5ANC

Mechanism of eIF6 release from the nascent 60S ribosomal subunit

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003735	molecular_function	structural constituent of ribosome
A	0005737	cellular_component	cytoplasm
A	0005840	cellular_component	ribosome
A	0006412	biological_process	translation
A	0022625	cellular_component	cytosolic large ribosomal subunit
A	0031012	cellular_component	extracellular matrix
B	0002181	biological_process	cytoplasmic translation
B	0003735	molecular_function	structural constituent of ribosome
B	0005840	cellular_component	ribosome
B	0006412	biological_process	translation
B	0019843	molecular_function	rRNA binding
B	0022625	cellular_component	cytosolic large ribosomal subunit
B	0031012	cellular_component	extracellular matrix
B	0045335	cellular_component	phagocytic vesicle
D	0003735	molecular_function	structural constituent of ribosome
D	0005840	cellular_component	ribosome
D	0006412	biological_process	translation
D	0022625	cellular_component	cytosolic large ribosomal subunit
D	0070180	molecular_function	large ribosomal subunit rRNA binding
E	0003735	molecular_function	structural constituent of ribosome
E	0005840	cellular_component	ribosome
E	0006412	biological_process	translation
E	0022625	cellular_component	cytosolic large ribosomal subunit
E	0031012	cellular_component	extracellular matrix
E	0070180	molecular_function	large ribosomal subunit rRNA binding
F	0003735	molecular_function	structural constituent of ribosome
F	0005811	cellular_component	lipid droplet
F	0005840	cellular_component	ribosome
F	0006412	biological_process	translation
F	0022625	cellular_component	cytosolic large ribosomal subunit
G	0003735	molecular_function	structural constituent of ribosome
H	0003735	molecular_function	structural constituent of ribosome
H	0005840	cellular_component	ribosome
H	0006412	biological_process	translation
J	0000922	cellular_component	spindle pole
J	0002244	biological_process	hematopoietic progenitor cell differentiation
J	0003723	molecular_function	RNA binding
J	0005515	molecular_function	protein binding
J	0005634	cellular_component	nucleus
J	0005654	cellular_component	nucleoplasm
J	0005730	cellular_component	nucleolus
J	0005737	cellular_component	cytoplasm
J	0005819	cellular_component	spindle
J	0005829	cellular_component	cytosol
J	0006364	biological_process	rRNA processing
J	0007052	biological_process	mitotic spindle organization
J	0008017	molecular_function	microtubule binding
J	0019843	molecular_function	rRNA binding
J	0030282	biological_process	bone mineralization
J	0030595	biological_process	leukocyte chemotaxis
J	0042254	biological_process	ribosome biogenesis
J	0042256	biological_process	cytosolic ribosome assembly
J	0043022	molecular_function	ribosome binding
J	0048539	biological_process	bone marrow development
K	0003924	molecular_function	GTPase activity
K	0005515	molecular_function	protein binding
K	0005525	molecular_function	GTP binding
K	0005829	cellular_component	cytosol
K	0042256	biological_process	cytosolic ribosome assembly
K	0043022	molecular_function	ribosome binding
K	0046039	biological_process	GTP metabolic process
K	1990904	cellular_component	ribonucleoprotein complex

Functional Information from PROSITE/UniProt

site_id	PS00474
Number of Residues	24
Details	RIBOSOMAL_L3 Ribosomal protein L3 signature. FaeneliDviGvTkGKGfnGvikR

Chain	Residue	Details
A	PHE212-ARG235

---

site_id	PS00700
Number of Residues	22
Details	RIBOSOMAL_L6_2 Ribosomal protein L6 signature 2. LrsaIkyKdvRkFlDGIYVseR

Chain	Residue	Details
B	LEU161-ARG182

---

site_id	PS01073
Number of Residues	18
Details	RIBOSOMAL_L24E Ribosomal protein L24e signature. YsEfkIyPArGmkFvRgD

Chain	Residue	Details
G	TYR8-ASP25

---

site_id	PS01257
Number of Residues	22
Details	RIBOSOMAL_L10E Ribosomal protein L10e signature. ADRlqtGMRgAFGKPmGtvARV

Chain	Residue	Details
F	ALA108-VAL129

---

site_id	PS01267
Number of Residues	20
Details	UPF0023 Uncharacterized protein family UPF0023 signature. EkdLDEVLqthsVFvnvsKG

Chain	Residue	Details
J	GLU44-GLY63

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	122
Details	Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	32
Details	Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	11
Details	Compositional bias: {"description":"Basic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"N-acetylserine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2005","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Claeys D."]}},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	255
Details	Domain: {"description":"tr-type G","evidences":[{"source":"PROSITE-ProRule","id":"PRU01059","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	10
Details	Compositional bias: {"description":"Polar residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	14
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---