1TCE


Conserved Protein Domain Family
SH2_SHC

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cd09925: SH2_SHC 
Click on image for an interactive view with Cn3D
Src homology 2 (SH2) domain found in SH2 adaptor protein C (SHC)
SHC is involved in a wide variety of pathways including regulating proliferation, angiogenesis, invasion and metastasis, and bone metabolism. An adapter protein, SHC has been implicated in Ras activation following the stimulation of a number of different receptors, including growth factors [insulin, epidermal growth factor (EGF), nerve growth factor, and platelet derived growth factor (PDGF)], cytokines [interleukins 2, 3, and 5], erythropoietin, and granulocyte/macrophage colony-stimulating factor, and antigens [T-cell and B-cell receptors]. SHC has been shown to bind to tyrosine-phosphorylated receptors, and receptor stimulation leads to tyrosine phosphorylation of SHC. Upon phosphorylation, SHC interacts with another adapter protein, Grb2, which binds to the Ras GTP/GDP exchange factor mSOS which leads to Ras activation. SHC is composed of an N-terminal domain that interacts with proteins containing phosphorylated tyrosines, a (glycine/proline)-rich collagen-homology domain that contains the phosphorylated binding site, and a C-terminal SH2 domain. SH2 has been shown to interact with the tyrosine-phosphorylated receptors of EGF and PDGF and with the tyrosine-phosphorylated C chain of the T-cell receptor, providing one of the mechanisms of T-cell-mediated Ras activation. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.
Statistics
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PSSM-Id: 198179
View PSSM: cd09925
Aligned: 14 rows
Threshold Bit Score: 163.286
Threshold Setting Gi: 308257022
Created: 25-Feb-2011
Updated: 17-Jan-2013
Structure
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Program:
Drawing:
Aligned Rows:
 
phosphotyrosinehydrophobic
Conserved site includes 8 residues -Click on image for an interactive view with Cn3D
Feature 1:phosphotyrosine binding pocket [polypeptide binding site]
Evidence:

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                       #               # #    #    #         ###                        
1TCE_A         1 AEQLRGEPWFHGKLSRREAEALLQLNGDFLVRESTTTPGQYVLTGSQs-GQPKHLLLVDPEGVVRTKDHRFESVSHLISY 79
gi 6911894   293 QCPLTAEVWFHAGISRPISERLLQQDGDFLVRESQGKRGQYVLTGLEg-KTPKHLLLIDPEGVVRTKDRIFDSISHLINY 371
gi 182691592 362 EDQLKREPWYQGKMSRKEAERLLKVNGDFLVRESTTTPGQYVLTGLQc-GQPKHLLLVDPEGVVRTKDHRFESVSHLISY 440
gi 25141253  203 TEDVVGKVWYHGNLSREDAQALLKTEGDFLVRQSDHTPGKYVLSGRTaeNEHKHLILLDNHNRVRTRDRTFSNISELIDY 282
gi 308257022 204 SDDVVGKVWFHGHLSRDDAQSLLTTAGDFLVRQSDHTSGKFVLSGLTtdGDHKHLILLDHQMRVRTRDHEFNNITELIDY 283
gi 113678838 398 EDQLRREMWYHGRMSRRDAENLLGRDGDFLVRDSATNPGQYVLTGMQc-GLPKHLLLVDPEGVVRTKDMLFESISHLINY 476
gi 326427778 365 QRELSAEPWFHGQVSRAAADSILQYDGDFFVRESMQSRGQYILSAMHk-GEKKHLLLVDPSGQVRTKDMAFDSVSHLINY 443
gi 327290517 504 EEQLKQEPWYHGKMSRKDAEKRLRADGDFLVRDSITNPGQYVLTGMHg-GQPKHLLLVDPEGVVRTKDALFESISHLINY 582
gi 108875255 298 KSQLLTESWYHGNISRAQSEHLLKNDGDFLVRESAGTPGQYVLTGMQn-NLPKHLLLIDPEGIVRTKDRIFESISHLINY 376
gi 48474337  371 LEELNAEPWYQGEMSRKEAEALLREDGDFLVRKSTTNPGSFVLTGMHn-GQAKHLLLVDPEGTIRTKDRVFDSISHLINY 449
                         90       100       110
                 ....*....|....*....|....*....|
Feature 1                                      
1TCE_A        80 HMDNHLPIISAGSELCl-----qQPVERKL 104
gi 6911894   372 HWAHALPIISEDSELVl-----rNPVRRPQ 396
gi 182691592 441 HMDNHLPIISAGSELCl-----qQPVERRQ 465
gi 25141253  283 HVNNGMAVRSEGRDREtsl-nliRPVPCPG 311
gi 308257022 284 HMTNGIAVRTERNAKGetsimllRPVPAPA 313
gi 113678838 477 HLTNKLPIVAAESELHl-----qQVVCRKI 501
gi 326427778 444 HLRARLPIISRGSRIVl-----gQAVRALP 468
gi 327290517 583 HLQNEQPIVAAESELHl------RQVVRWK 606
gi 108875255 377 HWTNSLPIISAESALLl-----rHPILRTT 401
gi 48474337  450 HLESSLPIVSAGSELCl-----qQPVERKP 474

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