Conserved Protein Domain Family
SH2_SHC

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cd09925: SH2_SHC 
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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:
Hierarchy
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Display:
 
phosphotyrosinehydrophobic
Conserved site includes 8 residues -Click on image for an interactive view with Cn3D
Feature 1:phosphotyrosine binding pocket [polypeptide binding site]
Evidence:

cd09925 is part of a hierarchy of related CD models.
Use the graphical representation to navigate this hierarchy.
cd09925 is a member of the superfamily cl15255.
cd00173:SH2cd09918:SH2_Nterm_SPT6_likecd09919:SH2_STAT_familycd09920:SH2_Cbl-b_TKBcd09921:SH2_Jak_familycd09923:SH2_SOCS_familycd09925:SH2_SHCcd09926:SH2_CRK_likecd09927:SH2_Tensin_likecd09928:SH2_Cterm_SPT6_likecd09929:SH2_BLNK_SLP-76cd09930:SH2_cSH2_p85_likecd09931:SH2_C-SH2_SHP_likecd09932:SH2_C-SH2_PLC_gamma_likecd09933:SH2_Src_familycd09934:SH2_Tec_familycd09935:SH2_ABLcd09937:SH2_csk_likecd09938:SH2_N-SH2_Zap70_Syk_likecd09939:SH2_STAP_familycd09940:SH2_Vav_familycd09941:SH2_Grb2_likecd09942:SH2_nSH2_p85_likecd09943:SH2_Nck_familycd09944:SH2_Grb7_familycd09945:SH2_SHB_SHD_SHE_SHF_likecd09946:SH2_HSH2_likecd10337:SH2_BCAR3cd10338:SH2_SHAcd10339:SH2_RIN_familycd10340:SH2_N-SH2_SHP_likecd10341:SH2_N-SH2_PLC_gamma_likecd10342:SH2_SAP1cd10343:SH2_SHIPcd10344:SH2_SLAPcd10345:SH2_C-SH2_Zap70_Syk_likecd10346:SH2_SH2B_familycd10347:SH2_Nterm_shark_likecd10348:SH2_Cterm_shark_likecd10349:SH2_SH2D2A_SH2D7cd10350:SH2_SH2D4Acd10351:SH2_SH2D4Bcd10352:SH2_a2chimerin_b2chimerincd10353:SH2_Nterm_RasGAPcd10354:SH2_Cterm_RasGAPcd10355:SH2_DAPP1_BAM32_likecd10356:SH2_ShkA_ShkCcd10357:SH2_ShkD_ShkEcd10358:SH2_PTK6_Brkcd10359:SH2_SH3BP2cd10360:SH2_Srmcd10361:SH2_Fps_familycd10362:SH2_Src_Lckcd10363:SH2_Src_HCKcd10364:SH2_Src_Lyncd10365:SH2_Src_Srccd10366:SH2_Src_Yescd10367:SH2_Src_Fgrcd10368:SH2_Src_Fyncd10369:SH2_Src_Frkcd10370:SH2_Src_Src42cd10371:SH2_Src_Blkcd10372:SH2_STAT1cd10373:SH2_STAT2cd10374:SH2_STAT3cd10375:SH2_STAT4cd10376:SH2_STAT5cd10377:SH2_STAT6cd10378:SH2_Jak1cd10379:SH2_Jak2cd10380:SH2_Jak3cd10381:SH2_Jak_Tyk2cd10382:SH2_SOCS1cd10383:SH2_SOCS2cd10384:SH2_SOCS3cd10385:SH2_SOCS4cd10386:SH2_SOCS5cd10387:SH2_SOCS6cd10388:SH2_SOCS7cd10389:SH2_SHBcd10390:SH2_SHDcd10391:SH2_SHEcd10392:SH2_SHFcd10393:SH2_RIN1cd10394:SH2_RIN2cd10395:SH2_RIN3cd10396:SH2_Tec_Itkcd10397:SH2_Tec_Btkcd10398:SH2_Tec_Txkcd10399:SH2_Tec_Bmxcd10400:SH2_SAP1acd10401:SH2_C-SH2_Syk_likecd10402:SH2_C-SH2_Zap70cd10403:SH2_STAP1cd10404:SH2_STAP2cd10405:SH2_Vav1cd10406:SH2_Vav2cd10407:SH2_Vav3cd10408:SH2_Nck1cd10409:SH2_Nck2cd10410:SH2_SH2B1cd10411:SH2_SH2B2cd10412:SH2_SH2B3cd10413:SH2_Grb7cd10414:SH2_Grb14cd10415:SH2_Grb10cd10416:SH2_SH2D2Acd10417:SH2_SH2D7cd10418:SH2_Src_Fyn_isoform_a_likecd10419:SH2_Src_Fyn_isoform_b_likecd10420:SH2_STAT5bcd10421:SH2_STAT5acd10718:SH2_CIS1TCE A18269159248474337119573552326934412113678838327290517691189424661606108875255251412533082570221585984543264277781TCE A1826915924847433711957355232693441211367883832729051769118942466160610887525525141253308257022158598454326427778
cd09925 Sequence Cluster
cd09925 Sequence Cluster
Sub-family Hierarchy
 cd09925 Branch
 Whole Hierarchy
 [Download CDTree]
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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