PDIA6_MOUSE - dbPTM
PDIA6_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PDIA6_MOUSE
UniProt AC Q922R8
Protein Name Protein disulfide-isomerase A6
Gene Name Pdia6
Organism Mus musculus (Mouse).
Sequence Length 440
Subcellular Localization Endoplasmic reticulum lumen . Cell membrane . Melanosome .
Protein Description May function as a chaperone that inhibits aggregation of misfolded proteins. [PubMed: 24508390 Negatively regulates the unfolded protein response (UPR) through binding to UPR sensors such as ERN1, which in turn inactivates ERN1 signaling (By similarity May also regulate the UPR via the EIF2AK3 UPR sensor (By similarity Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin (By similarity]
Protein Sequence MARLVLGLVSCTFFLAVSGLYSSSDDVIELTPSNFNREVIQSDGLWLVEFYAPWCGHCQRLTPEWKKAATALKDVVKVGAVNADKHQSLGGQYGVQGFPTIKIFGANKNKPEDYQGGRTGEAIVDAALSALRQLVKDRLGGRSGGYSSGKQGRGDSSSKKDVVELTDDTFDKNVLDSEDVWMVEFYAPWCGHCKNLEPEWAAAATEVKEQTKGKVKLAAVDATVNQVLASRYGIKGFPTIKIFQKGESPVDYDGGRTRSDIVSRALDLFSDNAPPPELLEIINEDIAKKTCEEHQLCVVAVLPHILDTGAAGRNSYLEVLLKLADKYKKKMWGWLWTEAGAQYELENALGIGGFGYPAMAAINARKMKFALLKGSFSEQGINEFLRELSFGRGSTAPVGGGSFPTITPREPWDGKDGELPVEDDIDLSDVELDDLEKDEL
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
70PhosphorylationPEWKKAATALKDVVK
HHHHHHHHHHHHHHH
37.0618779572
77UbiquitinationTALKDVVKVGAVNAD
HHHHHHHHCCCCCCC
34.50-
85UbiquitinationVGAVNADKHQSLGGQ
CCCCCCCCCHHHCCC
40.93-
88PhosphorylationVNADKHQSLGGQYGV
CCCCCCHHHCCCCCC
28.8026824392
129PhosphorylationAIVDAALSALRQLVK
HHHHHHHHHHHHHHH
22.1127180971
143PhosphorylationKDRLGGRSGGYSSGK
HHHHCCCCCCCCCCC
39.5825195567
146PhosphorylationLGGRSGGYSSGKQGR
HCCCCCCCCCCCCCC
11.8225195567
147PhosphorylationGGRSGGYSSGKQGRG
CCCCCCCCCCCCCCC
35.5725195567
148PhosphorylationGRSGGYSSGKQGRGD
CCCCCCCCCCCCCCC
41.3425195567
150AcetylationSGGYSSGKQGRGDSS
CCCCCCCCCCCCCCC
52.077970497
156PhosphorylationGKQGRGDSSSKKDVV
CCCCCCCCCCCCCEE
39.06-
158PhosphorylationQGRGDSSSKKDVVEL
CCCCCCCCCCCEEEC
47.91-
166PhosphorylationKKDVVELTDDTFDKN
CCCEEECCCCCCCCC
20.5126525534
169PhosphorylationVVELTDDTFDKNVLD
EEECCCCCCCCCCCC
36.2226525534
230PhosphorylationTVNQVLASRYGIKGF
HHHHHHHHHHCCCCC
23.13-
248PhosphorylationKIFQKGESPVDYDGG
EEEECCCCCCCCCCC
38.60-
257PhosphorylationVDYDGGRTRSDIVSR
CCCCCCCCHHHHHHH
37.4919854140
259PhosphorylationYDGGRTRSDIVSRAL
CCCCCCHHHHHHHHH
30.9519854140
373UbiquitinationKMKFALLKGSFSEQG
HHCEEHHHCCCCHHH
54.05-
375PhosphorylationKFALLKGSFSEQGIN
CEEHHHCCCCHHHHH
24.8227742792
377PhosphorylationALLKGSFSEQGINEF
EHHHCCCCHHHHHHH
30.6127742792
394PhosphorylationELSFGRGSTAPVGGG
HHHCCCCCCCCCCCC
21.7528464351
428PhosphorylationVEDDIDLSDVELDDL
CCCCCCHHHCCHHHH
35.5424925903

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 PDIA6_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PDIA6_MOUSE !!

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 PDIA6_MOUSE !!

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

Oops, there are no PPI records of PDIA6_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PDIA6_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, AND MASSSPECTROMETRY.

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