PAHX_HUMAN - dbPTM
PAHX_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PAHX_HUMAN
UniProt AC O14832
Protein Name Phytanoyl-CoA dioxygenase, peroxisomal
Gene Name PHYH
Organism Homo sapiens (Human).
Sequence Length 338
Subcellular Localization Peroxisome.
Protein Description Converts phytanoyl-CoA to 2-hydroxyphytanoyl-CoA..
Protein Sequence MEQLRAAARLQIVLGHLGRPSAGAVVAHPTSGTISSASFHPQQFQYTLDNNVLTLEQRKFYEENGFLVIKNLVPDADIQRFRNEFEKICRKEVKPLGLTVMRDVTISKSEYAPSEKMITKVQDFQEDKELFRYCTLPEILKYVECFTGPNIMAMHTMLINKPPDSGKKTSRHPLHQDLHYFPFRPSDLIVCAWTAMEHISRNNGCLVVLPGTHKGSLKPHDYPKWEGGVNKMFHGIQDYEENKARVHLVMEKGDTVFFHPLLIHGSGQNKTQGFRKAISCHFASADCHYIDVKGTSQENIEKEVVGIAHKFFGAENSVNLKDIWMFRARLVKGERTNL
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
8UbiquitinationMEQLRAAARLQIVLG
CHHHHHHHHHHHHHH		16.2521890473
8UbiquitinationMEQLRAAARLQIVLG
CHHHHHHHHHHHHHH		16.2521890473
20UbiquitinationVLGHLGRPSAGAVVA
HHHCCCCCCCCEEEE		27.0829967540
28UbiquitinationSAGAVVAHPTSGTIS
CCCEEEECCCCCCCC		17.9829967540
59SuccinylationVLTLEQRKFYEENGF
EEEHHHHHHHHHCCE		52.58-
59SuccinylationVLTLEQRKFYEENGF
EEEHHHHHHHHHCCE		52.58-
94UbiquitinationKICRKEVKPLGLTVM
HHHCHHCCCCCEEEE		35.3024816145
107PhosphorylationVMRDVTISKSEYAPS
EEEEEEECCCCCCCC		22.29-
108AcetylationMRDVTISKSEYAPSE
EEEEEECCCCCCCCH		43.3826051181
108SuccinylationMRDVTISKSEYAPSE
EEEEEECCCCCCCCH		43.3821890473
108UbiquitinationMRDVTISKSEYAPSE
EEEEEECCCCCCCCH		43.3822817900
108SuccinylationMRDVTISKSEYAPSE
EEEEEECCCCCCCCH		43.38-
109PhosphorylationRDVTISKSEYAPSEK
EEEEECCCCCCCCHH		29.1126356563
111PhosphorylationVTISKSEYAPSEKMI
EEECCCCCCCCHHHC		30.7926356563
114PhosphorylationSKSEYAPSEKMITKV
CCCCCCCCHHHCCEE		41.5026356563
116AcetylationSEYAPSEKMITKVQD
CCCCCCHHHCCEEHH		39.6825953088
118UbiquitinationYAPSEKMITKVQDFQ
CCCCHHHCCEEHHHH		5.0929967540
120AcetylationPSEKMITKVQDFQED
CCHHHCCEEHHHHHH		27.2925953088
120UbiquitinationPSEKMITKVQDFQED
CCHHHCCEEHHHHHH		27.2929967540
123UbiquitinationKMITKVQDFQEDKEL
HHCCEEHHHHHHHHH		50.6221890473
124UbiquitinationMITKVQDFQEDKELF
HCCEEHHHHHHHHHH		4.8529967540
126UbiquitinationTKVQDFQEDKELFRY
CEEHHHHHHHHHHHH		71.6729967540
128UbiquitinationVQDFQEDKELFRYCT
EHHHHHHHHHHHHCC		56.4129967540
131UbiquitinationFQEDKELFRYCTLPE
HHHHHHHHHHCCHHH		5.6929967540
133UbiquitinationEDKELFRYCTLPEIL
HHHHHHHHCCHHHHH		5.1829967540
202UbiquitinationAMEHISRNNGCLVVL
HHHHHHHCCCEEEEC		42.3229967540
204UbiquitinationEHISRNNGCLVVLPG
HHHHHCCCEEEECCC		15.0829967540
210UbiquitinationNGCLVVLPGTHKGSL
CCEEEECCCCCCCCC		33.7421890473
210UbiquitinationNGCLVVLPGTHKGSL
CCEEEECCCCCCCCC		33.7421890473
212UbiquitinationCLVVLPGTHKGSLKP
EEEECCCCCCCCCCC		20.6221890473
214UbiquitinationVVLPGTHKGSLKPHD
EECCCCCCCCCCCCC		50.4629967540
216PhosphorylationLPGTHKGSLKPHDYP
CCCCCCCCCCCCCCC		37.7124275569
218UbiquitinationGTHKGSLKPHDYPKW
CCCCCCCCCCCCCCC		41.8429967540
220UbiquitinationHKGSLKPHDYPKWEG
CCCCCCCCCCCCCCC		45.7229967540
222UbiquitinationGSLKPHDYPKWEGGV
CCCCCCCCCCCCCCH		12.0421890473
224UbiquitinationLKPHDYPKWEGGVNK
CCCCCCCCCCCCHHH		52.2029967540
226UbiquitinationPHDYPKWEGGVNKMF
CCCCCCCCCCHHHHH		52.8029967540
231UbiquitinationKWEGGVNKMFHGIQD
CCCCCHHHHHCCCCC		40.3029967540
231SuccinylationKWEGGVNKMFHGIQD
CCCCCHHHHHCCCCC		40.30-
231SuccinylationKWEGGVNKMFHGIQD
CCCCCHHHHHCCCCC		40.30-
233UbiquitinationEGGVNKMFHGIQDYE
CCCHHHHHCCCCCHH		5.2229967540
239PhosphorylationMFHGIQDYEENKARV
HHCCCCCHHHCCEEE		14.5727251275
252SuccinylationRVHLVMEKGDTVFFH
EEEEEEECCCEEEEE		43.95-
252SuccinylationRVHLVMEKGDTVFFH
EEEEEEECCCEEEEE		43.95-
296PhosphorylationYIDVKGTSQENIEKE
EEECCCCCHHHHHHH		44.1328348404
302UbiquitinationTSQENIEKEVVGIAH
CCHHHHHHHHHHHHH		52.6029967540
304UbiquitinationQENIEKEVVGIAHKF
HHHHHHHHHHHHHHH		7.6629967540
310MalonylationEVVGIAHKFFGAENS
HHHHHHHHHHCCCCC		33.1126320211
310UbiquitinationEVVGIAHKFFGAENS
HHHHHHHHHHCCCCC		33.1122817900
312UbiquitinationVGIAHKFFGAENSVN
HHHHHHHHCCCCCCC		12.3621890473
317PhosphorylationKFFGAENSVNLKDIW
HHHCCCCCCCHHHHH		12.149326940
325UbiquitinationVNLKDIWMFRARLVK
CCHHHHHHEEEEHHC		1.3421890473
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 PAHX_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PAHX_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 PAHX_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TM1L1_HUMANTOM1L1physical
16169070
FKBP4_HUMANFKBP4physical
10051602
A4_HUMANAPPphysical
21832049
FAM9B_HUMANFAM9Bphysical
25416956
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
266500Refsum disease (RD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00025Antihemophilic Factor
DB00126Vitamin C
Regulatory Network of PAHX_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory