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3WZZ

Crystal structure of PIP4KIIBETA

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005525molecular_functionGTP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005776cellular_componentautophagosome
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006629biological_processlipid metabolic process
A0007166biological_processcell surface receptor signaling pathway
A0010506biological_processregulation of autophagy
A0016020cellular_componentmembrane
A0016301molecular_functionkinase activity
A0016308molecular_function1-phosphatidylinositol-4-phosphate 5-kinase activity
A0016309molecular_function1-phosphatidylinositol-5-phosphate 4-kinase activity
A0016310biological_processphosphorylation
A0016740molecular_functiontransferase activity
A0042803molecular_functionprotein homodimerization activity
A0046488biological_processphosphatidylinositol metabolic process
A0046627biological_processnegative regulation of insulin receptor signaling pathway
A0046854biological_processphosphatidylinositol phosphate biosynthetic process
A0052742molecular_functionphosphatidylinositol kinase activity
A0061909biological_processautophagosome-lysosome fusion
A1902635biological_process1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate biosynthetic process
A2000786biological_processpositive regulation of autophagosome assembly
B0000166molecular_functionnucleotide binding
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005525molecular_functionGTP binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005776cellular_componentautophagosome
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006629biological_processlipid metabolic process
B0007166biological_processcell surface receptor signaling pathway
B0010506biological_processregulation of autophagy
B0016020cellular_componentmembrane
B0016301molecular_functionkinase activity
B0016308molecular_function1-phosphatidylinositol-4-phosphate 5-kinase activity
B0016309molecular_function1-phosphatidylinositol-5-phosphate 4-kinase activity
B0016310biological_processphosphorylation
B0016740molecular_functiontransferase activity
B0042803molecular_functionprotein homodimerization activity
B0046488biological_processphosphatidylinositol metabolic process
B0046627biological_processnegative regulation of insulin receptor signaling pathway
B0046854biological_processphosphatidylinositol phosphate biosynthetic process
B0052742molecular_functionphosphatidylinositol kinase activity
B0061909biological_processautophagosome-lysosome fusion
B1902635biological_process1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate biosynthetic process
B2000786biological_processpositive regulation of autophagosome assembly
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:26774281, ECO:0007744|PDB:3X03
ChainResidueDetails
AARG202
BARG202

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305|PubMed:26774281, ECO:0007744|PDB:3X04
ChainResidueDetails
AASN203
ALYS214
AASP369
BASN203
BLYS214
BASP369

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P48426
ChainResidueDetails
ALYS94
BLYS94

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS150
BLYS150

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q80XI4
ChainResidueDetails
ATHR322
BTHR322

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195
ChainResidueDetails
ASER326
BSER326

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 662
ChainResidueDetails
ALYS150electrostatic stabiliser
AASP278proton shuttle (general acid/base)

site_idMCSA2
Number of Residues2
DetailsM-CSA 662
ChainResidueDetails
BLYS150electrostatic stabiliser
BASP278proton shuttle (general acid/base)

217705

数据于2024-03-27公开中

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