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Mouse SHP2 / PTPN11  Protein

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Expression host: Human Cells  
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SHP2 / PTPN11 Summary & Protein Information

SHP2 / PTPN11 Background

Gene Summary: The protein encoded by this PTPN11 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 SHP2 protein contains two tandem Src homology-2 domains, which function as phospho-tyrosine binding domains and mediate the interaction of this PTP with its substrates. This SHP2 protein is widely expressed in most tissues and plays a regulatory role in various cell signaling events that are important for a diversity of cell functions, such as mitogenic activation, metabolic control, transcription regulation, and cell migration. Mutations in this gene are a cause of Noonan syndrome as well as acute myeloid leukemia. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, May 2012]
General information above from NCBI
Catalytic activity: Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate. {ECO:0000255|PROSITE-ProRule:PRU10044, ECO:0000269|PubMed:20170098}.
Subunit structure: Interacts with phosphorylated LIME1 and BCAR3. Interacts with SHB and INPP5D/SHIP1 (By similarity). Interacts with MILR1 (tyrosine-phosphorylated). Interacts with FLT1 (tyrosine-phosphorylated), FLT3 (tyrosine-phosphorylated), FLT4 (tyrosine-phosphorylated), KIT and GRB2. Interacts with PDGFRA (tyrosine phosphorylated). Interacts (via SH2 domain) with TEK/TIE2 (tyrosine phosphorylated) (By similarity). Interacts with PTPNS1 and CD84. Interacts with phosphorylated SIT1 and MPZL1. Interacts with FCRL3, FCRL4, FCRL6 and ANKHD1. Interacts with KIR2DL1; the interaction is enhanced by ARRB2. Interacts with GAB2. Interacts with TERT; the interaction retains TERT in the nucleus. Interacts with PECAM1 and FER. Interacts with EPHA2 (activated); participates in PTK2/FAK1 dephosphorylation in EPHA2 downstream signaling. Interacts with ROS1; mediates PTPN11 phosphorylation. Interacts with PDGFRB (tyrosine phosphorylated); this interaction increases the PTPN11 phosphatase activity. Interacts with GAREM isoform 1 (tyrosine phosphorylated); the interaction increases MAPK/ERK activity and does not affect the GRB2/SOS complex formation. {ECO:0000250, ECO:0000269|PubMed:10068651, ECO:0000269|PubMed:10209036, ECO:0000269|PubMed:10655584, ECO:0000269|PubMed:10681522, ECO:0000269|PubMed:11162587, ECO:0000269|PubMed:11389028, ECO:0000269|PubMed:11414741, ECO:0000269|PubMed:11433379, ECO:0000269|PubMed:12972546, ECO:0000269|PubMed:14597715, ECO:0000269|PubMed:15102829, ECO:0000269|PubMed:16885344, ECO:0000269|PubMed:16956752, ECO:0000269|PubMed:17213291, ECO:0000269|PubMed:18604210, ECO:0000269|PubMed:18829466, ECO:0000269|PubMed:19342684, ECO:0000269|PubMed:19509291, ECO:0000269|PubMed:20170098, ECO:0000269|PubMed:20494825, ECO:0000269|PubMed:7691811, ECO:0000269|PubMed:8810330, ECO:0000269|PubMed:9062191, ECO:0000269|PubMed:9600074}.
Domain: The SH2 domains repress phosphatase activity. Binding of these domains to phosphotyrosine-containing proteins relieves this auto-inhibition, possibly by inducing a conformational change in the enzyme.
Subcellular location: Cytoplasm.
Tissue specificity: Widely expressed, with highest levels in heart, brain, and skeletal muscle. {ECO:0000269|PubMed:1280823, ECO:0000269|PubMed:7681589, ECO:0000269|PubMed:8216283}.
Post-translational: Phosphorylated on Tyr-546 and Tyr-584 upon receptor protein tyrosine kinase activation; which creates a binding site for GRB2 and other SH2-containing proteins. Phosphorylated upon activation of the receptor-type kinase FLT3. Phosphorylated upon activation of the receptor-type kinase PDGFRA (By similarity). Phosphorylated by activated PDGFRB. {ECO:0000250, ECO:0000269|PubMed:20494825, ECO:0000269|PubMed:7681217, ECO:0000269|PubMed:7691811, ECO:0000269|PubMed:8041791}.
Involvement in disease: DISEASE: LEOPARD syndrome 1 (LPRD1) [MIM:151100]: A disorder characterized by lentigines, electrocardiographic conduction abnormalities, ocular hypertelorism, pulmonic stenosis, abnormalities of genitalia, retardation of growth, and sensorineural deafness. {ECO:0000269|PubMed:12058348, ECO:0000269|PubMed:14961557, ECO:0000269|PubMed:15121796, ECO:0000269|PubMed:15389709, ECO:0000269|PubMed:15520399, ECO:0000269|PubMed:15690106, ECO:0000269|PubMed:16679933, ECO:0000269|PubMed:24891296}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Noonan syndrome 1 (NS1) [MIM:163950]: A form of Noonan syndrome, a disease characterized by short stature, facial dysmorphic features such as hypertelorism, a downward eyeslant and low-set posteriorly rotated ears, and a high incidence of congenital heart defects and hypertrophic cardiomyopathy. Other features can include a short neck with webbing or redundancy of skin, deafness, motor delay, variable intellectual deficits, multiple skeletal defects, cryptorchidism, and bleeding diathesis. Individuals with Noonan syndrome are at risk of juvenile myelomonocytic leukemia, a myeloproliferative disorder characterized by excessive production of myelomonocytic cells. Some patients with NS1 develop multiple giant cell lesions of the jaw or other bony or soft tissues, which are classified as pigmented villonodular synovitis (PVNS) when occurring in the jaw or joints. {ECO:0000269|PubMed:11704759, ECO:0000269|PubMed:11992261, ECO:0000269|PubMed:12161469, ECO:0000269|PubMed:12325025, ECO:0000269|PubMed:12529711, ECO:0000269|PubMed:12634870, ECO:0000269|PubMed:12717436, ECO:0000269|PubMed:12739139, ECO:0000269|PubMed:12960218, ECO:0000269|PubMed:15384080, ECO:0000269|PubMed:15948193, ECO:0000269|PubMed:19020799, ECO:0000269|PubMed:24891296}. Note=The disease is caused by mutations affecting the gene represented in this entry. Mutations in PTPN11 account for more than 50% of the cases.; DISEASE: Leukemia, juvenile myelomonocytic (JMML) [MIM:607785]: An aggressive pediatric myelodysplastic syndrome/myeloproliferative disorder characterized by malignant transformation in the hematopoietic stem cell compartment with proliferation of differentiated progeny. Patients have splenomegaly, enlarged lymph nodes, rashes, and hemorrhages. {ECO:0000269|PubMed:12717436}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Metachondromatosis (MC) [MIM:156250]: A skeletal disorder with radiologic features of both multiple exostoses and Ollier disease, characterized by the presence of exostoses, commonly of the bones of the hands and feet, and enchondromas of the metaphyses of long bones and iliac crest. {ECO:0000269|PubMed:20577567}. Note=The disease is caused by mutations affecting the gene represented in this entry.
Sequence similarity: Belongs to the protein-tyrosine phosphatase family. Non-receptor class 2 subfamily. {ECO:0000305}.; Contains 2 SH2 domains. {ECO:0000255|PROSITE-ProRule:PRU00191}.; Contains 1 tyrosine-protein phosphatase domain. {ECO:0000255|PROSITE-ProRule:PRU00160}.
General information above from UniProt

SHP2, also known as PTPN11, belongs to the protein-tyrosine phosphatase(PTP) family, non-receptor class 2 subfamily. PTPs catalyze the removal of phosphate groups from tyrosine residues by the hydrolysis of phosphoric acid monoesters. They dephosphorylate EGFR, JAK2 and TYK2 kinases, promoting oncogenic transformation. SHP2 is widely expressed, with highest levels in heart, brain, and skeletal muscle. SHP2 acts downstream of various receptor and cytoplasmic protein tyrosine kinases to participate in the signal transduction from the cell surface to the nucleus. It also dephosphorylates ROCK2 at Tyr-722 resulting in stimulatation of its RhoA binding activity.

SHP2 / PTPN11 Alternative Name

CFC,NS1,SHP2,BPTP3,PTP2C,PTP-1D,SH-PTP2,SH-PTP3, [homo-sapiens]
BPTP3,CFC,NS1,protein-tyrosine phosphatase 1D,protein-tyrosine phosphatase 2C,PTP-1D,PTP2C,PTP-2C,SHP2,SH-PTP2,SH-PTP3,tyrosine-protein phosphatase non-receptor type 11, [human]
2700084A17Rik,AW536184,protein-tyrosine phosphatase SYP,PTP1D,PTP2C,SAP-2,SH2 domain-containing protein tyrosine phosphatase-2,Shp2,SHP-2,SH-PTP2,SH-PTP3,Syp,tyrosine-protein phosphatase non-receptor type 11, [mouse]
Sap-2,Syp,Shp2,PTP1D,PTP2C,SHP-2,SH-PTP2,SH-PTP3,AW536184,2700084A17Rik, [mus-musculus]

SHP2 / PTPN11 Related Studies

  • Ganju R K, et al. (2000) Beta-chemokine receptor CCR5 signals through SHP1, SHP2, and Syk. J Biol Chem. 275(23):17263-8.
  • Yin T, et al. (1997) Molecular characterization of specific interactions between SHP-2 phosphatase and JAK tyrosine kinases. J Biol Chem. 272(2):1032-7.
  • Kontaridis MI, et al. (2006) PTPN11 (Shp2) mutations in LEOPARD syndrome have dominant negative, not activating, effects. J Biol Chem. 281(10):6785-92.