Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

9RTW

Mammalian AP3 complex on tubular membranes (AP3 centered)

Functional Information from GO Data

Chain	GOid	namespace	contents
E	0000139	cellular_component	Golgi membrane
E	0000287	molecular_function	magnesium ion binding
E	0002090	biological_process	regulation of receptor internalization
E	0003723	molecular_function	RNA binding
E	0003924	molecular_function	GTPase activity
E	0003925	molecular_function	G protein activity
E	0005515	molecular_function	protein binding
E	0005525	molecular_function	GTP binding
E	0005737	cellular_component	cytoplasm
E	0005765	cellular_component	lysosomal membrane
E	0005794	cellular_component	Golgi apparatus
E	0005829	cellular_component	cytosol
E	0005886	cellular_component	plasma membrane
E	0005925	cellular_component	focal adhesion
E	0006878	biological_process	intracellular copper ion homeostasis
E	0006886	biological_process	intracellular protein transport
E	0006890	biological_process	retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum
E	0012505	cellular_component	endomembrane system
E	0014069	cellular_component	postsynaptic density
E	0016192	biological_process	vesicle-mediated transport
E	0019904	molecular_function	protein domain specific binding
E	0030017	cellular_component	sarcomere
E	0031252	cellular_component	cell leading edge
E	0032991	cellular_component	protein-containing complex
E	0034315	biological_process	regulation of Arp2/3 complex-mediated actin nucleation
E	0035964	biological_process	COPI-coated vesicle budding
E	0045202	cellular_component	synapse
E	0046836	biological_process	glycolipid transport
E	0060292	biological_process	long-term synaptic depression
E	0070062	cellular_component	extracellular exosome
E	0097061	biological_process	dendritic spine organization
E	0098586	biological_process	cellular response to virus
E	0160281	cellular_component	cytoplasmic side of trans-Golgi network membrane
E	1903292	biological_process	protein localization to Golgi membrane
E	1990386	biological_process	mitotic cleavage furrow ingression
F	0000139	cellular_component	Golgi membrane
F	0000287	molecular_function	magnesium ion binding
F	0002090	biological_process	regulation of receptor internalization
F	0003723	molecular_function	RNA binding
F	0003924	molecular_function	GTPase activity
F	0003925	molecular_function	G protein activity
F	0005515	molecular_function	protein binding
F	0005525	molecular_function	GTP binding
F	0005737	cellular_component	cytoplasm
F	0005765	cellular_component	lysosomal membrane
F	0005794	cellular_component	Golgi apparatus
F	0005829	cellular_component	cytosol
F	0005886	cellular_component	plasma membrane
F	0005925	cellular_component	focal adhesion
F	0006878	biological_process	intracellular copper ion homeostasis
F	0006886	biological_process	intracellular protein transport
F	0006890	biological_process	retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum
F	0012505	cellular_component	endomembrane system
F	0014069	cellular_component	postsynaptic density
F	0016192	biological_process	vesicle-mediated transport
F	0019904	molecular_function	protein domain specific binding
F	0030017	cellular_component	sarcomere
F	0031252	cellular_component	cell leading edge
F	0032991	cellular_component	protein-containing complex
F	0034315	biological_process	regulation of Arp2/3 complex-mediated actin nucleation
F	0035964	biological_process	COPI-coated vesicle budding
F	0045202	cellular_component	synapse
F	0046836	biological_process	glycolipid transport
F	0060292	biological_process	long-term synaptic depression
F	0070062	cellular_component	extracellular exosome
F	0097061	biological_process	dendritic spine organization
F	0098586	biological_process	cellular response to virus
F	0160281	cellular_component	cytoplasmic side of trans-Golgi network membrane
F	1903292	biological_process	protein localization to Golgi membrane
F	1990386	biological_process	mitotic cleavage furrow ingression
G	0000139	cellular_component	Golgi membrane
G	0000287	molecular_function	magnesium ion binding
G	0002090	biological_process	regulation of receptor internalization
G	0003723	molecular_function	RNA binding
G	0003924	molecular_function	GTPase activity
G	0003925	molecular_function	G protein activity
G	0005515	molecular_function	protein binding
G	0005525	molecular_function	GTP binding
G	0005737	cellular_component	cytoplasm
G	0005765	cellular_component	lysosomal membrane
G	0005794	cellular_component	Golgi apparatus
G	0005829	cellular_component	cytosol
G	0005886	cellular_component	plasma membrane
G	0005925	cellular_component	focal adhesion
G	0006878	biological_process	intracellular copper ion homeostasis
G	0006886	biological_process	intracellular protein transport
G	0006890	biological_process	retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum
G	0012505	cellular_component	endomembrane system
G	0014069	cellular_component	postsynaptic density
G	0016192	biological_process	vesicle-mediated transport
G	0019904	molecular_function	protein domain specific binding
G	0030017	cellular_component	sarcomere
G	0031252	cellular_component	cell leading edge
G	0032991	cellular_component	protein-containing complex
G	0034315	biological_process	regulation of Arp2/3 complex-mediated actin nucleation
G	0035964	biological_process	COPI-coated vesicle budding
G	0045202	cellular_component	synapse
G	0046836	biological_process	glycolipid transport
G	0060292	biological_process	long-term synaptic depression
G	0070062	cellular_component	extracellular exosome
G	0097061	biological_process	dendritic spine organization
G	0098586	biological_process	cellular response to virus
G	0160281	cellular_component	cytoplasmic side of trans-Golgi network membrane
G	1903292	biological_process	protein localization to Golgi membrane
G	1990386	biological_process	mitotic cleavage furrow ingression
H	0000139	cellular_component	Golgi membrane
H	0000287	molecular_function	magnesium ion binding
H	0002090	biological_process	regulation of receptor internalization
H	0003723	molecular_function	RNA binding
H	0003924	molecular_function	GTPase activity
H	0003925	molecular_function	G protein activity
H	0005515	molecular_function	protein binding
H	0005525	molecular_function	GTP binding
H	0005737	cellular_component	cytoplasm
H	0005765	cellular_component	lysosomal membrane
H	0005794	cellular_component	Golgi apparatus
H	0005829	cellular_component	cytosol
H	0005886	cellular_component	plasma membrane
H	0005925	cellular_component	focal adhesion
H	0006878	biological_process	intracellular copper ion homeostasis
H	0006886	biological_process	intracellular protein transport
H	0006890	biological_process	retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum
H	0012505	cellular_component	endomembrane system
H	0014069	cellular_component	postsynaptic density
H	0016192	biological_process	vesicle-mediated transport
H	0019904	molecular_function	protein domain specific binding
H	0030017	cellular_component	sarcomere
H	0031252	cellular_component	cell leading edge
H	0032991	cellular_component	protein-containing complex
H	0034315	biological_process	regulation of Arp2/3 complex-mediated actin nucleation
H	0035964	biological_process	COPI-coated vesicle budding
H	0045202	cellular_component	synapse
H	0046836	biological_process	glycolipid transport
H	0060292	biological_process	long-term synaptic depression
H	0070062	cellular_component	extracellular exosome
H	0097061	biological_process	dendritic spine organization
H	0098586	biological_process	cellular response to virus
H	0160281	cellular_component	cytoplasmic side of trans-Golgi network membrane
H	1903292	biological_process	protein localization to Golgi membrane
H	1990386	biological_process	mitotic cleavage furrow ingression
M	0005794	cellular_component	Golgi apparatus
M	0006886	biological_process	intracellular protein transport
M	0030131	cellular_component	clathrin adaptor complex
M	0030659	cellular_component	cytoplasmic vesicle membrane

Functional Information from PROSITE/UniProt

site_id	PS00989
Number of Residues	11
Details	CLAT_ADAPTOR_S Clathrin adaptor complexes small chain signature. LIYRhyatLYF

Chain	Residue	Details
S	LEU63-PHE73

site_id	PS00990
Number of Residues	21
Details	CLAT_ADAPTOR_M_1 Clathrin adaptor complexes medium chain signature 1. IPWRra.GvkYtnNeAYFDVVE

Chain	Residue	Details
M	ILE165-GLU185

site_id	PS00991
Number of Residues	15
Details	CLAT_ADAPTOR_M_2 Clathrin adaptor complexes medium chain signature 2. LsFIPPdGnFrLisY

Chain	Residue	Details
M	LEU248-TYR262

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	37
Details	Repeat: {"description":"HEAT 1"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	37
Details	Repeat: {"description":"HEAT 2"}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	37
Details	Repeat: {"description":"HEAT 3"}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	36
Details	Repeat: {"description":"HEAT 4"}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	38
Details	Repeat: {"description":"HEAT 5"}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	37
Details	Repeat: {"description":"HEAT 6"}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	35
Details	Repeat: {"description":"HEAT 7"}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	34
Details	Repeat: {"description":"HEAT 8"}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	37
Details	Repeat: {"description":"HEAT 9"}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	38
Details	Repeat: {"description":"HEAT 10"}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	37
Details	Repeat: {"description":"HEAT 11"}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17081983","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	32
Details	Binding site: {"evidences":[{"source":"PubMed","id":"7990966","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1HUR","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"14690595","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15308674","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7990966","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2010","submissionDatabase":"PDB data bank","title":"Crystal structure of ARFGAP1-ARF1 fusion protein.","authoringGroup":["Structural genomics consortium (SGC)."]}},{"source":"PDB","id":"1HUR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RE0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1U81","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3O47","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15308674","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7990966","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2010","submissionDatabase":"PDB data bank","title":"Crystal structure of ARFGAP1-ARF1 fusion protein.","authoringGroup":["Structural genomics consortium (SGC)."]}},{"source":"PDB","id":"1HUR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RE0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3O47","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)