PPID_HUMAN - dbPTM
PPID_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PPID_HUMAN
UniProt AC Q08752
Protein Name Peptidyl-prolyl cis-trans isomerase D {ECO:0000305}
Gene Name PPID {ECO:0000312|HGNC:HGNC:9257}
Organism Homo sapiens (Human).
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. [PubMed: 11350175]
Protein Sequence MSHPSPQAKPSNPSNPRVFFDVDIGGERVGRIVLELFADIVPKTAENFRALCTGEKGIGHTTGKPLHFKGCPFHRIIKKFMIQGGDFSNQNGTGGESIYGEKFEDENFHYKHDREGLLSMANAGRNTNGSQFFITTVPTPHLDGKHVVFGQVIKGIGVARILENVEVKGEKPAKLCVIAECGELKEGDDGGIFPKDGSGDSHPDFPEDADIDLKDVDKILLITEDLKNIGNTFFKSQNWEMAIKKYAEVLRYVDSSKAVIETADRAKLQPIALSCVLNIGACKLKMSNWQGAIDSCLEALELDPSNTKALYRRAQGWQGLKEYDQALADLKKAQGIAPEDKAIQAELLKVKQKIKAQKDKEKAVYAKMFA
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
2Phosphorylation------MSHPSPQAK
------CCCCCCCCC		44.0730619164
5Phosphorylation---MSHPSPQAKPSN
---CCCCCCCCCCCC		24.9928450419
9UbiquitinationSHPSPQAKPSNPSNP
CCCCCCCCCCCCCCC		43.67-
14PhosphorylationQAKPSNPSNPRVFFD
CCCCCCCCCCEEEEE		64.8123186163
43SumoylationLFADIVPKTAENFRA
HHHHHCHHHHHHHHH		49.85-
43UbiquitinationLFADIVPKTAENFRA
HHHHHCHHHHHHHHH		49.85-
43SumoylationLFADIVPKTAENFRA
HHHHHCHHHHHHHHH		49.85-
56AcetylationRALCTGEKGIGHTTG
HHHHCCCCCCCCCCC		58.1125953088
56UbiquitinationRALCTGEKGIGHTTG
HHHHCCCCCCCCCCC		58.11-
61PhosphorylationGEKGIGHTTGKPLHF
CCCCCCCCCCCCCCC		31.8428509920
62PhosphorylationEKGIGHTTGKPLHFK
CCCCCCCCCCCCCCC		37.2228509920
64AcetylationGIGHTTGKPLHFKGC
CCCCCCCCCCCCCCC		42.1726051181
64UbiquitinationGIGHTTGKPLHFKGC
CCCCCCCCCCCCCCC		42.17-
69UbiquitinationTGKPLHFKGCPFHRI
CCCCCCCCCCCHHHH		49.18-
79UbiquitinationPFHRIIKKFMIQGGD
CHHHHHHHHHEECCC		29.74-
102SumoylationGESIYGEKFEDENFH
CCCCCCCCCCCCCCC		50.09-
111UbiquitinationEDENFHYKHDREGLL
CCCCCCCCCCHHCHH		30.38-
130PhosphorylationAGRNTNGSQFFITTV
CCCCCCCCCEEEEEC		26.3625332170
154AcetylationVVFGQVIKGIGVARI
EEEEEEECCCCHHHH		45.6926051181
154UbiquitinationVVFGQVIKGIGVARI
EEEEEEECCCCHHHH		45.69-
168SumoylationILENVEVKGEKPAKL
HHHCEEECCCCCCEE		48.09-
168AcetylationILENVEVKGEKPAKL
HHHCEEECCCCCCEE		48.0926051181
168UbiquitinationILENVEVKGEKPAKL
HHHCEEECCCCCCEE		48.09-
168SumoylationILENVEVKGEKPAKL
HHHCEEECCCCCCEE		48.09-
171AcetylationNVEVKGEKPAKLCVI
CEEECCCCCCEEEEE		59.9726051181
174AcetylationVKGEKPAKLCVIAEC
ECCCCCCEEEEEEEC		51.4526051181
185AcetylationIAECGELKEGDDGGI
EEECCCCCCCCCCCC		56.1826051181
195UbiquitinationDDGGIFPKDGSGDSH
CCCCCCCCCCCCCCC		65.06-
198PhosphorylationGIFPKDGSGDSHPDF
CCCCCCCCCCCCCCC		49.9525159151
201PhosphorylationPKDGSGDSHPDFPED
CCCCCCCCCCCCCCC		40.2130266825
214UbiquitinationEDADIDLKDVDKILL
CCCCCCHHHHCEEEE		52.54-
2182-HydroxyisobutyrylationIDLKDVDKILLITED
CCHHHHCEEEEEEHH		34.79-
218UbiquitinationIDLKDVDKILLITED
CCHHHHCEEEEEEHH		34.7921890473
223PhosphorylationVDKILLITEDLKNIG
HCEEEEEEHHHHHHC		24.3420068231
227UbiquitinationLLITEDLKNIGNTFF
EEEEHHHHHHCHHHH		59.86-
232PhosphorylationDLKNIGNTFFKSQNW
HHHHHCHHHHHCCCH		25.8229978859
235MethylationNIGNTFFKSQNWEMA
HHCHHHHHCCCHHHH		47.11115975505
235UbiquitinationNIGNTFFKSQNWEMA
HHCHHHHHCCCHHHH		47.11-
236PhosphorylationIGNTFFKSQNWEMAI
HCHHHHHCCCHHHHH		24.4829978859
241SulfoxidationFKSQNWEMAIKKYAE
HHCCCHHHHHHHHHH		3.3630846556
244AcetylationQNWEMAIKKYAEVLR
CCHHHHHHHHHHHHH		30.1425953088
245AcetylationNWEMAIKKYAEVLRY
CHHHHHHHHHHHHHH		43.5125953088
245UbiquitinationNWEMAIKKYAEVLRY
CHHHHHHHHHHHHHH		43.51-
245MalonylationNWEMAIKKYAEVLRY
CHHHHHHHHHHHHHH		43.5126320211
246PhosphorylationWEMAIKKYAEVLRYV
HHHHHHHHHHHHHHH		11.73-
251MethylationKKYAEVLRYVDSSKA
HHHHHHHHHHCCCCH		34.31115488323
252PhosphorylationKYAEVLRYVDSSKAV
HHHHHHHHHCCCCHH		12.4019664994
257UbiquitinationLRYVDSSKAVIETAD
HHHHCCCCHHHHCCC		51.1021890473
257AcetylationLRYVDSSKAVIETAD
HHHHCCCCHHHHCCC		51.1023236377
2572-HydroxyisobutyrylationLRYVDSSKAVIETAD
HHHHCCCCHHHHCCC		51.10-
267UbiquitinationIETADRAKLQPIALS
HHCCCHHHCHHHHHH		48.85-
274PhosphorylationKLQPIALSCVLNIGA
HCHHHHHHHHEEECC		7.9927251275
275S-nitrosylationLQPIALSCVLNIGAC
CHHHHHHHHEEECCH		4.1419483679
275S-nitrosocysteineLQPIALSCVLNIGAC
CHHHHHHHHEEECCH		4.14-
282S-nitrosocysteineCVLNIGACKLKMSNW
HHEEECCHHCCCCCH		4.47-
282S-nitrosylationCVLNIGACKLKMSNW
HHEEECCHHCCCCCH		4.4719483679
283UbiquitinationVLNIGACKLKMSNWQ
HEEECCHHCCCCCHH		51.08-
283AcetylationVLNIGACKLKMSNWQ
HEEECCHHCCCCCHH		51.0825953088
285UbiquitinationNIGACKLKMSNWQGA
EECCHHCCCCCHHHH		26.27-
287PhosphorylationGACKLKMSNWQGAID
CCHHCCCCCHHHHHH		33.0718452278
296GlutathionylationWQGAIDSCLEALELD
HHHHHHHHHHHHHCC		3.3622555962
308UbiquitinationELDPSNTKALYRRAQ
HCCCCCHHHHHHHHH		40.42-
321UbiquitinationAQGWQGLKEYDQALA
HHHCHHHHHHHHHHH		62.14-
323PhosphorylationGWQGLKEYDQALADL
HCHHHHHHHHHHHHH		16.2727642862
331MalonylationDQALADLKKAQGIAP
HHHHHHHHHHCCCCC		46.7630639696
331UbiquitinationDQALADLKKAQGIAP
HHHHHHHHHHCCCCC		46.7621906983
341SumoylationQGIAPEDKAIQAELL
CCCCCCCHHHHHHHH		45.81-
341UbiquitinationQGIAPEDKAIQAELL
CCCCCCCHHHHHHHH		45.8121890473
341SumoylationQGIAPEDKAIQAELL
CCCCCCCHHHHHHHH		45.81-
349UbiquitinationAIQAELLKVKQKIKA
HHHHHHHHHHHHHHH		61.07-
365PhosphorylationKDKEKAVYAKMFA--
HHHHHHHHHHHCC--		12.8320736484
367UbiquitinationKEKAVYAKMFA----
HHHHHHHHHCC----		19.50-
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PPID_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 PPID_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HSP7C_HUMANHSPA8physical
15497503
HS90B_HUMANHSP90AB1physical
15497503
HAP1_HUMANHAP1physical
16169070
KAT7_HUMANKAT7physical
16169070
A4_HUMANAPPphysical
21832049
RACK1_HUMANGNB2L1physical
21146485
RS3_HUMANRPS3physical
21146485
HS90A_HUMANHSP90AA1physical
21146485
HS90B_HUMANHSP90AB1physical
21146485
XRCC6_HUMANXRCC6physical
21146485
ILF2_HUMANILF2physical
21146485
TBA1A_HUMANTUBA1Aphysical
21146485
TBB5_HUMANTUBBphysical
21146485
S10A2_HUMANS100A2physical
20188096
S10A6_HUMANS100A6physical
20188096
S10A1_HUMANS100A1physical
20188096
HS90A_HUMANHSP90AA1physical
20188096
HPRT_HUMANHPRT1physical
22863883
SERC_HUMANPSAT1physical
22863883
GPAM1_HUMANGPALPP1physical
25036637
AHSA1_HUMANAHSA1physical
25036637
CDC37_HUMANCDC37physical
25036637
TEBP_HUMANPTGES3physical
25036637
TRI27_HUMANTRIM27physical
25416956
HS90A_HUMANHSP90AA1physical
10642522
KPYM_HUMANPKMphysical
26344197
PSD12_HUMANPSMD12physical
26344197
SF01_HUMANSF1physical
26344197
DCUP_HUMANURODphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PPID_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198, AND MASSSPECTROMETRY.

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