ACP1

Acid phosphatase 1, soluble

PDB rendering based on 1bvh.

Available structures
PDB	1XWW, 5PNT

Identifiers

Symbols

ACP1; HAAP; MGC111030; MGC3499

External IDs

OMIM: 171500 HomoloGene: 38274 GeneCards: ACP1 Gene

Gene Ontology
Molecular function	• acid phosphatase activity • non-membrane spanning protein tyrosine phosphatase activity • hydrolase activity • identical protein binding
Cellular component	• soluble fraction • nucleus • cytoplasm • internal side of plasma membrane
Biological process	• protein amino acid dephosphorylation
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

n/a

n/a

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 2:
0.26 – 0.28 Mb

n/a

PubMed search

[1]

[2]

Low molecular weight phosphotyrosine protein phosphatase is an enzyme that in humans is encoded by the ACP1 gene.

The product of this gene belongs to the phosphotyrosine protein phosphatase family of proteins. It functions as an acid phosphatase and a protein tyrosine phosphatase by hydrolyzing protein tyrosine phosphate to protein tyrosine and orthophosphate. This enzyme also hydrolyzes orthophosphoric monoesters to alcohol and orthophosphate. This gene is genetically polymorphic, and three common alleles segregating at the corresponding locus give rise to six phenotypes. Each allele appears to encode at least two electrophoretically different isozymes, Bf and Bs, which are produced in allele-specific ratios. Three transcript variants encoding distinct isoforms have been identified for this gene.^[1]

Interactions

ACP1 has been shown to interact with EPH receptor A2^[2] and EPH receptor B1.^[3]

References

^ "Entrez Gene: ACP1 acid phosphatase 1, soluble". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=52.
^ Kikawa, Keith D; Vidale Derika R, Van Etten Robert L, Kinch Michael S (Oct. 2002). "Regulation of the EphA2 kinase by the low molecular weight tyrosine phosphatase induces transformation". J. Biol. Chem. (United States) 277 (42): 39274–9. doi:10.1074/jbc.M207127200. ISSN 0021-9258. PMID 12167657.
^ Stein, E; Lane A A, Cerretti D P, Schoecklmann H O, Schroff A D, Van Etten R L, Daniel T O (Mar. 1998). "Eph receptors discriminate specific ligand oligomers to determine alternative signaling complexes, attachment, and assembly responses". Genes Dev. (UNITED STATES) 12 (5): 667–78. doi:10.1101/gad.12.5.667. ISSN 0890-9369. PMC 316584. PMID 9499402. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=316584.

Junien C, Kaplan JC, Bernheim A, Berger R (1979). "Regional assignment of red cell acid phosphatase locus to band 2p25.". Hum. Genet. 48 (1): 17–21. doi:10.1007/BF00273269. PMID 457131.
Sensabaugh GF, Golden VL (1979). "Phenotype dependence in the inhibition of red cell acid phosphatase (ACP) by folates.". Am. J. Hum. Genet. 30 (5): 553–60. PMC 1685602. PMID 736044. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1685602.
Shekels LL, Smith AJ, Van Etten RL, Bernlohr DA (1993). "Identification of the adipocyte acid phosphatase as a PAO-sensitive tyrosyl phosphatase.". Protein Sci. 1 (6): 710–21. doi:10.1002/pro.5560010603. PMC 2142247. PMID 1304913. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2142247.
Wo YY, McCormack AL, Shabanowitz J, et al. (1992). "Sequencing, cloning, and expression of human red cell-type acid phosphatase, a cytoplasmic phosphotyrosyl protein phosphatase.". J. Biol. Chem. 267 (15): 10856–65. PMID 1587862.
Dissing J, Johnsen AH (1992). "Human red cell acid phosphatase (ACP1): the primary structure of the two pairs of isozymes encoded by the ACP1*A and ACP1*C alleles.". Biochim. Biophys. Acta 1121 (3): 261–8. doi:10.1016/0167-4838(92)90155-7. PMID 1627603.
Dissing J, Johnsen AH, Sensabaugh GF (1991). "Human red cell acid phosphatase (ACP1). The amino acid sequence of the two isozymes Bf and Bs encoded by the ACP1*B allele.". J. Biol. Chem. 266 (31): 20619–25. PMID 1939112.
Wakita Y, Narahara K, Takahashi Y, et al. (1986). "Duplication of 2p25: confirmation of the assignment of soluble acid phosphatase (ACP1) locus to 2p25.". Hum. Genet. 71 (3): 259–60. doi:10.1007/BF00284586. PMID 4065897.
Blake NM, Kirk RL, Barnes KR, Thompson JM (1974). "Expression of human red cell acid phosphatase activity in placenta and other tissues.". Jinrui Idengaku Zasshi 18 (1): 10–23. PMID 4356849.
Sensabaugh GF, Lazaruk KA (1993). "A TaqI site identifies the *A allele at the ACP1 locus.". Hum. Mol. Genet. 2 (7): 1079. doi:10.1093/hmg/2.7.1079-a. PMID 8364553.
Bryson GL, Massa H, Trask BJ, Van Etten RL (1996). "Gene structure, sequence, and chromosomal localization of the human red cell-type low-molecular-weight acid phosphotyrosyl phosphatase gene, ACP1.". Genomics 30 (2): 133–40. doi:10.1006/geno.1995.9893. PMID 8586411.
Tailor P, Gilman J, Williams S, et al. (1997). "Regulation of the low molecular weight phosphotyrosine phosphatase by phosphorylation at tyrosines 131 and 132.". J. Biol. Chem. 272 (9): 5371–4. doi:10.1074/jbc.272.9.5371. PMID 9038134.
Stein E, Lane AA, Cerretti DP, et al. (1998). "Eph receptors discriminate specific ligand oligomers to determine alternative signaling complexes, attachment, and assembly responses.". Genes Dev. 12 (5): 667–78. doi:10.1101/gad.12.5.667. PMC 316584. PMID 9499402. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=316584.
Modesti A, Marzocchini R, Raugei G, et al. (1998). "Cloning, expression and characterisation of a new human low Mr phosphotyrosine protein phosphatase originating by alternative splicing.". FEBS Lett. 431 (1): 111–5. doi:10.1016/S0014-5793(98)00732-7. PMID 9684876.
Zhang M, Stauffacher CV, Lin D, Van Etten RL (1998). "Crystal structure of a human low molecular weight phosphotyrosyl phosphatase. Implications for substrate specificity.". J. Biol. Chem. 273 (34): 21714–20. doi:10.1074/jbc.273.34.21714. PMID 9705307.
Tailor P, Gilman J, Williams S, Mustelin T (1999). "A novel isoform of the low molecular weight phosphotyrosine phosphatase, LMPTP-C, arising from alternative mRNA splicing.". Eur. J. Biochem. 262 (2): 277–82. doi:10.1046/j.1432-1327.1999.00353.x. PMID 10336608.
Huang L, Sankar S, Lin C, et al. (2000). "HCPTPA, a protein tyrosine phosphatase that regulates vascular endothelial growth factor receptor-mediated signal transduction and biological activity.". J. Biol. Chem. 274 (53): 38183–8. doi:10.1074/jbc.274.53.38183. PMID 10608891.
Nicolas G, Fournier CM, Galand C, et al. (2002). "Tyrosine phosphorylation regulates alpha II spectrin cleavage by calpain.". Mol. Cell. Biol. 22 (10): 3527–36. doi:10.1128/MCB.22.10.3527-3536.2002. PMC 133798. PMID 11971983. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=133798.
Bottini N, Stefanini L, Williams S, et al. (2002). "Activation of ZAP-70 through specific dephosphorylation at the inhibitory Tyr-292 by the low molecular weight phosphotyrosine phosphatase (LMPTP).". J. Biol. Chem. 277 (27): 24220–4. doi:10.1074/jbc.M202885200. PMID 11976341.
Bottini N, Ammendola M, Gloria-Bottini F (2002). "ACP1 is associated with allergy.". Allergy 57 (7): 651–2. doi:10.1034/j.1398-9995.2002.23722.x. PMID 12100313.
Kikawa KD, Vidale DR, Van Etten RL, Kinch MS (2002). "Regulation of the EphA2 kinase by the low molecular weight tyrosine phosphatase induces transformation.". J. Biol. Chem. 277 (42): 39274–9. doi:10.1074/jbc.M207127200. PMID 12167657.

PDB gallery

1bvh: SOLUTION STRUCTURE OF A LOW MOLECULAR WEIGHT PROTEIN TYROSINE PHOSPHATASE

1c0e: Active Site S19A Mutant of Bovine Heart Phosphotyrosyl Phosphatase

1dg9: CRYSTAL STRUCTURE OF BOVINE LOW MOLECULAR WEIGHT PTPASE COMPLEXED WITH HEPES

1phr: THE CRYSTAL STRUCTURE OF A LOW MOLECULAR PHOSPHOTYROSINE PROTEIN PHOSPHATASE

1pnt: CRYSTAL STRUCTURE OF BOVINE HEART PHOSPHOTYROSYL PHOSPHATASE AT 2.2 ANGSTROMS RESOLUTION

1xww: Crystal Structure of Human B-form Low Molecular Weight Phosphotyrosyl Phosphatase at 1.6 Angstrom Resolution

1z12: Crystal Structure of Bovine Low Molecular Weight PTPase Complexed with Vanadate

1z13: Crystal Structure of Bovine Low Molecular Weight PTPase Complexed with Molybdate

5pnt: CRYSTAL STRUCTURE OF A HUMAN LOW MOLECULAR WEIGHT PHOSPHOTYROSYL PHOSPHATASE. IMPLICATIONS FOR SUBSTRATE SPECIFICITY

Esterase: protein tyrosine phosphatases (EC 3.1.3.48)

Class I

Classical PTPs	Receptor type PTPs (PTPRA, PTPRB, PTPRC, PTPRD, PTPRE, PTPRF, PTPRG, PTPRH, PTPRJ, PTPRK, PTPRM, PTPRN, PTPRN2, PTPRO, PTPRQ, PTPRR, PTPRS, PTPRT, PTPRU, PTPRZ1, PTPRZ2) Non receptor type PTPs (PTPN1, PTPN2, PTPN3, PTPN4, PTPN5, PTPN6, PTPN7, PTPN9, PTPN11, PTPN12, PTPN13, PTPN14, PTPN18, PTPN20, PTPN21, PTPN22, PTPN23

VH1-like or dual specific phosphatases (DSPs)	MAPK phosphatases (MKPs) (DUSP1, DUSP2, DUSP4, DUSP5, DUSP6, DUSP7, DUSP8, DUSP9, DUSP10, DUSP16, MK-STYX) Slingshots (SSH1, SSH2, SSH3) PRLs (PTP4A1, PTP4A2, PTP4A3) CDC14s (CDC14A, CDC14B, CDKN3, PTP9Q22) Atypical DSPs (DUSP3, DUSP11, DUSP12, DUSP13A, DUSP13B, DUSP14, DUSP15, DUSP18, DUSP19, DUSP21, DUSP22, DUSP23, DUSP24, DUSP25, DUSP26, DUSP27, EMP2A, RNGTT, STYX) Phosphatase and tensin homologs (PTENs) (PTEN, TPIP, TPTE, TNS, TENC1) Myotubularins (MTM1, MTMR2, MTMR3, MTMR4, MTMR5, MTMR6, MTMR7, MTMR8, MTMR9, MTMR10, MTMR11, MTMR12, MTMR13, MTMR14, MTMR15)

Class II

ACP1

Class III

Cdc25: CDC25A, CDC25B, CDC25C

Class IV

Eyes absent homolog (EYA1, EYA2, EYA3, EYA4)

B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6

ACP1

Interactions

References

Further reading