PPIB_HUMAN - dbPTM
PPIB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PPIB_HUMAN
UniProt AC P23284
Protein Name Peptidyl-prolyl cis-trans isomerase B
Gene Name PPIB
Organism Homo sapiens (Human).
Sequence Length 216
Subcellular Localization Endoplasmic reticulum lumen . Melanosome . Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:17081065).
Protein Description PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding..
Protein Sequence MLRLSERNMKVLLAAALIAGSVFFLLLPGPSAADEKKKGPKVTVKVYFDLRIGDEDVGRVIFGLFGKTVPKTVDNFVALATGEKGFGYKNSKFHRVIKDFMIQGGDFTRGDGTGGKSIYGERFPDENFKLKHYGPGWVSMANAGKDTNGSQFFITTVKTAWLDGKHVVFGKVLEGMEVVRKVESTKTDSRDKPLKDVIIADCGKIEVEKPFAIAKE
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
45UbiquitinationKGPKVTVKVYFDLRI
CCCCEEEEEEEECEE		23.1133845483
45AcetylationKGPKVTVKVYFDLRI
CCCCEEEEEEEECEE		23.1126051181
47PhosphorylationPKVTVKVYFDLRIGD
CCEEEEEEEECEECC		5.9024719451
51MethylationVKVYFDLRIGDEDVG
EEEEEECEECCCCHH		32.46115488309
67UbiquitinationVIFGLFGKTVPKTVD
HHEEECCCCCCCCHH		38.7321906983
67AcetylationVIFGLFGKTVPKTVD
HHEEECCCCCCCCHH		38.7326051181
71UbiquitinationLFGKTVPKTVDNFVA
ECCCCCCCCHHCEEH		57.7722817900
71AcetylationLFGKTVPKTVDNFVA
ECCCCCCCCHHCEEH		57.7726051181
72PhosphorylationFGKTVPKTVDNFVAL
CCCCCCCCHHCEEHH		27.3321712546
81PhosphorylationDNFVALATGEKGFGY
HCEEHHHCCCCCCCC		46.88-
84UbiquitinationVALATGEKGFGYKNS
EHHHCCCCCCCCCCC		61.9721890473
84SuccinylationVALATGEKGFGYKNS
EHHHCCCCCCCCCCC		61.9721890473
84AcetylationVALATGEKGFGYKNS
EHHHCCCCCCCCCCC		61.9726051181
88PhosphorylationTGEKGFGYKNSKFHR
CCCCCCCCCCCCHHH		12.5321406692
89SuccinylationGEKGFGYKNSKFHRV
CCCCCCCCCCCHHHH		55.9423954790
89UbiquitinationGEKGFGYKNSKFHRV
CCCCCCCCCCCHHHH		55.9423000965
91PhosphorylationKGFGYKNSKFHRVIK
CCCCCCCCCHHHHEE		32.3328348404
92UbiquitinationGFGYKNSKFHRVIKD
CCCCCCCCHHHHEEC		55.3623000965
98AcetylationSKFHRVIKDFMIQGG
CCHHHHEECCEEECC		41.9025825284
98UbiquitinationSKFHRVIKDFMIQGG
CCHHHHEECCEEECC		41.9023000965
101SulfoxidationHRVIKDFMIQGGDFT
HHHEECCEEECCCCC		2.9921406390
109MethylationIQGGDFTRGDGTGGK
EECCCCCCCCCCCCC		40.99115488293
113PhosphorylationDFTRGDGTGGKSIYG
CCCCCCCCCCCCCCC		47.7223312004
116MalonylationRGDGTGGKSIYGERF
CCCCCCCCCCCCCCC		34.7226320211
116UbiquitinationRGDGTGGKSIYGERF
CCCCCCCCCCCCCCC		34.7223000965
116AcetylationRGDGTGGKSIYGERF
CCCCCCCCCCCCCCC		34.7226051181
117PhosphorylationGDGTGGKSIYGERFP
CCCCCCCCCCCCCCC		25.0728152594
119PhosphorylationGTGGKSIYGERFPDE
CCCCCCCCCCCCCCC		21.7428152594
122MethylationGKSIYGERFPDENFK
CCCCCCCCCCCCCCC		43.99115488301
129MethylationRFPDENFKLKHYGPG
CCCCCCCCCCEECCC		69.1166695413
129MalonylationRFPDENFKLKHYGPG
CCCCCCCCCCEECCC		69.1126320211
129UbiquitinationRFPDENFKLKHYGPG
CCCCCCCCCCEECCC		69.1122817900
129AcetylationRFPDENFKLKHYGPG
CCCCCCCCCCEECCC		69.1126822725
131AcetylationPDENFKLKHYGPGWV
CCCCCCCCEECCCEE		35.0625825284
131UbiquitinationPDENFKLKHYGPGWV
CCCCCCCCEECCCEE		35.0621890473
131MalonylationPDENFKLKHYGPGWV
CCCCCCCCEECCCEE		35.0626320211
133PhosphorylationENFKLKHYGPGWVSM
CCCCCCEECCCEEEE		24.3520068231
139PhosphorylationHYGPGWVSMANAGKD
EECCCEEEECCCCCC		12.9820068231
140SulfoxidationYGPGWVSMANAGKDT
ECCCEEEECCCCCCC		2.1130846556
145AcetylationVSMANAGKDTNGSQF
EEECCCCCCCCCCCE		59.9926051181
147PhosphorylationMANAGKDTNGSQFFI
ECCCCCCCCCCCEEE		44.9921712546
148N-linked_GlycosylationANAGKDTNGSQFFIT
CCCCCCCCCCCEEEE		59.25UniProtKB CARBOHYD
148N-linked_GlycosylationANAGKDTNGSQFFIT
CCCCCCCCCCCEEEE		59.2520068230
150PhosphorylationAGKDTNGSQFFITTV
CCCCCCCCCEEEEEE		26.3621712546
158UbiquitinationQFFITTVKTAWLDGK
CEEEEEEEEEEECCC		30.3621906983
159PhosphorylationFFITTVKTAWLDGKH
EEEEEEEEEEECCCC		20.8029396449
165MalonylationKTAWLDGKHVVFGKV
EEEEECCCCEEEEEE		32.6626320211
165UbiquitinationKTAWLDGKHVVFGKV
EEEEECCCCEEEEEE		32.6623000965
165AcetylationKTAWLDGKHVVFGKV
EEEEECCCCEEEEEE		32.6625825284
171UbiquitinationGKHVVFGKVLEGMEV
CCCEEEEEEECCCHH		31.9823000965
171AcetylationGKHVVFGKVLEGMEV
CCCEEEEEEECCCHH		31.9825825284
176SulfoxidationFGKVLEGMEVVRKVE
EEEEECCCHHEEEEE		2.2928465586
181UbiquitinationEGMEVVRKVESTKTD
CCCHHEEEEECCCCC		38.4524816145
184PhosphorylationEVVRKVESTKTDSRD
HHEEEEECCCCCCCC		37.8921406692
185PhosphorylationVVRKVESTKTDSRDK
HEEEEECCCCCCCCC		25.1821406692
187PhosphorylationRKVESTKTDSRDKPL
EEEECCCCCCCCCCC		39.0223927012
189PhosphorylationVESTKTDSRDKPLKD
EECCCCCCCCCCCCC		47.8430278072
192UbiquitinationTKTDSRDKPLKDVII
CCCCCCCCCCCCEEE		51.6533845483
192SuccinylationTKTDSRDKPLKDVII
CCCCCCCCCCCCEEE		51.6523954790
192AcetylationTKTDSRDKPLKDVII
CCCCCCCCCCCCEEE		51.6525953088
195UbiquitinationDSRDKPLKDVIIADC
CCCCCCCCCEEEECC		59.4833845483
195AcetylationDSRDKPLKDVIIADC
CCCCCCCCCEEEECC		59.4826822725
202S-palmitoylationKDVIIADCGKIEVEK
CCEEEECCCCEEEEC		4.4029575903
202GlutathionylationKDVIIADCGKIEVEK
CCEEEECCCCEEEEC		4.4022555962
202S-nitrosocysteineKDVIIADCGKIEVEK
CCEEEECCCCEEEEC		4.40-
202S-nitrosylationKDVIIADCGKIEVEK
CCEEEECCCCEEEEC		4.4022178444
204UbiquitinationVIIADCGKIEVEKPF
EEEECCCCEEEECCC		41.8623000965
204AcetylationVIIADCGKIEVEKPF
EEEECCCCEEEECCC		41.8626051181
209AcetylationCGKIEVEKPFAIAKE
CCCEEEECCCEECCC		51.0825825284
209SuccinylationCGKIEVEKPFAIAKE
CCCEEEECCCEECCC		51.08-
209SuccinylationCGKIEVEKPFAIAKE
CCCEEEECCCEECCC		51.0821890473
209UbiquitinationCGKIEVEKPFAIAKE
CCCEEEECCCEECCC		51.0823000965
215MalonylationEKPFAIAKE------
ECCCEECCC------		58.8226320211
215AcetylationEKPFAIAKE------
ECCCEECCC------		58.8225953088
215SuccinylationEKPFAIAKE------
ECCCEECCC------		58.8223954790
215UbiquitinationEKPFAIAKE------
ECCCEECCC------		58.8223000965
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PPIB_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 PPIB_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CAMLG_HUMANCAMLGphysical
7522304
UBL4A_HUMANUBL4Aphysical
22939629
RBMS1_HUMANRBMS1physical
22939629
TIM44_HUMANTIMM44physical
22939629
RRFM_HUMANMRRFphysical
22939629
RM53_HUMANMRPL53physical
22939629
SCO2_HUMANSCO2physical
22939629
THIK_HUMANACAA1physical
22939629
ZC11A_HUMANZC3H11Aphysical
22939629
RAGP1_HUMANRANGAP1physical
22939629
SUGP1_HUMANSUGP1physical
22939629
G3P_HUMANGAPDHphysical
22863883
PPP5_HUMANPPP5Cphysical
22863883
RIR1_HUMANRRM1physical
22863883
DDIT3_HUMANDDIT3physical
24270407
PEX19_HUMANPEX19physical
25416956
SGTA_HUMANSGTAphysical
25416956
UBQL1_HUMANUBQLN1physical
25416956
BANP_HUMANBANPphysical
25416956
ALDOC_HUMANALDOCphysical
26344197
GDIR3_HUMANARHGDIGphysical
26344197
ECHM_HUMANECHS1physical
26344197
IF5A2_HUMANEIF5A2physical
26344197
IF5AL_HUMANEIF5AL1physical
26344197
IF6_HUMANEIF6physical
26344197
ENOA_HUMANENO1physical
26344197
ENOG_HUMANENO2physical
26344197
ENOB_HUMANENO3physical
26344197
FKB1A_HUMANFKBP1Aphysical
26344197
FKBP2_HUMANFKBP2physical
26344197
CH10_HUMANHSPE1physical
26344197
PDIA1_HUMANP4HBphysical
26344197
PSA4_HUMANPSMA4physical
26344197
1433S_HUMANSFNphysical
26344197
TAGL_HUMANTAGLNphysical
26344197
UCHL3_HUMANUCHL3physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
259440Osteogenesis imperfecta 9 (OI9)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00172L-Proline
Regulatory Network of PPIB_HUMAN

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Related Literatures of Post-Translational Modification

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