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7V0X

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

Functional Information from GO Data
ChainGOidnamespacecontents
J0005198molecular_functionstructural molecule activity
J0005200molecular_functionstructural constituent of cytoskeleton
J0005515molecular_functionprotein binding
J0005737cellular_componentcytoplasm
J0005829cellular_componentcytosol
J0005856cellular_componentcytoskeleton
J0005886cellular_componentplasma membrane
J0006887biological_processexocytosis
J0006888biological_processendoplasmic reticulum to Golgi vesicle-mediated transport
J0007010biological_processcytoskeleton organization
J0007165biological_processsignal transduction
J0008093molecular_functioncytoskeletal anchor activity
J0009898cellular_componentcytoplasmic side of plasma membrane
J0010638biological_processpositive regulation of organelle organization
J0014731cellular_componentspectrin-associated cytoskeleton
J0016020cellular_componentmembrane
J0016323cellular_componentbasolateral plasma membrane
J0016529cellular_componentsarcoplasmic reticulum
J0019899molecular_functionenzyme binding
J0019903molecular_functionprotein phosphatase binding
J0030018cellular_componentZ disc
J0030507molecular_functionspectrin binding
J0030673cellular_componentaxolemma
J0031430cellular_componentM band
J0031672cellular_componentA band
J0042383cellular_componentsarcolemma
J0043005cellular_componentneuron projection
J0044325molecular_functiontransmembrane transporter binding
J0045199biological_processmaintenance of epithelial cell apical/basal polarity
J0045211cellular_componentpostsynaptic membrane
J0051117molecular_functionATPase binding
J0072659biological_processprotein localization to plasma membrane
J0170014cellular_componentankyrin-1 complex
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsMOD_RES: (3S)-3-hydroxyasparagine; by HIF1AN; partial => ECO:0000269|PubMed:21177872
ChainResidueDetails
JASN105
JASN233
JASN431
JASN464
JASN629
JASN662
JASN728
JASN761

site_idSWS_FT_FI2
Number of Residues9
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
JSER429
JSER759
JSER1396
JSER1486
JSER1666
JSER1671
JSER1686
JSER1690
JSER1696

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: (3S)-3-hydroxyaspartate; by HIF1AN; partial => ECO:0000269|PubMed:21177872
ChainResidueDetails
JASP695

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
JSER781
JSER856

site_idSWS_FT_FI5
Number of Residues5
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
JSER817
JSER834
JSER1428
JSER1523
JSER1533

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q02357
ChainResidueDetails
JTHR961
JTHR1400

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q02357
ChainResidueDetails
JTYR1073

site_idSWS_FT_FI8
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q02357
ChainResidueDetails
JSER1082
JSER1390
JSER1392
JSER1617

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
JTHR1378
JTHR1380

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PDB entries from 2024-09-04

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