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P15309

- PPAP_HUMAN

UniProt

P15309 - PPAP_HUMAN

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Protein

Prostatic acid phosphatase

Gene

ACPP

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

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. 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
Complete GO annotation...

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: UniProtKB
  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
Complete GO annotation...

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

BgeeiP15309.
CleanExiHS_ACPP.
ExpressionAtlasiP15309. baseline and differential.
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. 5 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.
GeneTreeiENSGT00530000062956.
HOGENOMiHOG000231439.
HOVERGENiHBG002203.
InParanoidiP15309.
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

        10         20         30         40         50
MRAAPLLLAR AASLSLGFLF LLFFWLDRSV LAKELKFVTL VFRHGDRSPI
60 70 80 90 100
DTFPTDPIKE SSWPQGFGQL TQLGMEQHYE LGEYIRKRYR KFLNESYKHE
110 120 130 140 150
QVYIRSTDVD RTLMSAMTNL AALFPPEGVS IWNPILLWQP IPVHTVPLSE
160 170 180 190 200
DQLLYLPFRN CPRFQELESE TLKSEEFQKR LHPYKDFIAT LGKLSGLHGQ
210 220 230 240 250
DLFGIWSKVY DPLYCESVHN FTLPSWATED TMTKLRELSE LSLLSLYGIH
260 270 280 290 300
KQKEKSRLQG GVLVNEILNH MKRATQIPSY KKLIMYSAHD TTVSGLQMAL
310 320 330 340 350
DVYNGLLPPY ASCHLTELYF EKGEYFVEMY YRNETQHEPY PLMLPGCSPS
360 370 380
CPLERFAELV GPVIPQDWST ECMTTNSHQG TEDSTD
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]
NP_001278966.1. NM_001292037.1. [P15309-3]
UniGeneiHs.433060.

Genome annotation databases

EnsembliENST00000336375; ENSP00000337471; ENSG00000014257. [P15309-1]
ENST00000351273; ENSP00000323036; ENSG00000014257. [P15309-2]
ENST00000475741; ENSP00000417744; ENSG00000014257. [P15309-3]
GeneIDi55.
KEGGihsa:55.
UCSCiuc003eon.3. human.
uc003eop.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 ]
NP_001278966.1. NM_001292037.1. [P15309-3 ]
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. 5 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 uc003eon.3. human.
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.
GeneTreei ENSGT00530000062956.
HOGENOMi HOG000231439.
HOVERGENi HBG002203.
InParanoidi P15309.
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

Bgeei P15309.
CleanExi HS_ACPP.
ExpressionAtlasi P15309. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 144 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