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3GD1

Structure of an Arrestin/Clathrin complex reveals a novel clathrin binding domain that modulates receptor trafficking

Functional Information from GO Data
ChainGOidnamespacecontents
C0000822molecular_functioninositol hexakisphosphate binding
C0001664molecular_functionG protein-coupled receptor binding
C0001934biological_processpositive regulation of protein phosphorylation
C0002029biological_processdesensitization of G protein-coupled receptor signaling pathway
C0002031biological_processG protein-coupled receptor internalization
C0002092biological_processpositive regulation of receptor internalization
C0005515molecular_functionprotein binding
C0005547molecular_functionphosphatidylinositol-3,4,5-trisphosphate binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0005905cellular_componentclathrin-coated pit
C0006511biological_processubiquitin-dependent protein catabolic process
C0007165biological_processsignal transduction
C0007601biological_processvisual perception
C0009968biological_processnegative regulation of signal transduction
C0015031biological_processprotein transport
C0030132cellular_componentclathrin coat of coated pit
C0030276molecular_functionclathrin binding
C0031143cellular_componentpseudopodium
C0031410cellular_componentcytoplasmic vesicle
C0031623biological_processreceptor internalization
C0032050molecular_functionclathrin heavy chain binding
C0033130molecular_functionacetylcholine receptor binding
C0035612molecular_functionAP-2 adaptor complex binding
C0036094molecular_functionsmall molecule binding
C0042995cellular_componentcell projection
C0045746biological_processnegative regulation of Notch signaling pathway
C0060090molecular_functionmolecular adaptor activity
C0070374biological_processpositive regulation of ERK1 and ERK2 cascade
C0072583biological_processclathrin-dependent endocytosis
E0000822molecular_functioninositol hexakisphosphate binding
E0001664molecular_functionG protein-coupled receptor binding
E0001934biological_processpositive regulation of protein phosphorylation
E0002029biological_processdesensitization of G protein-coupled receptor signaling pathway
E0002031biological_processG protein-coupled receptor internalization
E0002092biological_processpositive regulation of receptor internalization
E0005515molecular_functionprotein binding
E0005547molecular_functionphosphatidylinositol-3,4,5-trisphosphate binding
E0005634cellular_componentnucleus
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0005886cellular_componentplasma membrane
E0005905cellular_componentclathrin-coated pit
E0006511biological_processubiquitin-dependent protein catabolic process
E0007165biological_processsignal transduction
E0007601biological_processvisual perception
E0009968biological_processnegative regulation of signal transduction
E0015031biological_processprotein transport
E0030132cellular_componentclathrin coat of coated pit
E0030276molecular_functionclathrin binding
E0031143cellular_componentpseudopodium
E0031410cellular_componentcytoplasmic vesicle
E0031623biological_processreceptor internalization
E0032050molecular_functionclathrin heavy chain binding
E0033130molecular_functionacetylcholine receptor binding
E0035612molecular_functionAP-2 adaptor complex binding
E0036094molecular_functionsmall molecule binding
E0042995cellular_componentcell projection
E0045746biological_processnegative regulation of Notch signaling pathway
E0060090molecular_functionmolecular adaptor activity
E0070374biological_processpositive regulation of ERK1 and ERK2 cascade
E0072583biological_processclathrin-dependent endocytosis
I0005198molecular_functionstructural molecule activity
I0006886biological_processintracellular protein transport
I0016192biological_processvesicle-mediated transport
I0030130cellular_componentclathrin coat of trans-Golgi network vesicle
I0030132cellular_componentclathrin coat of coated pit
Functional Information from PROSITE/UniProt
site_idPS00295
Number of Residues19
DetailsARRESTINS Arrestins signature. FRYGrEDlDVLGLtFrKDL
ChainResidueDetails
CPHE61-LEU79

site_idPS00014
Number of Residues4
DetailsER_TARGET Endoplasmic reticulum targeting sequence. AEEL
ChainResidueDetails
IALA360-LEU363

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:Q00610
ChainResidueDetails
IALA2
CMET255
CLYS324
CLYS326
ELYS250
EMET255
ELYS324
ELYS326

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q00610
ChainResidueDetails
ISER67
ETYR47

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q68FD5
ChainResidueDetails
ITHR105

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q68FD5
ChainResidueDetails
ITYR184

221051

PDB entries from 2024-06-12

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