Conserved Protein Domain Family
SHC

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cd01209: SHC 
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SHC phosphotyrosine-binding (PTB) domain
SHC phosphotyrosine-binding (PTB) domain. SHC is a substrate for receptor tyrosine kinases, which can interact with phosphoproteins at NPXY motifs. SHC contains an PTB domain followed by an SH2 domain. PTB domains have a PH-like fold and are found in various eukaryotic signaling molecules. They were initially identified based upon their ability to recognize phosphorylated tyrosine residues In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. More recent studies have found that some types of PTB domains can bind to peptides which are not tyrosine phosphorylated or lack tyrosine residues altogether.
Statistics
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PSSM-Id: 176285
View PSSM: cd01209
Aligned: 6 rows
Threshold Bit Score: -1
Threshold Setting Gi: 0
Created: 1-Nov-2000
Updated: 17-Jan-2013
Structure
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Program:
Drawing:
Aligned Rows:
Hierarchy
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Display:
 
Conserved site includes 4 residues -Click on image for an interactive view with Cn3D
Feature 1:phosphotyrosine binding site [chemical binding site]
Evidence:
  • Structure:SHC PTB domain complexed with a TrkA receptor phosphopeptide
    View structure with Cn3D
  • Citation:PMID 8524391
  • Comment:Shc PTB domain interacts with beta turn-forming sequences amino-terminal to phosphotyrosine
  • Citation:PMID 7543098

cd01209 is part of a hierarchy of related CD models.
Use the graphical representation to navigate this hierarchy.
cd00821:PHcd00824:PTBIcd00835:RanBD_familycd00836:FERM_C-lobecd00837:EVH1_familycd00900:PH-likecd00934:PTBcd01201:PH_BEACHcd01202:PTB_FRS2cd01203:PTB_DOK1_DOK2_DOK3cd01204:PTB_IRScd01205:EVH1_WASP-likecd01206:EVH1_Homer_Veslcd01207:EVH1_Ena_VASP-likecd01208:PTB_X11cd01209:PTB_Shccd01210:PTB_EPS8cd01211:PTB_Rab6GAPcd01212:PTB_JIPcd01213:PTB_tensincd01214:PTB_FAM43Acd01215:PTB_Dabcd01216:Fe65cd01217:PTB_CG12581cd01218:PH_Phafin2-likecd01219:PH1_FGD1cd01220:PH1_FARP1-likecd01221:PH_ephexincd01222:PH_clgcd01223:PH_Vavcd01224:PH_Collybistin_ASEFcd01225:PH_Cool_Pixcd01226:PH_RalBD_exo84cd01227:PH_Dbscd01228:PH_BCR-relatedcd01229:PH_Ect2cd01230:PH1_Tiam1_2cd01231:PH_SH2B_familycd01232:PH_TRIOcd01233:PH_KIFIA_KIFIBcd01234:PH_CADPScd01235:PH_Sbf1_hMTMR5cd01236:PH_RIPcd01237:PH_fermitincd01238:PH_Btkcd01239:PH_PKDcd01240:PH_GRK2_subgroupcd01241:PH_PKBcd01242:PH_ROCKcd01243:PH_MRCKcd01244:PH_GAP1-likecd01245:PH_RasGAP_CG5898cd01246:PH_oxysterol_bpcd01247:PH_FAPP1_FAPP2cd01248:PH_PLC_ELMO1cd01249:BAR-PH_GRAF_familycd01250:PH_AGAPcd01251:PH2_ADAPcd01252:PH_GRP1-likecd01253:PH_ARHGAP21-likecd01254:PH_PLDcd01255:PH2_Tiam1_2cd01256:PH_dynamincd01257:PH_IRScd01258:PHsplit_syntrophincd01259:PH_APBB1IPcd01260:PH_CNK_mammalian-likecd01261:PH_SOScd01262:PH_PDK1cd01263:PH_anillincd01264:PH_MELT_VEPH1cd01265:PH_TBC1D2Acd01266:PH_Gab1_Gab2cd01267:CED6_AIDA1bcd01268:PTB_Numbcd01269:PTB_TBC1D1_likecd01270:PTB_CAPON-likecd01271:PTB2_Fe65cd01272:PTB1_Fe65cd01273:PTB_CED-6cd01274:PTB_Anks75041151079556249540891SHC A1N3H A1421198475041151079556249540891SHC A1N3H A14211984
cd01209 Sequence Cluster
cd01209 Sequence Cluster
Sub-family Hierarchy
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 cd01209 Branch
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CD Hierarchy
Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                  #                                                    
1SHC_A       28 HPNDKVMGPGVSYLVRYMGCVEVLQSMRALDFNTRTQVTREAISLVCEAVPgakgatrrrkpcsrplsSILGRSNLKFAG 107
1N3H_A       40 HPNDKVMGPGVSYLVRYMGCVEVLQSMRALDFNTRTQVTREAISLVCEAVPgakgatrrrkpcsrplsSILGRSNLKFAG 119
gi 1079556   22 YPDDVIMGVGVAFNVRYTGCVEVKTSMKSLDFETRTQLARECINRVCEAAGlksagk------rrltnFISDRPSMQHAG 95
gi 24954089  43 HPDDKVMGPGVPYLVRYMGCVEVLQSMRALDFNTRTQVTREAISLVCDAVPgakgamrrrktcgrslnSILGKSNLKFAG 122
gi 14211984 150 HPNDKVMGPGVSYLVRYMGCVEVLQSMRALDFNTRTQVTREAISLVCEAVPgakgatrrrkpcsrplsSILGRSNLKFAG 229
gi 7504115    7 SFAEELRSSGVSLSATYLGSVPVVESINVMVSEMRVQVVSECIQHVAATVGvtaar-------einpvVSRVIGEVKKEN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                      #                   #      #                     
1SHC_A      108 MPITLTVSTSSLNLMAAdckqIIANHhMQSISFASGGD--PDTAEYVAYVAKDPv-nQRACHILECPeglAQDVISTIGQ 184
1N3H_A      120 MPITLTVSTSSLNLMAAdckqIIANHhMQSISFASGGD--PDTAEYVAYVAKDPv-nQRACHILECPeglAQDVISTIGQ 196
gi 1079556   96 TNIIINVSSRALSLSNVetgeVIANHnMPRISFASGGD--NDTLDFLAYIAKNEd-eWAACYVLECAggqSEDLIVTIGK 172
gi 24954089 123 MPITLTVSTSSLNLMASdckqIIANHhMQSISFASGGD--PDTAEYVAYVAKDPv-nQRACHILECPeglAQDVISTIGQ 199
gi 14211984 230 MPITLTVSTSSLNLMAAdckqIIANHhMQSISFASGGD--PDTAEYVAYVAKDPv-nQRACHILECPeglAQDVISTIGQ 306
gi 7504115   80 FPVDINISSKMIKIIKQs--rLIQRHpFSFFSFGAQGQkgTDTELMFGYIAKNKdgtDRRCHVVFIEd--VHKLIDVLTT 155

                ....*....
Feature 1                
1SHC_A      185 AFELRFKQY 193
1N3H_A      197 AFELRFKQY 205
gi 1079556  173 AFALRFNAL 181
gi 24954089 200 AFELRFKQY 208
gi 14211984 307 AFELRFKQY 315
gi 7504115  156 AINVNTFDA 164

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Conserved site includes 4 residues -Click on image for an interactive view with Cn3D