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7V0M

Local refinement of ankyrin-1 (N-terminal half), class 1 of erythrocyte ankyrin-1 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0005198molecular_functionstructural molecule activity
A0005200molecular_functionstructural constituent of cytoskeleton
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005886cellular_componentplasma membrane
A0006887biological_processexocytosis
A0006888biological_processendoplasmic reticulum to Golgi vesicle-mediated transport
A0007010biological_processcytoskeleton organization
A0007165biological_processsignal transduction
A0008093molecular_functioncytoskeletal anchor activity
A0009898cellular_componentcytoplasmic side of plasma membrane
A0010638biological_processpositive regulation of organelle organization
A0014731cellular_componentspectrin-associated cytoskeleton
A0016020cellular_componentmembrane
A0016323cellular_componentbasolateral plasma membrane
A0016529cellular_componentsarcoplasmic reticulum
A0019899molecular_functionenzyme binding
A0019903molecular_functionprotein phosphatase binding
A0030018cellular_componentZ disc
A0030507molecular_functionspectrin binding
A0030673cellular_componentaxolemma
A0031430cellular_componentM band
A0031672cellular_componentA band
A0042383cellular_componentsarcolemma
A0043005cellular_componentneuron projection
A0044325molecular_functiontransmembrane transporter binding
A0045199biological_processmaintenance of epithelial cell apical/basal polarity
A0045211cellular_componentpostsynaptic membrane
A0051117molecular_functionATPase binding
A0072659biological_processprotein localization to plasma membrane
A0170014cellular_componentankyrin-1 complex
W0005452molecular_functionsolute:inorganic anion antiporter activity
W0005515molecular_functionprotein binding
W0005886cellular_componentplasma membrane
W0006811biological_processmonoatomic ion transport
W0006820biological_processmonoatomic anion transport
W0006821biological_processchloride transport
W0006873biological_processintracellular monoatomic ion homeostasis
W0007596biological_processblood coagulation
W0008509molecular_functionmonoatomic anion transmembrane transporter activity
W0009898cellular_componentcytoplasmic side of plasma membrane
W0015106molecular_functionbicarbonate transmembrane transporter activity
W0015108molecular_functionchloride transmembrane transporter activity
W0015297molecular_functionantiporter activity
W0015701biological_processbicarbonate transport
W0016020cellular_componentmembrane
W0016323cellular_componentbasolateral plasma membrane
W0017121biological_processplasma membrane phospholipid scrambling
W0030018cellular_componentZ disc
W0030492molecular_functionhemoglobin binding
W0030506molecular_functionankyrin binding
W0030863cellular_componentcortical cytoskeleton
W0035811biological_processnegative regulation of urine volume
W0042803molecular_functionprotein homodimerization activity
W0043495molecular_functionprotein-membrane adaptor activity
W0045852biological_processpH elevation
W0048821biological_processerythrocyte development
W0051453biological_processregulation of intracellular pH
W0055085biological_processtransmembrane transport
W0070062cellular_componentextracellular exosome
W0072562cellular_componentblood microparticle
W0072659biological_processprotein localization to plasma membrane
W0140900molecular_functionchloride:bicarbonate antiporter activity
W0170014cellular_componentankyrin-1 complex
W1902476biological_processchloride transmembrane transport
W1904539biological_processnegative regulation of glycolytic process through fructose-6-phosphate
Functional Information from PROSITE/UniProt
site_idPS00219
Number of Residues12
DetailsANION_EXCHANGER_1 Anion exchangers family signature 1. FGGLVRDIRRRY
ChainResidueDetails
WPHE379-TYR390

site_idPS00220
Number of Residues15
DetailsANION_EXCHANGER_2 Anion exchangers family signature 2. FLISLIFIYETFsKL
ChainResidueDetails
WPHE526-LEU540

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues540
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:26542571
ChainResidueDetails
WMET1-PRO403
WGLN457-LEU459
WPHE507-ARG518
WLYS592-ARG602
WTHR685-SER700
WLEU738-ARG760
WSER801-GLY838
WARG870-VAL911

site_idSWS_FT_FI2
Number of Residues23
DetailsTRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:26542571
ChainResidueDetails
WGLN404-LEU427
ASER759
ASER1396
ASER1486
ASER1666
ASER1671
ASER1686
ASER1690
ASER1696

site_idSWS_FT_FI3
Number of Residues82
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:26542571
ChainResidueDetails
WGLY428-MET435
WSER477-GLU485
WLYS542-THR570
WILE624-MET663

site_idSWS_FT_FI4
Number of Residues20
DetailsTRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:26542571
ChainResidueDetails
WGLY436-ALA456
ASER856

site_idSWS_FT_FI5
Number of Residues16
DetailsTRANSMEM: Discontinuously helical; Name=3 => ECO:0000269|PubMed:26542571
ChainResidueDetails
WLEU460-PHE476
ASER834
ASER1428
ASER1523
ASER1533

site_idSWS_FT_FI6
Number of Residues20
DetailsTRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:26542571
ChainResidueDetails
WTYR486-ALA506
ATHR1400

site_idSWS_FT_FI7
Number of Residues22
DetailsTRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:26542571
ChainResidueDetails
WTYR519-ILE541

site_idSWS_FT_FI8
Number of Residues20
DetailsTRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:26542571
ChainResidueDetails
WALA571-PHE591
ASER1390
ASER1392
ASER1617

site_idSWS_FT_FI9
Number of Residues20
DetailsTRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:26542571
ChainResidueDetails
WARG603-PHE623
ATHR1380

site_idSWS_FT_FI10
Number of Residues20
DetailsTRANSMEM: Helical; Name=8 => ECO:0000269|PubMed:26542571
ChainResidueDetails
WMET664-ILE684

site_idSWS_FT_FI11
Number of Residues18
DetailsTRANSMEM: Helical; Name=9 => ECO:0000269|PubMed:26542571
ChainResidueDetails
WGLY701-PHE719

site_idSWS_FT_FI12
Number of Residues17
DetailsTRANSMEM: Discontinuously helical; Name=10 => ECO:0000269|PubMed:26542571
ChainResidueDetails
WGLY720-ALA737

site_idSWS_FT_FI13
Number of Residues20
DetailsTRANSMEM: Helical; Name=11 => ECO:0000269|PubMed:26542571
ChainResidueDetails
WILE761-SER781

site_idSWS_FT_FI14
Number of Residues18
DetailsTRANSMEM: Helical; Name=12 => ECO:0000269|PubMed:26542571
ChainResidueDetails
WARG782-LEU800

site_idSWS_FT_FI15
Number of Residues30
DetailsINTRAMEM: Discontinuously helical => ECO:0000269|PubMed:26542571
ChainResidueDetails
WILE839-LEU869

site_idSWS_FT_FI16
Number of Residues1
DetailsSITE: Important for anion transport
ChainResidueDetails
WLYS590

site_idSWS_FT_FI17
Number of Residues1
DetailsSITE: Important for anion-proton cotransport
ChainResidueDetails
WGLU681

site_idSWS_FT_FI18
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0000269|PubMed:2790053, ECO:0000269|PubMed:701248
ChainResidueDetails
WMET1

site_idSWS_FT_FI19
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:10942405, ECO:0000269|PubMed:1998697
ChainResidueDetails
WTYR8
WTYR21

site_idSWS_FT_FI20
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:1998697
ChainResidueDetails
WTYR46

site_idSWS_FT_FI21
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P23562
ChainResidueDetails
WSER185

site_idSWS_FT_FI22
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P04919
ChainResidueDetails
WSER350

site_idSWS_FT_FI23
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:10942405
ChainResidueDetails
WTYR359
WTYR904

site_idSWS_FT_FI24
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:1885574
ChainResidueDetails
WCYS843

site_idSWS_FT_FI25
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:10861210, ECO:0000269|PubMed:24121512, ECO:0000269|PubMed:35835865
ChainResidueDetails
WASN642

227111

PDB entries from 2024-11-06

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