P15309 (PPAP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	386 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.11 Ref.13 Ref.15 Ref.18 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.11 Ref.13 Ref.15 Ref.18
Catalytic activity	A phosphate monoester + H2O = an alcohol + phosphate. Ref.11 A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate. Ref.11
Enzyme regulation	Phosphatase activity inhibited by L+-tartrate, and by its derivative, alpha-benzylaminobenzylphosphonic acid. Ref.10
Subunit structure	Homodimer; dimer formation is required for phosphatase activity By similarity.
Subcellular location	Isoform 1: Secreted Ref.12 Ref.14. 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.12 Ref.14
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 decreased in prostate cancer. Ref.12 Ref.19
Post-translational modification	N-glycosylated. High mannose content, partially sialylated and fucosylated biantennary complex. Also fucosylated with partially sialylated triantennary complex oligosaccharides. Ref.9 Ref.21 Ref.22 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.13 Ref.15
Miscellaneous	Used as a diagnostic tool for staging metastatic prostatic cancer.
Sequence similarities	Belongs to the histidine acid phosphatase family.

Ontologies

Keywords
Cellular component	Amyloid Cell membrane Lysosome Membrane Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal
Molecular function	Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	adenosine metabolic process Inferred from electronic annotation. Source: Compara nucleotide metabolic process Inferred from electronic annotation. Source: Compara purine nucleobase metabolic process Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi cisterna Inferred from electronic annotation. Source: Compara apical part of cell Inferred from electronic annotation. Source: Compara extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell filopodium Inferred from electronic annotation. Source: Compara integral to membrane Inferred from electronic annotation. Source: Compara intracellular Inferred from direct assay PubMed 17658863. Source: UniProtKB lysosomal membrane Inferred from electronic annotation. Source: UniProtKB-SubCell multivesicular body Inferred from electronic annotation. Source: Compara plasma membrane Inferred from direct assay PubMed 17658863. Source: UniProtKB secretory granule Inferred from electronic annotation. Source: Compara
Molecular_function	5'-nucleotidase activity Inferred from electronic annotation. Source: EC acid phosphatase activity Inferred from electronic annotation. Source: EC choline binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-1222012,EBI-1222012

Alternative products

This entry describes 2 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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 32

32

Chain

33 – 386

354

Prostatic acid phosphatase

PRO_0000023963

Peptide

248 – 286

39

PAPf39

PRO_0000411250

Sites

Active site

44

1

Nucleophile Ref.2

Active site

290

1

Proton donor Probable

Binding site

43

1

Substrate

Binding site

47

1

Substrate

Binding site

111

1

Substrate

Binding site

289

1

Substrate

Site

49

1

Important for substrate specificity

Site

138

1

Required for homodimerization By similarity

Site

144

1

Required for homodimerization By similarity

Site

206

1

Required for structural stability

Amino acid modifications

Glycosylation

94

1

N-linked (GlcNAc...) Ref.21

Glycosylation

220

1

N-linked (GlcNAc...) Ref.21 Ref.22

Glycosylation

333

1

N-linked (GlcNAc...) Ref.22

Disulfide bond

161 ↔ 372

Ref.2 Ref.21 Ref.22

Disulfide bond

215 ↔ 313

Ref.2 Ref.21 Ref.22

Disulfide bond

347 ↔ 351

Ref.2 Ref.21 Ref.22

Natural variations

Alternative sequence

380 – 386

7

GTEDSTD → VLKVIFAVAFCLISAVLMVL LFIHIRRGLCWQRESYGNI in isoform 2.

VSP_036023

Natural variant

15

1

S → N. Ref.8
Corresponds to variant rs17850347 [ dbSNP | Ensembl ].

VAR_047960

Natural variant

124

1

F → V. Ref.8
Corresponds to variant rs17856254 [ dbSNP | Ensembl ].

VAR_047961

Natural variant

226

1

W → R. Ref.8
Corresponds to variant rs17856253 [ dbSNP | Ensembl ].

VAR_047962

Natural variant

330

1

Y → H. Ref.8
Corresponds to variant rs17851392 [ dbSNP | Ensembl ].

VAR_047963

Natural variant

360

1

V → A. Ref.8
Corresponds to variant rs17850198 [ dbSNP | Ensembl ].

VAR_047964

Experimental info

Mutagenesis

206

1

W → F: Greatly reduced enzyme activity, marked decrease in structural stability, and increased binding of the inhibitor, L(+)-tartrate. Ref.10

Mutagenesis

206

1

W → L: Reduced enzyme activity, marked decrease in structural stability, and increased binding of the inhibitor, L(+)-tartrate. Ref.10

Sequence conflict

15 – 24

10

SLGFLFLLFF → AFASCFCFFC in CAA37673. Ref.5

Sequence conflict

15 – 24

10

SLGFLFLLFF → ALASCFCFFC in AAA60022. Ref.3

Sequence conflict

15 – 24

10

SLGFLFLLFF → ALASCFCFFC in CAA36422. Ref.4

Sequence conflict

46

1

D → H in CAA37673. Ref.5

Sequence conflict

66 – 73

8

GFGQLTQL → RIWPTHPA in CAA37673. Ref.5

Sequence conflict

66 – 73

8

GFGQLTQL → WIWPTHPA in CAA36422. Ref.4

Sequence conflict

95

1

E → D in AAA60022. Ref.3

Sequence conflict

116

1

A → R in AAA60022. Ref.3

Sequence conflict

139

1

Q → E in CAA37673. Ref.5

Sequence conflict

157

1

P → R in CAA37673. Ref.5

Sequence conflict

212

1

P → A in CAA36422. Ref.4

Sequence conflict

215

1

C → S in AAA60022. Ref.3

Sequence conflict

294

1

S → T in AAA60022. Ref.3

Sequence conflict

372

1

C → V in AAA60022. Ref.3

Sequence conflict

383

1

D → N in CAA37673. Ref.5

Secondary structure

1

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386

Helix Strand Turn

Details...

Beta strand

34 – 43

10

Helix

60 – 62

3

Helix

72 – 88

17

Turn

89 – 93

5

Helix

99 – 101

3

Beta strand

102 – 108

7

Helix

110 – 123

14

Helix

128 – 130

3

Beta strand

134 – 136

3

Beta strand

144 – 146

3

Helix

148 – 150

3

Beta strand

152 – 155

4

Helix

162 – 173

12

Helix

175 – 181

7

Helix

182 – 184

3

Helix

185 – 195

11

Helix

202 – 208

7

Helix

210 – 218

9

Helix

229 – 247

19

Beta strand

248 – 251

4

Helix

252 – 258

7

Helix

261 – 276

16

Beta strand

277 – 279

3

Beta strand

282 – 288

7

Helix

290 – 299

10

Beta strand

313 – 321

9

Beta strand

324 – 332

9

Beta strand

335 – 337

3

Beta strand

340 – 342

3

Beta strand

349 – 352

4

Helix

353 – 360

8

Helix

361 – 363

3

Helix

368 – 371

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Secreted PAP) (sPAP) [UniParc]. Last modified March 1, 1992. Version 3. Checksum: EF81E11DFAECADEA	FASTA	386	44,566
	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
	Isoform 2 (TMPase) (TM-PAP) (cellular PAP) (cPAP) [UniParc]. Checksum: 68E1131197595362	FASTA	418	48,336
	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 370 380 390 400 410 GPVIPQDWST ECMTTNSHQV LKVIFAVAFC LISAVLMVLL FIHIRRGLCW QRESYGNI

References

	« Hide 'large scale' referencesShow '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]	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. , 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].
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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. , Keppler O.T., Forssmann W.G., Kirchhoff F. Cell 131:1059-1071(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEOLYTIC PROCESSING, MASS SPECTROMETRY, ROLE IN HIV INFECTION.
[14]	"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], MASS SPECTROMETRY. Tissue: Placenta.
[15]	"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.
[16]	"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.
[17]	"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.
[18]	"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.
[19]	"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.
[20]	"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.
[21]	"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.
[22]	"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.
[23]	"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 , 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.
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.

IPI

IPI00289983.
IPI00396434.

PIR

JH0610.

RefSeq

NP_001090.2. NM_001099.4.
NP_001127666.1. NM_001134194.1.

UniGene

Hs.433060.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P15309.

ModBase

Search...

Protein-protein interaction databases

IntAct

P15309. 1 interaction.

STRING

9606.ENSP00000323036.

PTM databases

PhosphoSite

P15309.

Polymorphism databases

DMDM

130730.

Proteomic databases

PaxDb

P15309.

PRIDE

P15309.

Protocols and materials databases

DNASU

55.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000336375; ENSP00000337471; ENSG00000014257.
ENST00000351273; ENSP00000323036; ENSG00000014257.

GeneID

55.

KEGG

hsa:55.

UCSC

uc003eop.4. human.
uc010htp.2. human.

Organism-specific databases

CTD

55.

GeneCards

GC03P132036.

HGNC

HGNC:125. ACPP.

HPA

CAB000071.
HPA004335.

MIM

171790. gene.

neXtProt

NX_P15309.

PharmGKB

PA24449.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG85977.

HOGENOM

HOG000231439.

HOVERGEN

HBG002203.

KO

K14410.

OMA

FTLPSWA.

OrthoDB

EOG4NKBVM.

Enzyme and pathway databases

SABIO-RK

P15309.

Gene expression databases

ArrayExpress

P15309.

Bgee

P15309.

CleanEx

HS_ACPP.

Genevestigator

P15309.

GermOnline

ENSG00000014257. Homo sapiens.

Family and domain databases

InterPro

IPR000560. His_Pase_superF_clade-2.
[Graphical view]

Pfam

PF00328. His_Phos_2. 1 hit.
[Graphical view]

PROSITE

PS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
PS00778. HIS_ACID_PHOSPHAT_2. 1 hit.
[Graphical view]

ProtoNet

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Other

BindingDB

P15309.

ChEMBL

CHEMBL2633.

EvolutionaryTrace

P15309.

GenomeRNAi

55.

NextBio

221.

PMAP-CutDB

P15309.

SOURCE

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Entry information

Entry name

PPAP_HUMAN

Accession

Primary (citable) accession number: P15309
Secondary accession number(s): D3DNC6 , Q96KY0, Q96QK9, Q96QM0

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	March 1, 1992
Last modified:	May 1, 2013
This is version 128 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.