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Q86WA6

- BPHL_HUMAN

UniProt

Q86WA6 - BPHL_HUMAN

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Protein
Valacyclovir hydrolase
Gene
BPHL, MCNAA
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 Publication
Active sitei272 – 2721Charge relay system1 Publication

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 Publication
Add
BLAST
Chaini38 – 291254Valacyclovir hydrolase
PRO_0000017841Add
BLAST

Amino acid modifications

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

ArrayExpressiQ86WA6.
BgeeiQ86WA6.
CleanExiHS_BPHL.
GenevestigatoriQ86WA6.

Organism-specific databases

HPAiHPA036752.

Interactioni

Subunit structurei

Monomer. May also form homodimers.2 Publications

Protein-protein interaction databases

BioGridi107138. 3 interactions.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiQ86WA6.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0596.
HOGENOMiHOG000044258.
HOVERGENiHBG048762.
InParanoidiQ86WA6.
KOiK01175.
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

MVAVLGGRGV LRLRLLLSAL KPGIHVPRAG PAAAFGTSVT SAKVAVNGVQ    50
LHYQQTGEGD HAVLLLPGML GSGETDFGPQ LKNLNKKLFT VVAWDPRGYG 100
HSRPPDRDFP ADFFERDAKD AVDLMKALKF KKVSLLGWSD GGITALIAAA 150
KYPSYIHKMV IWGANAYVTD EDSMIYEGIR DVSKWSERTR KPLEALYGYD 200
YFARTCEKWV DGIRQFKHLP DGNICRHLLP RVQCPALIVH GEKDPLVPRF 250
HADFIHKHVK GSRLHLMPEG KHNLHLRFAD EFNKLAEDFL Q 291
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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3636MVAVL…AAAFG → MPRNLLYSLLSSHLSPHFS in isoform 2.
VSP_009115Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti182 – 1821V → R in CAA40859. 1 Publication
Sequence conflicti261 – 2611G → A in CAA40859. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
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. 3 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.
HOGENOMi HOG000044258.
HOVERGENi HBG048762.
InParanoidi Q86WA6.
KOi K01175.
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

ArrayExpressi Q86WA6.
Bgeei Q86WA6.
CleanExi HS_BPHL.
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: September 3, 2014
This is version 117 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

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