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5L0R

human POGLUT1 in complex with Notch1 EGF12 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
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0018242biological_processobsolete protein 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. ClDqigeFqCiC
ChainResidueDetails
BCYS467-CYS478

site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CiCmpGyeGVhC
ChainResidueDetails
BCYS476-CYS487

site_idPS01186
Number of Residues12
DetailsEGF_2 EGF-like domain signature 2. CiCmpGYegvh....C
ChainResidueDetails
BCYS476-CYS487

site_idPS01187
Number of Residues25
DetailsEGF_CA Calcium-binding EGF-like domain signature. DvNECvsnp..........Cqndat..ClDqigeFqC
ChainResidueDetails
BASP452-CYS476

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsRegion: {"description":"Interaction with the consensus sequence C-X-S-X-[PA]-C in peptide substrates","evidences":[{"source":"PubMed","id":"28775322","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"28775322","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"28775322","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5L0U","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsSite: {"description":"Interaction with the consensus sequence C-X-S-X-[PA]-C in peptide substrates","evidences":[{"source":"PubMed","id":"28775322","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"28775322","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5L0V","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues36
DetailsDomain: {"description":"EGF-like 12; calcium-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q07008","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsSite: {"description":"Interaction with DLL4","evidences":[{"source":"UniProtKB","id":"Q07008","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsGlycosylation: {"description":"O-linked (Glc...) serine","evidences":[{"source":"UniProtKB","id":"Q07008","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsGlycosylation: {"description":"O-linked (Fuc...) threonine","evidences":[{"source":"UniProtKB","id":"Q07008","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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