Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8QYJ

Human 20S proteasome assembly structure 1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000502	cellular_component	proteasome complex
A	0000932	cellular_component	P-body
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005839	cellular_component	proteasome core complex
A	0006511	biological_process	ubiquitin-dependent protein catabolic process
A	0009615	biological_process	response to virus
A	0019773	cellular_component	proteasome core complex, alpha-subunit complex
A	0034774	cellular_component	secretory granule lumen
A	0043161	biological_process	proteasome-mediated ubiquitin-dependent protein catabolic process
A	0051603	biological_process	proteolysis involved in protein catabolic process
A	0070062	cellular_component	extracellular exosome
A	1904813	cellular_component	ficolin-1-rich granule lumen
B	0000502	cellular_component	proteasome complex
B	0000932	cellular_component	P-body
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005839	cellular_component	proteasome core complex
B	0006511	biological_process	ubiquitin-dependent protein catabolic process
B	0019773	cellular_component	proteasome core complex, alpha-subunit complex
B	0043161	biological_process	proteasome-mediated ubiquitin-dependent protein catabolic process
B	0051603	biological_process	proteolysis involved in protein catabolic process
B	0070062	cellular_component	extracellular exosome
C	0000502	cellular_component	proteasome complex
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0005654	cellular_component	nucleoplasm
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0005839	cellular_component	proteasome core complex
C	0006511	biological_process	ubiquitin-dependent protein catabolic process
C	0019773	cellular_component	proteasome core complex, alpha-subunit complex
C	0042802	molecular_function	identical protein binding
C	0043161	biological_process	proteasome-mediated ubiquitin-dependent protein catabolic process
C	0051603	biological_process	proteolysis involved in protein catabolic process
C	0070062	cellular_component	extracellular exosome
D	0000502	cellular_component	proteasome complex
D	0005515	molecular_function	protein binding
D	0005576	cellular_component	extracellular region
D	0005634	cellular_component	nucleus
D	0005654	cellular_component	nucleoplasm
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0005839	cellular_component	proteasome core complex
D	0006511	biological_process	ubiquitin-dependent protein catabolic process
D	0019773	cellular_component	proteasome core complex, alpha-subunit complex
D	0034774	cellular_component	secretory granule lumen
D	0043161	biological_process	proteasome-mediated ubiquitin-dependent protein catabolic process
D	0051603	biological_process	proteolysis involved in protein catabolic process
D	0070062	cellular_component	extracellular exosome
D	1904813	cellular_component	ficolin-1-rich granule lumen
E	0000502	cellular_component	proteasome complex
E	0001530	molecular_function	lipopolysaccharide binding
E	0002376	biological_process	immune system process
E	0002862	biological_process	negative regulation of inflammatory response to antigenic stimulus
E	0005515	molecular_function	protein binding
E	0005634	cellular_component	nucleus
E	0005654	cellular_component	nucleoplasm
E	0005737	cellular_component	cytoplasm
E	0005813	cellular_component	centrosome
E	0005829	cellular_component	cytosol
E	0005839	cellular_component	proteasome core complex
E	0006511	biological_process	ubiquitin-dependent protein catabolic process
E	0019773	cellular_component	proteasome core complex, alpha-subunit complex
E	0043161	biological_process	proteasome-mediated ubiquitin-dependent protein catabolic process
E	0051603	biological_process	proteolysis involved in protein catabolic process
E	0070062	cellular_component	extracellular exosome
F	0000502	cellular_component	proteasome complex
F	0005515	molecular_function	protein binding
F	0005634	cellular_component	nucleus
F	0005654	cellular_component	nucleoplasm
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0005839	cellular_component	proteasome core complex
F	0006511	biological_process	ubiquitin-dependent protein catabolic process
F	0019773	cellular_component	proteasome core complex, alpha-subunit complex
F	0031625	molecular_function	ubiquitin protein ligase binding
F	0043161	biological_process	proteasome-mediated ubiquitin-dependent protein catabolic process
F	0051603	biological_process	proteolysis involved in protein catabolic process
F	0070062	cellular_component	extracellular exosome
G	0000502	cellular_component	proteasome complex
G	0000932	cellular_component	P-body
G	0003723	molecular_function	RNA binding
G	0004175	molecular_function	endopeptidase activity
G	0005515	molecular_function	protein binding
G	0005634	cellular_component	nucleus
G	0005654	cellular_component	nucleoplasm
G	0005737	cellular_component	cytoplasm
G	0005739	cellular_component	mitochondrion
G	0005829	cellular_component	cytosol
G	0005839	cellular_component	proteasome core complex
G	0005840	cellular_component	ribosome
G	0005929	cellular_component	cilium
G	0006511	biological_process	ubiquitin-dependent protein catabolic process
G	0016363	cellular_component	nuclear matrix
G	0019773	cellular_component	proteasome core complex, alpha-subunit complex
G	0030016	cellular_component	myofibril
G	0030017	cellular_component	sarcomere
G	0035639	molecular_function	purine ribonucleoside triphosphate binding
G	0043123	biological_process	positive regulation of canonical NF-kappaB signal transduction
G	0043161	biological_process	proteasome-mediated ubiquitin-dependent protein catabolic process
G	0050727	biological_process	regulation of inflammatory response
G	0051059	molecular_function	NF-kappaB binding
G	0051603	biological_process	proteolysis involved in protein catabolic process
G	0070062	cellular_component	extracellular exosome
H	0005515	molecular_function	protein binding
H	0005634	cellular_component	nucleus
H	0005737	cellular_component	cytoplasm
H	0005783	cellular_component	endoplasmic reticulum
H	0005829	cellular_component	cytosol
H	0016020	cellular_component	membrane
H	0016607	cellular_component	nuclear speck
H	0043248	biological_process	proteasome assembly
I	0005515	molecular_function	protein binding
I	0005634	cellular_component	nucleus
I	0005654	cellular_component	nucleoplasm
I	0005737	cellular_component	cytoplasm
I	0005783	cellular_component	endoplasmic reticulum
I	0005794	cellular_component	Golgi apparatus
I	0005829	cellular_component	cytosol
I	0021930	biological_process	cerebellar granule cell precursor proliferation
I	0043248	biological_process	proteasome assembly
I	0051131	biological_process	chaperone-mediated protein complex assembly
I	0060090	molecular_function	molecular adaptor activity
I	0070628	molecular_function	proteasome binding
I	0080129	biological_process	proteasome core complex assembly
I	0101031	cellular_component	protein folding chaperone complex
J	0005515	molecular_function	protein binding
J	0005634	cellular_component	nucleus
J	0005829	cellular_component	cytosol
J	0007094	biological_process	mitotic spindle assembly checkpoint signaling
J	0043066	biological_process	negative regulation of apoptotic process
J	0043248	biological_process	proteasome assembly
J	0051131	biological_process	chaperone-mediated protein complex assembly
J	0051726	biological_process	regulation of cell cycle
J	0060090	molecular_function	molecular adaptor activity
J	0101031	cellular_component	protein folding chaperone complex
K	0000502	cellular_component	proteasome complex
K	0004175	molecular_function	endopeptidase activity
K	0004298	molecular_function	threonine-type endopeptidase activity
K	0005515	molecular_function	protein binding
K	0005576	cellular_component	extracellular region
K	0005634	cellular_component	nucleus
K	0005654	cellular_component	nucleoplasm
K	0005737	cellular_component	cytoplasm
K	0005829	cellular_component	cytosol
K	0005839	cellular_component	proteasome core complex
K	0005929	cellular_component	cilium
K	0006508	biological_process	proteolysis
K	0008233	molecular_function	peptidase activity
K	0016604	cellular_component	nuclear body
K	0016787	molecular_function	hydrolase activity
K	0019774	cellular_component	proteasome core complex, beta-subunit complex
K	0034774	cellular_component	secretory granule lumen
K	0043161	biological_process	proteasome-mediated ubiquitin-dependent protein catabolic process
K	0051603	biological_process	proteolysis involved in protein catabolic process
K	1904813	cellular_component	ficolin-1-rich granule lumen
L	0005515	molecular_function	protein binding
L	0005829	cellular_component	cytosol
L	0032991	cellular_component	protein-containing complex
L	0043248	biological_process	proteasome assembly
L	0044877	molecular_function	protein-containing complex binding
L	0051131	biological_process	chaperone-mediated protein complex assembly
L	0060090	molecular_function	molecular adaptor activity
M	0005829	cellular_component	cytosol
M	0032991	cellular_component	protein-containing complex
M	0043248	biological_process	proteasome assembly
M	0044877	molecular_function	protein-containing complex binding

Functional Information from PROSITE/UniProt

site_id	PS00388
Number of Residues	23
Details	PROTEASOME_ALPHA_1 Proteasome alpha-type subunits signature. YsfslTtFSPsGKlvQIEYAlaA

Chain	Residue	Details
A	TYR6-ALA28
G	PHE9-ALA31
C	TYR3-ALA25
F	TYR8-ALA30
E	TYR6-ALA28
B	TYR5-ALA27
D	TYR8-ALA30

site_id	PS00854
Number of Residues	48
Details	PROTEASOME_BETA_1 Proteasome beta-type subunits signature. AGVvYkdGIVLGADtrategmvvadkncs.KihfispniyccgaGtaAD

Chain	Residue	Details
K	ALA47-ASP94
B	LEU35-ASP82

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P49722","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	9
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	11
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P17220","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17323924","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine; by ABL1 and ABL2","evidences":[{"source":"PubMed","id":"16678104","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	2
Details	Glycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	1
Details	Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"UniProtKB","id":"Q9Z2U1","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"16964243","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	1
Details	Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"UniProtKB","id":"P18420","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; alternate","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	1
Details	Glycosylation: {"description":"O-linked (GlcNAc) serine; alternate","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	3
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)"}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17323924","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q9QUM9","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	4
Details	Motif: {"description":"High-affinity association with the preproteasome"}

Chain

Residue

Details

site_id	SWS_FT_FI23
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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