The DOI matches its Crossref record; 48 of the 48 references it cites were found in a registry or an index.
Cloning and characterization of human SHIP, the 145-kD inositol 5- phosphatase that associates with SHC after cytokine stimulation
Abstract
We recently cloned and sequenced a cDNA encoding a 145-kD protein from the murine hematopoietic cell line B6SUtA, that becomes tyrosine phosphorylated and associated with Shc after cytokine stimulation. Based on its domains and enzymatic activity, we named this protein SHIP for SH2-containing inositol phosphatase (Damen et al, Proc Natl Acad Sci USA 93:1689, 1996). We describe here the cloning of the human homologue of murine SHIP (mSHIP) from a human megakaryocytic cell line (MO7e) lambda gt11 cDNA library using two nonoverlapping mSHIP cDNA fragments as probes. Northern blot analysis suggests that human SHIP (hSHIP) is expressed as a 5.3-kb mRNA in human bone marrow and a wide variety of other tissues. Sequence analysis of this cDNA predicts a protein of 1188 amino acids exhibiting 87.2% overall sequence identity with mSHIP. Contained within the defined open reading frame is an N-terminal, group l src homology 2 (SH2) domain; three NXXY motifs that, if phosphorylated, could be bound by phosphotyrosine binding (PTB) domains; a C-terminal proline-rich region; and two centrally located inositol polyphosphate 5-phosphatase motifs. Fluorescence in situ hybridization, using the full-length hSHIP cDNA as a probe, mapped hSHIP to the long arm of chromosome 2 at the border between 2q36 and 2q37.
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“SHIP1 was originally observed in hematopoietic cells after a variety of cytokines and growth factors induced the tyrosine phosphorylation of this 145-kDa protein [98–104].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [99]
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High-Resolution Mapping of Human Chromosome 11 by in Situ Hybridization with Cosmid Clones
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The IL-4 receptor: signaling mechanisms and biologic functions
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Inactivating mutations in an SH2 domain-encoding gene in X-linked lymphoproliferative syndrome
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Metadata
- Authors
- Ware, M., Rosten, P., Damen, J., Liu, L., Humphries, R., & Krystal, G.
- Affiliations
- Terry Fox Laboratory, British Columbia Cancer Research Center, Vancouver, Canada.
- Venue
- Blood
- Publisher
- American Society of Hematology
- Published
- 1996-10-15
- Volume
- 88
- Issue
- 8
- Pages
- 2833-2840
- ISSN
- 0006-4971 (ISSN-L)
- 1528-0020
- OpenAlex
- W2339933169
- Cited by
- 96
- References
- 48
- Citations by year
- 2026: 1 · 2024: 4 · 2023: 5 · 2022: 3 · 2020: 1 · 2019: 2 · 2018: 3 · 2017: 3 · 2016: 1 · 2015: 1 · 2014: 2 · 2013: 2 · 2012: 3
- FWCI
- 3.03
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Blood (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Life Sciences › Immunology and Microbiology › Immunology › Cytokine Signaling Pathways and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- ships, SH2 domain, phosphotyrosine binding domain, proline-rich region, inositol polyphosphate 5-phosphatase, cytokine induction, tyrosine phosphorylation, gene mapping
- MeSH terms
- Src Homology 2 Domain-Containing, Transforming Protein 1, Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases, Amino Acid Sequence, Cloning, Molecular, Humans, Leukemia, Megakaryoblastic, Acute, Molecular Sequence Data, Phosphoric Monoester Hydrolases, Phosphorylation, Protein Processing, Post-Translational, Proteins, Tumor Cells, Cultured, Sequence Alignment, Sequence Homology, Amino Acid, In Situ Hybridization, Fluorescence, DNA, Complementary, src Homology Domains, Adaptor Proteins, Vesicular Transport, Adaptor Proteins, Signal Transducing, GRB2 Adaptor Protein, Shc Signaling Adaptor Proteins
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- CoChat. (2026). Citation check: Cloning and characterization of human SHIP, the 145-kD inositol 5- phosphatase that associates with SHC after cytokine stimulation. https://app.cochat.ai/papers/10.1182/blood.v88.8.2833.bloodjournal8882833
- The paper
- Ware, M., Rosten, P., Damen, J., Liu, L., Humphries, R., & Krystal, G. (1996). Cloning and characterization of human SHIP, the 145-kD inositol 5- phosphatase that associates with SHC after cytokine stimulation. Blood. https://doi.org/10.1182/blood.v88.8.2833.bloodjournal8882833
