PPID_MOUSE - dbPTM
PPID_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PPID_MOUSE
UniProt AC Q9CR16
Protein Name Peptidyl-prolyl cis-trans isomerase D {ECO:0000305}
Gene Name Ppid {ECO:0000312|MGI:MGI:1914988}
Organism Mus musculus (Mouse).
Sequence Length 370
Subcellular Localization Cytoplasm . Nucleus, nucleolus . Nucleus, nucleoplasm .
Protein Description PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. Proposed to act as a co-chaperone in HSP90 complexes such as in unligated steroid receptors heterocomplexes. Different co-chaperones seem to compete for association with HSP90 thus establishing distinct HSP90-co-chaperone-receptor complexes with the potential to exert tissue-specific receptor activity control. May have a preference for estrogen receptor complexes and is not found in glucocorticoid receptor complexes. May be involved in cytoplasmic dynein-dependent movement of the receptor from the cytoplasm to the nucleus. May regulate MYB by inhibiting its DNA-binding activity. Involved in regulation of AHR signaling by promoting the formation of the AHR:ARNT dimer; the function is independent of HSP90 but requires the chaperone activity region. Involved in regulation of UV radiation-induced apoptosis..
Protein Sequence MSHASPAAKPSNSKNPRVFFDVDIGGERVGRIVLELFADIVPKTAENFRALCTGEKGTGSTTGKPLHFKGCPFHRIIKKFMIQGGDFSNQNGTGGESIYGEKFEDENFHYKHDREGLLSMANAGPNTNGSQFFITTVPTPHLDGKHVVFGQVIKGLGVARTLENVEVNGEKPAKLCVIAECGELKEGDDWGIFPKDGSGDSHPDFPEDADIDLKDVDKILLISEDLKNIGNTFFKSQNWEMAIKKYAKVLRYVDSSKAVIEKADRSRLQPIALSCVLNIGACKLKMSNWQGAIDSCLEALEMDPSNTKALYRKAQGWQGLKEYDQALADLKKAQEIAPGDKAIQAELLKVKQMIKAQKDKEKAVYAKMFA
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
5Phosphorylation---MSHASPAAKPSN
---CCCCCCCCCCCC		15.0625263469
9UbiquitinationSHASPAAKPSNSKNP
CCCCCCCCCCCCCCC		51.6022790023
14UbiquitinationAAKPSNSKNPRVFFD
CCCCCCCCCCCEEEE		75.1922790023
43AcetylationLFADIVPKTAENFRA
HHHHHCHHHHHHHHH		49.85-
64AcetylationGTGSTTGKPLHFKGC
CCCCCCCCCCCCCCC		42.1722826441
145AcetylationPTPHLDGKHVVFGQV
CCCCCCCCCEEEEEE		32.6620159966
154AcetylationVVFGQVIKGLGVART
EEEEEEEHHCCCEEE		49.5822826441
168UbiquitinationTLENVEVNGEKPAKL
EEECEEECCCCCCEE		39.1327667366
171AcetylationNVEVNGEKPAKLCVI
CEEECCCCCCEEEEE		52.2323806337
198PhosphorylationGIFPKDGSGDSHPDF
CCCCCCCCCCCCCCC		49.9528066266
201PhosphorylationPKDGSGDSHPDFPED
CCCCCCCCCCCCCCC		40.2128066266
218UbiquitinationIDLKDVDKILLISED
CCHHHHCEEEEEEHH		34.7922790023
227MalonylationLLISEDLKNIGNTFF
EEEEHHHHCCCHHHH		59.8626073543
227UbiquitinationLLISEDLKNIGNTFF
EEEEHHHHCCCHHHH		59.86-
227AcetylationLLISEDLKNIGNTFF
EEEEHHHHCCCHHHH		59.8622826441
247UbiquitinationEMAIKKYAKVLRYVD
HHHHHHHHHHHHHHC		12.3627667366
257MalonylationLRYVDSSKAVIEKAD
HHHHCCCHHHHHHHH		51.1026320211
257AcetylationLRYVDSSKAVIEKAD
HHHHCCCHHHHHHHH		51.102416087
262MalonylationSSKAVIEKADRSRLQ
CCHHHHHHHHHHCCH		44.4526320211
262UbiquitinationSSKAVIEKADRSRLQ
CCHHHHHHHHHHCCH		44.4527667366
262AcetylationSSKAVIEKADRSRLQ
CCHHHHHHHHHHCCH		44.452416095
274PhosphorylationRLQPIALSCVLNIGA
CCHHHHHHHHHHHCC		7.9924719451
283UbiquitinationVLNIGACKLKMSNWQ
HHHHCCCCCCCCCHH		51.0822790023
285UbiquitinationNIGACKLKMSNWQGA
HHCCCCCCCCCHHHH		26.27-
287PhosphorylationGACKLKMSNWQGAID
CCCCCCCCCHHHHHH		33.0728059163
311PhosphorylationPSNTKALYRKAQGWQ
CCHHHHHHHHHHCCH		18.2228059163
313UbiquitinationNTKALYRKAQGWQGL
HHHHHHHHHHCCHHH		31.3522790023
331AcetylationDQALADLKKAQEIAP
HHHHHHHHHHHHHCC		46.7623236377
331SuccinylationDQALADLKKAQEIAP
HHHHHHHHHHHHHCC		46.7623954790
341UbiquitinationQEIAPGDKAIQAELL
HHHCCCCHHHHHHHH		53.9922790023
341AcetylationQEIAPGDKAIQAELL
HHHCCCCHHHHHHHH		53.9923236377
349AcetylationAIQAELLKVKQMIKA
HHHHHHHHHHHHHHH		61.0722826441
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 PPID_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PPID_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 PPID_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PPID_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PPID_MOUSE

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Related Literatures of Post-Translational Modification

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