PPIB_MOUSE - dbPTM
PPIB_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PPIB_MOUSE
UniProt AC P24369
Protein Name Peptidyl-prolyl cis-trans isomerase B
Gene Name Ppib
Organism Mus musculus (Mouse).
Sequence Length 216
Subcellular Localization Endoplasmic reticulum lumen . Melanosome .
Protein Description PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding..
Protein Sequence MLRLSERNMKVLFAAALIVGSVVFLLLPGPSVANDKKKGPKVTVKVYFDLQIGDESVGRVVFGLFGKTVPKTVDNFVALATGEKGFGYKNSKFHRVIKDFMIQGGDFTRGDGTGGKSIYGERFPDENFKLKHYGPGWVSMANAGKDTNGSQFFITTVKTSWLDGKHVVFGKVLEGMDVVRKVESTKTDSRDKPLKDVIIVDSGKIEVEKPFAIAKE
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
67AcetylationVVFGLFGKTVPKTVD
EEEEECCCCCCCCHH
38.7323806337
67SuccinylationVVFGLFGKTVPKTVD
EEEEECCCCCCCCHH
38.7323806337
71AcetylationLFGKTVPKTVDNFVA
ECCCCCCCCHHCEEH
57.7722826441
84SuccinylationVALATGEKGFGYKNS
EHHHCCCCCCCCCCC
61.9722790023
84UbiquitinationVALATGEKGFGYKNS
EHHHCCCCCCCCCCC
61.97-
84AcetylationVALATGEKGFGYKNS
EHHHCCCCCCCCCCC
61.9722826441
89SuccinylationGEKGFGYKNSKFHRV
CCCCCCCCCCCHHHH
55.9423954790
89AcetylationGEKGFGYKNSKFHRV
CCCCCCCCCCCHHHH
55.946568837
98SuccinylationSKFHRVIKDFMIQGG
CCHHHHEECCEEECC
41.9023954790
98AcetylationSKFHRVIKDFMIQGG
CCHHHHEECCEEECC
41.9022826441
108PhosphorylationMIQGGDFTRGDGTGG
EEECCCCCCCCCCCC
38.1822817900
116AcetylationRGDGTGGKSIYGERF
CCCCCCCCCCCCCCC
34.7223806337
116SuccinylationRGDGTGGKSIYGERF
CCCCCCCCCCCCCCC
34.7223806337
129AcetylationRFPDENFKLKHYGPG
CCCCCCCCCCEECCC
69.1123864654
131AcetylationPDENFKLKHYGPGWV
CCCCCCCCEECCCEE
35.0622826441
158SuccinylationQFFITTVKTSWLDGK
EEEEEEEEEEECCCC
34.4523954790
165AcetylationKTSWLDGKHVVFGKV
EEEECCCCCEEEEEE
32.6623806337
165SuccinylationKTSWLDGKHVVFGKV
EEEECCCCCEEEEEE
32.6623806337
165UbiquitinationKTSWLDGKHVVFGKV
EEEECCCCCEEEEEE
32.66-
171AcetylationGKHVVFGKVLEGMDV
CCCEEEEEEEECCHH
31.9822826441
186AcetylationVRKVESTKTDSRDKP
EEEEECCCCCCCCCC
60.6623864654
187PhosphorylationRKVESTKTDSRDKPL
EEEECCCCCCCCCCC
39.02-
192AcetylationTKTDSRDKPLKDVII
CCCCCCCCCCCEEEE
51.6523806337
192SuccinylationTKTDSRDKPLKDVII
CCCCCCCCCCCEEEE
51.6523806337
209SuccinylationSGKIEVEKPFAIAKE
CCCEEEECCEEEECC
51.0823806337
209UbiquitinationSGKIEVEKPFAIAKE
CCCEEEECCEEEECC
51.08-
209SuccinylationSGKIEVEKPFAIAKE
CCCEEEECCEEEECC
51.08-
209AcetylationSGKIEVEKPFAIAKE
CCCEEEECCEEEECC
51.0823806337
215AcetylationEKPFAIAKE------
ECCEEEECC------
58.8223864654
215SuccinylationEKPFAIAKE------
ECCEEEECC------
58.8223954790

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 PPIB_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PPIB_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 PPIB_MOUSE !!

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

Oops, there are no PPI records of PPIB_MOUSE !!

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

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Related Literatures of Post-Translational Modification

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