Cloning of the genomic locus of mouse SH2 containing inositol 5-phosphatase (SHIP) and a novel 110-kDa splice isoform, SHIPδ

Genomics

Volumn 69, Issue 1, 2000, Pages 104-112

  Wolf, Ingrid ^a   Lucas, David M ^a   Algate, Paul A ^a   Rohrschneider, Larry R ^a  

^a USA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

INOSITOL DERIVATIVE;

ANIMAL CELL; ARTICLE; GENE DELETION; GENE LOCUS; HEMATOPOIESIS; MOLECULAR CLONING; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; RNA SPLICING; SPERMATOGENESIS;

ANIMALIA;

EID: 0034306539     PISSN: 08887543     EISSN: None     Source Type: Journal    
DOI: 10.1006/geno.2000.6324     Document Type: Article

References (35)

1. Organization and expression of eucaryotic split genes coding for proteins
2. The 145-kDa protein induced to associate with Shc by multiple cytokines is an inositol tetraphosphate and phosphatidylinositol 3,4,5-triphosphate 5-phosphatase
3. Multiple forms of the SH2-containing inositol phosphatase, SHIP, are generated by C-terminal truncation
4. Rapid production of full-length cDNAs from rare transcripts: Amplification using a single gene-specific oligonucleotide primer
5. The human SHIP gene is differentially expressed in cell lineages of the bone marrow and blood
6. The SH2 domain-containing inositol 5'-phosphatase (SHIP) recruits the p85 subunit of phosphoinositide 3-kinase during FcγRIIb1-mediated inhibition of B cell receptor signaling
7. Targeted disruption of SHIP leads to hemopoietic perturbations, lung pathology, and a shortened life span
8. The src homology 2-containing inositol phosphatase (SHIP) is the gatekeeper of mast cell degranulation
9. Multiple forms of an inositol polyphosphate 5-phosphatase form signaling complexes with Shc and Grb2
10. Developmentally regulated alternative splicing in a novel synaptojanin
11. The negative signaling molecule SH2 domain-containing inositol-polyphosphate 5-phosphatase (SHIP) binds to the tyrosine-phosphorylated beta subunit of the high affinity IgE receptor
12. Shc interaction with Src homology 2 domain containing inositol phosphatase (SHIP) in vivo requires the Shc-phosphotyrosine binding domain and two specific phosphotyrosines on SHIP
13. Erythropoietin induces the tyrosine phosphorylation of GAB1 and its association with SHC, SHP2, SHIP, and phosphatidylinositol 3-kinase
14. p150Ship, a signal transduction molecule with inositol polyphosphate-5-phosphatase activity
15. The Src homology 2 (SH2) domain of SH2-containing inositol phosphatase (SHIP) is essential for tyrosine phosphorylation of SHIP, its association with Shc, and its induction of apoptosis
16. Interleukin-3 induces the association of the inositol 5-phosphatase SHIP with SHP2
17. SHIP is a negative regulator of growth factor receptor-mediated PKB/Akt activation and myeloid cell survival
18. The SH2-containing inositol polyphosphate 5-phosphatase, ship, is expressed during hematopoiesis and spermatogenesis
19. A novel spliced form of SH2-containing inositol phosphatase SHIP is expressed during myeloid development
20. A presynaptic inositol-5-phosphatase
21. Role of the inositol phosphatase SHIP in negative regulation of the immune system by the receptor Fc(γ)RIIB
22. The inositol 5'-phosphatase SHIP binds to immunoreceptor signaling motifs and responds to high affinity IgE receptor aggregation
23. Identification of a second SH2-domain-containing protein closely related to the phosphatidylinositol polyphosphate 5-phosphatase SHIP
24. MatInd and MatInspector: New fast and versatile tools for detection of consensus matches in nucleotide sequence data
25. Tissue-specific alternative splicing generates two synaptojanin isoforms with differential membrane binding properties
26. Structure, function, and biology of SHIP proteins
27. The phosphatidylinositol polyphosphate 5-phosphatase SHIP and the protein tyrosine phosphatase SHP-2 form a complex in hematopoietic cells which can be regulated by BCR/ABL and growth factors
28. The mouse SHIP2 (Inppl1) gene: Complementary DNA, genomic structure, promoter analysis, and gene expression in the embryo and adult mouse
29. The crystal structure of an Eph receptor SAM domain reveals a mechanism for modular dimerization
30. Oligomeric structure of the human EphB2 receptor SAM domain
31. Negative signaling in B cells causes reduced Ras activity by reducing Shc-Grb2 interactions
32. Protein interactions of Src homology 2 (SH2) domain-containing inositol phosphatase (SHIP): Association with Shc displaces SHIP from FcγRIIb in B cells
33. Cloning and characterization of human SHIP, the 145-kD inositol 5-phosphatase that associates with SHC after cytokine stimulation
34. Fiz1, a novel zinc finger protein interacting with the receptor tyrosine kinase Flt3