2Y3A,3L4Q,3MTT


Conserved Protein Domain Family
iSH2_PIK3R2

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cd12926: iSH2_PIK3R2 
Click on image for an interactive view with Cn3D
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunit 2, PIK3R2, also called p85beta
PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation, and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. p85beta, also called PIK3R2, contains N-terminal SH3 and GAP domains. It is expressed ubiquitously but at lower levels than p85alpha. Its expression is increased in breast and colon cancer, correlates with tumor progression, and enhanced invasion. During viral infection, the viral nonstructural (NS1) protein binds p85beta specifically, which leads to PI3K activation and the promotion of viral replication. Mice deficient with PIK3R2 develop normally and exhibit moderate metabolic and immunological defects.
Statistics
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PSSM-Id: 214019
View PSSM: cd12926
Aligned: 7 rows
Threshold Bit Score: 244.992
Threshold Setting Gi: 285803627
Created: 31-Aug-2012
Updated: 17-Jan-2013
Structure
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Program:
Drawing:
Aligned Rows:
 
heterodimerNS1 interaction
Conserved site includes 43 residues -Click on image for an interactive view with Cn3D
Feature 1:heterodimer interface [polypeptide binding site]
Evidence:
  • Comment:Class IA PI3Ks consist of heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The C and R subunits interact mainly through the iSH2 domain of R subunits and the N-terminal ABD of C subunits.
  • Structure:2Y3A: Mus musculus p85beta iSH2 domain interacts with p110beta; contacts at 4A.
    View structure with Cn3D

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                             # ##   # #    # ##  ### ### ##  ## ##  ##  ##              
2Y3A_B        11 DSVEAVGAQLKVYHQQYQDKSREYDQLYEEYTRTSQELQMKRTAIEAFNETIKIFEEQGQTQEKCSKEYLERFRREGNeK 90
3L4Q_C        10 DSVEAVGAQLKVYHQQYQDKSREYDQLYEEYTRTSQELQMKRTAIEAFNETIKIFEEQGQTQEKSSKEYLERFRREGNeK 89
3MTT_A         6 DSVEAVGAQLKVYHQQYQDKSREYDQLYEEYTRTSQELQMKRTAIEAFNETIKIFEEQGQTQEKCSKEYLERFRREGNeK 85
gi 363743901 444 DSVEAVGEQLKVYHQQYQDKSWEYDLLYEEYTRTSQELQMKRTAIEAFNETIKIFEEQCQTQEKCSKEYIERFRREGNeK 523
gi 387017654 441 DSVEAVGEQLKVYHQQYQDKSREYDLLYEEYTRTSQELQMKRTAIEAFNETIKIFEEQCQTQEKCSRDYVERFRREGNeK 520
gi 40226308   33 DSVEAVGAQLKVYHQQYQDKSREYDQLYEEYTRTSQELQMKRTAIEAFNETIKIFEEQGQTQEKCSKEYLERFRREGNeK 112
gi 47086393  437 DSIEAVGEQLKVYHEQYQEKSREYDVLYEEYTRSSQELQMKRTAIEAFNETIKIFEEQCETQERLSRDSIEKFRREGNdK 516
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1        #  ##  #  ##  #   #           #  ##  #  ## ##  ##     #                         
2Y3A_B        91 EMQRILLNSERLKSRIAEIHESRTKLEQDLRAQASDNREIDKRMNSLKPDLMQLRKIRDQYLVWLTQKGARQRKINEWLG 170
3L4Q_C        90 EMQRILLNSERLKSRIAEIHESRTKLEQELRAQASDNREIDKRMNSLKPDLMQLRKIRDQYLVWLTQKGARQKKINEWLG 169
3MTT_A        86 EMQRILLNSERLKSRIAEIHESRTKLEQQLRAQASDNREIDKRMNSLKPDLMQLRKIRDQYLVWLTQKGARQKKINEWLG 165
gi 363743901 524 EVQRILMNSEKLKSRITEIHDSKMKLEQDLKKQASENREIDKRMNSLKPDLMQLRKLRDQYLVWLTQKGARQKKINEWLG 603
gi 387017654 521 EVQRIMMNSEKLKSRITEIHDSKMKLEQDLKQQASENREIDKRMNSLKPDLLQLRKLRDQYLVWLTQKGTRQKKINEWLG 600
gi 40226308  113 EMQRILLNSERLKSRIAEIHESRTKLEQQLRAQASDNREIDKRMNSLKPDLMQLRKIRDQYLVWLTQKGARQKKINEWLG 192
gi 47086393  517 EIERIQSNSEKLKSRVTEIHDSKRKLELDLKRQATDNREIDKLMNSLKPDLIQLRKLRDQYLVWLTQKGTRQRKINEWLG 596

                 .
Feature 1         
2Y3A_B       171 I 171
3L4Q_C       170 I 170
3MTT_A       166 I 166
gi 363743901 604 I 604
gi 387017654 601 I 601
gi 40226308  193 I 193
gi 47086393  597 I 597

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