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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8JQI

Cryo EM map of full length PLC gamma 2 and FGFR1 Kinase Domain

Functional Information from GO Data
ChainGOidnamespacecontents
A0001775biological_processcell activation
A0001784molecular_functionphosphotyrosine residue binding
A0001878biological_processresponse to yeast
A0002092biological_processpositive regulation of receptor internalization
A0002223biological_processstimulatory C-type lectin receptor signaling pathway
A0002224biological_processtoll-like receptor signaling pathway
A0002281biological_processmacrophage activation involved in immune response
A0002732biological_processpositive regulation of dendritic cell cytokine production
A0004435molecular_functionphosphatidylinositol-4,5-bisphosphate phospholipase C activity
A0004629molecular_functionphospholipase C activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006629biological_processlipid metabolic process
A0006661biological_processphosphatidylinositol biosynthetic process
A0007165biological_processsignal transduction
A0008081molecular_functionphosphoric diester hydrolase activity
A0009395biological_processphospholipid catabolic process
A0010628biological_processpositive regulation of gene expression
A0010634biological_processpositive regulation of epithelial cell migration
A0016042biological_processlipid catabolic process
A0016055biological_processWnt signaling pathway
A0016787molecular_functionhydrolase activity
A0019216biological_processregulation of lipid metabolic process
A0019722biological_processcalcium-mediated signaling
A0019901molecular_functionprotein kinase binding
A0030168biological_processplatelet activation
A0030183biological_processB cell differentiation
A0031663biological_processlipopolysaccharide-mediated signaling pathway
A0032481biological_processpositive regulation of type I interferon production
A0032587cellular_componentruffle membrane
A0032733biological_processpositive regulation of interleukin-10 production
A0032735biological_processpositive regulation of interleukin-12 production
A0032743biological_processpositive regulation of interleukin-2 production
A0032747biological_processpositive regulation of interleukin-23 production
A0032755biological_processpositive regulation of interleukin-6 production
A0032760biological_processpositive regulation of tumor necrosis factor production
A0035556biological_processintracellular signal transduction
A0038095biological_processFc-epsilon receptor signaling pathway
A0042113biological_processB cell activation
A0043122biological_processregulation of canonical NF-kappaB signal transduction
A0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
A0043410biological_processpositive regulation of MAPK cascade
A0045121cellular_componentmembrane raft
A0046488biological_processphosphatidylinositol metabolic process
A0048015biological_processphosphatidylinositol-mediated signaling
A0048471cellular_componentperinuclear region of cytoplasm
A0048678biological_processresponse to axon injury
A0050850biological_processpositive regulation of calcium-mediated signaling
A0050851biological_processantigen receptor-mediated signaling pathway
A0050852biological_processT cell receptor signaling pathway
A0050853biological_processB cell receptor signaling pathway
A0051209biological_processrelease of sequestered calcium ion into cytosol
A0051282biological_processregulation of sequestering of calcium ion
A0060100biological_processpositive regulation of phagocytosis, engulfment
A0060907biological_processpositive regulation of macrophage cytokine production
A0061760biological_processantifungal innate immune response
A0070062cellular_componentextracellular exosome
A0070884biological_processregulation of calcineurin-NFAT signaling cascade
A0071277biological_processcellular response to calcium ion
A0071396biological_processcellular response to lipid
A0097110molecular_functionscaffold protein binding
A0097708cellular_componentintracellular vesicle
A0140031molecular_functionphosphorylation-dependent protein binding
A0150078biological_processpositive regulation of neuroinflammatory response
A1900227biological_processpositive regulation of NLRP3 inflammasome complex assembly
A1902533biological_processpositive regulation of intracellular signal transduction
A1902808biological_processpositive regulation of cell cycle G1/S phase transition
A1903428biological_processpositive regulation of reactive oxygen species biosynthetic process
A1990782molecular_functionprotein tyrosine kinase binding
A1990858biological_processcellular response to lectin
B0004672molecular_functionprotein kinase activity
B0004713molecular_functionprotein tyrosine kinase activity
B0005007molecular_functionfibroblast growth factor receptor activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
B0008284biological_processpositive regulation of cell population proliferation
B0008543biological_processfibroblast growth factor receptor signaling pathway
B0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues31
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGCFGQVVlAeaigldkdkpnrvtk...VAVK
ChainResidueDetails
BLEU484-LYS514
site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CIHrDLAARNVLV
ChainResidueDetails
BCYS619-VAL631
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues111
DetailsDomain: {"description":"PH","evidences":[{"source":"PROSITE-ProRule","id":"PRU00145","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues144
DetailsDomain: {"description":"PI-PLC X-box","evidences":[{"source":"PROSITE-ProRule","id":"PRU00270","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues103
DetailsDomain: {"description":"SH2 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00191","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues89
DetailsDomain: {"description":"SH2 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00191","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues114
DetailsDomain: {"description":"PI-PLC Y-box","evidences":[{"source":"PROSITE-ProRule","id":"PRU00271","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues131
DetailsDomain: {"description":"C2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00041","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00270","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by BTK","evidences":[{"source":"PubMed","id":"11606584","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12181444","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues289
DetailsDomain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10028","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19224897","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues12
DetailsBinding site: {}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsSite: {"description":"Mediates interaction with PLCG1 and SHB"}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues3
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"16507368","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19224897","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8622701","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"16507368","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19224897","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19665973","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8622701","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"19224897","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8622701","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"19665973","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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