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CD45/PTPRC  Белок

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Хозяин экспрессии: Human Cells  
10086-H02H-50
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Хозяин экспрессии: Baculovirus-Insect Cells  
50713-M20B-20
50713-M20B-100
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Хозяин экспрессии: Human Cells  
50713-M02H1-50
50713-M02H1-100
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Хозяин экспрессии: Baculovirus-Insect Cells  
50713-MCCB-20
50713-MCCB-100
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CD45/PTPRC Related Area

CD45/PTPRC Связанные пути

CD45/PTPRC Краткая информация и сведения о белках

CD45/PTPRC Фон

Краткая информация о гене: The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP contains an extracellular domain, a single transmembrane segment and two tandem intracytoplasmic catalytic domains, and thus belongs to receptor type PTP. This gene is specifically expressed in hematopoietic cells. This PTP has been shown to be an essential regulator of T- and B-cell antigen receptor signaling. It functions through either direct interaction with components of the antigen receptor complexes, or by activating various Src family kinases required for the antigen receptor signaling. This PTP also suppresses JAK kinases, and thus functions as a regulator of cytokine receptor signaling. Four alternatively spliced transcripts variants of this gene, which encode distinct isoforms, have been reported.
General information above from NCBI
Каталитическая активность: Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate. {ECO:0000255|PROSITE-ProRule:PRU10044}.
Структура подгруппы: Binds GANAB and PRKCSH (By similarity). Interacts with SKAP1. Interacts with DPP4; the interaction is enhanced in a interleukin-12-dependent manner in activated lymphocytes. {ECO:0000250, ECO:0000269|PubMed:11909961, ECO:0000269|PubMed:12676959, ECO:0000269|PubMed:15684325}.
Домен: The first PTPase domain interacts with SKAP1.
Субклеточное местоположение: Membrane {ECO:0000269|PubMed:12676959}; Single-pass type I membrane protein {ECO:0000269|PubMed:12676959}. Membrane raft {ECO:0000269|PubMed:12676959}. Note=Colocalized with DPP4 in membrane rafts.
Посттрансляционный: Heavily N- and O-glycosylated. {ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973}.
Степень заражения: DISEASE: Severe combined immunodeficiency autosomal recessive T-cell-negative/B-cell-positive/NK-cell-positive (T(-)B(+)NK(+) SCID) [MIM:608971]: A form of severe combined immunodeficiency (SCID), a genetically and clinically heterogeneous group of rare congenital disorders characterized by impairment of both humoral and cell-mediated immunity, leukopenia, and low or absent antibody levels. Patients present in infancy recurrent, persistent infections by opportunistic organisms. The common characteristic of all types of SCID is absence of T-cell-mediated cellular immunity due to a defect in T-cell development. {ECO:0000269|PubMed:11145714}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Multiple sclerosis (MS) [MIM:126200]: A multifactorial, inflammatory, demyelinating disease of the central nervous system. Sclerotic lesions are characterized by perivascular infiltration of monocytes and lymphocytes and appear as indurated areas in pathologic specimens (sclerosis in plaques). The pathological mechanism is regarded as an autoimmune attack of the myelin sheath, mediated by both cellular and humoral immunity. Clinical manifestations include visual loss, extra-ocular movement disorders, paresthesias, loss of sensation, weakness, dysarthria, spasticity, ataxia and bladder dysfunction. Genetic and environmental factors influence susceptibility to the disease. {ECO:0000269|PubMed:11101853}. Note=Disease susceptibility may be associated with variations affecting the gene represented in this entry.
Сходство последовательностей: Belongs to the protein-tyrosine phosphatase family. Receptor class 1/6 subfamily. {ECO:0000305}.; Contains 2 fibronectin type-III domains. {ECO:0000255|PROSITE-ProRule:PRU00316}.; Contains 2 tyrosine-protein phosphatase domains. {ECO:0000255|PROSITE-ProRule:PRU00160}.
General information above from UniProt

The cluster of differentiation (CD) system is commonly used as cell markers in immunophynotyping. Different kinds of cells in the immune system can be identified through the surface CD molecules which associating with the immune function of the cell. There are more than 320 CD unique clusters and subclusters have been identified. Some of the CD molecules serve as receptors or ligands important to the cell through initiating a signal cascade which then alter the behavior of the cell. Some CD proteins do not take part in cell signal process but have other functions such as cell adhesion. Protein tyrosine phosphatase, receptor type C (CD45), also known as PTPRC is a member of the protein tyrosine phosphatase (PTP) family which is known for its function to serve as signaling molecules and to regulate a variety of cellular processes such as cell proliferation, differentiation, mitotic cycle and oncogenic transformation. CD45 is found expression specifically in hemotopietic cells. CD45 consists of an extracellular domain, a single transmembrane segment and two tandem intracytoplasmic catalytic domains. It serves as an essential regulator of T-cell and B-cell antigen receptor signaling through either direct interaction with components of the antigen receptor complexs or by activating various Src family kinases required for the antigen receptor signaling and it also can suppress JAK kinases.

CD45/PTPRC Альтернативное название

CD45/PTPRC Связанные исследования

  • Zola H, et al. (2007) CD molecules 2006-human cell differentiation molecules. J Immunol Methods. 318 (1-2): 1-5.
  • Ho IC, et al. (2009) GATA3 and the T-cell lineage: essential functions before and after T-helper-2-cell differentiation. Nat Rev Immunol. 9 (2): 125-35.
  • Matesanz-Isabel J, et al. (2011) New B-cell CD molecules. Immunology Letters.134 (2): 104-12.
  • Irie-Sasaki J, et al. (2001) CD45 is a JAK phosphatase and negatively regulates cytokine receptor signaling. Nature. 409: 349-54.
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