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P15309 (PPAP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Prostatic acid phosphatase

Short name=PAP
EC=3.1.3.2
Alternative name(s):
5'-nucleotidase
Short name=5'-NT
EC=3.1.3.5
Ecto-5'-nucleotidase
Thiamine monophosphatase
Short name=TMPase

Cleaved into the following chain:

  1. PAPf39
Gene names
Name:ACPP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length386 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.14 Ref.16 Ref.18 Ref.21

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. Ref.14 Ref.16 Ref.18 Ref.21

Catalytic activity

A phosphate monoester + H2O = an alcohol + phosphate. Ref.14

A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate. Ref.14

Enzyme regulation

Phosphatase activity inhibited by L+-tartrate, and by its derivative, alpha-benzylaminobenzylphosphonic acid. Ref.13

Subunit structure

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

Subcellular location

Isoform 1: Secreted Ref.15 Ref.17.

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. Ref.15 Ref.17

Tissue specificity

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 decreasedin prostate cancer. Ref.15 Ref.22

Post-translational modification

N-glycosylated. High mannose content, partially sialylated and fucosylated biantennary complex. Also fucosylated with partially sialylated triantennary complex oligosaccharides. Ref.12 Ref.24 Ref.25

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. Ref.16 Ref.18

Miscellaneous

Used as a diagnostic tool for staging metastatic prostatic cancer.

Sequence similarities

Belongs to the histidine acid phosphatase family.

Ontologies

Keywords
   Cellular componentAmyloid
Cell membrane
Lysosome
Membrane
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processadenosine metabolic process

Inferred from direct assay PubMed 18940592. Source: UniProt

dephosphorylation

Inferred from mutant phenotype PubMed 8132635. Source: UniProt

nucleotide metabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of adenosine receptor signaling pathway

Inferred from mutant phenotype PubMed 18940592PubMed 22389722. Source: UniProt

purine nucleobase metabolic process

Inferred from electronic annotation. Source: Ensembl

regulation of sensory perception of pain

Inferred from mutant phenotype PubMed 18940592PubMed 22389722. Source: UniProt

thiamine metabolic process

Inferred from sequence or structural similarity. Source: UniProt

   Cellular_componentGolgi cisterna

Inferred from electronic annotation. Source: Ensembl

apical part of cell

Inferred from electronic annotation. Source: Ensembl

extracellular space

Inferred from direct assay Ref.14. Source: UniProt

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

filopodium

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Inferred from electronic annotation. Source: Ensembl

intracellular

Inferred from direct assay PubMed 17658863. Source: UniProtKB

lysosomal membrane

Inferred from direct assay Ref.17. Source: UniProtKB

multivesicular body

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 21630459. Source: UniProt

plasma membrane

Inferred from direct assay PubMed 17658863. Source: UniProtKB

secretory granule

Inferred from electronic annotation. Source: Ensembl

vesicle membrane

Inferred from sequence or structural similarity. Source: UniProt

   Molecular_function5'-nucleotidase activity

Inferred from direct assay PubMed 18940592. Source: UniProt

acid phosphatase activity

Inferred from mutant phenotype PubMed 8132635. Source: UniProt

choline binding

Inferred from electronic annotation. Source: Ensembl

identical protein binding

Inferred from physical interaction Ref.16. Source: IntAct

lysophosphatidic acid phosphatase activity

Inferred from direct assay Ref.14. Source: UniProt

phosphatase activity

Inferred from mutant phenotype PubMed 18940592PubMed 22389722. Source: UniProt

protein binding

Inferred from physical interaction PubMed 11067847PubMed 9705354. Source: IntAct

thiamine phosphate phosphatase activity

Inferred from sequence or structural similarity. Source: UniProt

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-1222012,EBI-1222012
ERBB2P046263EBI-1222012,EBI-641062

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P15309-1)

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.
Isoform 2 (identifier: P15309-2)

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
Isoform 3 (identifier: P15309-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232
Chain33 – 386354Prostatic acid phosphatase
PRO_0000023963
Peptide248 – 28639PAPf39
PRO_0000411250

Sites

Active site441Nucleophile Ref.2
Active site2901Proton donor Probable
Binding site431Substrate
Binding site471Substrate
Binding site1111Substrate
Binding site2891Substrate
Site491Important for substrate specificity
Site1381Required for homodimerization By similarity
Site1441Required for homodimerization By similarity
Site2061Required for structural stability

Amino acid modifications

Glycosylation941N-linked (GlcNAc...) Ref.24
Glycosylation2201N-linked (GlcNAc...) Ref.24 Ref.25
Glycosylation3331N-linked (GlcNAc...) Ref.25
Disulfide bond161 ↔ 372 Ref.2 Ref.24 Ref.25
Disulfide bond215 ↔ 313 Ref.2 Ref.24 Ref.25
Disulfide bond347 ↔ 351 Ref.2 Ref.24 Ref.25

Natural variations

Alternative sequence153 – 18533Missing in isoform 3.
VSP_053360
Alternative sequence380 – 3867GTEDSTD → VLKVIFAVAFCLISAVLMVL LFIHIRRGLCWQRESYGNI in isoform 2.
VSP_036023
Natural variant151S → N. Ref.11
Corresponds to variant rs17850347 [ dbSNP | Ensembl ].
VAR_047960
Natural variant1241F → V. Ref.11
Corresponds to variant rs17856254 [ dbSNP | Ensembl ].
VAR_047961
Natural variant2261W → R. Ref.11
Corresponds to variant rs17856253 [ dbSNP | Ensembl ].
VAR_047962
Natural variant3301Y → H. Ref.11
Corresponds to variant rs17851392 [ dbSNP | Ensembl ].
VAR_047963
Natural variant3601V → A. Ref.11
Corresponds to variant rs17850198 [ dbSNP | Ensembl ].
VAR_047964

Experimental info

Mutagenesis2061W → F: Greatly reduced enzyme activity, marked decrease in structural stability, and increased binding of the inhibitor, L(+)-tartrate. Ref.13
Mutagenesis2061W → L: Reduced enzyme activity, marked decrease in structural stability, and increased binding of the inhibitor, L(+)-tartrate. Ref.13
Sequence conflict15 – 2410SLGFLFLLFF → AFASCFCFFC in CAA37673. Ref.5
Sequence conflict15 – 2410SLGFLFLLFF → ALASCFCFFC in AAA60022. Ref.3
Sequence conflict15 – 2410SLGFLFLLFF → ALASCFCFFC in CAA36422. Ref.4
Sequence conflict461D → H in CAA37673. Ref.5
Sequence conflict66 – 738GFGQLTQL → RIWPTHPA in CAA37673. Ref.5
Sequence conflict66 – 738GFGQLTQL → WIWPTHPA in CAA36422. Ref.4
Sequence conflict951E → D in AAA60022. Ref.3
Sequence conflict1161A → R in AAA60022. Ref.3
Sequence conflict1391Q → E in CAA37673. Ref.5
Sequence conflict1571P → R in CAA37673. Ref.5
Sequence conflict2121P → A in CAA36422. Ref.4
Sequence conflict2151C → S in AAA60022. Ref.3
Sequence conflict2941S → T in AAA60022. Ref.3
Sequence conflict3721C → V in AAA60022. Ref.3
Sequence conflict3831D → N in CAA37673. Ref.5

Secondary structure

.......................................................... 386
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Secreted PAP) (sPAP) [UniParc].

Last modified March 1, 1992. Version 3.
Checksum: EF81E11DFAECADEA

FASTA38644,566
        10         20         30         40         50         60 
MRAAPLLLAR AASLSLGFLF LLFFWLDRSV LAKELKFVTL VFRHGDRSPI DTFPTDPIKE 

        70         80         90        100        110        120 
SSWPQGFGQL TQLGMEQHYE LGEYIRKRYR KFLNESYKHE QVYIRSTDVD RTLMSAMTNL 

       130        140        150        160        170        180 
AALFPPEGVS IWNPILLWQP IPVHTVPLSE DQLLYLPFRN CPRFQELESE TLKSEEFQKR 

       190        200        210        220        230        240 
LHPYKDFIAT LGKLSGLHGQ DLFGIWSKVY DPLYCESVHN FTLPSWATED TMTKLRELSE 

       250        260        270        280        290        300 
LSLLSLYGIH KQKEKSRLQG GVLVNEILNH MKRATQIPSY KKLIMYSAHD TTVSGLQMAL 

       310        320        330        340        350        360 
DVYNGLLPPY ASCHLTELYF EKGEYFVEMY YRNETQHEPY PLMLPGCSPS CPLERFAELV 

       370        380 
GPVIPQDWST ECMTTNSHQG TEDSTD 

« Hide

Isoform 2 (TMPase) (TM-PAP) (cellular PAP) (cPAP) [UniParc].

Checksum: 68E1131197595362
Show »

FASTA41848,336
Isoform 3 [UniParc].

Checksum: C3E376122B63DA82
Show »

FASTA35340,443

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Prostatic acid phosphatase is not a prostate specific target."
Quintero I.B., Araujo C.L., Pulkka A.E., Wirkkala R.S., Herrala A.M., Eskelinen E.-L., Jokitalo E., Hellstroem P.A., Tuominen H.J., Hirvikoski P.P., Vihko P.T.
Cancer Res. 67:6549-6554(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[16]"Semen-derived amyloid fibrils drastically enhance HIV infection."
Munch J., Rucker E., Standker L., Adermann K., Goffinet C., Schindler M., Wildum S., Chinnadurai R., Rajan D., Specht A., Gimenez-Gallego G., Sanchez P.C., Fowler D.M., Koulov A., Kelly J.W., Mothes W., Grivel J.C., Margolis L. expand/collapse author list , Keppler O.T., Forssmann W.G., Kirchhoff F.
Cell 131:1059-1071(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING, IDENTIFICATION BY MASS SPECTROMETRY, ROLE IN HIV INFECTION.
[17]"Integral and associated lysosomal membrane proteins."
Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B., Schaefer H., Elsaesser H.-P., Mann M., Hasilik A.
Traffic 8:1676-1686(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M97589 expand/collapse EMBL AC list , 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 expand/collapse EMBL AC list , 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.
CCDSCCDS3073.1. [P15309-1]
CCDS46916.1. [P15309-2]
PIRJH0610.
RefSeqNP_001090.2. NM_001099.4. [P15309-1]
NP_001127666.1. NM_001134194.1. [P15309-2]
UniGeneHs.433060.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
DisProtDP00628.
ProteinModelPortalP15309.
SMRP15309. Positions 33-375.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106571. 3 interactions.
IntActP15309. 3 interactions.
MINTMINT-6780778.
STRING9606.ENSP00000323036.

Chemistry

BindingDBP15309.
ChEMBLCHEMBL2633.

PTM databases

PhosphoSiteP15309.

Polymorphism databases

DMDM130730.

Proteomic databases

MaxQBP15309.
PaxDbP15309.
PRIDEP15309.

Protocols and materials databases

DNASU55.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000336375; ENSP00000337471; ENSG00000014257. [P15309-1]
ENST00000351273; ENSP00000323036; ENSG00000014257. [P15309-2]
ENST00000475741; ENSP00000417744; ENSG00000014257. [P15309-3]
GeneID55.
KEGGhsa:55.
UCSCuc003eop.4. human. [P15309-2]
uc010htp.2. human. [P15309-1]

Organism-specific databases

CTD55.
GeneCardsGC03P132036.
HGNCHGNC:125. ACPP.
HPACAB000071.
HPA004335.
MIM171790. gene.
neXtProtNX_P15309.
PharmGKBPA24449.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG85977.
HOGENOMHOG000231439.
HOVERGENHBG002203.
KOK14410.
OMAFTLPSWA.
OrthoDBEOG7GXPBJ.
PhylomeDBP15309.
TreeFamTF312893.

Enzyme and pathway databases

SABIO-RKP15309.

Gene expression databases

ArrayExpressP15309.
BgeeP15309.
CleanExHS_ACPP.
GenevestigatorP15309.

Family and domain databases

Gene3D3.40.50.1240. 1 hit.
InterProIPR000560. His_Pase_superF_clade-2.
IPR029033. His_PPase_superfam.
[Graphical view]
PfamPF00328. His_Phos_2. 1 hit.
[Graphical view]
SUPFAMSSF53254. SSF53254. 1 hit.
PROSITEPS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
PS00778. HIS_ACID_PHOSPHAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP15309.
GeneWikiProstatic_acid_phosphatase.
GenomeRNAi55.
NextBio221.
PMAP-CutDBP15309.
PROP15309.
SOURCESearch...

Entry information

Entry namePPAP_HUMAN
AccessionPrimary (citable) accession number: P15309
Secondary accession number(s): D3DNC6 expand/collapse secondary AC list , Q5FBY0, Q96KY0, Q96QK9, Q96QM0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: March 1, 1992
Last modified: July 9, 2014
This is version 141 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM