HYES_HUMAN - dbPTM
HYES_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HYES_HUMAN
UniProt AC P34913
Protein Name Bifunctional epoxide hydrolase 2
Gene Name EPHX2
Organism Homo sapiens (Human).
Sequence Length 555
Subcellular Localization Cytoplasm. Peroxisome.
Protein Description Bifunctional enzyme. [PubMed: 12574510 The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides]
Protein Sequence MTLRAAVFDLDGVLALPAVFGVLGRTEEALALPRGLLNDAFQKGGPEGATTRLMKGEITLSQWIPLMEENCRKCSETAKVCLPKNFSIKEIFDKAISARKINRPMLQAALMLRKKGFTTAILTNTWLDDRAERDGLAQLMCELKMHFDFLIESCQVGMVKPEPQIYKFLLDTLKASPSEVVFLDDIGANLKPARDLGMVTILVQDTDTALKELEKVTGIQLLNTPAPLPTSCNPSDMSHGYVTVKPRVRLHFVELGSGPAVCLCHGFPESWYSWRYQIPALAQAGYRVLAMDMKGYGESSAPPEIEEYCMEVLCKEMVTFLDKLGLSQAVFIGHDWGGMLVWYMALFYPERVRAVASLNTPFIPANPNMSPLESIKANPVFDYQLYFQEPGVAEAELEQNLSRTFKSLFRASDESVLSMHKVCEAGGLFVNSPEEPSLSRMVTEEEIQFYVQQFKKSGFRGPLNWYRNMERNWKWACKSLGRKILIPALMVTAEKDFVLVPQMSQHMEDWIPHLKRGHIEDCGHWTQMDKPTEVNQILIKWLDSDARNPPVVSKM
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
2Phosphorylation------MTLRAAVFD
------CCHHHEEEC		25.5824043423
18UbiquitinationDGVLALPAVFGVLGR
CHHHHHHHHHHHHCC		15.3229967540
23UbiquitinationLPAVFGVLGRTEEAL
HHHHHHHHCCCHHHH		3.8329967540
26PhosphorylationVFGVLGRTEEALALP
HHHHHCCCHHHHHCC		36.0624043423
28UbiquitinationGVLGRTEEALALPRG
HHHCCCHHHHHCCHH		48.6629967540
31UbiquitinationGRTEEALALPRGLLN
CCCHHHHHCCHHHHH		23.6729967540
36UbiquitinationALALPRGLLNDAFQK
HHHCCHHHHHHHHHH		4.2229967540
41UbiquitinationRGLLNDAFQKGGPEG
HHHHHHHHHHCCCCC		9.5829967540
43AcetylationLLNDAFQKGGPEGAT
HHHHHHHHCCCCCHH		60.4219608861
43UbiquitinationLLNDAFQKGGPEGAT
HHHHHHHHCCCCCHH		60.4229967540
55UbiquitinationGATTRLMKGEITLSQ
CHHHHHHCCEEEHHH		58.97-
55SuccinylationGATTRLMKGEITLSQ
CHHHHHHCCEEEHHH		58.97-
55SuccinylationGATTRLMKGEITLSQ
CHHHHHHCCEEEHHH		58.97-
79UbiquitinationRKCSETAKVCLPKNF
HHCCCHHCEECCCCC		40.68-
84UbiquitinationTAKVCLPKNFSIKEI
HHCEECCCCCCHHHH		58.6429967540
89UbiquitinationLPKNFSIKEIFDKAI
CCCCCCHHHHHHHHH		43.4929967540
94UbiquitinationSIKEIFDKAISARKI
CHHHHHHHHHHHHHC		36.5529967540
94AcetylationSIKEIFDKAISARKI
CHHHHHHHHHHHHHC		36.5520167786
108UbiquitinationINRPMLQAALMLRKK
CCHHHHHHHHHHHHC		9.9029967540
114AcetylationQAALMLRKKGFTTAI
HHHHHHHHCCCEEEE		53.977265669
115AcetylationAALMLRKKGFTTAIL
HHHHHHHCCCEEEEE		53.477265679
121UbiquitinationKKGFTTAILTNTWLD
HCCCEEEEEECCCCC		4.5929967540
125UbiquitinationTTAILTNTWLDDRAE
EEEEEECCCCCHHHH		23.3629967540
138UbiquitinationAERDGLAQLMCELKM
HHHCCHHHHHHHHHH		34.4729967540
167AcetylationKPEPQIYKFLLDTLK
CCCHHHHHHHHHHHC		31.037706921
172PhosphorylationIYKFLLDTLKASPSE
HHHHHHHHHCCCCCC		30.0823403867
174UbiquitinationKFLLDTLKASPSEVV
HHHHHHHCCCCCCEE		49.2429967540
174AcetylationKFLLDTLKASPSEVV
HHHHHHHCCCCCCEE		49.24156287
191AcetylationDDIGANLKPARDLGM
CCCCCCCCCCHHHCC		36.1225953088
191UbiquitinationDDIGANLKPARDLGM
CCCCCCCCCCHHHCC		36.1229967540
215AcetylationTALKELEKVTGIQLL
HHHHHHHHHHCEEEC		58.69-
245UbiquitinationSHGYVTVKPRVRLHF
CCCEEEECCCEEEEE		20.10-
296PhosphorylationLAMDMKGYGESSAPP
EEEECCCCCCCCCCH		16.52-
299PhosphorylationDMKGYGESSAPPEIE
ECCCCCCCCCCHHHH		27.69-
308PhosphorylationAPPEIEEYCMEVLCK
CCHHHHHHHHHHHHH		5.59-
319PhosphorylationVLCKEMVTFLDKLGL
HHHHHHHHHHHHCCC		19.7123403867
340UbiquitinationGHDWGGMLVWYMALF
ECCHHHHHHHHHHHH		2.5029967540
353UbiquitinationLFYPERVRAVASLNT
HHCHHHHHHHHCCCC		29.5729967540
355UbiquitinationYPERVRAVASLNTPF
CHHHHHHHHCCCCCC		2.3229967540
368UbiquitinationPFIPANPNMSPLESI
CCCCCCCCCCCHHHH		43.2929967540
370PhosphorylationIPANPNMSPLESIKA
CCCCCCCCCHHHHCC		32.7327050516
374PhosphorylationPNMSPLESIKANPVF
CCCCCHHHHCCCCCC		36.7524719451
383NitrationKANPVFDYQLYFQEP
CCCCCCEEEEEECCC		6.75-
406UbiquitinationQNLSRTFKSLFRASD
HHHHHHHHHHHHCCC		45.7129967540
412PhosphorylationFKSLFRASDESVLSM
HHHHHHCCCHHHHHH		37.34-
412UbiquitinationFKSLFRASDESVLSM
HHHHHHCCCHHHHHH		37.3429967540
417UbiquitinationRASDESVLSMHKVCE
HCCCHHHHHHHHHHH		5.3929967540
421UbiquitinationESVLSMHKVCEAGGL
HHHHHHHHHHHCCCE		39.6829967540
421SuccinylationESVLSMHKVCEAGGL
HHHHHHHHHHHCCCE		39.68-
421SuccinylationESVLSMHKVCEAGGL
HHHHHHHHHHHCCCE		39.68-
425UbiquitinationSMHKVCEAGGLFVNS
HHHHHHHCCCEECCC		16.5429967540
430UbiquitinationCEAGGLFVNSPEEPS
HHCCCEECCCCCCCC		9.2529967540
439PhosphorylationSPEEPSLSRMVTEEE
CCCCCCHHHCCCHHH		23.7530624053
443PhosphorylationPSLSRMVTEEEIQFY
CCHHHCCCHHHHHHH		28.4730624053
449UbiquitinationVTEEEIQFYVQQFKK
CCHHHHHHHHHHHHH		8.7329967540
450PhosphorylationTEEEIQFYVQQFKKS
CHHHHHHHHHHHHHC		4.8730624053
455AcetylationQFYVQQFKKSGFRGP
HHHHHHHHHCCCCCC		41.512380563
455SuccinylationQFYVQQFKKSGFRGP
HHHHHHHHHCCCCCC		41.51-
455UbiquitinationQFYVQQFKKSGFRGP
HHHHHHHHHCCCCCC		41.51-
455SuccinylationQFYVQQFKKSGFRGP
HHHHHHHHHCCCCCC		41.51-
456UbiquitinationFYVQQFKKSGFRGPL
HHHHHHHHCCCCCCC		58.04-
462UbiquitinationKKSGFRGPLNWYRNM
HHCCCCCCCHHHHCC		20.4729967540
464UbiquitinationSGFRGPLNWYRNMER
CCCCCCCHHHHCCHH		36.5529967540
466NitrationFRGPLNWYRNMERNW
CCCCCHHHHCCHHHH		7.34-
474UbiquitinationRNMERNWKWACKSLG
HCCHHHHHHHHHHHC		28.5829967540
477UbiquitinationERNWKWACKSLGRKI
HHHHHHHHHHHCCCC		2.7529967540
478UbiquitinationRNWKWACKSLGRKIL
HHHHHHHHHHCCCCC		40.7529967540
483UbiquitinationACKSLGRKILIPALM
HHHHHCCCCCEEHHH		39.8129967540
487UbiquitinationLGRKILIPALMVTAE
HCCCCCEEHHHHCCC		18.8529967540
515UbiquitinationEDWIPHLKRGHIEDC
HHHHHHHHCCCCCCC		53.9829967540
522OtherKRGHIEDCGHWTQMD
HCCCCCCCCCCCCCC		2.5321164107
530UbiquitinationGHWTQMDKPTEVNQI
CCCCCCCCCCHHHHH		48.7929967540
540UbiquitinationEVNQILIKWLDSDAR
HHHHHHHHHHCCCCC		37.9529967540
544PhosphorylationILIKWLDSDARNPPV
HHHHHHCCCCCCCCC		30.8828857561
554UbiquitinationRNPPVVSKM------
CCCCCCCCC------		36.70-
554SuccinylationRNPPVVSKM------
CCCCCCCCC------		36.70-
554SuccinylationRNPPVVSKM------
CCCCCCCCC------		36.70-
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 HYES_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HYES_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 HYES_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HYES_HUMANEPHX2physical
15196990
HYES_HUMANEPHX2physical
15096040
MVP_HUMANMVPphysical
21988832
HYES_HUMANEPHX2physical
16322563
HDHD1_HUMANHDHD1physical
26344197
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
There are no disease associations of PTM sites.
Regulatory Network of HYES_HUMAN

loading...

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-43, AND MASS SPECTROMETRY.

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