DPM3_HUMAN - dbPTM
DPM3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DPM3_HUMAN
UniProt AC Q9P2X0
Protein Name Dolichol-phosphate mannosyltransferase subunit 3
Gene Name DPM3
Organism Homo sapiens (Human).
Sequence Length 92
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein.
Protein Description Stabilizer subunit of the dolichol-phosphate mannose (DPM) synthase complex; tethers catalytic subunit DPM1 to the ER..
Protein Sequence MTKLAQWLWGLAILGSTWVALTTGALGLELPLSCQEVLWPLPAYLLVSAGCYALGTVGYRVATFHDCEDAARELQSQIQEARADLARRGLRF
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
63O-linked_GlycosylationTVGYRVATFHDCEDA
CCCEEEEECCCHHHH
20.74310709277
63PhosphorylationTVGYRVATFHDCEDA
CCCEEEEECCCHHHH
20.74-

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 DPM3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DPM3_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 DPM3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DPM1_HUMANDPM1physical
16280320

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DPM3_HUMAN

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Related Literatures of Post-Translational Modification

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