1CM8


Conserved Protein Domain Family
STKc_p38gamma

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cd07880: STKc_p38gamma 
Click on image for an interactive view with Cn3D
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase (also called MAPK12)
STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38gamma/MAPK12 is predominantly expressed in skeletal muscle. Unlike p38alpha and p38beta, p38gamma is insensitive to pyridinylimidazoles. It displays an antagonizing function compared to p38alpha. p38gamma inhibits, while p38alpha stimulates, c-Jun phosphorylation and AP-1 mediated transcription. p38gamma also plays a role in the signaling between Ras and the estrogen receptor and has been implicated to increase cell invasion and breast cancer progression. In Xenopus, p38gamma is critical in the meiotic maturation of oocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.
Statistics
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PSSM-Id: 143385
Aligned: 3 rows
Threshold Bit Score: 694.004
Created: 24-Sep-2008
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
  next features
Conserved site includes 23 residues -Click on image for an interactive view with Cn3D
Feature 1:ATP binding site [chemical binding site]
Evidence:
  • Structure:1CM8_B; Human p38gamma binds Mg2AMP-PNP ; defined at 4A contacts.
  • Comment:This binding site includes some residues which are disordered in the structural evidence.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                              ##   # ##            # #                     #        # # 
1CM8_B        11 FYRQEVtKTAWEVRAVYRDLQpVGSGAYGAVCSAVDGRTGAKVAIKKLYRPFQSELFAKRAYRELRLLKHMRHENVIGLL 90  human
NP_001082596  11 YYTQEVnKTVWEVKERYRELLaVGSGAYGIVCSSLDTRTGTKVAIKKLYRPFQSELFAKRAYRELRLLKHMQHENVIGLL 90  African clawed ...
O42376         9 YFRQEInKTIWEVPDRYKDLKqVGTGAYGTVCYALDRRTGAKVAIKKLHRPFQSDLFAKRAYRELRLLKHMKHDNVIGLV 88  zebrafish
Feature 1                        # ####  #                                     # # ##           #
1CM8_B        91 DVFTPDETLDDFTDFYLVMPFMGTDLGKLMKheKLGEDRIQFLVYQMLKGLRYIHAAGIIHRDLKPGNLAVNEDCELKIL 170 human
NP_001082596  91 DVFTPDTNLDKFNDFYLVMPFMGTDLGKIMKheKLSEDRIQFLVYQILRGLKYIHSAGIIHRDLKPGNLAVNEDCELKIL 170 African clawed ...
O42376        89 DVFTADLSLDRFHDFYLVMPFMGTDLGKLMKmeRLSEERVQYLVYQMLKGLKYIHAAGIIHRDLKPGNLAINEECELKIL 168 zebrafish
Feature 1        # #                                                                             
1CM8_B       171 DFGLARQADSEMXGXVVTRWYRAPEVILNWMRYTQTVDIWSVGCIMAEMITGKTLFKGSDHLDQLKEIMKVTGTPPAEFV 250 human
NP_001082596 171 DFGLARHTDSEMTGYVVTRWYRAPEVILNWMHYTQTVDIWSVGCIMAEMYTGRPLFKGNDHLNQLTEIMKITGTPTQDFV 250 African clawed ...
O42376       169 DFGLARQTDSEMTGYVVTRWYRAPEVILSWMHYTQTVDIWSVGCIMAEMLLGKPLFKGHDHLDQLMEIMKVTGTPSKEFT 248 zebrafish
Feature 1                                                                                        
1CM8_B       251 QRLQsDEAKNYMKGLPELEKKDFASILTNaSPLAVNLLEKMLVLDAEQRVTAGEALAHPYFeSLHDTEDEPqvQKYDDSF 330 human
NP_001082596 251 QKLQsTDAKNYIKSLPKVQKKDFGSLLRYaNPLAVNILEKMLVLDAEKRITATEALAHAYFeQFHDIDDETeaEPYDDSF 330 African clawed ...
O42376       249 AKLQsEDARNYVTKLPRFRKKDLRILLPNvNPQAIKVLDGMLLLDPESRITAAEALAFPFFsEFREPEEETeaPPYDHSL 328 zebrafish
Feature 1                               
1CM8_B       331 DDvdRTLDEWKRVTYKEVLSFKP 353 human
NP_001082596 331 DNvnLPLEEWKRLTHEELTSFEP 353 African clawed frog
O42376       329 DEadQSLEQWKRLTFTEILTFQP 351 zebrafish

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