4AZN

Murine epidermal fatty acid-binding protein (FABP5), apo form, poly- his tag-mediated crystal packing

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001972	molecular_function	retinoic acid binding
A	0005324	molecular_function	long-chain fatty acid transmembrane transporter activity
A	0005504	molecular_function	fatty acid binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006006	biological_process	glucose metabolic process
A	0006629	biological_process	lipid metabolic process
A	0006656	biological_process	phosphatidylcholine biosynthetic process
A	0006869	biological_process	lipid transport
A	0008289	molecular_function	lipid binding
A	0010829	biological_process	negative regulation of D-glucose transmembrane transport
A	0014069	cellular_component	postsynaptic density
A	0015908	biological_process	fatty acid transport
A	0015909	biological_process	long-chain fatty acid transport
A	0031392	biological_process	regulation of prostaglandin biosynthetic process
A	0035360	biological_process	positive regulation of peroxisome proliferator activated receptor signaling pathway
A	0042593	biological_process	glucose homeostasis
A	0042802	molecular_function	identical protein binding
A	0045202	cellular_component	synapse
A	0051930	biological_process	regulation of sensory perception of pain
A	0098921	biological_process	retrograde trans-synaptic signaling by endocannabinoid
A	0098978	cellular_component	glutamatergic synapse
A	0099092	cellular_component	postsynaptic density, intracellular component
A	0099178	biological_process	regulation of retrograde trans-synaptic signaling by endocanabinoid
A	0099524	cellular_component	postsynaptic cytosol
A	0120162	biological_process	positive regulation of cold-induced thermogenesis
A	1990379	biological_process	lipid transport across blood-brain barrier
B	0001972	molecular_function	retinoic acid binding
B	0005324	molecular_function	long-chain fatty acid transmembrane transporter activity
B	0005504	molecular_function	fatty acid binding
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006006	biological_process	glucose metabolic process
B	0006629	biological_process	lipid metabolic process
B	0006656	biological_process	phosphatidylcholine biosynthetic process
B	0006869	biological_process	lipid transport
B	0008289	molecular_function	lipid binding
B	0010829	biological_process	negative regulation of D-glucose transmembrane transport
B	0014069	cellular_component	postsynaptic density
B	0015908	biological_process	fatty acid transport
B	0015909	biological_process	long-chain fatty acid transport
B	0031392	biological_process	regulation of prostaglandin biosynthetic process
B	0035360	biological_process	positive regulation of peroxisome proliferator activated receptor signaling pathway
B	0042593	biological_process	glucose homeostasis
B	0042802	molecular_function	identical protein binding
B	0045202	cellular_component	synapse
B	0051930	biological_process	regulation of sensory perception of pain
B	0098921	biological_process	retrograde trans-synaptic signaling by endocannabinoid
B	0098978	cellular_component	glutamatergic synapse
B	0099092	cellular_component	postsynaptic density, intracellular component
B	0099178	biological_process	regulation of retrograde trans-synaptic signaling by endocanabinoid
B	0099524	cellular_component	postsynaptic cytosol
B	0120162	biological_process	positive regulation of cold-induced thermogenesis
B	1990379	biological_process	lipid transport across blood-brain barrier

Functional Information from PROSITE/UniProt

site_id	PS00214
Number of Residues	18
Details	FABP Cytosolic fatty-acid binding proteins signature. GKWrLmeShGFEeYMKEL

Chain	Residue	Details
A	GLY9-LEU26

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	20
Details	Motif: {"description":"Nuclear localization signal","evidences":[{"source":"UniProtKB","id":"Q01469","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"24531463","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4AZQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"24531463","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4AZP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4AZQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"24531463","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4AZP","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"UniProtKB","id":"Q01469","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P55053","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q01469","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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