PPARA_HUMAN - dbPTM
PPARA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PPARA_HUMAN
UniProt AC Q07869
Protein Name Peroxisome proliferator-activated receptor alpha
Gene Name PPARA
Organism Homo sapiens (Human).
Sequence Length 468
Subcellular Localization Nucleus.
Protein Description Ligand-activated transcription factor. Key regulator of lipid metabolism. Activated by the endogenous ligand 1-palmitoyl-2-oleoyl-sn-glycerol-3-phosphocholine (16:0/18:1-GPC). Activated by oleylethanolamide, a naturally occurring lipid that regulates satiety. Receptor for peroxisome proliferators such as hypolipidemic drugs and fatty acids. Regulates the peroxisomal beta-oxidation pathway of fatty acids. Functions as transcription activator for the ACOX1 and P450 genes. Transactivation activity requires heterodimerization with RXRA and is antagonized by NR2C2. May be required for the propagation of clock information to metabolic pathways regulated by PER2..
Protein Sequence MVDTESPLCPLSPLEAGDLESPLSEEFLQEMGNIQEISQSIGEDSSGSFGFTEYQYLGSCPGSDGSVITDTLSPASSPSSVTYPVVPGSVDESPSGALNIECRICGDKASGYHYGVHACEGCKGFFRRTIRLKLVYDKCDRSCKIQKKNRNKCQYCRFHKCLSVGMSHNAIRFGRMPRSEKAKLKAEILTCEHDIEDSETADLKSLAKRIYEAYLKNFNMNKVKARVILSGKASNNPPFVIHDMETLCMAEKTLVAKLVANGIQNKEAEVRIFHCCQCTSVETVTELTEFAKAIPGFANLDLNDQVTLLKYGVYEAIFAMLSSVMNKDGMLVAYGNGFITREFLKSLRKPFCDIMEPKFDFAMKFNALELDDSDISLFVAAIICCGDRPGLLNVGHIEKMQEGIVHVLRLHLQSNHPDDIFLFPKLLQKMADLRQLVTEHAQLVQIIKKTESDAALHPLLQEIYRDMY
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
6Phosphorylation--MVDTESPLCPLSP
--CCCCCCCCCCCCC		25.8418079279
12PhosphorylationESPLCPLSPLEAGDL
CCCCCCCCCCCCCCC		16.7522817900
21PhosphorylationLEAGDLESPLSEEFL
CCCCCCCCCCCHHHH		38.1422817900
38PhosphorylationMGNIQEISQSIGEDS
CCCHHHHHHHHCCCC		19.6824275569
45PhosphorylationSQSIGEDSSGSFGFT
HHHHCCCCCCCCCCE		32.0924275569
163PhosphorylationCRFHKCLSVGMSHNA
CCHHHHHHHCCCHHH		26.5422210691
179PhosphorylationRFGRMPRSEKAKLKA
HCCCCCHHHHHHHHH		37.2622817900
185SumoylationRSEKAKLKAEILTCE
HHHHHHHHHEEEECC		43.18-
185SumoylationRSEKAKLKAEILTCE
HHHHHHHHHEEEECC		43.18-
230PhosphorylationVKARVILSGKASNNP
CEEEEEECCCCCCCC		27.4222817900
280PhosphorylationFHCCQCTSVETVTEL
EEECCCCCCCCHHHH		26.11-
311PhosphorylationDQVTLLKYGVYEAIF
CHHHHHHHHHHHHHH		16.2823403867
314PhosphorylationTLLKYGVYEAIFAML
HHHHHHHHHHHHHHH		8.6923403867
323PhosphorylationAIFAMLSSVMNKDGM
HHHHHHHHHHCCCCC		22.7923403867
340PhosphorylationAYGNGFITREFLKSL
EECCCCHHHHHHHHC		23.1423403867
358SumoylationFCDIMEPKFDFAMKF
CCCCCCCCCCHHHHC		44.23-
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
12SPhosphorylationKinaseMAPK-FAMILY-GPS
12SPhosphorylationKinaseMAPK_GROUP-PhosphoELM
21SPhosphorylationKinaseMAPK-FAMILY-GPS
21SPhosphorylationKinaseMAPK_GROUP-PhosphoELM
179SPhosphorylationKinasePRKCAP17252
GPS
179SPhosphorylationKinasePRKCBP05771-2
GPS
230SPhosphorylationKinasePRKCAP17252
GPS
230SPhosphorylationKinasePRKCBP05771-2
GPS
280SPhosphorylationKinaseGSK3AP49840
PSP
280SPhosphorylationKinaseGSK3AP18265
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PPARA_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 PPARA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STAC3_HUMANSTAC3physical
16189514
NCOA1_HUMANNCOA1physical
9407140
EP300_HUMANEP300physical
9407140
FABPL_HUMANFABP1physical
11226238
NRIP1_HUMANNRIP1physical
9626662
NCOA1_HUMANNCOA1physical
9626662
EP300_HUMANEP300physical
10336495
NCOR1_HUMANNCOR1physical
10336495
HELZ2_HUMANHELZ2physical
12189208
RXRA_HUMANRXRAphysical
10195690
NCOR2_HUMANNCOR2physical
11845213
NR1H3_HUMANNR1H3physical
8621574
HS90A_HUMANHSP90AA1physical
12482853
AIP_HUMANAIPphysical
12482853
LPIN1_HUMANLPIN1physical
20385772
NCOR1_HUMANNCOR1physical
19955185
NCOR2_HUMANNCOR2physical
19955185
STP1_HUMANTNP1physical
21967852
CHD9_HUMANCHD9physical
16554032
RXRA_HUMANRXRAphysical
12562861
ANM1_HUMANPRMT1physical
23455924
ANM8_HUMANPRMT8physical
23455924
SIR1_HUMANSIRT1physical
19356714
RXRA_HUMANRXRAphysical
22205725
RXRB_HUMANRXRBphysical
22205725
RXRG_HUMANRXRGphysical
22205725
RXRA_HUMANRXRAphysical
15888456
NCOA1_HUMANNCOA1physical
15888456
NCOA2_HUMANNCOA2physical
15888456
NCOA3_HUMANNCOA3physical
15888456
NCOA1_HUMANNCOA1physical
12163133
GRB2_HUMANGRB2physical
25814554
BCL2_HUMANBCL2physical
26556865
UB2R1_HUMANCDC34physical
26556865
EP300_HUMANEP300physical
18797151
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
DB01393Bezafibrate
DB00636Clofibrate
DB01039Fenofibrate
DB01241Gemfibrozil
DB00328Indomethacin
Regulatory Network of PPARA_HUMAN

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Related Literatures of Post-Translational Modification

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