmembrane
B0016323cellular_componentbasolateral plasma membrane
B0017121biological_processplasma membrane phospholipid scrambling
B0030018cellular_componentZ disc
B0030492molecular_functionhemoglobin binding
B0030506molecular_functionankyrin binding
B0030863cellular_componentcortical cytoskeleton
B0035811biological_processnegative regulation of urine volume
B0036296biological_processresponse to increased oxygen levels
B0042803molecular_functionprotein homodimerization activity
B0043495molecular_functionprotein-membrane adaptor activity
B0045852biological_processpH elevation
B0048821biological_processerythrocyte development
B0051453biological_processregulation of intracellular pH
B0055085biological_processtransmembrane transport
B0070062cellular_componentextracellular exosome
B0072562cellular_componentblood microparticle
B0072659biological_processprotein localization to plasma membrane
B0140900molecular_functionchloride:bicarbonate antiporter activity
B0170014cellular_componentankyrin-1 complex
B1902476biological_processchloride transmembrane transport
B1904539biological_processnegative regulation of glycolytic process through fructose-6-phosphate
E0000902biological_processcell morphogenesis
E0003810molecular_functionprotein-glutamine gamma-glutamyltransferase activity
E0005200molecular_functionstructural constituent of cytoskeleton
E0005515molecular_functionprotein binding
E0005524molecular_functionATP binding
E0005856cellular_componentcytoskeleton
E0005886cellular_componentplasma membrane
E0007010biological_processcytoskeleton organization
E0008360biological_processregulation of cell shape
E0016020cellular_componentmembrane
E0018149biological_processpeptide cross-linking
E0020027biological_processhemoglobin metabolic process
E0030863cellular_componentcortical cytoskeleton
E0043249biological_processerythrocyte maturation
E0048536biological_processspleen development
E0050801biological_processmonoatomic ion homeostasis
E0060586biological_processmulticellular organismal-level iron ion homeostasis
E0071944cellular_componentcell periphery
E0170014cellular_componentankyrin-1 complex
G0005198molecular_functionstructural molecule activity
G0005200molecular_functionstructural constituent of cytoskeleton
G0005515molecular_functionprotein binding
G0005737cellular_componentcytoplasm
G0005829cellular_componentcytosol
G0005856cellular_componentcytoskeleton
G0005886cellular_componentplasma membrane
G0006887biological_processexocytosis
G0006888biological_processendoplasmic reticulum to Golgi vesicle-mediated transport
G0007010biological_processcytoskeleton organization
G0007165biological_processsignal transduction
G0008093molecular_functioncytoskeletal anchor activity
G0009898cellular_componentcytoplasmic side of plasma membrane
G0014731cellular_componentspectrin-associated cytoskeleton
G0016020cellular_componentmembrane
G0016323cellular_componentbasolateral plasma membrane
G0016529cellular_componentsarcoplasmic reticulum
G0019899molecular_functionenzyme binding
G0019903molecular_functionprotein phosphatase binding
G0030018cellular_componentZ disc
G0030507molecular_functionspectrin binding
G0030673cellular_componentaxolemma
G0031430cellular_componentM band
G0031672cellular_componentA band
G0042383cellular_componentsarcolemma
G0043005cellular_componentneuron projection
G0044325molecular_functiontransmembrane transporter binding
G0045199biological_processmaintenance of epithelial cell apical/basal polarity
G0045211cellular_componentpostsynaptic membrane
G0048193biological_processGolgi vesicle transport
G0051117molecular_functionATPase binding
G0071944cellular_componentcell periphery
G0072659biological_processprotein localization to plasma membrane
G0170014cellular_componentankyrin-1 complex
Functional Information from PROSITE/UniProt
site_idPS00219
Number of Residues12
DetailsANION_EXCHANGER_1 Anion exchangers family signature 1. FGGLVRDIRRRY
ChainResidueDetails
APHE379-TYR390

site_idPS00220
Number of Residues15
DetailsANION_EXCHANGER_2 Anion exchangers family signature 2. FLISLIFIYETFsKL
ChainResidueDetails
APHE526-LEU540

site_idPS00547
Number of Residues18
DetailsTRANSGLUTAMINASES Transglutaminases active site. GQAWVlAAVacTvLRCLG
ChainResidueDetails
EGLY266-GLY283

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues46
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues164
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues150
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues32
DetailsTransmembrane: {"description":"Discontinuously helical; Name=3","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues44
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=8","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues36
DetailsTransmembrane: {"description":"Helical; Name=9","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues34
DetailsTransmembrane: {"description":"Discontinuously helical; Name=10","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=11","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues36
DetailsTransmembrane: {"description":"Helical; Name=12","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues60
DetailsIntramembrane: {"description":"Discontinuously helical","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues18
DetailsRegion: {"description":"Interaction with ANK1","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues142
DetailsRegion: {"description":"Involved in anion transport"}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues2
DetailsSite: {"description":"Important for anion transport"}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues2
DetailsSite: {"description":"Important for anion-proton cotransport"}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"1998697","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P23562","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI22
Number of Residues2
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"PubMed","id":"1885574","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI23
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"10861210","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24121512","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35835865","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI24
Number of Residues53
DetailsRegion: {"description":"Dimerization arm"}
ChainResidueDetails

site_idSWS_FT_FI25
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P04919","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI26
Number of Residues8
DetailsRegion: {"description":"Band 3 binding","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI27
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by PKA","evidences":[{"source":"PubMed","id":"8499466","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI28
Number of Residues27
DetailsRepeat: {"description":"ANK 5"}
ChainResidueDetails

site_idSWS_FT_FI29
Number of Residues29
DetailsRepeat: {"description":"ANK 6"}
ChainResidueDetails

site_idSWS_FT_FI30
Number of Residues29
DetailsRepeat: {"description":"ANK 7"}
ChainResidueDetails

site_idSWS_FT_FI31
Number of Residues29
DetailsRepeat: {"description":"ANK 8"}
ChainResidueDetails

site_idSWS_FT_FI32
Number of Residues29
DetailsRepeat: {"description":"ANK 9"}
ChainResidueDetails

site_idSWS_FT_FI33
Number of Residues29
DetailsRepeat: {"description":"ANK 10"}
ChainResidueDetails

site_idSWS_FT_FI34
Number of Residues29
DetailsRepeat: {"description":"ANK 11"}
ChainResidueDetails

site_idSWS_FT_FI35
Number of Residues29
DetailsRepeat: {"description":"ANK 12"}
ChainResidueDetails

site_idSWS_FT_FI36
Number of Residues29
DetailsRepeat: {"description":"ANK 13"}
ChainResidueDetails

site_idSWS_FT_FI37
Number of Residues29
DetailsRepeat: {"description":"ANK 14"}
ChainResidueDetails

site_idSWS_FT_FI38
Number of Residues29
DetailsRepeat: {"description":"ANK 15"}
ChainResidueDetails

site_idSWS_FT_FI39
Number of Residues29
DetailsRepeat: {"description":"ANK 16"}
ChainResidueDetails

site_idSWS_FT_FI40
Number of Residues29
DetailsRepeat: {"description":"ANK 17"}
ChainResidueDetails

site_idSWS_FT_FI41
Number of Residues29
DetailsRepeat: {"description":"ANK 18"}
ChainResidueDetails

site_idSWS_FT_FI42
Number of Residues29
DetailsRepeat: {"description":"ANK 19"}
ChainResidueDetails

site_idSWS_FT_FI43
Number of Residues29
DetailsRepeat: {"description":"ANK 20"}
ChainResidueDetails

site_idSWS_FT_FI44
Number of Residues29
DetailsRepeat: {"description":"ANK 21"}
ChainResidueDetails

site_idSWS_FT_FI45
Number of Residues29
DetailsRepeat: {"description":"ANK 22"}
ChainResidueDetails

site_idSWS_FT_FI46
Number of Residues29
DetailsRepeat: {"description":"ANK 23"}
ChainResidueDetails

site_idSWS_FT_FI47
Number of Residues7
DetailsModified residue: {"description":"(3S)-3-hydroxyasparagine; by HIF1AN; partial","evidences":[{"source":"PubMed","id":"21177872","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI48
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI49
Number of Residues1
DetailsModified residue: {"description":"(3S)-3-hydroxyaspartate; by HIF1AN; partial","evidences":[{"source":"PubMed","id":"21177872","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI50
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

244349

PDB entries from 2025-11-05

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