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4RM9

Crystal structure of human ezrin in space group C2221

Functional Information from GO Data
ChainGOidnamespacecontents
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0001650cellular_componentfibrillar center
A0001726cellular_componentruffle
A0001772cellular_componentimmunological synapse
A0001931cellular_componenturopod
A0001951biological_processintestinal D-glucose absorption
A0003376biological_processsphingosine-1-phosphate receptor signaling pathway
A0003723molecular_functionRNA binding
A0003779molecular_functionactin binding
A0005515molecular_functionprotein binding
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005768cellular_componentendosome
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005884cellular_componentactin filament
A0005886cellular_componentplasma membrane
A0005902cellular_componentmicrovillus
A0005903cellular_componentbrush border
A0005912cellular_componentadherens junction
A0005925cellular_componentfocal adhesion
A0005938cellular_componentcell cortex
A0007159biological_processleukocyte cell-cell adhesion
A0008017molecular_functionmicrotubule binding
A0008092molecular_functioncytoskeletal protein binding
A0008360biological_processregulation of cell shape
A0008361biological_processregulation of cell size
A0010628biological_processpositive regulation of gene expression
A0010737biological_processprotein kinase A signaling
A0015629cellular_componentactin cytoskeleton
A0016020cellular_componentmembrane
A0016323cellular_componentbasolateral plasma membrane
A0016324cellular_componentapical plasma membrane
A0019904molecular_functionprotein domain specific binding
A0022612biological_processgland morphogenesis
A0022614biological_processmembrane to membrane docking
A0030033biological_processmicrovillus assembly
A0030036biological_processactin cytoskeleton organization
A0030175cellular_componentfilopodium
A0030863cellular_componentcortical cytoskeleton
A0030953biological_processastral microtubule organization
A0031503biological_processprotein-containing complex localization
A0031528cellular_componentmicrovillus membrane
A0031623biological_processreceptor internalization
A0031982cellular_componentvesicle
A0032532biological_processregulation of microvillus length
A0032587cellular_componentruffle membrane
A0032703biological_processnegative regulation of interleukin-2 production
A0032956biological_processregulation of actin cytoskeleton organization
A0032991cellular_componentprotein-containing complex
A0034236molecular_functionprotein kinase A catalytic subunit binding
A0034237molecular_functionprotein kinase A regulatory subunit binding
A0035088biological_processestablishment or maintenance of apical/basal cell polarity
A0036064cellular_componentciliary basal body
A0040018biological_processpositive regulation of multicellular organism growth
A0042802molecular_functionidentical protein binding
A0042995cellular_componentcell projection
A0043622biological_processcortical microtubule organization
A0044548molecular_functionS100 protein binding
A0044853cellular_componentplasma membrane raft
A0045177cellular_componentapical part of cell
A0045198biological_processestablishment of epithelial cell apical/basal polarity
A0045296molecular_functioncadherin binding
A0045732biological_processpositive regulation of protein catabolic process
A0046847biological_processfilopodium assembly
A0048471cellular_componentperinuclear region of cytoplasm
A0050839molecular_functioncell adhesion molecule binding
A0050860biological_processnegative regulation of T cell receptor signaling pathway
A0051015molecular_functionactin filament binding
A0051017biological_processactin filament bundle assembly
A0051018molecular_functionprotein kinase A binding
A0051117molecular_functionATPase binding
A0051660biological_processestablishment of centrosome localization
A0061028biological_processestablishment of endothelial barrier
A0070062cellular_componentextracellular exosome
A0070373biological_processnegative regulation of ERK1 and ERK2 cascade
A0071320biological_processcellular response to cAMP
A0071944cellular_componentcell periphery
A0072659biological_processprotein localization to plasma membrane
A0072697biological_processprotein localization to cell cortex
A0097718molecular_functiondisordered domain specific binding
A0098974biological_processpostsynaptic actin cytoskeleton organization
A1901222biological_processregulation of non-canonical NF-kappaB signal transduction
A1902115biological_processregulation of organelle assembly
A1902896biological_processterminal web assembly
A1902966biological_processpositive regulation of protein localization to early endosome
A1903078biological_processpositive regulation of protein localization to plasma membrane
A1903753biological_processnegative regulation of p38MAPK cascade
A2000643biological_processpositive regulation of early endosome to late endosome transport
Functional Information from PROSITE/UniProt
site_idPS00660
Number of Residues31
DetailsFERM_1 FERM domain signature 1. WLkldKkVsaQe.Vrkenplq.FkfrakFYpeD
ChainResidueDetails
ATRP58-ASP88

site_idPS00661
Number of Residues30
DetailsFERM_2 FERM domain signature 2. HaehrgmlkdNAmleYLki.AqdLemYGiNY
ChainResidueDetails
AHIS176-TYR205

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS60

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by PDGFR => ECO:0000269|PubMed:1382070, ECO:0000269|PubMed:18046454
ChainResidueDetails
ATYR146

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by PDGFR => ECO:0000269|PubMed:1382070
ChainResidueDetails
ATYR354

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER366

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:18046454
ChainResidueDetails
ATYR478

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P26040
ChainResidueDetails
ASER535

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by ROCK2 and PKC/PRKCI => ECO:0000305|PubMed:18270268
ChainResidueDetails
ATHR567

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PDB entries from 2024-05-01

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