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2JO1

Structure of the Na,K-ATPase regulatory protein FXYD1 in micelles

Functional Information from GO Data
ChainGOidnamespacecontents
A0005254molecular_functionchloride channel activity
A0005886cellular_componentplasma membrane
A0005890cellular_componentsodium:potassium-exchanging ATPase complex
A0005901cellular_componentcaveola
A0006811biological_processmonoatomic ion transport
A0006813biological_processpotassium ion transport
A0006814biological_processsodium ion transport
A0006821biological_processchloride transport
A0006936biological_processmuscle contraction
A0008016biological_processregulation of heart contraction
A0010734biological_processnegative regulation of protein glutathionylation
A0014704cellular_componentintercalated disc
A0016020cellular_componentmembrane
A0016324cellular_componentapical plasma membrane
A0017080molecular_functionsodium channel regulator activity
A0030315cellular_componentT-tubule
A0042383cellular_componentsarcolemma
A0043269biological_processregulation of monoatomic ion transport
A0044325molecular_functiontransmembrane transporter binding
A0086036biological_processregulation of cardiac muscle cell membrane potential
A0099106molecular_functionion channel regulator activity
A1902476biological_processchloride transmembrane transport
A1903278biological_processpositive regulation of sodium ion export across plasma membrane
A2000649biological_processregulation of sodium ion transmembrane transporter activity
Functional Information from PROSITE/UniProt
site_idPS01310
Number of Residues14
DetailsFXYD FXYD family signature. DpFtYDyqSLQigG
ChainResidueDetails
AASP7-GLY20

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
AGLU1-SER15

site_idSWS_FT_FI2
Number of Residues20
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
ALEU16-LEU36

site_idSWS_FT_FI3
Number of Residues35
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
ASER37-ARG72

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: S-glutathionyl cysteine; alternate => ECO:0000250|UniProtKB:P56513
ChainResidueDetails
ACYS42

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q9Z239
ChainResidueDetails
ATHR59

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9Z239
ChainResidueDetails
ASER62

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKA and PKC => ECO:0000250|UniProtKB:P56513
ChainResidueDetails
ASER63

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:21868384
ChainResidueDetails
ASER68

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by PKC => ECO:0000250|UniProtKB:P56513
ChainResidueDetails
ATHR69

site_idSWS_FT_FI10
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:21868384
ChainResidueDetails
ACYS40

site_idSWS_FT_FI11
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine; alternate => ECO:0000269|PubMed:21868384
ChainResidueDetails
ACYS42

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PDB entries from 2024-07-24

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