Sequence Detail

ID/Version

P29351 Q63872 Q63873 Q63874 Q9QVA8 Q9R0V6 O35128 Q921G3 Q9QVA6 Q9QVA7 (UniProt | EBI)

Last sequence update: 2002-07-11
Last annotation update: 2024-03-27

Sequence description from provider

RecName: Full=Tyrosine-protein phosphatase non-receptor type 6; EC=3.1.3.48;AltName: Full=70Z-SHP;AltName: Full=Hematopoietic cell protein-tyrosine phosphatase;AltName: Full=PTPTY-42;AltName: Full=Protein-tyrosine phosphatase 1C; Short=PTP

Provider

SWISS-PROT

Sequence

Polypeptide 595 aa

Source

Organism mouse

See UniProt | EBI for source

Annotated genes and markers

Follow the symbol links to get more information on the GO terms, expression assays, orthologs, phenotypic alleles, and other information for the genes or markers below.

Type	Symbol	Name	GO Terms	Expression Assays	Orthologs	Phenotypic Alleles
Gene	Ptpn6	protein tyrosine phosphatase, non-receptor type 6	106	105	3	24

Sequence references in MGI

J:2618 Yi TL, et al., Protein tyrosine phosphatase containing SH2 domains: characterization, preferential expression in hematopoietic cells, and localization to human chromosome 12p12-p13. Mol Cell Biol. 1992 Feb;12(2):836-46
J:14935 Shultz LD, et al., Mutations at the murine motheaten locus are within the hematopoietic cell protein-tyrosine phosphatase (Hcph) gene. Cell. 1993 Jul 2;73(7):1445-54
J:29004 Yi T, et al., Identification of novel protein tyrosine phosphatases of hematopoietic cells by polymerase chain reaction amplification. Blood. 1991 Nov 1;78(9):2222-8
J:32702 Matthews RJ, et al., Characterization of hematopoietic intracellular protein tyrosine phosphatases: description of a phosphatase containing an SH2 domain and another enriched in proline-, glutamic acid-, serine-, and threonine-rich sequences. Mol Cell Biol. 1992 May;12(5):2396-405
J:45711 Ansari-Lari MA, et al., Comparative sequence analysis of a gene-rich cluster at human chromosome 12p13 and its syntenic region in mouse chromosome 6. Genome Res. 1998 Jan;8(1):29-40
J:49645 Veillette A, et al., High expression of inhibitory receptor SHPS-1 and its association with protein-tyrosine phosphatase SHP-1 in macrophages. J Biol Chem. 1998 Aug 28;273(35):22719-28
J:51814 Huber M, et al., The carboxyl-terminal region of biliary glycoprotein controls its tyrosine phosphorylation and association with protein-tyrosine phosphatases SHP-1 and SHP-2 in epithelial cells. J Biol Chem. 1999 Jan 1;274(1):335-44
J:56522 Martin A, et al., Murine SHP-1 splice variants with altered Src homology 2 (SH2) domains. Implications for the SH2-mediated intramolecular regulation of SHP-1. J Biol Chem. 1999 Jul 30;274(31):21725-34
J:86931 Chung DH, et al., CMRF-35-like molecule-1, a novel mouse myeloid receptor, can inhibit osteoclast formation. J Immunol. 2003 Dec 15;171(12):6541-8
J:143718 Trost M, et al., The phagosomal proteome in interferon-gamma-activated macrophages. Immunity. 2009 Jan;30(1):143-54
J:161854 Hitomi K, et al., An immunoglobulin-like receptor, Allergin-1, inhibits immunoglobulin E-mediated immediate hypersensitivity reactions. Nat Immunol. 2010 Jul;11(7):601-7
J:168664 Babij P, et al., New variants in the Enpp1 and Ptpn6 genes cause low BMD, crystal-related arthropathy, and vascular calcification. J Bone Miner Res. 2009 Sep;24(9):1552-64
J:201266 Mazharian A, et al., Mice lacking the ITIM-containing receptor G6b-B exhibit macrothrombocytopenia and aberrant platelet function. Sci Signal. 2012;5(248):ra78
J:231275 Muller MM, et al., Homophilic adhesion and CEACAM1-S regulate dimerization of CEACAM1-L and recruitment of SHP-2 and c-Src. J Cell Biol. 2009 Nov 16;187(4):569-81
J:292518 Huttlin EL, et al., A tissue-specific atlas of mouse protein phosphorylation and expression. Cell. 2010 Dec 23;143(7):1174-89
J:314642 Wang LL, et al., Specificity of the SH2 domains of SHP-1 in the interaction with the immunoreceptor tyrosine-based inhibitory motif-bearing receptor gp49B. J Immunol. 1999 Feb 1;162(3):1318-23
J:314643 Lu-Kuo JM, et al., gp49B1 inhibits IgE-initiated mast cell activation through both immunoreceptor tyrosine-based inhibitory motifs, recruitment of src homology 2 domain-containing phosphatase-1, and suppression of early and late calcium mobilization. J Biol Chem. 1999 Feb 26;274(9):5791-6