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.[5]
Clinically, increased expression of ACP1 is a biomarker for poor prognosis in prostate cancer has been linked to worse clinical behaviour of prostate cancer, possibly outperforming the widely used Gleason grading system with respect to this important parameter.[6] Also in other cancers, e.g. colon cancer, high ACP1 protein levels are linked to aggressive disease.[7] It has been suggested that ACP1 acts as a bona fide oncogene, but for now this notion remains unproven even if ACP1 overexpression drives cells towards a Warburg effect-like glycolytic phenotype.[8] Apart from cancer, ACP1 has also been linked to osteoporosis as the enzyme plays an important role in the interaction of the osteocyte with the bone environment,[9] while its inhibition appears useful for counteracting experimental [venous thromboembolism].[10] Currently, there are no clinically approved inhibitors that allow targeting ACP1 in patients.
Interactionsedit
ACP1 has been shown to interact with EPH receptor A2[11] and EPH receptor B1.[12] The proto-oncogene Src has been suggested to be a direct target for ACP1 tyrosine phosphatase activity, but this has not been formally proven.[13]
Referencesedit
^ abcGRCh38: Ensembl release 89: ENSG00000143727 – Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000044573 – Ensembl, May 2017
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Ruela-de-Sousa RR, Hoekstra E, Hoogland AM, Souza Queiroz KC, Peppelenbosch MP, Stubbs AP, et al. (April 2016). "Low-Molecular-Weight Protein Tyrosine Phosphatase Predicts Prostate Cancer Outcome by Increasing the Metastatic Potential". European Urology. 69 (4): 710–719. doi:10.1016/j.eururo.2015.06.040. PMID 26159288.
^Faria AV, Yu B, Mommersteeg M, de Souza-Oliveira PF, Andrade SS, Spaander MC, et al. (January 2022). "Platelet-dependent signaling and Low Molecular Weight Protein Tyrosine Phosphatase expression promote aggressive phenotypic changes in gastrointestinal cancer cells". Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1868 (1): 166280. doi:10.1016/j.bbadis.2021.166280. PMID 34610471.
^Faria AV, Tornatore TF, Milani R, Queiroz KC, Sampaio IH, Fonseca EM, et al. (November 2017). "Oncophosphosignaling Favors a Glycolytic Phenotype in Human Drug Resistant Leukemia". Journal of Cellular Biochemistry. 118 (11): 3846–3854. doi:10.1002/jcb.26034. PMID 28387439. S2CID 3915599.
^Fernandes GV, Cavagis AD, Ferreira CV, Olej B, Leão M, Yano CL, et al. (June 2014). "Osteoblast adhesion dynamics: a possible role for ROS and LMW-PTP". Journal of Cellular Biochemistry. 115 (6): 1063–1069. doi:10.1002/jcb.24691. PMID 24123071. S2CID 7383008.
^Faria AV, Andrade SS, Reijm AN, Spaander MC, de Maat MP, Peppelenbosch MP, et al. (June 2019). "Targeting Tyrosine Phosphatases by 3-Bromopyruvate Overcomes Hyperactivation of Platelets from Gastrointestinal Cancer Patients". Journal of Clinical Medicine. 8 (7): 936. doi:10.3390/jcm8070936. PMC6678874. PMID 31261776.
^Kikawa KD, Vidale DR, Van Etten RL, Kinch MS (October 2002). "Regulation of the EphA2 kinase by the low molecular weight tyrosine phosphatase induces transformation". The Journal of Biological Chemistry. 277 (42): 39274–39279. doi:10.1074/jbc.M207127200. PMID 12167657.
^Stein E, Lane AA, Cerretti DP, Schoecklmann HO, Schroff AD, Van Etten RL, Daniel TO (March 1998). "Eph receptors discriminate specific ligand oligomers to determine alternative signaling complexes, attachment, and assembly responses". Genes & Development. 12 (5): 667–678. doi:10.1101/gad.12.5.667. PMC316584. PMID 9499402.
^Zambuzzi WF, Granjeiro JM, Parikh K, Yuvaraj S, Peppelenbosch MP, Ferreira CV (2008). "Modulation of Src activity by low molecular weight protein tyrosine phosphatase during osteoblast differentiation". Cellular Physiology and Biochemistry. 22 (5–6): 497–506. doi:10.1159/000185506. PMID 19088431.
External linksedit
Human ACP1 genome location and ACP1 gene details page in the UCSC Genome Browser.
Overview of all the structural information available in the PDB for UniProt: P24666 (Human Low molecular weight phosphotyrosine protein phosphatase) at the PDBe-KB.
Overview of all the structural information available in the PDB for UniProt: Q9D358 (Mouse Low molecular weight phosphotyrosine protein phosphatase) at the PDBe-KB.
Further readingedit
Junien C, Kaplan JC, Bernheim A, Berger R (April 1979). "Regional assignment of red cell acid phosphatase locus to band 2p25". Human Genetics. 48 (1): 17–21. doi:10.1007/BF00273269. PMID 457131. S2CID 422040.
Sensabaugh GF, Golden VL (September 1978). "Phenotype dependence in the inhibition of red cell acid phosphatase (ACP) by folates". American Journal of Human Genetics. 30 (5): 553–560. PMC1685602. PMID 736044.
Shekels LL, Smith AJ, Van Etten RL, Bernlohr DA (June 1992). "Identification of the adipocyte acid phosphatase as a PAO-sensitive tyrosyl phosphatase". Protein Science. 1 (6): 710–721. doi:10.1002/pro.5560010603. PMC2142247. PMID 1304913.
Wo YY, McCormack AL, Shabanowitz J, Hunt DF, Davis JP, Mitchell GL, Van Etten RL (May 1992). "Sequencing, cloning, and expression of human red cell-type acid phosphatase, a cytoplasmic phosphotyrosyl protein phosphatase". The Journal of Biological Chemistry. 267 (15): 10856–10865. doi:10.1016/S0021-9258(19)50097-7. PMID 1587862.
Dissing J, Johnsen AH (June 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". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1121 (3): 261–268. doi:10.1016/0167-4838(92)90155-7. PMID 1627603.
Dissing J, Johnsen AH, Sensabaugh GF (November 1991). "Human red cell acid phosphatase (ACP1). The amino acid sequence of the two isozymes Bf and Bs encoded by the ACP1*B allele". The Journal of Biological Chemistry. 266 (31): 20619–20625. doi:10.1016/S0021-9258(18)54754-2. PMID 1939112.
Wakita Y, Narahara K, Takahashi Y, Kikkawa K, Kimura S, Oda M, Kimoto H (1986). "Duplication of 2p25: confirmation of the assignment of soluble acid phosphatase (ACP1) locus to 2p25". Human Genetics. 71 (3): 259–260. doi:10.1007/BF00284586. PMID 4065897. S2CID 10610694.
Blake NM, Kirk RL, Barnes KR, Thompson JM (June 1973). "Expression of human red cell acid phosphatase activity in placenta and other tissues". Jinrui Idengaku Zasshi. The Japanese Journal of Human Genetics. 18 (1): 10–23. PMID 4356849.
Sensabaugh GF, Lazaruk KA (July 1993). "A TaqI site identifies the *A allele at the ACP1 locus". Human Molecular Genetics. 2 (7): 1079. doi:10.1093/hmg/2.7.1079-a. PMID 8364553.
Bryson GL, Massa H, Trask BJ, Van Etten RL (November 1995). "Gene structure, sequence, and chromosomal localization of the human red cell-type low-molecular-weight acid phosphotyrosyl phosphatase gene, ACP1". Genomics. 30 (2): 133–140. doi:10.1006/geno.1995.9893. PMID 8586411.
Tailor P, Gilman J, Williams S, Couture C, Mustelin T (February 1997). "Regulation of the low molecular weight phosphotyrosine phosphatase by phosphorylation at tyrosines 131 and 132". The Journal of Biological Chemistry. 272 (9): 5371–5374. doi:10.1074/jbc.272.9.5371. PMID 9038134.
Stein E, Lane AA, Cerretti DP, Schoecklmann HO, Schroff AD, Van Etten RL, Daniel TO (March 1998). "Eph receptors discriminate specific ligand oligomers to determine alternative signaling complexes, attachment, and assembly responses". Genes & Development. 12 (5): 667–678. doi:10.1101/gad.12.5.667. PMC316584. PMID 9499402.
Modesti A, Marzocchini R, Raugei G, Chiti F, Sereni A, Magherini F, Ramponi G (July 1998). "Cloning, expression and characterisation of a new human low Mr phosphotyrosine protein phosphatase originating by alternative splicing". FEBS Letters. 431 (1): 111–115. doi:10.1016/S0014-5793(98)00732-7. PMID 9684876. S2CID 38383291.
Zhang M, Stauffacher CV, Lin D, Van Etten RL (August 1998). "Crystal structure of a human low molecular weight phosphotyrosyl phosphatase. Implications for substrate specificity". The Journal of Biological Chemistry. 273 (34): 21714–21720. doi:10.1074/jbc.273.34.21714. PMID 9705307.
Tailor P, Gilman J, Williams S, Mustelin T (June 1999). "A novel isoform of the low molecular weight phosphotyrosine phosphatase, LMPTP-C, arising from alternative mRNA splicing". European Journal of Biochemistry. 262 (2): 277–282. doi:10.1046/j.1432-1327.1999.00353.x. PMID 10336608.
Huang L, Sankar S, Lin C, Kontos CD, Schroff AD, Cha EH, et al. (December 1999). "HCPTPA, a protein tyrosine phosphatase that regulates vascular endothelial growth factor receptor-mediated signal transduction and biological activity". The Journal of Biological Chemistry. 274 (53): 38183–38188. doi:10.1074/jbc.274.53.38183. PMID 10608891.
Nicolas G, Fournier CM, Galand C, Malbert-Colas L, Bournier O, Kroviarski Y, et al. (May 2002). "Tyrosine phosphorylation regulates alpha II spectrin cleavage by calpain". Molecular and Cellular Biology. 22 (10): 3527–3536. doi:10.1128/MCB.22.10.3527-3536.2002. PMC133798. PMID 11971983.
Bottini N, Stefanini L, Williams S, Alonso A, Jascur T, Abraham RT, et al. (July 2002). "Activation of ZAP-70 through specific dephosphorylation at the inhibitory Tyr-292 by the low molecular weight phosphotyrosine phosphatase (LMPTP)". The Journal of Biological Chemistry. 277 (27): 24220–24224. doi:10.1074/jbc.M202885200. PMID 11976341.
Bottini N, Ammendola M, Gloria-Bottini F (July 2002). "ACP1 is associated with allergy". Allergy. 57 (7): 651–652. doi:10.1034/j.1398-9995.2002.23722.x. PMID 12100313. S2CID 42578825.
Kikawa KD, Vidale DR, Van Etten RL, Kinch MS (October 2002). "Regulation of the EphA2 kinase by the low molecular weight tyrosine phosphatase induces transformation". The Journal of Biological Chemistry. 277 (42): 39274–39279. doi:10.1074/jbc.M207127200. PMID 12167657.
This article on a gene on human chromosome 2 is a stub. You can help Wikipedia by expanding it.
acp1, molecular, weight, phosphotyrosine, protein, phosphatase, enzyme, that, humans, encoded, gene, available, structurespdbortholog, search, pdbe, rcsblist, codes1xww, 3n8i, 4z99, 4z9a, 4z9b, 5pntidentifiersaliases, haap, acid, phosphatase, soluble, lmwptp, . Low molecular weight phosphotyrosine protein phosphatase is an enzyme that in humans is encoded by the ACP1 gene ACP1Available structuresPDBOrtholog search PDBe RCSBList of PDB id codes1XWW 3N8I 4Z99 4Z9A 4Z9B 5PNTIdentifiersAliasesACP1 HAAP LMW PTP acid phosphatase 1 soluble LMWPTP acid phosphatase 1External IDsOMIM 171500 MGI 87881 HomoloGene 38274 GeneCards ACP1EC number3 1 3 2Gene location Human Chr Chromosome 2 human 1 Band2p25 3Start264 140 bp 1 End278 283 bp 1 Gene location Mouse Chr Chromosome 12 mouse 2 Band12 12 A2Start30 943 325 bp 2 End30 961 588 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed inspermAchilles tendonleft adrenal glandislet of Langerhansbody of pancreasembryoganglionic eminencerectumpalpebral conjunctivagallbladderTop expressed inyolk sacspermatidspermatocytemorulasuperior frontal gyruslipneural tubeproximal tubulesecondary oocyteduodenumMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functionprotein tyrosine phosphatase activity phosphatase activity phosphoprotein phosphatase activity hydrolase activity protein binding non membrane spanning protein tyrosine phosphatase activity acid phosphatase activityCellular componentcytoplasm cytoplasmic side of plasma membrane extracellular exosome cytosol sarcolemmaBiological processprotein dephosphorylation peptidyl tyrosine dephosphorylationSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez5211431EnsemblENSG00000143727ENSMUSG00000044573UniProtP24666Q9D358RefSeq mRNA NM 001040649NM 004300NM 007099NM 177554NM 001110239NM 021330RefSeq protein NP 001035739NP 004291NP 009030NP 001103709NP 067305Location UCSC Chr 2 0 26 0 28 MbChr 12 30 94 30 96 MbPubMed search 3 4 WikidataView Edit HumanView Edit MouseThe 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 5 Contents 1 Clinical significance 2 Interactions 3 References 4 External links 5 Further readingClinical significance editClinically increased expression of ACP1 is a biomarker for poor prognosis in prostate cancer has been linked to worse clinical behaviour of prostate cancer possibly outperforming the widely used Gleason grading system with respect to this important parameter 6 Also in other cancers e g colon cancer high ACP1 protein levels are linked to aggressive disease 7 It has been suggested that ACP1 acts as a bona fide oncogene but for now this notion remains unproven even if ACP1 overexpression drives cells towards a Warburg effect like glycolytic phenotype 8 Apart from cancer ACP1 has also been linked to osteoporosis as the enzyme plays an important role in the interaction of the osteocyte with the bone environment 9 while its inhibition appears useful for counteracting experimental venous thromboembolism 10 Currently there are no clinically approved inhibitors that allow targeting ACP1 in patients Interactions editACP1 has been shown to interact with EPH receptor A2 11 and EPH receptor B1 12 The proto oncogene Src has been suggested to be a direct target for ACP1 tyrosine phosphatase activity but this has not been formally proven 13 References edit a b c GRCh38 Ensembl release 89 ENSG00000143727 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000044573 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Mouse PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Entrez Gene ACP1 acid phosphatase 1 soluble Ruela de Sousa RR Hoekstra E Hoogland AM Souza Queiroz KC Peppelenbosch MP Stubbs AP et al April 2016 Low Molecular Weight Protein Tyrosine Phosphatase Predicts Prostate Cancer Outcome by Increasing the Metastatic Potential European Urology 69 4 710 719 doi 10 1016 j eururo 2015 06 040 PMID 26159288 Faria AV Yu B Mommersteeg M de Souza Oliveira PF Andrade SS Spaander MC et al January 2022 Platelet dependent signaling and Low Molecular Weight Protein Tyrosine Phosphatase expression promote aggressive phenotypic changes in gastrointestinal cancer cells Biochimica et Biophysica Acta BBA Molecular Basis of Disease 1868 1 166280 doi 10 1016 j bbadis 2021 166280 PMID 34610471 Faria AV Tornatore TF Milani R Queiroz KC Sampaio IH Fonseca EM et al November 2017 Oncophosphosignaling Favors a Glycolytic Phenotype in Human Drug Resistant Leukemia Journal of Cellular Biochemistry 118 11 3846 3854 doi 10 1002 jcb 26034 PMID 28387439 S2CID 3915599 Fernandes GV Cavagis AD Ferreira CV Olej B Leao M Yano CL et al June 2014 Osteoblast adhesion dynamics a possible role for ROS and LMW PTP Journal of Cellular Biochemistry 115 6 1063 1069 doi 10 1002 jcb 24691 PMID 24123071 S2CID 7383008 Faria AV Andrade SS Reijm AN Spaander MC de Maat MP Peppelenbosch MP et al June 2019 Targeting Tyrosine Phosphatases by 3 Bromopyruvate Overcomes Hyperactivation of Platelets from Gastrointestinal Cancer Patients Journal of Clinical Medicine 8 7 936 doi 10 3390 jcm8070936 PMC 6678874 PMID 31261776 Kikawa KD Vidale DR Van Etten RL Kinch MS October 2002 Regulation of the EphA2 kinase by the low molecular weight tyrosine phosphatase induces transformation The Journal of Biological Chemistry 277 42 39274 39279 doi 10 1074 jbc M207127200 PMID 12167657 Stein E Lane AA Cerretti DP Schoecklmann HO Schroff AD Van Etten RL Daniel TO March 1998 Eph receptors discriminate specific ligand oligomers to determine alternative signaling complexes attachment and assembly responses Genes amp Development 12 5 667 678 doi 10 1101 gad 12 5 667 PMC 316584 PMID 9499402 Zambuzzi WF Granjeiro JM Parikh K Yuvaraj S Peppelenbosch MP Ferreira CV 2008 Modulation of Src activity by low molecular weight protein tyrosine phosphatase during osteoblast differentiation Cellular Physiology and Biochemistry 22 5 6 497 506 doi 10 1159 000185506 PMID 19088431 External links editHuman ACP1 genome location and ACP1 gene details page in the UCSC Genome Browser Overview of all the structural information available in the PDB for UniProt P24666 Human Low molecular weight phosphotyrosine protein phosphatase at the PDBe KB Overview of all the structural information available in the PDB for UniProt Q9D358 Mouse Low molecular weight phosphotyrosine protein phosphatase at the PDBe KB Further reading editJunien C Kaplan JC Bernheim A Berger R April 1979 Regional assignment of red cell acid phosphatase locus to band 2p25 Human Genetics 48 1 17 21 doi 10 1007 BF00273269 PMID 457131 S2CID 422040 Sensabaugh GF Golden VL September 1978 Phenotype dependence in the inhibition of red cell acid phosphatase ACP by folates American Journal of Human Genetics 30 5 553 560 PMC 1685602 PMID 736044 Shekels LL Smith AJ Van Etten RL Bernlohr DA June 1992 Identification of the adipocyte acid phosphatase as a PAO sensitive tyrosyl phosphatase Protein Science 1 6 710 721 doi 10 1002 pro 5560010603 PMC 2142247 PMID 1304913 Wo YY McCormack AL Shabanowitz J Hunt DF Davis JP Mitchell GL Van Etten RL May 1992 Sequencing cloning and expression of human red cell type acid phosphatase a cytoplasmic phosphotyrosyl protein phosphatase The Journal of Biological Chemistry 267 15 10856 10865 doi 10 1016 S0021 9258 19 50097 7 PMID 1587862 Dissing J Johnsen AH June 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 Biochimica et Biophysica Acta BBA Protein Structure and Molecular Enzymology 1121 3 261 268 doi 10 1016 0167 4838 92 90155 7 PMID 1627603 Dissing J Johnsen AH Sensabaugh GF November 1991 Human red cell acid phosphatase ACP1 The amino acid sequence of the two isozymes Bf and Bs encoded by the ACP1 B allele The Journal of Biological Chemistry 266 31 20619 20625 doi 10 1016 S0021 9258 18 54754 2 PMID 1939112 Wakita Y Narahara K Takahashi Y Kikkawa K Kimura S Oda M Kimoto H 1986 Duplication of 2p25 confirmation of the assignment of soluble acid phosphatase ACP1 locus to 2p25 Human Genetics 71 3 259 260 doi 10 1007 BF00284586 PMID 4065897 S2CID 10610694 Blake NM Kirk RL Barnes KR Thompson JM June 1973 Expression of human red cell acid phosphatase activity in placenta and other tissues Jinrui Idengaku Zasshi The Japanese Journal of Human Genetics 18 1 10 23 PMID 4356849 Sensabaugh GF Lazaruk KA July 1993 A TaqI site identifies the A allele at the ACP1 locus Human Molecular Genetics 2 7 1079 doi 10 1093 hmg 2 7 1079 a PMID 8364553 Bryson GL Massa H Trask BJ Van Etten RL November 1995 Gene structure sequence and chromosomal localization of the human red cell type low molecular weight acid phosphotyrosyl phosphatase gene ACP1 Genomics 30 2 133 140 doi 10 1006 geno 1995 9893 PMID 8586411 Tailor P Gilman J Williams S Couture C Mustelin T February 1997 Regulation of the low molecular weight phosphotyrosine phosphatase by phosphorylation at tyrosines 131 and 132 The Journal of Biological Chemistry 272 9 5371 5374 doi 10 1074 jbc 272 9 5371 PMID 9038134 Stein E Lane AA Cerretti DP Schoecklmann HO Schroff AD Van Etten RL Daniel TO March 1998 Eph receptors discriminate specific ligand oligomers to determine alternative signaling complexes attachment and assembly responses Genes amp Development 12 5 667 678 doi 10 1101 gad 12 5 667 PMC 316584 PMID 9499402 Modesti A Marzocchini R Raugei G Chiti F Sereni A Magherini F Ramponi G July 1998 Cloning expression and characterisation of a new human low Mr phosphotyrosine protein phosphatase originating by alternative splicing FEBS Letters 431 1 111 115 doi 10 1016 S0014 5793 98 00732 7 PMID 9684876 S2CID 38383291 Zhang M Stauffacher CV Lin D Van Etten RL August 1998 Crystal structure of a human low molecular weight phosphotyrosyl phosphatase Implications for substrate specificity The Journal of Biological Chemistry 273 34 21714 21720 doi 10 1074 jbc 273 34 21714 PMID 9705307 Tailor P Gilman J Williams S Mustelin T June 1999 A novel isoform of the low molecular weight phosphotyrosine phosphatase LMPTP C arising from alternative mRNA splicing European Journal of Biochemistry 262 2 277 282 doi 10 1046 j 1432 1327 1999 00353 x PMID 10336608 Huang L Sankar S Lin C Kontos CD Schroff AD Cha EH et al December 1999 HCPTPA a protein tyrosine phosphatase that regulates vascular endothelial growth factor receptor mediated signal transduction and biological activity The Journal of Biological Chemistry 274 53 38183 38188 doi 10 1074 jbc 274 53 38183 PMID 10608891 Nicolas G Fournier CM Galand C Malbert Colas L Bournier O Kroviarski Y et al May 2002 Tyrosine phosphorylation regulates alpha II spectrin cleavage by calpain Molecular and Cellular Biology 22 10 3527 3536 doi 10 1128 MCB 22 10 3527 3536 2002 PMC 133798 PMID 11971983 Bottini N Stefanini L Williams S Alonso A Jascur T Abraham RT et al July 2002 Activation of ZAP 70 through specific dephosphorylation at the inhibitory Tyr 292 by the low molecular weight phosphotyrosine phosphatase LMPTP The Journal of Biological Chemistry 277 27 24220 24224 doi 10 1074 jbc M202885200 PMID 11976341 Bottini N Ammendola M Gloria Bottini F July 2002 ACP1 is associated with allergy Allergy 57 7 651 652 doi 10 1034 j 1398 9995 2002 23722 x PMID 12100313 S2CID 42578825 Kikawa KD Vidale DR Van Etten RL Kinch MS October 2002 Regulation of the EphA2 kinase by the low molecular weight tyrosine phosphatase induces transformation The Journal of Biological Chemistry 277 42 39274 39279 doi 10 1074 jbc M207127200 PMID 12167657 nbsp This article on a gene on human chromosome 2 is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title ACP1 amp oldid 1192931039, wikipedia, wiki, book, books, library,
