PPIF_HUMAN - dbPTM
PPIF_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PPIF_HUMAN
UniProt AC P30405
Protein Name Peptidyl-prolyl cis-trans isomerase F, mitochondrial
Gene Name PPIF
Organism Homo sapiens (Human).
Sequence Length 207
Subcellular Localization Mitochondrion matrix .
Protein Description PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. [PubMed: 20676357 Involved in regulation of the mitochondrial permeability transition pore (mPTP It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probability of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated. In cooperation with mitochondrial TP53 is involved in activating oxidative stress-induced necrosis. Involved in modulation of mitochondrial membrane F(1)F(0) ATP synthase activity and regulation of mitochondrial matrix adenine nucleotide levels. Has anti-apoptotic activity independently of mPTP and in cooperation with BCL2 inhibits cytochrome c-dependent apoptosis.]
Protein Sequence MLALRCGSRWLGLLSVPRSVPLRLPAARACSKGSGDPSSSSSSGNPLVYLDVDANGKPLGRVVLELKADVVPKTAENFRALCTGEKGFGYKGSTFHRVIPSFMCQAGDFTNHNGTGGKSIYGSRFPDENFTLKHVGPGVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESFGSKSGRTSKKIVITDCGQLS
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
15PhosphorylationSRWLGLLSVPRSVPL
CEEEECCCCCCCCCC		34.8124719451
31PhosphorylationLPAARACSKGSGDPS
CHHHHHHHCCCCCCC		38.78-
34PhosphorylationARACSKGSGDPSSSS
HHHHHCCCCCCCCCC		43.70-
38PhosphorylationSKGSGDPSSSSSSGN
HCCCCCCCCCCCCCC		47.8228450419
39PhosphorylationKGSGDPSSSSSSGNP
CCCCCCCCCCCCCCC		39.3628450419
40PhosphorylationGSGDPSSSSSSGNPL
CCCCCCCCCCCCCCE		38.2828450419
41PhosphorylationSGDPSSSSSSGNPLV
CCCCCCCCCCCCCEE		30.3928450419
42PhosphorylationGDPSSSSSSGNPLVY
CCCCCCCCCCCCEEE		44.1828450419
43PhosphorylationDPSSSSSSGNPLVYL
CCCCCCCCCCCEEEE		44.5328450419
57AcetylationLDVDANGKPLGRVVL
EEECCCCCEECEEEE		36.5623236377
67MalonylationGRVVLELKADVVPKT
CEEEEEEECEECCCC		32.9226320211
67SuccinylationGRVVLELKADVVPKT
CEEEEEEECEECCCC		32.92-
67SuccinylationGRVVLELKADVVPKT
CEEEEEEECEECCCC		32.9227452117
67AcetylationGRVVLELKADVVPKT
CEEEEEEECEECCCC		32.9223954790
73SumoylationLKADVVPKTAENFRA
EECEECCCCHHHHHH		49.0819608861
73UbiquitinationLKADVVPKTAENFRA
EECEECCCCHHHHHH		49.0821890473
73UbiquitinationLKADVVPKTAENFRA
EECEECCCCHHHHHH		49.0821890473
73SumoylationLKADVVPKTAENFRA
EECEECCCCHHHHHH		49.08-
73AcetylationLKADVVPKTAENFRA
EECEECCCCHHHHHH		49.0819608861
86MalonylationRALCTGEKGFGYKGS
HHHHCCCCCCCCCCC		61.9726320211
86UbiquitinationRALCTGEKGFGYKGS
HHHHCCCCCCCCCCC		61.97-
86AcetylationRALCTGEKGFGYKGS
HHHHCCCCCCCCCCC		61.9723954790
86SuccinylationRALCTGEKGFGYKGS
HHHHCCCCCCCCCCC		61.9727452117
86SuccinylationRALCTGEKGFGYKGS
HHHHCCCCCCCCCCC		61.97-
90PhosphorylationTGEKGFGYKGSTFHR
CCCCCCCCCCCCCHH		15.2021406692
91SuccinylationGEKGFGYKGSTFHRV
CCCCCCCCCCCCHHH		46.9227452117
91AcetylationGEKGFGYKGSTFHRV
CCCCCCCCCCCCHHH		46.9226051181
101PhosphorylationTFHRVIPSFMCQAGD
CCHHHCCCCEEECCC		17.9426126808
118MalonylationNHNGTGGKSIYGSRF
CCCCCCCCCCCCCCC		34.7226320211
118AcetylationNHNGTGGKSIYGSRF
CCCCCCCCCCCCCCC		34.7226051181
119PhosphorylationHNGTGGKSIYGSRFP
CCCCCCCCCCCCCCC		25.0728060719
121PhosphorylationGTGGKSIYGSRFPDE
CCCCCCCCCCCCCCC		19.0128060719
123PhosphorylationGGKSIYGSRFPDENF
CCCCCCCCCCCCCCC		17.4925159151
149PhosphorylationMANAGPNTNGSQFFI
ECCCCCCCCCCCEEE		44.05-
167SuccinylationKTDWLDGKHVVFGHV
ECCCCCCCEEEEEEH		32.6623954790
167AcetylationKTDWLDGKHVVFGHV
ECCCCCCCEEEEEEH		32.6623236377
167MalonylationKTDWLDGKHVVFGHV
ECCCCCCCEEEEEEH		32.6626320211
175MalonylationHVVFGHVKEGMDVVK
EEEEEEHHCCHHHHH		42.7626320211
175SuccinylationHVVFGHVKEGMDVVK
EEEEEEHHCCHHHHH		42.7623954790
175SuccinylationHVVFGHVKEGMDVVK
EEEEEEHHCCHHHHH		42.76-
175AcetylationHVVFGHVKEGMDVVK
EEEEEEHHCCHHHHH		42.7626051181
182SuccinylationKEGMDVVKKIESFGS
HCCHHHHHHHHHCCC		48.1323954790
182AcetylationKEGMDVVKKIESFGS
HCCHHHHHHHHHCCC		48.132401487
183SuccinylationEGMDVVKKIESFGSK
CCHHHHHHHHHCCCC		39.8427452117
183MalonylationEGMDVVKKIESFGSK
CCHHHHHHHHHCCCC		39.8426320211
183AcetylationEGMDVVKKIESFGSK
CCHHHHHHHHHCCCC		39.8411792725
186PhosphorylationDVVKKIESFGSKSGR
HHHHHHHHCCCCCCC		38.0821406692
189PhosphorylationKKIESFGSKSGRTSK
HHHHHCCCCCCCCCC		22.9525159151
190SuccinylationKIESFGSKSGRTSKK
HHHHCCCCCCCCCCE		58.26-
190SuccinylationKIESFGSKSGRTSKK
HHHHCCCCCCCCCCE		58.26-
190MalonylationKIESFGSKSGRTSKK
HHHHCCCCCCCCCCE		58.2626320211
190UbiquitinationKIESFGSKSGRTSKK
HHHHCCCCCCCCCCE		58.2621890473
190MethylationKIESFGSKSGRTSKK
HHHHCCCCCCCCCCE		58.26-
191PhosphorylationIESFGSKSGRTSKKI
HHHCCCCCCCCCCEE		34.8923312004
203S-nitrosylationKKIVITDCGQLS---
CEEEEEECCCCC---		2.54-
203S-nitrosocysteineKKIVITDCGQLS---
CEEEEEECCCCC---		2.54-
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
31SPhosphorylationKinaseAKT2P31751
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
167KAcetylation

-
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 PPIF_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ADT1_HUMANSLC25A4physical
12149099
VDAC3_HUMANVDAC3physical
22939629
VATE1_HUMANATP6V1E1physical
22939629
SOSB1_HUMANNABP2physical
22939629
SUGP1_HUMANSUGP1physical
22939629
TIM44_HUMANTIMM44physical
22939629
STX7_HUMANSTX7physical
22939629
MPLKI_HUMANMPLKIPphysical
22939629
RBMS1_HUMANRBMS1physical
22939629
RRFM_HUMANMRRFphysical
22939629
RM14_HUMANMRPL14physical
22939629
ZC11A_HUMANZC3H11Aphysical
22939629
RRBP1_HUMANRRBP1physical
22939629
RM53_HUMANMRPL53physical
22939629
SLIRP_HUMANSLIRPphysical
22939629
TPX2_HUMANTPX2physical
22939629
SRPRB_HUMANSRPRBphysical
22939629
RAGP1_HUMANRANGAP1physical
22939629
UBE4B_HUMANUBE4Bphysical
22939629
PTN11_HUMANPTPN11physical
22939629
ABI2_HUMANABI2physical
25416956
BANP_HUMANBANPphysical
25416956
CKLF5_HUMANCMTM5physical
25416956
GSTK1_HUMANGSTK1physical
26344197
S10AA_HUMANS100A10physical
26344197
TNG2_HUMANTANGO2physical
26344197
TBL1R_HUMANTBL1XR1physical
26344197
BANP_HUMANBANPphysical
21516116
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
DB00091Cyclosporine
DB00172L-Proline
Regulatory Network of PPIF_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-167, AND MASS SPECTROMETRY.

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