BPHL_HUMAN - dbPTM
BPHL_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BPHL_HUMAN
UniProt AC Q86WA6
Protein Name Valacyclovir hydrolase
Gene Name BPHL
Organism Homo sapiens (Human).
Sequence Length 291
Subcellular Localization
Protein Description Serine hydrolase that catalyzes the hydrolytic activation of amino acid ester prodrugs of nucleoside analogs such as valacyclovir and valganciclovir. Activates valacyclovir to acyclovir. May play a role in detoxification processes. It is a specific alpha-amino acid ester hydrolase that prefers small, hydrophobic, and aromatic side chains and does not have a stringent requirement for the leaving group other than preferring a primary alcohol..
Protein Sequence MVAVLGGRGVLRLRLLLSALKPGIHVPRAGPAAAFGTSVTSAKVAVNGVQLHYQQTGEGDHAVLLLPGMLGSGETDFGPQLKNLNKKLFTVVAWDPRGYGHSRPPDRDFPADFFERDAKDAVDLMKALKFKKVSLLGWSDGGITALIAAAKYPSYIHKMVIWGANAYVTDEDSMIYEGIRDVSKWSERTRKPLEALYGYDYFARTCEKWVDGIRQFKHLPDGNICRHLLPRVQCPALIVHGEKDPLVPRFHADFIHKHVKGSRLHLMPEGKHNLHLRFADEFNKLAEDFLQ
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
18PhosphorylationLRLRLLLSALKPGIH
HHHHHHHHHHCCCCC		31.37-
70 (in isoform 2)Ubiquitination-6.4721890473
86AcetylationPQLKNLNKKLFTVVA
HHHHHHCCCEEEEEE		54.76-
87UbiquitinationQLKNLNKKLFTVVAW
HHHHHCCCEEEEEEE		48.0021890473
87 (in isoform 1)Ubiquitination-48.0021890473
119AcetylationDFFERDAKDAVDLMK
HHHHCCHHHHHHHHH		50.97-
126AcetylationKDAVDLMKALKFKKV
HHHHHHHHHHCCCEE		58.8419608861
126SuccinylationKDAVDLMKALKFKKV
HHHHHHHHHHCCCEE		58.84-
126SuccinylationKDAVDLMKALKFKKV
HHHHHHHHHHCCCEE		58.84-
126MalonylationKDAVDLMKALKFKKV
HHHHHHHHHHCCCEE		58.8426320211
1262-HydroxyisobutyrylationKDAVDLMKALKFKKV
HHHHHHHHHHCCCEE		58.84-
131AcetylationLMKALKFKKVSLLGW
HHHHHCCCEEEEEEE		51.1630587215
132AcetylationMKALKFKKVSLLGWS
HHHHCCCEEEEEEEC		39.9430587221
151AcetylationTALIAAAKYPSYIHK
HHHHHHHHCCHHHHC		53.6325038526
154PhosphorylationIAAAKYPSYIHKMVI
HHHHHCCHHHHCHHH		33.3622210691
167PhosphorylationVIWGANAYVTDEDSM
HHCCCCEEECCCCHH		12.0422210691
169PhosphorylationWGANAYVTDEDSMIY
CCCCEEECCCCHHHH		22.4622210691
174 (in isoform 2)Ubiquitination-6.1421890473
183PhosphorylationYEGIRDVSKWSERTR
HHHCCCHHHHCHHHC		32.47-
184SuccinylationEGIRDVSKWSERTRK
HHCCCHHHHCHHHCC		55.37-
184SuccinylationEGIRDVSKWSERTRK
HHCCCHHHHCHHHCC		55.37-
186PhosphorylationIRDVSKWSERTRKPL
CCCHHHHCHHHCCHH		22.4228857561
191 (in isoform 1)Ubiquitination-54.0321890473
191AcetylationKWSERTRKPLEALYG
HHCHHHCCHHHHHHC		54.0366723391
191SuccinylationKWSERTRKPLEALYG
HHCHHHCCHHHHHHC		54.03-
191SuccinylationKWSERTRKPLEALYG
HHCHHHCCHHHHHHC		54.0327452117
191UbiquitinationKWSERTRKPLEALYG
HHCHHHCCHHHHHHC		54.0321890473
217MalonylationVDGIRQFKHLPDGNI
HHHHHHCCCCCCCCH		35.5732601280
217AcetylationVDGIRQFKHLPDGNI
HHHHHHCCCCCCCCH		35.5725953088
2432-HydroxyisobutyrylationALIVHGEKDPLVPRF
EEEECCCCCCCCCCC		70.05-
243AcetylationALIVHGEKDPLVPRF
EEEECCCCCCCCCCC		70.0525038526
243SuccinylationALIVHGEKDPLVPRF
EEEECCCCCCCCCCC		70.0527452117
257MalonylationFHADFIHKHVKGSRL
CCHHHHHHHCCCCCE		45.3226320211
257AcetylationFHADFIHKHVKGSRL
CCHHHHHHHCCCCCE		45.3223954790
257UbiquitinationFHADFIHKHVKGSRL
CCHHHHHHHCCCCCE		45.32-
260AcetylationDFIHKHVKGSRLHLM
HHHHHHCCCCCEEEC		51.382403327
260SuccinylationDFIHKHVKGSRLHLM
HHHHHHCCCCCEEEC		51.38-
260SuccinylationDFIHKHVKGSRLHLM
HHHHHHCCCCCEEEC		51.38-
271MalonylationLHLMPEGKHNLHLRF
EEECCCCCCCCHHHC		27.8826320211
271SuccinylationLHLMPEGKHNLHLRF
EEECCCCCCCCHHHC		27.88-
271SuccinylationLHLMPEGKHNLHLRF
EEECCCCCCCCHHHC		27.88-
271AcetylationLHLMPEGKHNLHLRF
EEECCCCCCCCHHHC		27.8825825284
277MethylationGKHNLHLRFADEFNK
CCCCCHHHCHHHHHH		17.60-
284AcetylationRFADEFNKLAEDFLQ
HCHHHHHHHHHHHHC		55.1625038526
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 BPHL_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BPHL_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 BPHL_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MUTA_HUMANMUTphysical
26186194
SETD3_HUMANSETD3physical
26186194
PPP5_HUMANPPP5Cphysical
26186194
TTC19_HUMANTTC19physical
26186194
C1TM_HUMANMTHFD1Lphysical
26344197
SETD3_HUMANSETD3physical
28514442
TTC19_HUMANTTC19physical
28514442
PPP5_HUMANPPP5Cphysical
28514442
CH60_HUMANHSPD1physical
28514442
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 BPHL_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-126 AND LYS-257, AND MASSSPECTROMETRY.

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