DOPP1_HUMAN - dbPTM
DOPP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DOPP1_HUMAN
UniProt AC Q86YN1
Protein Name Dolichyldiphosphatase 1
Gene Name DOLPP1
Organism Homo sapiens (Human).
Sequence Length 238
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein.
Protein Description Required for efficient N-glycosylation. Necessary for maintaining optimal levels of dolichol-linked oligosaccharides. Hydrolyzes dolichyl pyrophosphate at a very high rate and dolichyl monophosphate at a much lower rate. Does not act on phosphatidate (By similarity)..
Protein Sequence MAADGQCSLPASWRPVTLTHVEYPAGDLSGHLLAYLSLSPVFVIVGFVTLIIFKRELHTISFLGGLALNEGVNWLIKNVIQEPRPCGGPHTAVGTKYGMPSSHSQFMWFFSVYSFLFLYLRMHQTNNARFLDLLWRHVLSLGLLAVAFLVSYSRVYLLYHTWSQVLYGGIAGGLMAIAWFIFTQEVLTPLFPRIAAWPVSEFFLIRDTSLIPNVLWFEYTVTRAEARNRQRKLGTKLQ
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
235PhosphorylationNRQRKLGTKLQ----
HHHHHHCCCCC----
38.7329496963

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 DOPP1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DOPP1_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 DOPP1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HPHL1_HUMANHEPHL1physical
26186194
SBP1_HUMANSELENBP1physical
26186194
LYG2_HUMANLYG2physical
26186194
ASSY_HUMANASS1physical
26186194
LRC15_HUMANLRRC15physical
26186194
PKP3_HUMANPKP3physical
26186194
SBP1_HUMANSELENBP1physical
28514442
HPHL1_HUMANHEPHL1physical
28514442
LRC15_HUMANLRRC15physical
28514442
LYG2_HUMANLYG2physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DOPP1_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP