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4MH0

Selective activation of Epac1 and Epac2

Functional Information from GO Data
ChainGOidnamespacecontents
E0005085molecular_functionguanyl-nucleotide exchange factor activity
E0007264biological_processsmall GTPase-mediated signal transduction
R0000166molecular_functionnucleotide binding
R0003924molecular_functionGTPase activity
R0003925molecular_functionG protein activity
R0005515molecular_functionprotein binding
R0005525molecular_functionGTP binding
R0005737cellular_componentcytoplasm
R0005811cellular_componentlipid droplet
R0005829cellular_componentcytosol
R0005886cellular_componentplasma membrane
R0005911cellular_componentcell-cell junction
R0007165biological_processsignal transduction
R0007264biological_processsmall GTPase-mediated signal transduction
R0008283biological_processcell population proliferation
R0016020cellular_componentmembrane
R0016787molecular_functionhydrolase activity
R0017156biological_processcalcium-ion regulated exocytosis
R0019003molecular_functionGDP binding
R0032486biological_processRap protein signal transduction
R0033625biological_processpositive regulation of integrin activation
R0035577cellular_componentazurophil granule membrane
R0044877molecular_functionprotein-containing complex binding
R0045121cellular_componentmembrane raft
R0045955biological_processnegative regulation of calcium ion-dependent exocytosis
R0051649biological_processestablishment of localization in cell
R0061028biological_processestablishment of endothelial barrier
R0070062cellular_componentextracellular exosome
R0070161cellular_componentanchoring junction
R0070374biological_processpositive regulation of ERK1 and ERK2 cascade
R0071320biological_processcellular response to cAMP
R0098978cellular_componentglutamatergic synapse
R0099010biological_processmodification of postsynaptic structure
R1901888biological_processregulation of cell junction assembly
R2000114biological_processregulation of establishment of cell polarity
R2000301biological_processnegative regulation of synaptic vesicle exocytosis
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE HR4 E 1001
ChainResidue
EPHE367
EARG414
EALA415
EALA416
EARG448
ELEU449
ELYS450
EGLU451
ELYS489
EHOH1118
EHOH1122
EVAL386
EILE388
EVAL394
ELEU397
EASP401
EPHE403
EGLY404
EALA407

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HR4 E 1002
ChainResidue
EVAL365
EASN368
EVAL387
EILE388
EGLY392
ESER417
EVAL419
EHIS537
EGLN539
ESER541
EGLN542
ELYS556
EASP594
EMET597
EMET598
EHOH1187
EHOH1234

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 R 201
ChainResidue
RSER11
RGLY12
RGLY13
RVAL14
RGLY15
RLYS16
RSER17
RALA59
RHOH302
RHOH309

Functional Information from PROSITE/UniProt
site_idPS00720
Number of Residues30
DetailsRASGEF Ras Guanine-nucleotide exchange factors domain signature. IPFmPllIkDMtfthegnktfidnl.....................VNFeK
ChainResidueDetails
EILE903-LYS932

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"O95398","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsMotif: {"description":"Effector region","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues17
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18309292","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22577140","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"ADP-ribosylserine; by botulinum toxin","evidences":[{"source":"PubMed","id":"3141412","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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