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P15309

- PPAP_HUMAN

UniProt

P15309 - PPAP_HUMAN

Protein

Prostatic acid phosphatase

Gene

ACPP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 3 (01 Mar 1992)
      Previous versions | rss
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    Functioni

    A non-specific tyrosine phosphatase that dephosphorylates a diverse number of substrates under acidic conditions (pH 4-6) including alkyl, aryl, and acyl orthophosphate monoesters and phosphorylated proteins. Has lipid phosphatase activity and inactivates lysophosphatidic acid in seminal plasma.
    Isoform 2: the cellular form also has ecto-5'-nucleotidase activity in dorsal root ganglion (DRG) neurons. Generates adenosine from AMP which acts as a pain suppressor. Acts as a tumor suppressor of prostate cancer through dephosphorylation of ERBB2 and deactivation of MAPK-mediated signaling.

    Catalytic activityi

    A phosphate monoester + H2O = an alcohol + phosphate.1 Publication
    A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.1 Publication

    Enzyme regulationi

    Phosphatase activity inhibited by L+-tartrate, and by its derivative, alpha-benzylaminobenzylphosphonic acid.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei43 – 431Substrate
    Active sitei44 – 441Nucleophile1 Publication
    Binding sitei47 – 471Substrate
    Sitei49 – 491Important for substrate specificity
    Binding sitei111 – 1111Substrate
    Sitei138 – 1381Required for homodimerizationBy similarity
    Sitei144 – 1441Required for homodimerizationBy similarity
    Sitei206 – 2061Required for structural stability
    Binding sitei289 – 2891Substrate
    Active sitei290 – 2901Proton donor1 Publication

    GO - Molecular functioni

    1. 5'-nucleotidase activity Source: UniProt
    2. acid phosphatase activity Source: UniProt
    3. choline binding Source: Ensembl
    4. identical protein binding Source: IntAct
    5. lysophosphatidic acid phosphatase activity Source: UniProt
    6. phosphatase activity Source: UniProt
    7. protein binding Source: IntAct
    8. thiamine phosphate phosphatase activity Source: UniProt

    GO - Biological processi

    1. adenosine metabolic process Source: UniProt
    2. dephosphorylation Source: UniProt
    3. nucleotide metabolic process Source: Ensembl
    4. positive regulation of adenosine receptor signaling pathway Source: UniProt
    5. purine nucleobase metabolic process Source: Ensembl
    6. regulation of sensory perception of pain Source: UniProt
    7. thiamine metabolic process Source: UniProt

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    SABIO-RKP15309.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Prostatic acid phosphatase (EC:3.1.3.2)
    Short name:
    PAP
    Alternative name(s):
    5'-nucleotidase (EC:3.1.3.5)
    Short name:
    5'-NT
    Ecto-5'-nucleotidase
    Thiamine monophosphatase
    Short name:
    TMPase
    Cleaved into the following chain:
    Gene namesi
    Name:ACPP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:125. ACPP.

    Subcellular locationi

    Isoform 2 : Cell membrane; Single-pass type I membrane protein. Lysosome membrane; Single-pass type I membrane protein
    Note: Appears to shuttle between the cell membrane and intracellular vesicles. Colocalizes with FLOT1 at cell membrane and in intracellular vesicles. Colocalizes with LAMP2 on the lysosome membrane.

    GO - Cellular componenti

    1. apical part of cell Source: Ensembl
    2. extracellular space Source: UniProt
    3. extracellular vesicular exosome Source: UniProt
    4. filopodium Source: Ensembl
    5. Golgi cisterna Source: Ensembl
    6. integral component of membrane Source: Ensembl
    7. intracellular Source: UniProtKB
    8. lysosomal membrane Source: UniProtKB
    9. multivesicular body Source: Ensembl
    10. nucleus Source: UniProt
    11. plasma membrane Source: UniProtKB
    12. secretory granule Source: Ensembl
    13. vesicle membrane Source: UniProt

    Keywords - Cellular componenti

    Amyloid, Cell membrane, Lysosome, Membrane, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi206 – 2061W → F: Greatly reduced enzyme activity, marked decrease in structural stability, and increased binding of the inhibitor, L(+)-tartrate. 1 Publication
    Mutagenesisi206 – 2061W → L: Reduced enzyme activity, marked decrease in structural stability, and increased binding of the inhibitor, L(+)-tartrate. 1 Publication

    Organism-specific databases

    PharmGKBiPA24449.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3232Add
    BLAST
    Chaini33 – 386354Prostatic acid phosphatasePRO_0000023963Add
    BLAST
    Peptidei248 – 28639PAPf39PRO_0000411250Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi94 – 941N-linked (GlcNAc...)1 Publication
    Disulfide bondi161 ↔ 372
    Disulfide bondi215 ↔ 313
    Glycosylationi220 – 2201N-linked (GlcNAc...)2 Publications
    Glycosylationi333 – 3331N-linked (GlcNAc...)1 Publication
    Disulfide bondi347 ↔ 351

    Post-translational modificationi

    N-glycosylated. High mannose content, partially sialylated and fucosylated biantennary complex. Also fucosylated with partially sialylated triantennary complex oligosaccharides.2 Publications
    Proteolytically cleaved in seminal fluid to produce several peptides. Peptide PAPf39, the most prominent, forms amyloid beta-sheet fibrils, SEVI (semen-derived enhancer of viral infection) which entrap HIV virions, attach them to target cells and enhance infection. SEVI amyloid fibrils are degraded by polyphenol epigallocatechin-3-gallate (EGCG), a constituent of green tea. Target cell attachment and enhancement of HIV infection is inhibited by surfen. Also similarly boosts XMRV (xenotropic murine leukemia virus-related virus) infection.2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP15309.
    PaxDbiP15309.
    PRIDEiP15309.

    PTM databases

    PhosphoSiteiP15309.

    Miscellaneous databases

    PMAP-CutDBP15309.

    Expressioni

    Tissue specificityi

    Highly expressed in the prostate, restricted to glandular and ductal epithelial cells. Also expressed in bladder, kidney, pancreas, lung, cervix, testis and ovary. Weak expression in a subset of pancreatic islet cells, squamous epithelia, the pilosebaceous unit, colonic neuroendocrine cells and skin adnexal structures. Isoform 2 also expressed in the sarcolemma of skeletal muscle. Levels of this cellular isoform decreased in prostate cancer.2 Publications

    Gene expression databases

    ArrayExpressiP15309.
    BgeeiP15309.
    CleanExiHS_ACPP.
    GenevestigatoriP15309.

    Organism-specific databases

    HPAiCAB000071.
    HPA004335.

    Interactioni

    Subunit structurei

    Homodimer; dimer formation is required for phosphatase activity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself4EBI-1222012,EBI-1222012

    Protein-protein interaction databases

    BioGridi106571. 3 interactions.
    IntActiP15309. 3 interactions.
    MINTiMINT-6780778.
    STRINGi9606.ENSP00000323036.

    Structurei

    Secondary structure

    1
    386
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi34 – 4310
    Helixi60 – 623
    Helixi72 – 8817
    Turni89 – 935
    Helixi99 – 1013
    Beta strandi102 – 1087
    Helixi110 – 12314
    Helixi128 – 1303
    Beta strandi134 – 1363
    Beta strandi144 – 1463
    Helixi148 – 1503
    Beta strandi152 – 1554
    Helixi162 – 17312
    Helixi175 – 1817
    Helixi182 – 1843
    Helixi185 – 19511
    Helixi202 – 2087
    Helixi210 – 2189
    Helixi229 – 24719
    Beta strandi248 – 2514
    Helixi252 – 2587
    Helixi261 – 27616
    Beta strandi277 – 2793
    Beta strandi282 – 2887
    Helixi290 – 29910
    Beta strandi313 – 3219
    Beta strandi324 – 3329
    Beta strandi335 – 3373
    Beta strandi340 – 3423
    Beta strandi349 – 3524
    Helixi353 – 3608
    Helixi361 – 3633
    Helixi368 – 3714

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CVIX-ray3.20A/B/C/D33-374[»]
    1ND5X-ray2.90A/B/C/D33-386[»]
    1ND6X-ray2.40A/B/C/D33-386[»]
    2HPAX-ray2.90A/B/C/D33-374[»]
    2L3HNMR-A248-286[»]
    2L77NMR-A248-286[»]
    2L79NMR-A248-286[»]
    3PPDX-ray1.50A260-265[»]
    DisProtiDP00628.
    ProteinModelPortaliP15309.
    SMRiP15309. Positions 33-375.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP15309.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histidine acid phosphatase family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG85977.
    HOGENOMiHOG000231439.
    HOVERGENiHBG002203.
    KOiK14410.
    OMAiFTLPSWA.
    OrthoDBiEOG7GXPBJ.
    PhylomeDBiP15309.
    TreeFamiTF312893.

    Family and domain databases

    Gene3Di3.40.50.1240. 1 hit.
    InterProiIPR000560. His_Pase_superF_clade-2.
    IPR029033. His_PPase_superfam.
    [Graphical view]
    PfamiPF00328. His_Phos_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF53254. SSF53254. 1 hit.
    PROSITEiPS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
    PS00778. HIS_ACID_PHOSPHAT_2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P15309-1) [UniParc]FASTAAdd to Basket

    Also known as: Secreted PAP, sPAP

    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

    MRAAPLLLAR AASLSLGFLF LLFFWLDRSV LAKELKFVTL VFRHGDRSPI    50
    DTFPTDPIKE SSWPQGFGQL TQLGMEQHYE LGEYIRKRYR KFLNESYKHE 100
    QVYIRSTDVD RTLMSAMTNL AALFPPEGVS IWNPILLWQP IPVHTVPLSE 150
    DQLLYLPFRN CPRFQELESE TLKSEEFQKR LHPYKDFIAT LGKLSGLHGQ 200
    DLFGIWSKVY DPLYCESVHN FTLPSWATED TMTKLRELSE LSLLSLYGIH 250
    KQKEKSRLQG GVLVNEILNH MKRATQIPSY KKLIMYSAHD TTVSGLQMAL 300
    DVYNGLLPPY ASCHLTELYF EKGEYFVEMY YRNETQHEPY PLMLPGCSPS 350
    CPLERFAELV GPVIPQDWST ECMTTNSHQG TEDSTD 386
    Length:386
    Mass (Da):44,566
    Last modified:March 1, 1992 - v3
    Checksum:iEF81E11DFAECADEA
    GO
    Isoform 2 (identifier: P15309-2) [UniParc]FASTAAdd to Basket

    Also known as: TMPase, TM-PAP, cellular PAP, cPAP

    The sequence of this isoform differs from the canonical sequence as follows:
         380-386: GTEDSTD → VLKVIFAVAFCLISAVLMVLLFIHIRRGLCWQRESYGNI

    Show »
    Length:418
    Mass (Da):48,336
    Checksum:i68E1131197595362
    GO
    Isoform 3 (identifier: P15309-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         153-185: Missing.

    Show »
    Length:353
    Mass (Da):40,443
    Checksum:iC3E376122B63DA82
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti15 – 2410SLGFLFLLFF → AFASCFCFFC in CAA37673. (PubMed:2395659)Curated
    Sequence conflicti15 – 2410SLGFLFLLFF → ALASCFCFFC in AAA60022. (PubMed:2712834)Curated
    Sequence conflicti15 – 2410SLGFLFLLFF → ALASCFCFFC in CAA36422. (PubMed:2842184)Curated
    Sequence conflicti46 – 461D → H in CAA37673. (PubMed:2395659)Curated
    Sequence conflicti66 – 738GFGQLTQL → RIWPTHPA in CAA37673. (PubMed:2395659)Curated
    Sequence conflicti66 – 738GFGQLTQL → WIWPTHPA in CAA36422. (PubMed:2842184)Curated
    Sequence conflicti95 – 951E → D in AAA60022. (PubMed:2712834)Curated
    Sequence conflicti116 – 1161A → R in AAA60022. (PubMed:2712834)Curated
    Sequence conflicti139 – 1391Q → E in CAA37673. (PubMed:2395659)Curated
    Sequence conflicti157 – 1571P → R in CAA37673. (PubMed:2395659)Curated
    Sequence conflicti212 – 2121P → A in CAA36422. (PubMed:2842184)Curated
    Sequence conflicti215 – 2151C → S in AAA60022. (PubMed:2712834)Curated
    Sequence conflicti294 – 2941S → T in AAA60022. (PubMed:2712834)Curated
    Sequence conflicti372 – 3721C → V in AAA60022. (PubMed:2712834)Curated
    Sequence conflicti383 – 3831D → N in CAA37673. (PubMed:2395659)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti15 – 151S → N.1 Publication
    Corresponds to variant rs17850347 [ dbSNP | Ensembl ].
    VAR_047960
    Natural varianti124 – 1241F → V.1 Publication
    Corresponds to variant rs17856254 [ dbSNP | Ensembl ].
    VAR_047961
    Natural varianti226 – 2261W → R.1 Publication
    Corresponds to variant rs17856253 [ dbSNP | Ensembl ].
    VAR_047962
    Natural varianti330 – 3301Y → H.1 Publication
    Corresponds to variant rs17851392 [ dbSNP | Ensembl ].
    VAR_047963
    Natural varianti360 – 3601V → A.1 Publication
    Corresponds to variant rs17850198 [ dbSNP | Ensembl ].
    VAR_047964

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei153 – 18533Missing in isoform 3. 2 PublicationsVSP_053360Add
    BLAST
    Alternative sequencei380 – 3867GTEDSTD → VLKVIFAVAFCLISAVLMVL LFIHIRRGLCWQRESYGNI in isoform 2. 1 PublicationVSP_036023

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M97589
    , M97580, M97581, M97582, M97583, M97584, M97585, M97586, M97587, M97588 Genomic DNA. Translation: AAA60021.1.
    M34840 mRNA. Translation: AAA69694.1.
    M24902 mRNA. Translation: AAA60022.1.
    X52174 mRNA. Translation: CAA36422.1.
    X53605 mRNA. Translation: CAA37673.1.
    U07097
    , U07083, U07085, U07086, U07088, U07091, U07092, U07093, U07095 Genomic DNA. Translation: AAB60640.1.
    AB102888 mRNA. Translation: BAD89417.1.
    AK300540 mRNA. Translation: BAG62248.1.
    AC020633 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW79203.1.
    CH471052 Genomic DNA. Translation: EAW79205.1.
    BC007460 mRNA. Translation: AAH07460.1.
    BC008493 mRNA. Translation: AAH08493.1.
    BC016344 mRNA. Translation: AAH16344.1.
    CCDSiCCDS3073.1. [P15309-1]
    CCDS46916.1. [P15309-2]
    PIRiJH0610.
    RefSeqiNP_001090.2. NM_001099.4. [P15309-1]
    NP_001127666.1. NM_001134194.1. [P15309-2]
    UniGeneiHs.433060.

    Genome annotation databases

    EnsembliENST00000336375; ENSP00000337471; ENSG00000014257. [P15309-1]
    ENST00000351273; ENSP00000323036; ENSG00000014257. [P15309-2]
    ENST00000475741; ENSP00000417744; ENSG00000014257. [P15309-3]
    GeneIDi55.
    KEGGihsa:55.
    UCSCiuc003eop.4. human. [P15309-2]
    uc010htp.2. human. [P15309-1]

    Polymorphism databases

    DMDMi130730.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M97589
    , M97580 , M97581 , M97582 , M97583 , M97584 , M97585 , M97586 , M97587 , M97588 Genomic DNA. Translation: AAA60021.1 .
    M34840 mRNA. Translation: AAA69694.1 .
    M24902 mRNA. Translation: AAA60022.1 .
    X52174 mRNA. Translation: CAA36422.1 .
    X53605 mRNA. Translation: CAA37673.1 .
    U07097
    , U07083 , U07085 , U07086 , U07088 , U07091 , U07092 , U07093 , U07095 Genomic DNA. Translation: AAB60640.1 .
    AB102888 mRNA. Translation: BAD89417.1 .
    AK300540 mRNA. Translation: BAG62248.1 .
    AC020633 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW79203.1 .
    CH471052 Genomic DNA. Translation: EAW79205.1 .
    BC007460 mRNA. Translation: AAH07460.1 .
    BC008493 mRNA. Translation: AAH08493.1 .
    BC016344 mRNA. Translation: AAH16344.1 .
    CCDSi CCDS3073.1. [P15309-1 ]
    CCDS46916.1. [P15309-2 ]
    PIRi JH0610.
    RefSeqi NP_001090.2. NM_001099.4. [P15309-1 ]
    NP_001127666.1. NM_001134194.1. [P15309-2 ]
    UniGenei Hs.433060.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CVI X-ray 3.20 A/B/C/D 33-374 [» ]
    1ND5 X-ray 2.90 A/B/C/D 33-386 [» ]
    1ND6 X-ray 2.40 A/B/C/D 33-386 [» ]
    2HPA X-ray 2.90 A/B/C/D 33-374 [» ]
    2L3H NMR - A 248-286 [» ]
    2L77 NMR - A 248-286 [» ]
    2L79 NMR - A 248-286 [» ]
    3PPD X-ray 1.50 A 260-265 [» ]
    DisProti DP00628.
    ProteinModelPortali P15309.
    SMRi P15309. Positions 33-375.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106571. 3 interactions.
    IntActi P15309. 3 interactions.
    MINTi MINT-6780778.
    STRINGi 9606.ENSP00000323036.

    Chemistry

    BindingDBi P15309.
    ChEMBLi CHEMBL2633.

    PTM databases

    PhosphoSitei P15309.

    Polymorphism databases

    DMDMi 130730.

    Proteomic databases

    MaxQBi P15309.
    PaxDbi P15309.
    PRIDEi P15309.

    Protocols and materials databases

    DNASUi 55.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000336375 ; ENSP00000337471 ; ENSG00000014257 . [P15309-1 ]
    ENST00000351273 ; ENSP00000323036 ; ENSG00000014257 . [P15309-2 ]
    ENST00000475741 ; ENSP00000417744 ; ENSG00000014257 . [P15309-3 ]
    GeneIDi 55.
    KEGGi hsa:55.
    UCSCi uc003eop.4. human. [P15309-2 ]
    uc010htp.2. human. [P15309-1 ]

    Organism-specific databases

    CTDi 55.
    GeneCardsi GC03P132036.
    HGNCi HGNC:125. ACPP.
    HPAi CAB000071.
    HPA004335.
    MIMi 171790. gene.
    neXtProti NX_P15309.
    PharmGKBi PA24449.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG85977.
    HOGENOMi HOG000231439.
    HOVERGENi HBG002203.
    KOi K14410.
    OMAi FTLPSWA.
    OrthoDBi EOG7GXPBJ.
    PhylomeDBi P15309.
    TreeFami TF312893.

    Enzyme and pathway databases

    SABIO-RK P15309.

    Miscellaneous databases

    EvolutionaryTracei P15309.
    GeneWikii Prostatic_acid_phosphatase.
    GenomeRNAii 55.
    NextBioi 221.
    PMAP-CutDB P15309.
    PROi P15309.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P15309.
    Bgeei P15309.
    CleanExi HS_ACPP.
    Genevestigatori P15309.

    Family and domain databases

    Gene3Di 3.40.50.1240. 1 hit.
    InterProi IPR000560. His_Pase_superF_clade-2.
    IPR029033. His_PPase_superfam.
    [Graphical view ]
    Pfami PF00328. His_Phos_2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53254. SSF53254. 1 hit.
    PROSITEi PS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
    PS00778. HIS_ACID_PHOSPHAT_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure of human prostatic acid phosphatase gene."
      Sharief F.S., Li S.S.-L.
      Biochem. Biophys. Res. Commun. 184:1468-1476(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    2. "Covalent structure, disulfide bonding, and identification of reactive surface and active site residues of human prostatic acid phosphatase."
      van Etten R.L., Davidson R., Stevis P.E., Macarthur H., Moore D.L.
      J. Biol. Chem. 266:2313-2319(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS, ACTIVE SITE.
    3. "Human prostatic acid phosphatase: cDNA cloning, gene mapping and protein sequence homology with lysosomal acid phosphatase."
      Sharief F.S., Lee H., Leuderman M.M., Lundwall A., Deaven L.L., Lee C.-L., Li S.S.-L.
      Biochem. Biophys. Res. Commun. 160:79-86(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "Molecular cloning and sequence analysis of cDNA encoding human prostatic acid phosphatase."
      Vihko P., Virkkunen P., Henttu P., Roiko K., Solin T., Huhtala M.L.
      FEBS Lett. 236:275-281(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
      Tissue: Prostate.
    5. "Nucleotide sequence of human prostatic acid phosphatase determined from a full-length cDNA clone."
      Tailor P.G., Govindan M.V., Patel P.C.
      Nucleic Acids Res. 18:4928-4928(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Prostate.
    6. "Nucleotide sequence of human prostatic acid phosphatase ACPP gene, including seven Alu repeats."
      Sharief F.S., Li S.S.-L.
      Biochem. Mol. Biol. Int. 33:561-565(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    7. "Acid phosphatase prostate mRNA,nirs splice variant1."
      Sameshima E., Tabata Y., Hayashi A., Iida K., Mitsuyama M., Kanai S., Furuya T., Saito T.
      Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    8. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Prostate.
    9. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. "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] (ISOFORMS 1 AND 2), VARIANTS ASN-15; VAL-124; ARG-226; HIS-330 AND ALA-360.
      Tissue: Prostate.
    12. "Structures of the carbohydrate moieties of human prostatic acid phosphatase elucidated by H1 nuclear magnetic resonance spectroscopy."
      Risley J.M., Van Etten R.L.
      Arch. Biochem. Biophys. 258:404-412(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE OF CARBOHYDRATES.
    13. "Covalent modification and site-directed mutagenesis of an active site tryptophan of human prostatic acid phosphatase."
      Zhang Z., Ostanin K., Van Etten R.L.
      Acta Biochim. Pol. 44:659-672(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, ENZYME REGULATION, MUTAGENESIS OF TRP-206.
    14. "Prostatic acid phosphatase degrades lysophosphatidic acid in seminal plasma."
      Tanaka M., Kishi Y., Takanezawa Y., Kakehi Y., Aoki J., Arai H.
      FEBS Lett. 571:197-204(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME ACTIVITY.
    15. Cited for: ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    16. Cited for: PROTEOLYTIC PROCESSING, IDENTIFICATION BY MASS SPECTROMETRY, ROLE IN HIV INFECTION.
    17. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Placenta.
    18. "Fibrils of prostatic acid phosphatase fragments boost infections with XMRV (xenotropic murine leukemia virus-related virus), a human retrovirus associated with prostate cancer."
      Hong S., Klein E.A., Das Gupta J., Hanke K., Weight C.J., Nguyen C., Gaughan C., Kim K.A., Bannert N., Kirchhoff F., Munch J., Silverman R.H.
      J. Virol. 83:6995-7003(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING, ROLE IN XMRV INFECTION.
    19. "The main green tea polyphenol epigallocatechin-3-gallate counteracts semen-mediated enhancement of HIV infection."
      Hauber I., Hohenberg H., Holstermann B., Hunstein W., Hauber J.
      Proc. Natl. Acad. Sci. U.S.A. 106:9033-9038(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEGRADATION OF SEVI AMYLOID FIBRILS.
    20. "Aminoquinoline surfen inhibits the action of SEVI (semen-derived enhancer of viral infection)."
      Roan N.R., Sowinski S., Munch J., Kirchhoff F., Greene W.C.
      J. Biol. Chem. 285:1861-1869(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INHIBITION OF SEVI ACTIVITY.
    21. "Human prostatic acid phosphatase, an authentic tyrosine phosphatase, dephosphorylates ErbB-2 and regulates prostate cancer cell growth."
      Chuang T.D., Chen S.J., Lin F.F., Veeramani S., Kumar S., Batra S.K., Tu Y., Lin M.F.
      J. Biol. Chem. 285:23598-23606(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    22. "Prostatic acid phosphatase expression in human tissues."
      Graddis T.J., McMahan C.J., Tamman J., Page K.J., Trager J.B.
      Int. J. Clin. Exp. Pathol. 4:295-306(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    23. "Structural origins of L(+)-tartrate inhibition of human prostatic acid phosphatase."
      Lacount M.W., Handy G., Lebioda L.
      J. Biol. Chem. 273:30406-30409(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH N-PROPYL-L-TARTRAMATE.
    24. "Crystal structure of human prostatic acid phosphatase."
      Jakob C.G., Lewinski K., Kuciel R., Ostrowski W., Lebioda L.
      Prostate 42:211-218(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 33-374, DISULFIDE BONDS, GLYCOSYLATION AT ASN-94 AND ASN-220.
    25. "Crystal structures of human prostatic acid phosphatase in complex with a phosphate ion and alpha-benzylaminobenzylphosphonic acid update the mechanistic picture and offer new insights into inhibitor design."
      Ortlund E., LaCount M.W., Lebioda L.
      Biochemistry 42:383-389(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 33-386 IN COMPLEX WITH A PHOSPHATE ION AND INHIBITOR ALPHA-BENZYLAMINOBENZYLPHOSPHONIC ACID, DISULFIDE BONDS, GLYCOSYLATION AT ASN-220 AND ASN-333.
    26. "NMR structure in a membrane environment reveals putative amyloidogenic regions of the SEVI precursor peptide PAP(248-286)."
      Nanga R.P., Brender J.R., Vivekanandan S., Popovych N., Ramamoorthy A.
      J. Am. Chem. Soc. 131:17972-17979(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 248-286.

    Entry informationi

    Entry nameiPPAP_HUMAN
    AccessioniPrimary (citable) accession number: P15309
    Secondary accession number(s): D3DNC6
    , Q5FBY0, Q96KY0, Q96QK9, Q96QM0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: March 1, 1992
    Last modified: October 1, 2014
    This is version 143 of the entry and version 3 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

    Miscellaneous

    Used as a diagnostic tool for staging metastatic prostatic cancer.

    Keywords - Technical termi

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

    Documents

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

    External Data

    Dasty 3