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5L0V

human POGLUT1 in complex with 2F-glucose modified EGF(+) 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. CvNtvgsYtClC
ChainResidueDetails
BCYS16-CYS27

site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. ClCppGftGPnC
ChainResidueDetails
BCYS25-CYS36

site_idPS01186
Number of Residues12
DetailsEGF_2 EGF-like domain signature 2. ClCppGFtgpn....C
ChainResidueDetails
BCYS25-CYS36

site_idPS01187
Number of Residues25
DetailsEGF_CA Calcium-binding EGF-like domain signature. DiDECasnp..........Cqnggt..CvNtvgsYtC
ChainResidueDetails
BASP1-CYS25

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:28775322
ChainResidueDetails
AASP133

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:28775322, ECO:0007744|PDB:5L0U
ChainResidueDetails
ATYR177
ASER212
AARG218
AVAL274

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Interaction with the consensus sequence C-X-S-X-[PA]-C in peptide substrates => ECO:0000269|PubMed:28775322
ChainResidueDetails
AARG132
AGLN240

site_idSWS_FT_FI4
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:28775322, ECO:0007744|PDB:5L0V
ChainResidueDetails
AASN40
AASN53
AASN204
AASN373

226707

PDB entries from 2024-10-30

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