PGLT1_HUMAN - dbPTM
PGLT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PGLT1_HUMAN
UniProt AC Q8NBL1
Protein Name Protein O-glucosyltransferase 1 {ECO:0000305}
Gene Name POGLUT1 {ECO:0000312|HGNC:HGNC:22954}
Organism Homo sapiens (Human).
Sequence Length 392
Subcellular Localization Endoplasmic reticulum lumen .
Protein Description Dual specificity glycosyltransferase that catalyzes the transfer of glucose and xylose from UDP-glucose and UDP-xylose, respectively, to a serine residue found in the consensus sequence of C-X-S-X-P-C. [PubMed: 21081508]
Protein Sequence MEWWASSPLRLWLLLFLLPSAQGRQKESGSKWKVFIDQINRSLENYEPCSSQNCSCYHGVIEEDLTPFRGGISRKMMAEVVRRKLGTHYQITKNRLYRENDCMFPSRCSGVEHFILEVIGRLPDMEMVINVRDYPQVPKWMEPAIPVFSFSKTSEYHDIMYPAWTFWEGGPAVWPIYPTGLGRWDLFREDLVRSAAQWPWKKKNSTAYFRGSRTSPERDPLILLSRKNPKLVDAEYTKNQAWKSMKDTLGKPAAKDVHLVDHCKYKYLFNFRGVAASFRFKHLFLCGSLVFHVGDEWLEFFYPQLKPWVHYIPVKTDLSNVQELLQFVKANDDVAQEIAERGSQFIRNHLQMDDITCYWENLLSEYSKFLSYNVTRRKGYDQIIPKMLKTEL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
6Phosphorylation--MEWWASSPLRLWL
--CCHHHCCHHHHHH
20.8320068231
7Phosphorylation-MEWWASSPLRLWLL
-CCHHHCCHHHHHHH
21.8720068231
20PhosphorylationLLLFLLPSAQGRQKE
HHHHHCHHHCCCCCC
32.9420068231
40N-linked_GlycosylationKVFIDQINRSLENYE
CHHHHHHHHHHHCCC
23.1228775322
53N-linked_GlycosylationYEPCSSQNCSCYHGV
CCCCCCCCCEEECCC
22.9328775322
84UbiquitinationMAEVVRRKLGTHYQI
HHHHHHHHCCCCEEE
40.48-
87PhosphorylationVVRRKLGTHYQITKN
HHHHHCCCCEEECCC
28.0421406692
89PhosphorylationRRKLGTHYQITKNRL
HHHCCCCEEECCCCE
11.0521406692
92PhosphorylationLGTHYQITKNRLYRE
CCCCEEECCCCEECC
13.5221406692
93UbiquitinationGTHYQITKNRLYREN
CCCEEECCCCEECCC
41.52-
109PhosphorylationCMFPSRCSGVEHFIL
CCCCCCCCCHHHHHH
44.7722210691
149PhosphorylationEPAIPVFSFSKTSEY
CCCCCEEECCCCCCC
28.9224719451
151PhosphorylationAIPVFSFSKTSEYHD
CCCEEECCCCCCCCC
33.5522210691
194PhosphorylationFREDLVRSAAQWPWK
HHHHHHHHHHHCCCC
22.0727251275
204N-linked_GlycosylationQWPWKKKNSTAYFRG
HCCCCCCCCCCCCCC
54.1728775322
204N-linked_GlycosylationQWPWKKKNSTAYFRG
HCCCCCCCCCCCCCC
54.1728775322
230UbiquitinationLLSRKNPKLVDAEYT
EEECCCCCCCCCHHH
71.22-
238UbiquitinationLVDAEYTKNQAWKSM
CCCCHHHHHHHHHHH
46.27-
277PhosphorylationNFRGVAASFRFKHLF
CCCCHHHCCCHHHHH
13.7623532336
372PhosphorylationEYSKFLSYNVTRRKG
HHHHHHCCCCCCCCC
18.79-
373N-linked_GlycosylationYSKFLSYNVTRRKGY
HHHHHCCCCCCCCCC
25.8828775322

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of PGLT1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PGLT1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PGLT1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBR4_HUMANUBR4physical
26186194
CALX_HUMANCANXphysical
26186194
ZZEF1_HUMANZZEF1physical
26186194
HECD3_HUMANHECTD3physical
26186194
CGAT2_HUMANCSGALNACT2physical
26186194
PON2_HUMANPON2physical
26186194
KCMF1_HUMANKCMF1physical
26186194
CGAT2_HUMANCSGALNACT2physical
28514442
CALX_HUMANCANXphysical
28514442
LYAG_HUMANGAAphysical
28514442
PON2_HUMANPON2physical
28514442
PIGT_HUMANPIGTphysical
28514442
HECD3_HUMANHECTD3physical
28514442
ZZEF1_HUMANZZEF1physical
28514442
UBR5_HUMANUBR5physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615696Dowling-Degos disease 4 (DDD4)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PGLT1_HUMAN

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Related Literatures of Post-Translational Modification

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