Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7V0K

Consensus refinement of human erythrocyte ankyrin-1 complex (Composite map)

This is a non-PDB format compatible entry.

Functional Information from GO Data

Chain	GOid	namespace	contents
D	0016020	cellular_component	membrane
H	0005198	molecular_function	structural molecule activity
H	0005200	molecular_function	structural constituent of cytoskeleton
H	0005515	molecular_function	protein binding
H	0005737	cellular_component	cytoplasm
H	0005829	cellular_component	cytosol
H	0005856	cellular_component	cytoskeleton
H	0005886	cellular_component	plasma membrane
H	0006887	biological_process	exocytosis
H	0006888	biological_process	endoplasmic reticulum to Golgi vesicle-mediated transport
H	0007010	biological_process	cytoskeleton organization
H	0007165	biological_process	signal transduction
H	0008093	molecular_function	cytoskeletal anchor activity
H	0009898	cellular_component	cytoplasmic side of plasma membrane
H	0010638	biological_process	positive regulation of organelle organization
H	0014731	cellular_component	spectrin-associated cytoskeleton
H	0016020	cellular_component	membrane
H	0016323	cellular_component	basolateral plasma membrane
H	0016529	cellular_component	sarcoplasmic reticulum
H	0019899	molecular_function	enzyme binding
H	0019903	molecular_function	protein phosphatase binding
H	0030018	cellular_component	Z disc
H	0030507	molecular_function	spectrin binding
H	0030673	cellular_component	axolemma
H	0031430	cellular_component	M band
H	0031672	cellular_component	A band
H	0042383	cellular_component	sarcolemma
H	0043005	cellular_component	neuron projection
H	0044325	molecular_function	transmembrane transporter binding
H	0045199	biological_process	maintenance of epithelial cell apical/basal polarity
H	0045211	cellular_component	postsynaptic membrane
H	0048193	biological_process	Golgi vesicle transport
H	0051117	molecular_function	ATPase binding
H	0071944	cellular_component	cell periphery
H	0072659	biological_process	protein localization to plasma membrane
H	0170014	cellular_component	ankyrin-1 complex
K	0005886	cellular_component	plasma membrane
K	0008519	molecular_function	ammonium channel activity
K	0016020	cellular_component	membrane
K	0072488	biological_process	ammonium transmembrane transport
K	0097272	biological_process	ammonium homeostasis
K	0170014	cellular_component	ankyrin-1 complex
L	0005515	molecular_function	protein binding
L	0005886	cellular_component	plasma membrane
L	0006873	biological_process	intracellular monoatomic ion homeostasis
L	0008519	molecular_function	ammonium channel activity
L	0015200	molecular_function	methylammonium transmembrane transporter activity
L	0015670	biological_process	carbon dioxide transport
L	0015701	biological_process	bicarbonate transport
L	0016020	cellular_component	membrane
L	0022840	molecular_function	leak channel activity
L	0030506	molecular_function	ankyrin binding
L	0035378	biological_process	carbon dioxide transmembrane transport
L	0035379	molecular_function	carbon dioxide transmembrane transporter activity
L	0048821	biological_process	erythrocyte development
L	0060586	biological_process	multicellular organismal-level iron ion homeostasis
L	0072488	biological_process	ammonium transmembrane transport
L	0072489	biological_process	methylammonium transmembrane transport
L	0097272	biological_process	ammonium homeostasis
L	0098662	biological_process	inorganic cation transmembrane transport
L	0170014	cellular_component	ankyrin-1 complex
N	0016020	cellular_component	membrane
O	0005452	molecular_function	solute:inorganic anion antiporter activity
O	0005515	molecular_function	protein binding
O	0005737	cellular_component	cytoplasm
O	0005886	cellular_component	plasma membrane
O	0006811	biological_process	monoatomic ion transport
O	0006820	biological_process	monoatomic anion transport
O	0006821	biological_process	chloride transport
O	0006873	biological_process	intracellular monoatomic ion homeostasis
O	0007596	biological_process	blood coagulation
O	0008092	molecular_function	cytoskeletal protein binding
O	0008509	molecular_function	monoatomic anion transmembrane transporter activity
O	0009898	cellular_component	cytoplasmic side of plasma membrane
O	0015106	molecular_function	bicarbonate transmembrane transporter activity
O	0015108	molecular_function	chloride transmembrane transporter activity
O	0015297	molecular_function	antiporter activity
O	0015701	biological_process	bicarbonate transport
O	0016020	cellular_component	membrane
O	0016323	cellular_component	basolateral plasma membrane
O	0017121	biological_process	plasma membrane phospholipid scrambling
O	0030018	cellular_component	Z disc
O	0030492	molecular_function	hemoglobin binding
O	0030506	molecular_function	ankyrin binding
O	0030863	cellular_component	cortical cytoskeleton
O	0035811	biological_process	negative regulation of urine volume
O	0042803	molecular_function	protein homodimerization activity
O	0043495	molecular_function	membrane-membrane adaptor activity
O	0045852	biological_process	pH elevation
O	0048821	biological_process	erythrocyte development
O	0051453	biological_process	regulation of intracellular pH
O	0055085	biological_process	transmembrane transport
O	0070062	cellular_component	extracellular exosome
O	0072562	cellular_component	blood microparticle
O	0072659	biological_process	protein localization to plasma membrane
O	0140900	molecular_function	chloride:bicarbonate antiporter activity
O	0170014	cellular_component	ankyrin-1 complex
O	1902476	biological_process	chloride transmembrane transport
O	1904539	biological_process	negative regulation of glycolytic process through fructose-6-phosphate
P	0005452	molecular_function	solute:inorganic anion antiporter activity
P	0005515	molecular_function	protein binding
P	0005737	cellular_component	cytoplasm
P	0005886	cellular_component	plasma membrane
P	0006811	biological_process	monoatomic ion transport
P	0006820	biological_process	monoatomic anion transport
P	0006821	biological_process	chloride transport
P	0006873	biological_process	intracellular monoatomic ion homeostasis
P	0007596	biological_process	blood coagulation
P	0008092	molecular_function	cytoskeletal protein binding
P	0008509	molecular_function	monoatomic anion transmembrane transporter activity
P	0009898	cellular_component	cytoplasmic side of plasma membrane
P	0015106	molecular_function	bicarbonate transmembrane transporter activity
P	0015108	molecular_function	chloride transmembrane transporter activity
P	0015297	molecular_function	antiporter activity
P	0015701	biological_process	bicarbonate transport
P	0016020	cellular_component	membrane
P	0016323	cellular_component	basolateral plasma membrane
P	0017121	biological_process	plasma membrane phospholipid scrambling
P	0030018	cellular_component	Z disc
P	0030492	molecular_function	hemoglobin binding
P	0030506	molecular_function	ankyrin binding
P	0030863	cellular_component	cortical cytoskeleton
P	0035811	biological_process	negative regulation of urine volume
P	0042803	molecular_function	protein homodimerization activity
P	0043495	molecular_function	membrane-membrane adaptor activity
P	0045852	biological_process	pH elevation
P	0048821	biological_process	erythrocyte development
P	0051453	biological_process	regulation of intracellular pH
P	0055085	biological_process	transmembrane transport
P	0070062	cellular_component	extracellular exosome
P	0072562	cellular_component	blood microparticle
P	0072659	biological_process	protein localization to plasma membrane
P	0140900	molecular_function	chloride:bicarbonate antiporter activity
P	0170014	cellular_component	ankyrin-1 complex
P	1902476	biological_process	chloride transmembrane transport
P	1904539	biological_process	negative regulation of glycolytic process through fructose-6-phosphate
Q	0005515	molecular_function	protein binding
Q	0005886	cellular_component	plasma membrane
Q	0006873	biological_process	intracellular monoatomic ion homeostasis
Q	0008519	molecular_function	ammonium channel activity
Q	0015200	molecular_function	methylammonium transmembrane transporter activity
Q	0015670	biological_process	carbon dioxide transport
Q	0015701	biological_process	bicarbonate transport
Q	0016020	cellular_component	membrane
Q	0022840	molecular_function	leak channel activity
Q	0030506	molecular_function	ankyrin binding
Q	0035378	biological_process	carbon dioxide transmembrane transport
Q	0035379	molecular_function	carbon dioxide transmembrane transporter activity
Q	0048821	biological_process	erythrocyte development
Q	0060586	biological_process	multicellular organismal-level iron ion homeostasis
Q	0072488	biological_process	ammonium transmembrane transport
Q	0072489	biological_process	methylammonium transmembrane transport
Q	0097272	biological_process	ammonium homeostasis
Q	0098662	biological_process	inorganic cation transmembrane transport
Q	0170014	cellular_component	ankyrin-1 complex
W	0005452	molecular_function	solute:inorganic anion antiporter activity
W	0005515	molecular_function	protein binding
W	0005737	cellular_component	cytoplasm
W	0005886	cellular_component	plasma membrane
W	0006811	biological_process	monoatomic ion transport
W	0006820	biological_process	monoatomic anion transport
W	0006821	biological_process	chloride transport
W	0006873	biological_process	intracellular monoatomic ion homeostasis
W	0007596	biological_process	blood coagulation
W	0008092	molecular_function	cytoskeletal protein binding
W	0008509	molecular_function	monoatomic anion transmembrane transporter activity
W	0009898	cellular_component	cytoplasmic side of plasma membrane
W	0015106	molecular_function	bicarbonate transmembrane transporter activity
W	0015108	molecular_function	chloride transmembrane transporter activity
W	0015297	molecular_function	antiporter activity
W	0015701	biological_process	bicarbonate transport
W	0016020	cellular_component	membrane
W	0016323	cellular_component	basolateral plasma membrane
W	0017121	biological_process	plasma membrane phospholipid scrambling
W	0030018	cellular_component	Z disc
W	0030492	molecular_function	hemoglobin binding
W	0030506	molecular_function	ankyrin binding
W	0030863	cellular_component	cortical cytoskeleton
W	0035811	biological_process	negative regulation of urine volume
W	0042803	molecular_function	protein homodimerization activity
W	0043495	molecular_function	membrane-membrane adaptor activity
W	0045852	biological_process	pH elevation
W	0048821	biological_process	erythrocyte development
W	0051453	biological_process	regulation of intracellular pH
W	0055085	biological_process	transmembrane transport
W	0070062	cellular_component	extracellular exosome
W	0072562	cellular_component	blood microparticle
W	0072659	biological_process	protein localization to plasma membrane
W	0140900	molecular_function	chloride:bicarbonate antiporter activity
W	0170014	cellular_component	ankyrin-1 complex
W	1902476	biological_process	chloride transmembrane transport
W	1904539	biological_process	negative regulation of glycolytic process through fructose-6-phosphate
X	0000902	biological_process	cell morphogenesis
X	0003810	molecular_function	protein-glutamine gamma-glutamyltransferase activity
X	0005200	molecular_function	structural constituent of cytoskeleton
X	0005515	molecular_function	protein binding
X	0005524	molecular_function	ATP binding
X	0005737	cellular_component	cytoplasm
X	0005856	cellular_component	cytoskeleton
X	0005886	cellular_component	plasma membrane
X	0007010	biological_process	cytoskeleton organization
X	0008360	biological_process	regulation of cell shape
X	0016020	cellular_component	membrane
X	0018149	biological_process	peptide cross-linking
X	0020027	biological_process	hemoglobin metabolic process
X	0030863	cellular_component	cortical cytoskeleton
X	0043249	biological_process	erythrocyte maturation
X	0048536	biological_process	spleen development
X	0050801	biological_process	monoatomic ion homeostasis
X	0060586	biological_process	multicellular organismal-level iron ion homeostasis
X	0071944	cellular_component	cell periphery
X	0170014	cellular_component	ankyrin-1 complex

Functional Information from PROSITE/UniProt

site_id	PS00012
Number of Residues	16
Details	PHOSPHOPANTETHEINE Phosphopantetheine attachment site. KYGFSSVGINLLVAAL

Chain	Residue	Details
L	LYS74-LEU89

site_id	PS00219
Number of Residues	12
Details	ANION_EXCHANGER_1 Anion exchangers family signature 1. FGGLVRDIRRRY

Chain	Residue	Details
W	PHE379-TYR390

site_id	PS00220
Number of Residues	15
Details	ANION_EXCHANGER_2 Anion exchangers family signature 2. FLISLIFIYETFsKL

Chain	Residue	Details
W	PHE526-LEU540

site_id	PS00312
Number of Residues	10
Details	GLYCOPHORIN_A Glycophorin A signature. IIfGVMAGVI

Chain	Residue	Details
N	ILE95-ILE104

site_id	PS00547
Number of Residues	18
Details	TRANSGLUTAMINASES Transglutaminases active site. GQAWVlAAVacTvLRCLG

Chain	Residue	Details
X	GLY266-GLY283

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	648
Details	Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	156
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	70
Details	Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	29
Details	Repeat: {"description":"ANK 1"}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	29
Details	Repeat: {"description":"ANK 2"}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	29
Details	Repeat: {"description":"ANK 3"}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	29
Details	Repeat: {"description":"ANK 4"}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	27
Details	Repeat: {"description":"ANK 5"}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	29
Details	Repeat: {"description":"ANK 6"}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	29
Details	Repeat: {"description":"ANK 7"}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	29
Details	Repeat: {"description":"ANK 8"}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	29
Details	Repeat: {"description":"ANK 9"}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	29
Details	Repeat: {"description":"ANK 10"}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	29
Details	Repeat: {"description":"ANK 11"}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	29
Details	Repeat: {"description":"ANK 12"}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	3
Details	Modified residue: {"description":"(3S)-3-hydroxyasparagine; by HIF1AN; partial","evidences":[{"source":"PubMed","id":"21177872","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	18
Details	Region: {"description":"(Microbial infection) Interaction with P.falciparum (isolate K1) FBPA","evidences":[{"source":"PubMed","id":"2204832","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"10942405","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1998697","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	46
Details	Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	164
Details	Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI23
Number of Residues	40
Details	Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI24
Number of Residues	150
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI25
Number of Residues	32
Details	Transmembrane: {"description":"Discontinuously helical; Name=3","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI26
Number of Residues	40
Details	Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI27
Number of Residues	44
Details	Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI28
Number of Residues	40
Details	Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI29
Number of Residues	40
Details	Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI30
Number of Residues	40
Details	Transmembrane: {"description":"Helical; Name=8","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI31
Number of Residues	36
Details	Transmembrane: {"description":"Helical; Name=9","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI32
Number of Residues	34
Details	Transmembrane: {"description":"Discontinuously helical; Name=10","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI33
Number of Residues	40
Details	Transmembrane: {"description":"Helical; Name=11","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI34
Number of Residues	36
Details	Transmembrane: {"description":"Helical; Name=12","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI35
Number of Residues	60
Details	Intramembrane: {"description":"Discontinuously helical","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI36
Number of Residues	9
Details	Region: {"description":"Interaction with ANK1","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI37
Number of Residues	142
Details	Region: {"description":"Involved in anion transport"}

Chain

Residue

Details

site_id	SWS_FT_FI38
Number of Residues	2
Details	Site: {"description":"Important for anion transport"}

Chain

Residue

Details

site_id	SWS_FT_FI39
Number of Residues	2
Details	Site: {"description":"Important for anion-proton cotransport"}

Chain

Residue

Details

site_id	SWS_FT_FI40
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P23562","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI41
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P04919","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI42
Number of Residues	2
Details	Lipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"PubMed","id":"1885574","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI43
Number of Residues	2
Details	Glycosylation: {"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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI44
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"1998697","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI45
Number of Residues	8
Details	Region: {"description":"Band 3 binding","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI46
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by PKA","evidences":[{"source":"PubMed","id":"8499466","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI47
Number of Residues	44
Details	Transmembrane: {"description":"Helical"}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		Validation report (PDF)