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6JLD

Crystal structure of a human ependymin related protein

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005543molecular_functionphospholipid binding
A0005576cellular_componentextracellular region
A0005764cellular_componentlysosome
A0007160biological_processcell-matrix adhesion
A0008289molecular_functionlipid binding
A0042802molecular_functionidentical protein binding
A0043202cellular_componentlysosomal lumen
A1905573molecular_functionganglioside GM1 binding
A1990764biological_processmyofibroblast contraction
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005543molecular_functionphospholipid binding
B0005576cellular_componentextracellular region
B0005764cellular_componentlysosome
B0007160biological_processcell-matrix adhesion
B0008289molecular_functionlipid binding
B0042802molecular_functionidentical protein binding
B0043202cellular_componentlysosomal lumen
B1905573molecular_functionganglioside GM1 binding
B1990764biological_processmyofibroblast contraction
C0005509molecular_functioncalcium ion binding
C0005515molecular_functionprotein binding
C0005543molecular_functionphospholipid binding
C0005576cellular_componentextracellular region
C0005764cellular_componentlysosome
C0007160biological_processcell-matrix adhesion
C0008289molecular_functionlipid binding
C0042802molecular_functionidentical protein binding
C0043202cellular_componentlysosomal lumen
C1905573molecular_functionganglioside GM1 binding
C1990764biological_processmyofibroblast contraction
D0005509molecular_functioncalcium ion binding
D0005515molecular_functionprotein binding
D0005543molecular_functionphospholipid binding
D0005576cellular_componentextracellular region
D0005764cellular_componentlysosome
D0007160biological_processcell-matrix adhesion
D0008289molecular_functionlipid binding
D0042802molecular_functionidentical protein binding
D0043202cellular_componentlysosomal lumen
D1905573molecular_functionganglioside GM1 binding
D1990764biological_processmyofibroblast contraction
Functional Information from PROSITE/UniProt
site_idPS00898
Number of Residues12
DetailsEPENDYMIN_1 Ependymins signature 1. DQATKQCSkMTL
ChainResidueDetails
AASP107-LEU118

site_idPS00899
Number of Residues14
DetailsEPENDYMIN_2 Ependymins signature 2. FtPPSTCQMAqLEK
ChainResidueDetails
APHE204-LYS217

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:30729188
ChainResidueDetails
AASN130
BASN130
CASN130
DASN130

site_idSWS_FT_FI2
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN182
BASN182
CASN182
DASN182

222926

PDB entries from 2024-07-24

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