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4R0Z

A conserved phosphorylation switch controls the interaction between cadherin and beta-catenin in vitro and in vivo

Functional Information from GO Data
ChainGOidnamespacecontents
A0000132biological_processestablishment of mitotic spindle orientation
A0003713molecular_functiontranscription coactivator activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005912cellular_componentadherens junction
A0007155biological_processcell adhesion
A0009792biological_processembryo development ending in birth or egg hatching
A0010172biological_processembryonic body morphogenesis
A0016342cellular_componentcatenin complex
A0016477biological_processcell migration
A0016922molecular_functionnuclear receptor binding
A0019901molecular_functionprotein kinase binding
A0019903molecular_functionprotein phosphatase binding
A0019904molecular_functionprotein domain specific binding
A0030866biological_processcortical actin cytoskeleton organization
A0032880biological_processregulation of protein localization
A0042074biological_processcell migration involved in gastrulation
A0044331biological_processcell-cell adhesion mediated by cadherin
A0045294molecular_functionalpha-catenin binding
A0045296molecular_functioncadherin binding
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0051782biological_processnegative regulation of cell division
A0060070biological_processcanonical Wnt signaling pathway
A0070161cellular_componentanchoring junction
A0070986biological_processleft/right axis specification
A0098609biological_processcell-cell adhesion
A0140678molecular_functionmolecular function inhibitor activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT A 1001
ChainResidue
AASN360
ALYS365
AHIS400
AARG404

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FMT A 1002
ChainResidue
AHIS507
AGLN565
ATYR599

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FMT A 1003
ChainResidue
ALEU328
AGLN330
ALEU331
AHOH1121
AHOH1165
AHOH1221
ATYR296
AASN327

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PDB entries from 2024-07-31

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