PPIG_HUMAN - dbPTM
PPIG_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PPIG_HUMAN
UniProt AC Q13427
Protein Name Peptidyl-prolyl cis-trans isomerase G
Gene Name PPIG
Organism Homo sapiens (Human).
Sequence Length 754
Subcellular Localization Nucleus matrix . Nucleus speckle . Colocalizes with RNA splicing factors at nuclear speckles.
Protein Description PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. [PubMed: 20676357 May be implicated in the folding, transport, and assembly of proteins. May play an important role in the regulation of pre-mRNA splicing.]
Protein Sequence MGIKVQRPRCFFDIAINNQPAGRVVFELFSDVCPKTCENFRCLCTGEKGTGKSTQKPLHYKSCLFHRVVKDFMVQGGDFSEGNGRGGESIYGGFFEDESFAVKHNKEFLLSMANRGKDTNGSQFFITTKPTPHLDGHHVVFGQVISGQEVVREIENQKTDAASKPFAEVRILSCGELIPKSKVKKEEKKRHKSSSSSSSSSSDSDSSSDSQSSSDSSDSESATEEKSKKRKKKHRKNSRKHKKEKKKRKKSKKSASSESEAENLEAQPQSTVRPEEIPPIPENRFLMRKSPPKADEKERKNRERERERECNPPNSQPASYQRRLLVTRSGRKIKGRGPRRYRTPSRSRSRDRFRRSETPPHWRQEMQRAQRMRVSSGERWIKGDKSELNEIKENQRSPVRVKERKITDHRNVSESPNRKNEKEKKVKDHKSNSKERDIRRNSEKDDKYKNKVKKRAKSKSRSKSKEKSKSKERDSKHNRNEEKRMRSRSKGRDHENVKEKEKQSDSKGKDQERSRSKEKSKQLESKSNEHDHSKSKEKDRRAQSRSRECDITKGKHSYNSRTRERSRSRDRSRRVRSRTHDRDRSRSKEYHRYREQEYRRRGRSRSRERRTPPGRSRSKDRRRRRRDSRSSEREESQSRNKDKYRNQESKSSHRKENSESEKRMYSKSRDHNSSNNSREKKADRDQSPFSKIKQSSQDNELKSSMLKNKEDEKIRSSVEKENQKSKGQENDHVHEKNKKFDHESSPGTDEDKSG
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
10GlutathionylationIKVQRPRCFFDIAIN
CCCCCCCEEEEEEEC
4.4022555962
33GlutathionylationFELFSDVCPKTCENF
HHHHCCCCCHHCCCC
3.2522555962
35AcetylationLFSDVCPKTCENFRC
HHCCCCCHHCCCCEE
61.7626051181
48AcetylationRCLCTGEKGTGKSTQ
EEEEECCCCCCCCCC
64.2226051181
70AcetylationCLFHRVVKDFMVQGG
HHHHHHHHHHEEECC
42.2526051181
158AcetylationVREIENQKTDAASKP
HHHHHHCCCCCCCCC
61.0125953088
158UbiquitinationVREIENQKTDAASKP
HHHHHHCCCCCCCCC
61.0132015554
159PhosphorylationREIENQKTDAASKPF
HHHHHCCCCCCCCCC
22.5521406692
163O-linked_GlycosylationNQKTDAASKPFAEVR
HCCCCCCCCCCCEEE
42.4530379171
163PhosphorylationNQKTDAASKPFAEVR
HCCCCCCCCCCCEEE
42.4521406692
1642-HydroxyisobutyrylationQKTDAASKPFAEVRI
CCCCCCCCCCCEEEE
39.15-
164AcetylationQKTDAASKPFAEVRI
CCCCCCCCCCCEEEE
39.1526051181
173PhosphorylationFAEVRILSCGELIPK
CCEEEEEECCCCCCH
20.0825159151
174GlutathionylationAEVRILSCGELIPKS
CEEEEEECCCCCCHH
4.3822555962
182UbiquitinationGELIPKSKVKKEEKK
CCCCCHHHCCHHHHH
65.29-
193PhosphorylationEEKKRHKSSSSSSSS
HHHHHCCCCCCCCCC
29.36-
195PhosphorylationKKRHKSSSSSSSSSS
HHHCCCCCCCCCCCC
41.13-
196PhosphorylationKRHKSSSSSSSSSSD
HHCCCCCCCCCCCCC
35.87-
197PhosphorylationRHKSSSSSSSSSSDS
HCCCCCCCCCCCCCC
35.87-
198PhosphorylationHKSSSSSSSSSSDSD
CCCCCCCCCCCCCCC
35.87-
199PhosphorylationKSSSSSSSSSSDSDS
CCCCCCCCCCCCCCC
35.87-
200PhosphorylationSSSSSSSSSSDSDSS
CCCCCCCCCCCCCCC
35.49-
201PhosphorylationSSSSSSSSSDSDSSS
CCCCCCCCCCCCCCC
39.86-
202PhosphorylationSSSSSSSSDSDSSSD
CCCCCCCCCCCCCCC
42.98-
204PhosphorylationSSSSSSDSDSSSDSQ
CCCCCCCCCCCCCCC
41.14-
206PhosphorylationSSSSDSDSSSDSQSS
CCCCCCCCCCCCCCC
35.38-
207PhosphorylationSSSDSDSSSDSQSSS
CCCCCCCCCCCCCCC
43.06-
208PhosphorylationSSDSDSSSDSQSSSD
CCCCCCCCCCCCCCC
45.28-
212PhosphorylationDSSSDSQSSSDSSDS
CCCCCCCCCCCCCCC
35.4430576142
213PhosphorylationSSSDSQSSSDSSDSE
CCCCCCCCCCCCCCH
30.4428985074
214PhosphorylationSSDSQSSSDSSDSES
CCCCCCCCCCCCCHH
46.92-
216PhosphorylationDSQSSSDSSDSESAT
CCCCCCCCCCCHHHH
37.6828985074
217PhosphorylationSQSSSDSSDSESATE
CCCCCCCCCCHHHHH
50.58-
219PhosphorylationSSSDSSDSESATEEK
CCCCCCCCHHHHHHH
35.08-
221PhosphorylationSDSSDSESATEEKSK
CCCCCCHHHHHHHHH
44.4330576142
223PhosphorylationSSDSESATEEKSKKR
CCCCHHHHHHHHHHH
54.69-
251PhosphorylationEKKKRKKSKKSASSE
HHHHHHHHHHCCCCH
48.6429116813
254PhosphorylationKRKKSKKSASSESEA
HHHHHHHCCCCHHHH
36.8026503892
256PhosphorylationKKSKKSASSESEAEN
HHHHHCCCCHHHHHH
41.5526503892
257PhosphorylationKSKKSASSESEAENL
HHHHCCCCHHHHHHH
44.8726503892
259PhosphorylationKKSASSESEAENLEA
HHCCCCHHHHHHHHC
44.0129255136
270PhosphorylationNLEAQPQSTVRPEEI
HHHCCCCCCCCHHHC
35.2428450419
271PhosphorylationLEAQPQSTVRPEEIP
HHCCCCCCCCHHHCC
18.4528450419
290PhosphorylationNRFLMRKSPPKADEK
CCCCCCCCCCCCCHH
35.7530266825
315PhosphorylationRECNPPNSQPASYQR
HHCCCCCCCCCHHHH
43.2317525332
319PhosphorylationPPNSQPASYQRRLLV
CCCCCCCHHHHHEEE
28.6028674419
320PhosphorylationPNSQPASYQRRLLVT
CCCCCCHHHHHEEEE
14.24-
329PhosphorylationRRLLVTRSGRKIKGR
HHEEEECCCCCCCCC
33.3224732914
341PhosphorylationKGRGPRRYRTPSRSR
CCCCCCCCCCCCCCC
21.8130242111
343PhosphorylationRGPRRYRTPSRSRSR
CCCCCCCCCCCCCCH
19.3830242111
345PhosphorylationPRRYRTPSRSRSRDR
CCCCCCCCCCCCHHH
42.1330242111
347PhosphorylationRYRTPSRSRSRDRFR
CCCCCCCCCCHHHHH
38.6620068231
349PhosphorylationRTPSRSRSRDRFRRS
CCCCCCCCHHHHHCC
39.5220068231
356PhosphorylationSRDRFRRSETPPHWR
CHHHHHCCCCCHHHH
41.3818388127
358PhosphorylationDRFRRSETPPHWRQE
HHHHCCCCCHHHHHH
43.2818388127
375PhosphorylationRAQRMRVSSGERWIK
HHHHHHCCCCCHHHC
23.4330266825
376PhosphorylationAQRMRVSSGERWIKG
HHHHHCCCCCHHHCC
41.6430266825
386PhosphorylationRWIKGDKSELNEIKE
HHHCCCHHHHHHHHH
52.6423927012
392SumoylationKSELNEIKENQRSPV
HHHHHHHHHHCCCCC
44.4228112733
392UbiquitinationKSELNEIKENQRSPV
HHHHHHHHHHCCCCC
44.4232015554
397PhosphorylationEIKENQRSPVRVKER
HHHHHCCCCCCCCEE
20.2722167270
407PhosphorylationRVKERKITDHRNVSE
CCCEECCCCCCCCCC
28.8723403867
413PhosphorylationITDHRNVSESPNRKN
CCCCCCCCCCCCCCC
35.5929255136
415PhosphorylationDHRNVSESPNRKNEK
CCCCCCCCCCCCCHH
21.7029255136
431PhosphorylationKKVKDHKSNSKERDI
HHHHHHHCCHHHHHH
42.8030576142
433PhosphorylationVKDHKSNSKERDIRR
HHHHHCCHHHHHHHH
42.8827422710
442PhosphorylationERDIRRNSEKDDKYK
HHHHHHHHHHHHHHH
44.1824719451
447AcetylationRNSEKDDKYKNKVKK
HHHHHHHHHHHHHHH
69.167491897
449AcetylationSEKDDKYKNKVKKRA
HHHHHHHHHHHHHHH
56.917491909
458PhosphorylationKVKKRAKSKSRSKSK
HHHHHHHHHHHHHHH
34.5726074081
459UbiquitinationVKKRAKSKSRSKSKE
HHHHHHHHHHHHHHH
49.54-
460PhosphorylationKKRAKSKSRSKSKEK
HHHHHHHHHHHHHHH
49.2126074081
462PhosphorylationRAKSKSRSKSKEKSK
HHHHHHHHHHHHHHH
48.6626074081
463UbiquitinationAKSKSRSKSKEKSKS
HHHHHHHHHHHHHHH
65.52-
464PhosphorylationKSKSRSKSKEKSKSK
HHHHHHHHHHHHHHH
47.4926074081
468PhosphorylationRSKSKEKSKSKERDS
HHHHHHHHHHHHHHH
43.1626074081
487PhosphorylationNEEKRMRSRSKGRDH
HHHHHHHHHHCCCCH
31.4026074081
489PhosphorylationEKRMRSRSKGRDHEN
HHHHHHHHCCCCHHH
40.4825849741
509UbiquitinationKQSDSKGKDQERSRS
HHHCCCCHHHHHHHH
61.0324816145
525O-linked_GlycosylationEKSKQLESKSNEHDH
HHHHHHHHHCCCCCC
50.4030379171
525PhosphorylationEKSKQLESKSNEHDH
HHHHHHHHHCCCCCC
50.4024719451
527PhosphorylationSKQLESKSNEHDHSK
HHHHHHHCCCCCCHH
57.6520068231
533PhosphorylationKSNEHDHSKSKEKDR
HCCCCCCHHHHHHHH
44.6929743597
535PhosphorylationNEHDHSKSKEKDRRA
CCCCCHHHHHHHHHH
49.4123312004
544PhosphorylationEKDRRAQSRSRECDI
HHHHHHHHHHCCCCC
31.1023401153
546PhosphorylationDRRAQSRSRECDITK
HHHHHHHHCCCCCCC
37.3623401153
552PhosphorylationRSRECDITKGKHSYN
HHCCCCCCCCCCCCC
22.0926552605
557PhosphorylationDITKGKHSYNSRTRE
CCCCCCCCCCCHHHH
29.5124719451
558PhosphorylationITKGKHSYNSRTRER
CCCCCCCCCCHHHHH
19.5124719451
560PhosphorylationKGKHSYNSRTRERSR
CCCCCCCCHHHHHHH
27.1330576142
562PhosphorylationKHSYNSRTRERSRSR
CCCCCCHHHHHHHHH
36.3830576142
566PhosphorylationNSRTRERSRSRDRSR
CCHHHHHHHHHHHHH
29.8320068231
568PhosphorylationRTRERSRSRDRSRRV
HHHHHHHHHHHHHHH
39.5220068231
572PhosphorylationRSRSRDRSRRVRSRT
HHHHHHHHHHHHHHC
28.8220068231
585PhosphorylationRTHDRDRSRSKEYHR
HCCCCCHHHHHHHHH
45.2425849741
587PhosphorylationHDRDRSRSKEYHRYR
CCCCHHHHHHHHHHH
30.9625849741
590PhosphorylationDRSRSKEYHRYREQE
CHHHHHHHHHHHHHH
8.7124144214
598PhosphorylationHRYREQEYRRRGRSR
HHHHHHHHHHHCCCC
14.7630242111
604PhosphorylationEYRRRGRSRSRERRT
HHHHHCCCCCCCCCC
37.1120068231
606PhosphorylationRRRGRSRSRERRTPP
HHHCCCCCCCCCCCC
39.4820068231
611PhosphorylationSRSRERRTPPGRSRS
CCCCCCCCCCCCCCH
39.8028355574
616PhosphorylationRRTPPGRSRSKDRRR
CCCCCCCCCHHHHHH
46.9828348404
618PhosphorylationTPPGRSRSKDRRRRR
CCCCCCCHHHHHHHH
39.9120068231
628PhosphorylationRRRRRRDSRSSEREE
HHHHHHHHHHHHHHH
32.0527794612
630PhosphorylationRRRRDSRSSEREESQ
HHHHHHHHHHHHHHH
40.2725849741
631PhosphorylationRRRDSRSSEREESQS
HHHHHHHHHHHHHHH
39.2925849741
636PhosphorylationRSSEREESQSRNKDK
HHHHHHHHHHHHHHH
28.8027794612
638PhosphorylationSEREESQSRNKDKYR
HHHHHHHHHHHHHHH
47.2924144214
649PhosphorylationDKYRNQESKSSHRKE
HHHHCHHHHHHHHHH
28.2430576142
658O-linked_GlycosylationSSHRKENSESEKRMY
HHHHHHCCHHHHHHH
43.5230379171
658PhosphorylationSSHRKENSESEKRMY
HHHHHHCCHHHHHHH
43.5224275748
660PhosphorylationHRKENSESEKRMYSK
HHHHCCHHHHHHHHH
48.5229052541
666PhosphorylationESEKRMYSKSRDHNS
HHHHHHHHHHCCCCC
18.1424719451
673PhosphorylationSKSRDHNSSNNSREK
HHHCCCCCCCCHHHH
30.90-
674PhosphorylationKSRDHNSSNNSREKK
HHCCCCCCCCHHHHH
45.40-
677PhosphorylationDHNSSNNSREKKADR
CCCCCCCHHHHHCCC
46.17-
687PhosphorylationKKADRDQSPFSKIKQ
HHCCCCCCHHHHHHH
32.0029255136
690PhosphorylationDRDQSPFSKIKQSSQ
CCCCCHHHHHHHHHH
36.5322167270
693SumoylationQSPFSKIKQSSQDNE
CCHHHHHHHHHHCHH
48.1128112733
695PhosphorylationPFSKIKQSSQDNELK
HHHHHHHHHHCHHHH
25.6029255136
696PhosphorylationFSKIKQSSQDNELKS
HHHHHHHHHCHHHHH
38.7723401153
703PhosphorylationSQDNELKSSMLKNKE
HHCHHHHHHHHCCHH
33.3428555341
716PhosphorylationKEDEKIRSSVEKENQ
HHHHHHHHHHHHHHH
42.0622167270
717PhosphorylationEDEKIRSSVEKENQK
HHHHHHHHHHHHHHH
25.1722167270
720AcetylationKIRSSVEKENQKSKG
HHHHHHHHHHHHCCC
60.8620167786
724AcetylationSVEKENQKSKGQEND
HHHHHHHHCCCCCCH
66.7620167786
725PhosphorylationVEKENQKSKGQENDH
HHHHHHHCCCCCCHH
32.0526074081
744PhosphorylationNKKFDHESSPGTDED
CCCCCCCCCCCCCCC
38.1129255136
745PhosphorylationKKFDHESSPGTDEDK
CCCCCCCCCCCCCCC
25.1029255136
748PhosphorylationDHESSPGTDEDKSG-
CCCCCCCCCCCCCC-
39.3329255136
753PhosphorylationPGTDEDKSG------
CCCCCCCCC------
63.1623927012

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 PPIG_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PPIG_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 PPIG_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PININ_HUMANPNNphysical
15358154
RPB1_MOUSEPolr2aphysical
9153302
PR40A_HUMANPRPF40Aphysical
22365833
PR38A_HUMANPRPF38Aphysical
22365833
SLU7_HUMANSLU7physical
22365833
PCBP1_HUMANPCBP1physical
22365833
NKAP_HUMANNKAPphysical
22365833
ZCH10_HUMANZCCHC10physical
22365833
RBM39_HUMANRBM39physical
25416956
PNMA2_HUMANPNMA2physical
25416956
THAP1_HUMANTHAP1physical
25416956
COAC_HUMANPPCDCphysical
25416956
CEP70_HUMANCEP70physical
25416956
KCTD6_HUMANKCTD6physical
25416956
BEND7_HUMANBEND7physical
25416956

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
DB00172L-Proline
Regulatory Network of PPIG_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254; SER-256; SER-257;SER-259; SER-356; THR-358; SER-397; SER-687; SER-744; SER-745; THR-748AND SER-753, AND MASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315 AND SER-696, ANDMASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413 AND SER-415, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254; SER-256; SER-257;SER-259; SER-290; SER-356; THR-358; SER-397; SER-413; SER-415;SER-568; SER-572; THR-611 AND SER-687, AND MASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356; THR-358 ANDSER-415, AND MASS SPECTROMETRY.

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