ACP1

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1XWW, 3N8I, 4Z99, 4Z9A, 4Z9B, 5PNT

Identifiers

Aliases

ACP1, HAAP, LMW-PTP, acid phosphatase 1, soluble

External IDs

MGI: 87881 HomoloGene: 38274 GeneCards: ACP1

EC number

3.1.3.2

Gene ontology
Molecular function	• protein tyrosine phosphatase activity • phosphatase activity • phosphoprotein phosphatase activity • hydrolase activity • protein binding • non-membrane spanning protein tyrosine phosphatase activity • acid phosphatase activity
Cellular component	• cytoplasm • cytoplasmic side of plasma membrane • extracellular exosome
Biological process	• protein dephosphorylation • peptidyl-tyrosine dephosphorylation
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


52


11431

Ensembl


ENSG00000143727


ENSMUSG00000044573

UniProt


P24666


Q9D358

RefSeq (mRNA)


NM_001040649 NM_004300 NM_007099 NM_177554


NM_001110239 NM_021330

RefSeq (protein)


NP_004291.1 NP_009030.1


NP_001103709.1 NP_067305.2

Location (UCSC)

Chr 2: 0.26 – 0.28 Mb

Chr 12: 30.89 – 30.91 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

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.^[3]

Interactions

ACP1 has been shown to interact with EPH receptor A2^[4] and EPH receptor B1.^[5]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ "Entrez Gene: ACP1 acid phosphatase 1, soluble".
↑ Kikawa, Keith D; Vidale Derika R; Van Etten Robert L; Kinch Michael S (October 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 (March 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.

External links

Human ACP1 genome location and ACP1 gene details page in the UCSC Genome Browser.

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.". American Journal of Human Genetics. 30 (5): 553–60. PMC 1685602. PMID 736044.
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.
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.
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.
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

EYA1
EYA2
EYA3
EYA4

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ACP1

Interactions

References

External links

Further reading