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5L0S

human POGLUT1 in complex with Factor VII EGF1 and UDP

Functional Information from GO Data
ChainGOidnamespacecontents
A0001756biological_processsomitogenesis
A0005783cellular_componentendoplasmic reticulum
A0005788cellular_componentendoplasmic reticulum lumen
A0006486biological_processprotein glycosylation
A0006493biological_processprotein O-linked glycosylation
A0007369biological_processgastrulation
A0008593biological_processregulation of Notch signaling pathway
A0010470biological_processregulation of gastrulation
A0012505cellular_componentendomembrane system
A0016757molecular_functionglycosyltransferase activity
A0018242biological_processprotein O-linked glycosylation via serine
A0035251molecular_functionUDP-glucosyltransferase activity
A0035252molecular_functionUDP-xylosyltransferase activity
A0045747biological_processpositive regulation of Notch signaling pathway
A0046527molecular_functionglucosyltransferase activity
A0048318biological_processaxial mesoderm development
A0048339biological_processparaxial mesoderm development
A0060537biological_processmuscle tissue development
A0072359biological_processcirculatory system development
A0140561molecular_functionEGF-domain serine glucosyltransferase activity
A0140562molecular_functionEGF-domain serine xylosyltransferase activity
B0005509molecular_functioncalcium ion binding
Functional Information from PROSITE/UniProt
site_idPS00010
Number of Residues12
DetailsASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CkDqlqsYiCfC
ChainResidueDetails
BCYS61-CYS72

site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CfClpAfeGRnC
ChainResidueDetails
BCYS70-CYS81

site_idPS01187
Number of Residues25
DetailsEGF_CA Calcium-binding EGF-like domain signature. DgDQCassp..........Cqnggs..CkDqlqsYiC
ChainResidueDetails
BASP46-CYS70

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsSITE: Important for S-112 for O-xylosylation
ChainResidueDetails
BSER53

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: (3R)-3-hydroxyaspartate => ECO:0000269|PubMed:3264725
ChainResidueDetails
BASP63
ASER212
AARG218
AVAL274

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: O-linked (Xyl...) serine; alternate => ECO:0000269|PubMed:1904059, ECO:0000269|PubMed:2129367, ECO:0000269|PubMed:21949356, ECO:0000269|PubMed:2511201
ChainResidueDetails
BSER52
AGLN240

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: O-linked (Fuc) serine => ECO:0000269|PubMed:1904059, ECO:0000269|PubMed:9023546
ChainResidueDetails
BSER60
AASN53
AASN204
AASN373

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PDB entries from 2024-07-17

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