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Conserved domains on  [gi|530360601|ref|XP_005263534|]
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ERBB receptor feedback inhibitor 1 isoform X2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Inhibitor_Mig-6 super family cl13070
EGFR receptor inhibitor Mig-6; When the kinase domain of EGFR binds to segment one of Mitogen ...
264-316 4.56e-10

EGFR receptor inhibitor Mig-6; When the kinase domain of EGFR binds to segment one of Mitogen induced gene 6 (Mig-6), EGFR becomes inactive due to the conformation it adopts which is Src/CDK like. The binding of the two proteins prevents EGFR acting as a cyclin-like activator for other kinase domains.The structure of Mig-6(1) consists of alpha helices-G and -H with a polar surface and hydrophobic residues for interactions with EGFR. A critical step for the activation of EGFR is the formation of an asymmetric dimer involving the kinase domains of the protein. Since Mig-6 binds to the kinase domain it blocks this process and EGFR becomes inactive.


The actual alignment was detected with superfamily member pfam11555:

Pssm-ID: 463294 [Multi-domain]  Cd Length: 74  Bit Score: 55.39  E-value: 4.56e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360601  264 RPPKVPPREPLSPSNSRTPSPK-------------SLPSYLNG----VMPPTQSFAPDPKYVSSKALQRQ 316
Cdd:pfam11555   1 RPPQIPPRDPLSQPGSRTPSPMglvvgspqqpathSYSSYLSTspgkLMPTTQSFASDPKYAAPKVIQAQ 70
 
Name Accession Description Interval E-value
Inhibitor_Mig-6 pfam11555
EGFR receptor inhibitor Mig-6; When the kinase domain of EGFR binds to segment one of Mitogen ...
264-316 4.56e-10

EGFR receptor inhibitor Mig-6; When the kinase domain of EGFR binds to segment one of Mitogen induced gene 6 (Mig-6), EGFR becomes inactive due to the conformation it adopts which is Src/CDK like. The binding of the two proteins prevents EGFR acting as a cyclin-like activator for other kinase domains.The structure of Mig-6(1) consists of alpha helices-G and -H with a polar surface and hydrophobic residues for interactions with EGFR. A critical step for the activation of EGFR is the formation of an asymmetric dimer involving the kinase domains of the protein. Since Mig-6 binds to the kinase domain it blocks this process and EGFR becomes inactive.


Pssm-ID: 463294 [Multi-domain]  Cd Length: 74  Bit Score: 55.39  E-value: 4.56e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360601  264 RPPKVPPREPLSPSNSRTPSPK-------------SLPSYLNG----VMPPTQSFAPDPKYVSSKALQRQ 316
Cdd:pfam11555   1 RPPQIPPRDPLSQPGSRTPSPMglvvgspqqpathSYSSYLSTspgkLMPTTQSFASDPKYAAPKVIQAQ 70
 
Name Accession Description Interval E-value
Inhibitor_Mig-6 pfam11555
EGFR receptor inhibitor Mig-6; When the kinase domain of EGFR binds to segment one of Mitogen ...
264-316 4.56e-10

EGFR receptor inhibitor Mig-6; When the kinase domain of EGFR binds to segment one of Mitogen induced gene 6 (Mig-6), EGFR becomes inactive due to the conformation it adopts which is Src/CDK like. The binding of the two proteins prevents EGFR acting as a cyclin-like activator for other kinase domains.The structure of Mig-6(1) consists of alpha helices-G and -H with a polar surface and hydrophobic residues for interactions with EGFR. A critical step for the activation of EGFR is the formation of an asymmetric dimer involving the kinase domains of the protein. Since Mig-6 binds to the kinase domain it blocks this process and EGFR becomes inactive.


Pssm-ID: 463294 [Multi-domain]  Cd Length: 74  Bit Score: 55.39  E-value: 4.56e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360601  264 RPPKVPPREPLSPSNSRTPSPK-------------SLPSYLNG----VMPPTQSFAPDPKYVSSKALQRQ 316
Cdd:pfam11555   1 RPPQIPPRDPLSQPGSRTPSPMglvvgspqqpathSYSSYLSTspgkLMPTTQSFASDPKYAAPKVIQAQ 70
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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