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Protein Tyrosine Phosphatases in the Human Genome
Open accessAbstract
Tyrosine phosphorylation is catalyzed by protein tyrosine kinases, which are represented by 90 genes in the human genome. Here, we present the set of 107 genes in the human genome that encode members of the four protein tyrosine phosphatase (PTP) families. The four families of PTPases, their substrates, structure, function, regulation, and the role of these enzymes in human disease will be discussed.
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“Twenty-five genes encode for DUSPs in the human genome, with DUSP24 and DUSP27 lacking enzymatic activity.12”
From Molecular basis of MAP kinase regulation (2013) · cites this paper as [12]
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Cites
The protein kinase complement of the human genome
Manning, G., Whyte, D. B., Martinez, R., Hunter, T., & Sudarsanam, S. (2002) · Science · doi:10.1126/science.1075762 · Cited by 8,145
Self-citationElchebly, M., Payette, P., Michaliszyn, E., Cromlish, W., Collins, S., Loy, A. L., Normandin, D., Cheng, A., Himms-Hagen, J., Chan, C.-C., et al. (1999) · Science · doi:10.1126/science.283.5407.1544 · Cited by 2,210
Liaw, D., Marsh, D. J., Li, J., Dahia, P. L. M., Wang, S. I., Zheng, Z., Bose, S., Call, K. M., Tsou, H. C., Peacoke, M., et al. (1997) · Nature Genetics · doi:10.1038/ng0597-64 · Cited by 2,067
Mutations in PTPN11, encoding the protein tyrosine phosphatase SHP-2, cause Noonan syndrome
Tartaglia, M., Mehler, E. L., Goldberg, R. B., Zampino, G., Brunner, H. G., Kremer, H., van der Burgt, I., Crosby, A. H., Ion, A., Jeffery, S., et al. (2001) · Nature Genetics · doi:10.1038/ng772 · Cited by 1,736
A functional variant of lymphoid tyrosine phosphatase is associated with type I diabetes
Bottini, N., Musumeci, L., Alonso, A., Rahmouni, S., Nika, K., Rostamkhani, M., MacMurray, J. P., Meloni, T., Lucarelli, P., Pellecchia, M., et al. (2004) · Nature Genetics · doi:10.1038/ng1323 · Cited by 1,419
Self-citationA thousand and one protein kinases
Hunter, T. R. (1987) · Cell · doi:10.1016/0092-8674(87)90509-5 · Cited by 1,057
Self-citationCrystal Structure of the Tyrosine Phosphatase SHP-2
Hof, P., Pluskey, S., Dhe‐Paganon, S., Eck, M. J., & Shoelson, S. E. (1998) · Cell · doi:10.1016/s0092-8674(00)80938-1 · Cited by 997
Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate
Salmeen, A., Andersen, J. N., Myers, M. P., Meng, T.-C., Hinks, J. A., Tonks, N. K., & Barford, D. (2003) · Nature · doi:10.1038/nature01680 · Cited by 951
Protein Tyrosine Phosphatases: A Diverse Family of Intracellular and Transmembrane Enzymes
Fischer, E. H., Charbonneau, H., & Tonks, N. K. (1991) · Science · doi:10.1126/science.1650499 · Cited by 950
CRYSTAL STRUCTURE OF HUMAN PROTEIN TYROSINE PHOSPHATASE 1B
Barford, D., Flint, A. J., & Tonks, N. K. (1994) · Science · doi:10.1126/science.8128219 · Cited by 761
Research works printed but not linked: 3
- Alonso, 2004, VHY, a novel, myristylated, testis-restricted, dual-specific protein phosphatase related to VHX, J. Biol. Chem., in press
- Bottini, 2002, LMPTP and human disease, Arch. Immol. Ther. Exp., 50, 95
- Bult, 1997, Step, Eur. J. Cell Biol., 72, 337
Cited by
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Sallee, J. L., Wittchen, E. S., & Burridge, K. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.r600003200 · Cited by 113
5-Arylidene-2,4-thiazolidinediones as inhibitors of protein tyrosine phosphatases
Maccari, R., Paoli, P., Ottanà, R., Jacomelli, M., Ciurleo, R., Manao, G., Steindl, T. M., Langer, T., Vigorita, M. G., & Camici, G. (2007) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2007.05.027 · Cited by 113
Targeting the PTPome in human disease
Tautz, L., Pellecchia, M., & Mustelin, T. (2006) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.10.1.157 · Cited by 111
Self-citationDeficiency of MIP/MTMR14 phosphatase induces a muscle disorder by disrupting Ca2+ homeostasis
Shen, J., Yu, W., Brotto, M. A. P., Scherman, J. A., Guo, C., Stoddard, C. E., Nosek, T. M., Valdivia, H. H., & Qu, C. (2009) · Nature Cell Biology · doi:10.1038/ncb1884 · Cited by 112
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Xu, Y., Tan, L.-J., Grachtchouk, V., Voorhees, J. J., & Fisher, G. J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m507722200 · Cited by 112
Redox regulation of the protein tyrosine phosphatase PTP1B in cancer cells
Lou, Y., Chen, Y., Hsu, S.-F., Chen, R., Lee, C., Khoo, K., Tonks, N. K., & Meng, T. (2007) · FEBS Journal · doi:10.1111/j.1742-4658.2007.06173.x · Cited by 115
Yan, G., Xiao, C., He, G., Yin, X., Chen, N., Cao, Y., & He, Q. (2010) · PROTEOMICS · doi:10.1002/pmic.200900662 · Cited by 112
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Foster, M. W., Forrester, M. T., & Stamler, J. S. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900729106 · Cited by 113
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Makagiansar, I. T., Williams, S., Mustelin, T., & Stallcup, W. B. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200612084 · Cited by 113
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Monick, M. M., Powers, L. S., Barrett, C. W., Hinde, S. L., Ashare, A., Groskreutz, D. J., Nyunoya, T., Coleman, M. C., Spitz, D. R., & Hunninghake, G. W. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.180.11.7485 · Cited by 110
Recent development of small molecular specific inhibitor of protein tyrosine phosphatase 1B
Lee, S., & Wang, Q. (2006) · Medicinal Research Reviews · doi:10.1002/med.20079 · Cited by 109
Jin, C. Y., He, J., Zou, J., Xuan, W., Fu, T., Wang, R., & Tan, W. (2019) · Nature Communications · doi:10.1038/s41467-019-10639-6 · Cited by 109
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Liu, H., Galka, M., Mori, E., Liu, X., Lin, Y., Wei, R., Pittock, P., Voss, C., Dhami, G. K., Li, X., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.04.025 · Cited by 109
Hafizi, S., Ibraimi, F., & Dahlbäck, B. (2005) · The FASEB Journal · doi:10.1096/fj.04-2532fje · Cited by 105
Scior, T., Guevara-García, J. A., Do, Q., Bernard, P., & Laufer, S. (2016) · Current Medicinal Chemistry · doi:10.2174/0929867323666160321121138 · Cited by 105
Campos, A., & Clemente‐Blanco, A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21020446 · Cited by 114
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Self-citationRegulation of TCR signalling by tyrosine phosphatases: from immune homeostasis to autoimmunity
Stanford, S. M., Rapini, N., & Bottini, N. (2012) · Immunology · doi:10.1111/j.1365-2567.2012.03591.x · Cited by 105
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Lin, S., Chien, C., Lee, J., Yeh, Y.-C., Hsu, K., Lai, Y.-Y., Lin, S.-C., & Tsai, S. (2011) · Journal of Clinical Investigation · doi:10.1172/jci44362 · Cited by 104
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Pan, C., Gnad, F., Olsen, J. V., & Mann, M. (2008) · PROTEOMICS · doi:10.1002/pmic.200800105 · Cited by 103
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Dagnell, M., Frijhoff, J., Pader, I., Augsten, M., Boivin, B., Xu, J., Mandal, P. K., Tonks, N. K., Hellberg, C. B., Conrad, M., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1302891110 · Cited by 100
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Yang, J., Groen, A. J., Lemeer, S., Jans, A., Slijper, M., Roe, S. M., den Hertog, J., & Barford, D. (2006) · Biochemistry · doi:10.1021/bi061546m · Cited by 99
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Lorenzo, Ó., Urbé, S., & Clague, M. J. (2006) · Journal of Cell Science · doi:10.1242/jcs.03040 · Cited by 100
Porcel, B. M., Denœud, F., Opperdoes, F. R., Noël, B., Madoui, M., Hammarton, T. C., Field, M. C., Silva, C. D., Couloux, A., Poulain, J., et al. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004007 · Cited by 94
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Lim, S.-H., Kwon, S., Lee, M. K., Moon, J., Jeong, D. G., Park, E., Kim, S. J., Park, B. C., Lee, S. C., Ryu, S.-E., et al. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.289 · Cited by 86
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Xia, T., Yi, X.-M., Wu, X., Shang, J., & Shu, H. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1906431116 · Cited by 83
Protein tyrosine phosphatase structure–function relationships in regulation and pathogenesis
Böhmer, F., Szedlacsek, S. E., Tabernero, L., Östman, A., & den Hertog, J. (2012) · FEBS Journal · doi:10.1111/j.1742-4658.2012.08655.x · Cited by 85
Kim, D. J., Tremblay, M. L., & DiGiovanni, J. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010290 · Cited by 83
Lu, X., Chen, J., Sasmono, R. T., Hsi, E. D., Sarosiek, K. A., Tiganis, T., & Lossos, I. S. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01234-06 · Cited by 87
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Metadata
- Authors
- Alonso, A., Sasin, J., Bottini, N., Friedberg, I., Friedberg, I., Osterman, A., Godzik, A., Hunter, T., Dixon, J., & Mustelin, T.
- Affiliations
- Sanford Burnham Prebys Medical Discovery Institute (US)
- Salk Institute for Biological Studies (US)
- University of California San Diego (US)
- Corresponding author
- Mustelin, Tomas
- ORCID
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2004-06
- Volume
- 117
- Issue
- 6
- Pages
- 699-711
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2043617798
- Cited by
- 1,886
- References
- 75
- Citations by year
- 2026: 34 · 2025: 30 · 2024: 63 · 2023: 62 · 2022: 56 · 2021: 78 · 2020: 67 · 2019: 77 · 2018: 69 · 2017: 95 · 2016: 67 · 2015: 97 · 2014: 110 · 2013: 133 · 2012: 118
- FWCI
- 7.71
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 3333 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Keywords
- protein tyrosine phosphatase, human genome, tyrosine phosphorylation, tyrosine kinase, enzyme structure-function, enzyme regulation, human disease
- MeSH terms
- Amino Acid Sequence, Humans, Phosphorylation, Phylogeny, Tyrosine, Signal Transduction, Genome, Human, Gene Expression Regulation, Enzymologic, Protein Tyrosine Phosphatases, Protein Structure, Tertiary
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