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Q86WA6

- BPHL_HUMAN

UniProt

Q86WA6 - BPHL_HUMAN

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Protein

Valacyclovir hydrolase

Gene

BPHL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei139 – 1391Nucleophile1 Publication
Sitei140 – 1401Binding of alpha-amino group of substrate
Active sitei244 – 2441Charge relay system1 PublicationPROSITE-ProRule annotation
Active sitei272 – 2721Charge relay system1 PublicationPROSITE-ProRule annotation

GO - Molecular functioni

  1. hydrolase activity Source: UniProtKB-KW

GO - Biological processi

  1. cellular amino acid metabolic process Source: ProtInc
  2. response to toxic substance Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

SABIO-RKQ86WA6.

Protein family/group databases

MEROPSiS33.982.

Names & Taxonomyi

Protein namesi
Recommended name:
Valacyclovir hydrolase (EC:3.1.-.-)
Short name:
VACVase
Short name:
Valacyclovirase
Alternative name(s):
Biphenyl hydrolase-like protein
Biphenyl hydrolase-related protein
Short name:
Bph-rp
Breast epithelial mucin-associated antigen
Short name:
MCNAA
Gene namesi
Name:BPHL
Synonyms:MCNAA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:1094. BPHL.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. mitochondrion Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi139 – 1391S → A: <0.1% of wild type activity. 1 Publication
Mutagenesisi244 – 2441D → N: <0.1% of wild type activity. 1 Publication
Mutagenesisi272 – 2721H → A: Complete loss of activity. 1 Publication

Organism-specific databases

PharmGKBiPA25402.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 37371 PublicationAdd
BLAST
Chaini38 – 291254Valacyclovir hydrolasePRO_0000017841Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei86 – 861N6-acetyllysineBy similarity
Modified residuei119 – 1191N6-acetyllysineBy similarity
Modified residuei126 – 1261N6-acetyllysine; alternate1 Publication
Modified residuei126 – 1261N6-succinyllysine; alternateBy similarity
Modified residuei184 – 1841N6-succinyllysineBy similarity
Modified residuei191 – 1911N6-acetyllysine; alternateBy similarity
Modified residuei191 – 1911N6-succinyllysine; alternateBy similarity
Modified residuei217 – 2171N6-acetyllysineBy similarity
Modified residuei243 – 2431N6-acetyllysineBy similarity
Modified residuei260 – 2601N6-acetyllysine; alternateBy similarity
Modified residuei260 – 2601N6-succinyllysine; alternateBy similarity
Modified residuei271 – 2711N6-acetyllysine; alternateBy similarity
Modified residuei271 – 2711N6-succinyllysine; alternateBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ86WA6.
PaxDbiQ86WA6.
PRIDEiQ86WA6.

PTM databases

PhosphoSiteiQ86WA6.

Expressioni

Tissue specificityi

Expressed at high levels in liver and kidney and lower levels in heart, intestine and skeletal muscle.1 Publication

Gene expression databases

BgeeiQ86WA6.
CleanExiHS_BPHL.
ExpressionAtlasiQ86WA6. baseline and differential.
GenevestigatoriQ86WA6.

Organism-specific databases

HPAiHPA036752.

Interactioni

Subunit structurei

Monomer. May also form homodimers.2 Publications

Protein-protein interaction databases

BioGridi107138. 7 interactions.

Structurei

Secondary structure

1
291
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi40 – 467Combined sources
Beta strandi49 – 579Combined sources
Beta strandi60 – 667Combined sources
Helixi73 – 764Combined sources
Helixi78 – 836Combined sources
Turni86 – 883Combined sources
Beta strandi89 – 946Combined sources
Helixi113 – 12715Combined sources
Beta strandi131 – 1388Combined sources
Helixi140 – 15112Combined sources
Turni153 – 1553Combined sources
Beta strandi156 – 1638Combined sources
Helixi170 – 1778Combined sources
Helixi182 – 1843Combined sources
Helixi187 – 19711Combined sources
Helixi199 – 21416Combined sources
Helixi215 – 2184Combined sources
Helixi220 – 2223Combined sources
Beta strandi223 – 2253Combined sources
Helixi226 – 2316Combined sources
Beta strandi236 – 2416Combined sources
Beta strandi245 – 2473Combined sources
Helixi249 – 25810Combined sources
Beta strandi263 – 2675Combined sources
Helixi274 – 2774Combined sources
Helixi279 – 29012Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OCGX-ray1.75A38-291[»]
2OCIX-ray1.90A38-291[»]
2OCKX-ray1.85A38-291[»]
2OCLX-ray1.90A38-291[»]
ProteinModelPortaliQ86WA6.
SMRiQ86WA6. Positions 38-291.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ86WA6.

Family & Domainsi

Sequence similaritiesi

Belongs to the AB hydrolase superfamily. Lipase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0596.
GeneTreeiENSGT00390000004746.
HOGENOMiHOG000044258.
HOVERGENiHBG048762.
InParanoidiQ86WA6.
KOiK18399.
OMAiGYDYFAR.
OrthoDBiEOG741Z38.
PhylomeDBiQ86WA6.
TreeFamiTF318389.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00120. LIPASE_SER. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q86WA6-1) [UniParc]FASTAAdd to Basket

Also known as: Beta

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVAVLGGRGV LRLRLLLSAL KPGIHVPRAG PAAAFGTSVT SAKVAVNGVQ
60 70 80 90 100
LHYQQTGEGD HAVLLLPGML GSGETDFGPQ LKNLNKKLFT VVAWDPRGYG
110 120 130 140 150
HSRPPDRDFP ADFFERDAKD AVDLMKALKF KKVSLLGWSD GGITALIAAA
160 170 180 190 200
KYPSYIHKMV IWGANAYVTD EDSMIYEGIR DVSKWSERTR KPLEALYGYD
210 220 230 240 250
YFARTCEKWV DGIRQFKHLP DGNICRHLLP RVQCPALIVH GEKDPLVPRF
260 270 280 290
HADFIHKHVK GSRLHLMPEG KHNLHLRFAD EFNKLAEDFL Q
Length:291
Mass (Da):32,543
Last modified:June 1, 2003 - v1
Checksum:i830B948492160244
GO
Isoform 2 (identifier: Q86WA6-2) [UniParc]FASTAAdd to Basket

Also known as: Alpha

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: MVAVLGGRGVLRLRLLLSALKPGIHVPRAGPAAAFG → MPRNLLYSLLSSHLSPHFS

Show »
Length:274
Mass (Da):31,107
Checksum:i12B7F8595B0EBB0C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti182 – 1821V → R in CAA40859. (PubMed:2393862)Curated
Sequence conflicti261 – 2611G → A in CAA40859. (PubMed:2393862)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3636MVAVL…AAAFG → MPRNLLYSLLSSHLSPHFS in isoform 2. 2 PublicationsVSP_009115Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X81372 mRNA. Translation: CAA57137.1.
AJ617684 mRNA. Translation: CAE85120.1.
AL031963 Genomic DNA. Translation: CAD70626.1.
AL031963 Genomic DNA. Translation: CAD70627.1.
CH471087 Genomic DNA. Translation: EAW55122.1.
BC106901 mRNA. Translation: AAI06902.1.
X57653 mRNA. Translation: CAA40859.1.
CCDSiCCDS4483.2. [Q86WA6-1]
PIRiA56716.
RefSeqiNP_004323.2. NM_004332.2. [Q86WA6-1]
UniGeneiHs.10136.

Genome annotation databases

EnsembliENST00000380375; ENSP00000369734; ENSG00000137274. [Q86WA6-2]
ENST00000380379; ENSP00000369739; ENSG00000137274. [Q86WA6-1]
ENST00000434640; ENSP00000390472; ENSG00000137274. [Q86WA6-2]
GeneIDi670.
KEGGihsa:670.
UCSCiuc003muy.3. human. [Q86WA6-2]
uc003mva.3. human. [Q86WA6-1]

Polymorphism databases

DMDMi39931107.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X81372 mRNA. Translation: CAA57137.1 .
AJ617684 mRNA. Translation: CAE85120.1 .
AL031963 Genomic DNA. Translation: CAD70626.1 .
AL031963 Genomic DNA. Translation: CAD70627.1 .
CH471087 Genomic DNA. Translation: EAW55122.1 .
BC106901 mRNA. Translation: AAI06902.1 .
X57653 mRNA. Translation: CAA40859.1 .
CCDSi CCDS4483.2. [Q86WA6-1 ]
PIRi A56716.
RefSeqi NP_004323.2. NM_004332.2. [Q86WA6-1 ]
UniGenei Hs.10136.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2OCG X-ray 1.75 A 38-291 [» ]
2OCI X-ray 1.90 A 38-291 [» ]
2OCK X-ray 1.85 A 38-291 [» ]
2OCL X-ray 1.90 A 38-291 [» ]
ProteinModelPortali Q86WA6.
SMRi Q86WA6. Positions 38-291.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107138. 7 interactions.

Protein family/group databases

MEROPSi S33.982.

PTM databases

PhosphoSitei Q86WA6.

Polymorphism databases

DMDMi 39931107.

Proteomic databases

MaxQBi Q86WA6.
PaxDbi Q86WA6.
PRIDEi Q86WA6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000380375 ; ENSP00000369734 ; ENSG00000137274 . [Q86WA6-2 ]
ENST00000380379 ; ENSP00000369739 ; ENSG00000137274 . [Q86WA6-1 ]
ENST00000434640 ; ENSP00000390472 ; ENSG00000137274 . [Q86WA6-2 ]
GeneIDi 670.
KEGGi hsa:670.
UCSCi uc003muy.3. human. [Q86WA6-2 ]
uc003mva.3. human. [Q86WA6-1 ]

Organism-specific databases

CTDi 670.
GeneCardsi GC06P003118.
H-InvDB HIX0020996.
HGNCi HGNC:1094. BPHL.
HPAi HPA036752.
MIMi 603156. gene.
neXtProti NX_Q86WA6.
PharmGKBi PA25402.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0596.
GeneTreei ENSGT00390000004746.
HOGENOMi HOG000044258.
HOVERGENi HBG048762.
InParanoidi Q86WA6.
KOi K18399.
OMAi GYDYFAR.
OrthoDBi EOG741Z38.
PhylomeDBi Q86WA6.
TreeFami TF318389.

Enzyme and pathway databases

SABIO-RK Q86WA6.

Miscellaneous databases

ChiTaRSi BPHL. human.
EvolutionaryTracei Q86WA6.
GenomeRNAii 670.
NextBioi 2744.
PROi Q86WA6.
SOURCEi Search...

Gene expression databases

Bgeei Q86WA6.
CleanExi HS_BPHL.
ExpressionAtlasi Q86WA6. baseline and differential.
Genevestigatori Q86WA6.

Family and domain databases

Gene3Di 3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
[Graphical view ]
SUPFAMi SSF53474. SSF53474. 1 hit.
PROSITEi PS00120. LIPASE_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression analysis of a novel human serine hydrolase with sequence similarity to prokaryotic enzymes involved in the degradation of aromatic compounds."
    Puente X.S., Lopez-Otin C.
    J. Biol. Chem. 270:12926-12932(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 152-158; 181-184 AND 209-214, TISSUE SPECIFICITY.
    Tissue: Mammary carcinoma.
  2. Puente X.S.
    Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1 AND 2).
    Tissue: Mammary carcinoma.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  6. "Cloning and sequencing of a complementary DNA encoding a M(r) 70,000 human breast epithelial mucin-associated antigen."
    Larocca D., Peterson J.A., Walkup G., Urrea R., Ceriani R.L.
    Cancer Res. 50:5925-5930(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 182-280.
  7. "Identification of a human valacyclovirase: biphenyl hydrolase-like protein as valacyclovir hydrolase."
    Kim I., Chu X.-Y., Kim S., Provoda C.J., Lee K.-D., Amidon G.L.
    J. Biol. Chem. 278:25348-25356(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 38-56, CHARACTERIZATION.
  8. "Structural characterization and chromosomal localization of the gene encoding human biphenyl hydrolase-related protein (BPHL)."
    Puente X.S., Pendas A.M., Lopez-Otin C.
    Genomics 51:459-462(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHROMOSOMAL LOCATION.
  9. Kim I.
    Submitted (DEC-2003) to UniProtKB
    Cited for: SUBUNIT.
  10. "A novel nucleoside prodrug-activating enzyme: substrate specificity of biphenyl hydrolase-like protein."
    Kim I., Song X., Vig B.S., Mittal S., Shin H.-C., Lorenzi P.J., Amidon G.L.
    Mol. Pharm. 1:117-127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBSTRATE SPECIFICITY.
  11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-126, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Molecular basis of prodrug activation by human valacyclovirase, an alpha-amino acid ester hydrolase."
    Lai L., Xu Z., Zhou J., Lee K.D., Amidon G.L.
    J. Biol. Chem. 283:9318-9327(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 38-291, FUNCTION, SUBUNIT, ACTIVE SITES, MUTAGENESIS OF SER-139; ASP-244 AND HIS-272.

Entry informationi

Entry nameiBPHL_HUMAN
AccessioniPrimary (citable) accession number: Q86WA6
Secondary accession number(s): Q00306, Q13855, Q3KP51
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: June 1, 2003
Last modified: November 26, 2014
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3